|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-861 |
0e+00 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 1719.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 1 MPVTNLAELDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVEDKVIKNHFASEYIYNKY 80
Cdd:PRK13805 6 MAVTNVAELDALVEKAKKAQEEFATFTQEQVDKIVRAAALAALDARIPLAKMAVEETGRGVVEDKVIKNHFASEYIYNSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 81 KDEKTCGILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAA 160
Cdd:PRK13805 86 KDEKTVGVIEEDDEFGIIEIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAAVAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 161 GAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTF 240
Cdd:PRK13805 166 GAPKDIIQWIEEPSVELTNALMNHPGIALILATGGPGMVKAAYSSGKPALGVGAGNVPAYIDKTADIKRAVNDILLSKTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 241 DNGVVCASEQAVIVMDEVYDEVKERFATHKAHVLSKADADKVRKVLL--IDGALNAKIVGQPATKIAEMAGVKVPADTKI 318
Cdd:PRK13805 246 DNGMICASEQAVIVDDEIYDEVKEEFASHGAYFLNKKELKKLEKFIFgkENGALNADIVGQSAYKIAEMAGFKVPEDTKI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 319 LVGEgIGEVSYDDEFAHEKLSPTLGMFRASSFENAVDQAVKMVEIGGIGHTSGLYTDQDvnaDRIRYFGDRLKTARILVN 398
Cdd:PRK13805 326 LIAE-VKGVGESEPLSHEKLSPVLAMYKAKDFEDAVEKAEKLVEFGGLGHTAVIYTNDD---ELIKEFGLRMKACRILVN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 399 IPTTHGGIGDLYNfNVAPSLTLGCGSWGGNSISENVGPKHLINKKIVAKRAENMLWHKLPKSIYFRRGSLPVALGDLEGK 478
Cdd:PRK13805 402 TPSSQGGIGDLYN-KLAPSLTLGCGSWGGNSVSENVGAKHLLNIKTVAKRRENMQWFKVPKKIYFERGSLPYLLDELDGK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 479 KRAFLVTDRFLFNNGYADEVVSLLKA--QGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWV 556
Cdd:PRK13805 481 KRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 557 MYEHPETHFEELAMRFMDIRKRIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVDAN 636
Cdd:PRK13805 561 FYEHPETDFEDLAQKFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPN 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 637 LVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGAKDPIAREKVHNAATIAGVAFANA 716
Cdd:PRK13805 641 LVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAKDPEAREKMHNASTIAGMAFANA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 717 FLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPtKQTAFSQYDRPQARRRYAEVADHLGLsqPGDRTAQKIER 796
Cdd:PRK13805 721 FLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPP-KQAAFPQYEYPRADERYAEIARHLGL--PGSTTEEKVES 797
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910047 797 LLGWLEELKLALDIPASIQAAGVNEADFLAKVDELAVEAFDDQCTGANPRYPLISELKEVLLASY 861
Cdd:PRK13805 798 LIKAIEELKAELGIPMSIKEAGVDEADFLAKLDELAELAFDDQCTGANPRYPLISELKEILLDAY 862
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
9-448 |
0e+00 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 731.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 9 LDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVEDKVIKNHFASEYIYNKYKDEKTCGI 88
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVEDKVIKNHFASEYVYNDIKDMKTVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 89 LEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIG 168
Cdd:cd07122 81 IEEDEEKGIVEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAGAPEGLIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 169 WIDQPSVELSNALMKHEGIALILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCAS 248
Cdd:cd07122 161 WIEEPSIELTQELMKHPDVDLILATGGPGMVKAAYSSGKPAIGVGPGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 249 EQAVIVMDEVYDEVKERFATHKAHVLSKADADKVRKVLLIDGA-LNAKIVGQPATKIAEMAGVKVPADTKILVGEgIGEV 327
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRGAYFLNEEEKEKLEKALFDDGGtLNPDIVGKSAQKIAELAGIEVPEDTKVLVAE-ETGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 328 SYDDEFAHEKLSPTLGMFRASSFENAVDQAVKMVEIGGIGHTSGLYTDqdvNADRIRYFGDRLKTARILVNIPTTHGGIG 407
Cdd:cd07122 320 GPEEPLSREKLSPVLAFYRAEDFEEALEKARELLEYGGAGHTAVIHSN---DEEVIEEFALRMPVSRILVNTPSSLGGIG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 520910047 408 DLYNFnVAPSLTLGCGSWGGNSISENVGPKHLINKKIVAKR 448
Cdd:cd07122 397 DTYNG-LAPSLTLGCGSWGGNSTSDNVGPKHLLNIKRVAYR 436
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
456-858 |
0e+00 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 709.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 456 KLPKSIYFRRGSLPVALGDLEGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQ 535
Cdd:cd08178 1 KVPPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 PDVILALGGGSPMDAAKIMWVMYEHPETHFEELAMRFMDIRKRIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQT 615
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKD 695
Cdd:cd08178 161 GKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNG-ND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 696 PIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKQTAFSQYDRPQARRRYA 775
Cdd:cd08178 240 IEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQAAFPQYKYYVAKERYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 776 EVADHLGLsqPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFLAKVDELAVEAFDDQCTGANPRYPLISELKE 855
Cdd:cd08178 320 EIADLLGL--GGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDKLAEDAFDDQCTGANPRYPLISELKE 397
|
...
gi 520910047 856 VLL 858
Cdd:cd08178 398 ILL 400
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
9-448 |
0e+00 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 658.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 9 LDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVEDKVIKNHFASEYIYNKYKDEKTCGI 88
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 89 LEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIG 168
Cdd:cd07081 81 LTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPENLIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 169 WIDQPSVELSNALMKHEGIALILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCAS 248
Cdd:cd07081 161 WIDNPSIELAQRLMKFPGIGLLLATGGPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 249 EQAVIVMDEVYDEVKERFATHKAHVLSKADADKVRKVLLIDGALNAKIVGQPATKIAEMAGVKVPADTKILvgegIGEVS 328
Cdd:cd07081 241 EQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGDVNRDIVGQDAYKIAAAAGLKVPQETRIL----IGEVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 329 YDDE---FAHEKLSPTLGMFRASSFENAVDQAVKMVEIGGIGHTSGLYTDQDVNADRIRYFGDRLKTARILVNIPTTHGG 405
Cdd:cd07081 317 SLAEhepFAHEKLSPVLAMYRAANFADADAKALALKLEGGCGHTSAMYSDNIKAIENMNQFANAMKTSRFVKNGPCSQGG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 520910047 406 IGDLYNFNVAPSLTLGCGSWGGNSISENVGPKHLINKKIVAKR 448
Cdd:cd07081 397 LGDLYNFRGWPSMTLGCGTWGGNSVSENVGPKHLVNLKTVALR 439
|
|
| EutH_ACDH |
TIGR02518 |
acetaldehyde dehydrogenase (acetylating); |
12-446 |
1.50e-158 |
|
acetaldehyde dehydrogenase (acetylating);
Pssm-ID: 131570 Cd Length: 488 Bit Score: 473.20 E-value: 1.50e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 12 LVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVEDKVIKNHFASEYIYNKYKDEKTCGILEE 91
Cdd:TIGR02518 13 LIRSAKVAQKKLANMTQEQIDKIVKAIVDAAYENAVKLAKMANEETGFGKWEDKVIKNVFAATIVYDSIKDMKTIGILSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 92 DDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIGWID 171
Cdd:TIGR02518 93 DKEKKVIEIAVPVGVVAGLIPSTNPTSTAIYKTLISIKARNAIVFSPHPNAKKCIIETVKLMRKAAEEAGAPEGAIGCIT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 172 QPSVELSNALMKHEGIALILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQA 251
Cdd:TIGR02518 173 VPTIEGTNELMKNKDTSLILATGGEAMVKAAYSSGTPAIGVGPGNGPAYIERTANVKKAVRDIIDSKTFDNGTICASEQS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 252 VIVMDEVYDEVKERFATHKAHVLSKADADKVRKVLL-IDGALNAKIVGQPATKIAEMAGVKVPADTKILVGEGIGeVSYD 330
Cdd:TIGR02518 253 IIVEECNKDAVVEELKKQGGYFLTAEEAEKLGKFILrPNGTMNPQIVGKSPQVIANLAGLTVPEDAKVLIGEQNG-VGNK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 331 DEFAHEKLSPTLGMFRASSFENAVDQAVKMVEIGGIGHTSGLYTDqdvNADRIRYFGDRLKTARILVNIPTTHGGIGDly 410
Cdd:TIGR02518 332 NPYSREKLTTILAFYTEENWHEACELSIELLQNEGAGHTLIIHSE---NKDIVREFALKKPVSRMLVNTGGSLGGIGA-- 406
|
410 420 430
....*....|....*....|....*....|....*.
gi 520910047 411 NFNVAPSLTLGCGSWGGNSISENVGPKHLINKKIVA 446
Cdd:TIGR02518 407 TTNLVPAFTLGCGAVGGSSTSDNITPENLINIRRVA 442
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
451-861 |
3.33e-157 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 465.75 E-value: 3.33e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 451 NMLWHKLPKSIYFRRGSLPvALGDL---EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKG 527
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALA-ELGEElkrLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 528 AEQMRSFQPDVILALGGGSPMDAAKIMWVMYEHPEThfeelAMRFMDIRKriykfpKMGQKAELVCITTTSGTGSEVTPF 607
Cdd:COG1454 80 AAAAREFGADVVIALGGGSAIDAAKAIALLATNPGD-----LEDYLGIKK------VPGPPLPLIAIPTTAGTGSEVTPF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 608 AVVTDDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPS 687
Cdd:COG1454 149 AVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 688 SYANGaKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydr 767
Cdd:COG1454 229 AVADG-DDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA--------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 768 PQARRRYAEVADHLGLSqPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRY 847
Cdd:COG1454 293 PAAPERYAEIARALGLD-VGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDL----PELAELALADRCLANNPRP 367
|
410
....*....|....
gi 520910047 848 PLISELKEVLLASY 861
Cdd:COG1454 368 LTEEDIEAILRAAY 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
457-862 |
3.71e-157 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 465.51 E-value: 3.71e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGSLPvALGDLEGKkRAFLVTD-RFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQ 535
Cdd:cd08179 4 VPRDIYFGEGALE-YLKTLKGK-RAFIVTGgGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 PDVILALGGGSPMDAAKIMWVMYEHPETHFEELAMRFmdirkriyKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQT 615
Cdd:cd08179 82 PDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPF--------PLPELRKKARFIAIPSTSGTGSEVTRASVITDTEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKD 695
Cdd:cd08179 154 GIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGG-KD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 696 PIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDnptkqtafsqydrPQARRRYA 775
Cdd:cd08179 233 LEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKD-------------PEARARYA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 776 evADHLGLSQpgdrtAQKIERLLGWLEELKLALDIPASIQAAGVNEADFLAKVDELAVEAFDDQCTGANPRYPLISELKE 855
Cdd:cd08179 300 --ALLIGLTD-----EELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNDACTGTNPRKPTVEEMKE 372
|
....*..
gi 520910047 856 VLLASYY 862
Cdd:cd08179 373 LLKAAYY 379
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
14-447 |
7.13e-123 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 377.72 E-value: 7.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 14 ARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESG-------------MGIVEDKVIKNHFASEYIYNKy 80
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiamMGCSESKLYKNIDTERGITAS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 81 kDEKTCGILEEDdSMGTMTIAEPVGIICGIVPTTNPTStAIFKSLISLKTRNGIIFSPHPRAKnSTNDAAKLVLDAAVAA 160
Cdd:cd07077 80 -VGHIQDVLLPD-NGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAP-FTNRALALLFQAADAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 161 GAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGMVKAAYSS--GKPAIGVGAGNVPVVIDETADIKRAVASVLMSK 238
Cdd:cd07077 156 HGPKILVLYVPHPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 239 TFDNgVVCASEQAVIVMDEVYDEVKERFATHKAhvlskadadkvrkvllidgalnakivgqpatkiaeMAGVKVPADTKI 318
Cdd:cd07077 236 FFDQ-NACASEQNLYVVDDVLDPLYEEFKLKLV-----------------------------------VEGLKVPQETKP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 319 LVGEGIGEvsyDDEFAHEKLSPTLGMFRASSFENAVDQAVKMVEIGGIGHTSGLYTDQDVNADrirYFGDRLKTARILVN 398
Cdd:cd07077 280 LSKETTPS---FDDEALESMTPLECQFRVLDVISAVENAWMIIESGGGPHTRCVYTHKINKVD---DFVQYIDTASFYPN 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 520910047 399 IPTTHGGiGDLYNFNVAPSLTLGCGSWGGnsisENVGPKHLINKKIVAK 447
Cdd:cd07077 354 ESSKKGR-GAFAGKGVERIVTSGMNNIFG----AGVGHDALRPLKRLVR 397
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
458-853 |
1.21e-119 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 367.70 E-value: 1.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGSLPvALGDL--EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQ 535
Cdd:pfam00465 1 PTRIVFGAGALA-ELGEElkRLGARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 PDVILALGGGSPMDAAKIMWVMYEHPETHFEELamrfmdirkriYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQT 615
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL-----------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKD 695
Cdd:pfam00465 149 GEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADG-ED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 696 PIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRRYA 775
Cdd:pfam00465 228 LEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA---------------PAAPEKLA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520910047 776 EVADHLGlsqpGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRYPLISEL 853
Cdd:pfam00465 293 QLARALG----EDSDEEAAEEAIEALRELLRELGLPTTLSELGVTEEDL----DALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
458-849 |
6.20e-116 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 358.30 E-value: 6.20e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGSLpVALGDL---EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSF 534
Cdd:cd08551 1 PTRIVFGAGAL-ARLGEElkaLGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 535 QPDVILALGGGSPMDAAKIMWVMYEHPETHFEELAMRfmdirkriyKFPKmgQKAELVCITTTSGTGSEVTPFAVVTDDQ 614
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIG---------KVPK--PGLPLIAIPTTAGTGSEVTPNAVITDPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 615 TGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaK 694
Cdd:cd08551 149 TGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADG-S 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 695 DPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPtkqtafsqydrpqarRRY 774
Cdd:cd08551 228 DLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACP---------------EKY 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910047 775 AEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRYPL 849
Cdd:cd08551 293 AEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDI----PELAEDAMKSGRLLSNNPRPL 363
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
454-857 |
1.95e-114 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 354.61 E-value: 1.95e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 454 WHKLPKSIYFRRGSLPvALGDLEGKkRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRS 533
Cdd:cd14862 2 WYFSSPKIVFGEDALS-HLEQLSGK-RALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 534 FQPDVILALGGGSPMDAAKIMWVMYEHPETHFEEL-AMRFMDIRKriykfpkmgqKAELVCITTTSGTGSEVTPFAVVTD 612
Cdd:cd14862 80 FEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDIsPLDLLGLRK----------KAKLIAIPTTSGTGSEATWAIVLTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 613 DQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANG 692
Cdd:cd14862 150 TEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 693 aKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDnptkqtafsqydrpqARR 772
Cdd:cd14862 230 -DDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKV---------------TDE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 773 RYAEVADHLGLSQPGDRTAQKierLLGWLEELKLALDIPASIQAAGVNEADFLAKVDELAVEAFDDQCTGANPRYPLISE 852
Cdd:cd14862 294 RYDLLKLLGIEARDEEEALKK---LVEAIRELYKEVGQPLSIKDLGISEEEFEEKLDELVEYAMEDSCTITSPRPPSEED 370
|
....*
gi 520910047 853 LKEVL 857
Cdd:cd14862 371 LKKLF 375
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
456-858 |
8.53e-114 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 351.41 E-value: 8.53e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 456 KLPKSIYFRRGSLPvALGDLEGKkRAFLVTDRFLFNNGYADEVVSLLKaQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQ 535
Cdd:cd08180 2 SLKTKIYSGEDSLE-RLKELKGK-RVFIVTDPFMVKSGMVDKVTDELD-KSNEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 PDVILALGGGSPMDAAKimwvmyehpethfeelAMRFMdirkrIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQT 615
Cdd:cd08180 79 PDTIIALGGGSAIDAAK----------------AIIYF-----ALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKD 695
Cdd:cd08180 138 GIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDG-DD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 696 PIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYnandnptkqtafsqydrpqarrrya 775
Cdd:cd08180 217 LEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF------------------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 776 evadhlglsqpgdrtaqkierLLGWLEELKLALDIPASIQAAGVNEADFLAKVDELAVEAFDDQCTGANPRYPLISELKE 855
Cdd:cd08180 272 ---------------------LIAAIRRLNKKLGIPSTLKELGIDEEEFEKAIDEMAEAALADRCTATNPRKPTAEDLIE 330
|
...
gi 520910047 856 VLL 858
Cdd:cd08180 331 LLR 333
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
458-861 |
6.30e-102 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 322.17 E-value: 6.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGS---LPVALGDLEGKkRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSF 534
Cdd:cd08194 1 PRTIIIGGGAleeLGEEAASLGGK-RALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 535 QPDVILALGGGSPMDAAKIMWVMYEHPEthfeelamrfmDIRKriYKFPKMGQKA--ELVCITTTSGTGSEVTPFAVVTD 612
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGG-----------PIRD--YMGPRKVDKPglPLIAIPTTAGTGSEVTRFTVITD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 613 DQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANG 692
Cdd:cd08194 147 TETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 693 aKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTkqtafsqydrpqarr 772
Cdd:cd08194 227 -DDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPE--------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 773 RYAEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPaSIQAAGVNEADFLAKVDELAVEAFDDQCTGANPRYPLISE 852
Cdd:cd08194 291 RYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDKMAEDALASGSPANNPRVPTKEE 369
|
....*....
gi 520910047 853 LKEVLLASY 861
Cdd:cd08194 370 IIELYREAW 378
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
457-857 |
2.01e-99 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 315.26 E-value: 2.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGSLPVALGDL--EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSF 534
Cdd:cd08176 5 LNPTSYFGWGAIEEIGEEAkkRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 535 QPDVILALGGGSPMDAAKIMWVMYEHPethfeelamrFMDIRKRIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQ 614
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGIIVANP----------GADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 615 TGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaK 694
Cdd:cd08176 155 KKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANP-N 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 695 DPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKqtafsqydrpqarrrY 774
Cdd:cd08176 234 NVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEK---------------Y 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 775 AEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADflakVDELAVEAFDDQCTGANPRYPLISELK 854
Cdd:cd08176 299 RDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEED----IEALAEDALNDVCTPGNPREATKEDII 374
|
...
gi 520910047 855 EVL 857
Cdd:cd08176 375 ALY 377
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
457-856 |
4.88e-95 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 303.67 E-value: 4.88e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGSLPvALGDL---EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRS 533
Cdd:cd08188 5 IPPVNLFGPGCLK-EIGDElkkLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 534 FQPDVILALGGGSPMDAAKIMWVMYEHPEthfeelamrfmDIRKR--IYKFPKMGqkAELVCITTTSGTGSEVTPFAVVT 611
Cdd:cd08188 84 NGCDFIISVGGGSAHDCAKAIGILATNGG-----------EIEDYegVDKSKKPG--LPLIAINTTAGTASEVTRFAVIT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 612 DDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYAN 691
Cdd:cd08188 151 DEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 692 GaKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNandnptkqtafsqydRPQAR 771
Cdd:cd08188 231 G-KDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFN---------------LPACP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 772 RRYAEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRYPLIS 851
Cdd:cd08188 295 ERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDF----PLLAENALKDACGPTNPRQATKE 370
|
....*
gi 520910047 852 ELKEV 856
Cdd:cd08188 371 DVIAI 375
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
477-861 |
3.04e-93 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 299.07 E-value: 3.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 477 GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWV 556
Cdd:cd14863 26 GCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 557 MYEHPEThfeelAMRFMDIRKRIYKFPKmgqkaELVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVDAN 636
Cdd:cd14863 106 LLTNPGP-----IIDYALAGPPVPKPGI-----PLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 637 LVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKDPIAREKVHNAATIAGVAFANA 716
Cdd:cd14863 176 LTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDG-DNLEARENMLLASNLAGIAFNNA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 717 FLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKqtafsqydrpqarrrYAEVADHLGLSQPGDRTAQKIER 796
Cdd:cd14863 255 GTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEK---------------VKKIAKALGVSFPGESDEELGEA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910047 797 LLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRYPLISELKEVLLASY 861
Cdd:cd14863 320 VADAIREFMKELGIPSLFEDYGIDKEDL----DKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
467-848 |
8.51e-91 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 292.45 E-value: 8.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 467 SLPVALGDLeGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGS 546
Cdd:cd08189 17 QLPEALKKL-GIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 547 PMDAAKIMWVMYEHPETHFEELAmRFMDIRKRIykfpkmgqkAELVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYEL 626
Cdd:cd08189 96 VIDCAKVIAARAANPKKSVRKLK-GLLKVRKKL---------PPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 627 TPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGAkDPIAREKVHNAA 706
Cdd:cd08189 166 IPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGS-DLEARENMLLAS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 707 TIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNandnptkqtafsqydRPQARRRYAEVADHLGLSQP 786
Cdd:cd08189 245 YYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFY---------------GPAAEKRLAELADAAGLGDS 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520910047 787 GDRTAQKIERLLGWLEELKLALDIPASIqaAGVNEADFlakvDELAVEAFDDqctgANPRYP 848
Cdd:cd08189 310 GESDSEKAEAFIAAIRELNRRMGIPTTL--EELKEEDI----PEIAKRALKE----ANPLYP 361
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
7-407 |
3.98e-90 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 293.73 E-value: 3.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 7 AELDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVEDKVIKNHFASEyiynkykdeKTC 86
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETGMGRVEDKIAKNVAAAE---------KTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 87 GIleEDDSM------GTMTIAE--PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAV 158
Cdd:PRK15398 107 GV--EDLTTealtgdNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 159 AAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSK 238
Cdd:PRK15398 185 AAGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKGA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 239 TFDNGVVCASEQAVIVMDEVYDEVKERFATHKAHVLSKADADKVRKVLLIDG-ALNAKIVGQPATKIAEMAGVKVPADTK 317
Cdd:PRK15398 265 SFDNNLPCIAEKEVIVVDSVADELMRLMEKNGAVLLTAEQAEKLQKVVLKNGgTVNKKWVGKDAAKILEAAGINVPKDTR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 318 ILvgegIGEVSYDDEFA-HEKLSPTLGMFRASSFENAVDQAVKmVEiGGIGHTSGLYTDqdvNADRIRYFGDRLKTARIL 396
Cdd:PRK15398 345 LL----IVETDANHPFVvTELMMPVLPVVRVKDVDEAIALAVK-LE-HGNRHTAIMHSR---NVDNLNKMARAIQTSIFV 415
|
410
....*....|.
gi 520910047 397 VNIPtTHGGIG 407
Cdd:PRK15398 416 KNGP-SYAGLG 425
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
466-861 |
5.75e-89 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 287.90 E-value: 5.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 466 GSLPVALGDLeGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGG 545
Cdd:cd14865 17 ENLPAELARL-GARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGIIAVGGG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 546 SPMDAAKIMWVMYEHPETHFEELAMRFMDIRKRIykfPkmgqkaeLVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYE 625
Cdd:cd14865 96 SVIDTAKGVNILLSEGGDDLDDYGGANRLTRPLK---P-------LIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 626 LTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKDPIAREKVHNA 705
Cdd:cd14865 166 LLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNG-KDLEARLALAIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 706 ATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRRYAEVADHLGLSQ 785
Cdd:cd14865 245 ATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNL---------------DAAAERYAELALALAYGV 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520910047 786 --PGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRYPLISELKEVLLASY 861
Cdd:cd14865 310 tpAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQL----EAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
7-408 |
8.74e-86 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 281.05 E-value: 8.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 7 AELDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVEDKVIKNHFASEyiynkykdeKTC 86
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETGMGRVEDKIAKNHLAAE---------KTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 87 GIleEDDSM------GTMTIAE--PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAV 158
Cdd:cd07121 75 GT--EDLTTtawsgdNGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 159 AAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSK 238
Cdd:cd07121 153 EAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 239 TFDNGVVCASEQAVIVMDEVYDEVKERFATHKAHVLSKADADKVRKVLLIDG---ALNAKIVGQPATKIAEMAGVKVPAD 315
Cdd:cd07121 233 SFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEVVLLTNkgaTPNKKWVGKDASKILKAAGIEVPAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 316 TKILvgegIGEVSYDDEFA-HEKLSPTLGMFRASSFENAVDQAVKmVEiGGIGHTSGLYTDqdvNADRIRYFGDRLKTAR 394
Cdd:cd07121 313 IRLI----IVETDKDHPFVvEEQMMPILPVVRVKNFDEAIELAVE-LE-HGNRHTAIIHSK---NVENLTKMARAMQTTI 383
|
410
....*....|....*
gi 520910047 395 ILVNIPTTHG-GIGD 408
Cdd:cd07121 384 FVKNGPSYAGlGVGG 398
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-857 |
2.84e-83 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 272.45 E-value: 2.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGSLPvALGDLEGK--KRAFLVTDR-FLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRS 533
Cdd:cd08185 3 QPTRILFGAGKLN-ELGEEALRpgKKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 534 FQPDVILALGGGSPMDAAKIMWVMYEHPETHFEelamrfmdirkriYKFPKMGQKAE------LVCITTTSGTGSEVTPF 607
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWD-------------YIFGGTGKGPPpekalpIIAIPTTAGTGSEVDPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 608 AVVTDDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPS 687
Cdd:cd08185 149 AVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 688 SYANGAkDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEF-HLPHGLANSLLMANVVRYNANDNPTKqtafsqyd 766
Cdd:cd08185 229 AVKDGS-DLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEK-------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 767 rpqarrrYAEVADHLGLSQPGDRTAQK-IERLLGWLEELKLALdipaSIQAAGVNEADFlakvDELAVEAFD--DQCTGA 843
Cdd:cd08185 300 -------FAFVARAEASGLSDAKAAEDfIEALRKLLKDIGLDD----LLSDLGVTEEDI----PWLAENAMEtmGGLFAN 364
|
410
....*....|....
gi 520910047 844 NPRYPLISELKEVL 857
Cdd:cd08185 365 NPVELTEEDIVEIY 378
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
461-860 |
4.45e-83 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 271.69 E-value: 4.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 461 IYFRRGS---LPVALGDLeGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPD 537
Cdd:cd14861 6 IRFGAGAiaeLPEELKAL-GIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 538 VILALGGGSPMDAAKIMWVMYEHPE--THFEELAMRFMDIRKRIykfpkmgqkAELVCITTTSGTGSEVTPFAVVTDDQT 615
Cdd:cd14861 85 GIIALGGGSAIDAAKAIALMATHPGplWDYEDGEGGPAAITPAV---------PPLIAIPTTAGTGSEVGRAAVITDDDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGAkD 695
Cdd:cd14861 156 GRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGS-D 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 696 PIAREKVHNAATIAGVAFANAfLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNandnptkqtafsqydRPQARRRYA 775
Cdd:cd14861 235 LEARGEMMMAALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFN---------------RPAVEDKLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 776 EVADHLGLSQPGDrtaqkiERLLGWLEELKLALDIPASIQAAGVNEADflakVDELAVEAFDDQCTGANPRYPLISELKE 855
Cdd:cd14861 299 RLARALGLGLGGF------DDFIAWVEDLNERLGLPATLSELGVTEDD----LDELAELALADPCHATNPRPVTAEDYRA 368
|
....*
gi 520910047 856 VLLAS 860
Cdd:cd14861 369 LLREA 373
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
477-856 |
9.20e-80 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 262.86 E-value: 9.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 477 GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWV 556
Cdd:cd17814 25 GARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 557 MYEHPethfeelamrfMDIRKR--IYKFPKMGqkAELVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVD 634
Cdd:cd17814 105 VVSNG-----------GHILDYegVDKVRRPL--PPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 635 ANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANgAKDPIAREKVHNAATIAGVAFA 714
Cdd:cd17814 172 PETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAD-PDDLEAREKMMLASLQAGLAFS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 715 NAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRRYAEVADHLGLSQPGDRTAQKI 794
Cdd:cd17814 251 NASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF---------------PAAPERYRKIAEAMGLDVDGLDDEEVA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520910047 795 ERLLGWLEELKLALDIPASIQAAGVNEADflakVDELAVEAFDDQCTGANPRYPLISELKEV 856
Cdd:cd17814 316 ERLIEAIRDLREDLGIPETLSELGVDEED----IPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
458-835 |
1.48e-78 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 259.75 E-value: 1.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGSLpVALGDL---EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSF 534
Cdd:cd08193 4 VPRIICGAGAA-ARLGELlreLGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 535 QPDVILALGGGSPMDAAKIMWVmyehpethfeeLAMRFMDIRkRIYKFPKM-GQKAELVCITTTSGTGSEVTPFAVVTDD 613
Cdd:cd08193 83 GADGVIGFGGGSSMDVAKLVAL-----------LAGSDQPLD-DIYGVGKAtGPRLPLILVPTTAGTGSEVTPISIVTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 614 QTgAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVS-VLANEYSDGQALQALKLLKEYLPSSYANG 692
Cdd:cd08193 151 ET-EKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 693 aKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARR 772
Cdd:cd08193 230 -SDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL---------------PAAEA 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520910047 773 RYAEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADflakVDELAVEA 835
Cdd:cd08193 294 LYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEED----LPMLAEDA 352
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
457-856 |
2.33e-78 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 259.29 E-value: 2.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGSLPVALGDLE--GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSF 534
Cdd:TIGR02638 6 LNETSYFGAGAIEDIVDEVKrrGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 535 QPDVILALGGGSPMDAAKIMWVMYEHPEthfeelamrFMDIRKRIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQ 614
Cdd:TIGR02638 86 GADYLIAIGGGSPIDTAKAIGIISNNPE---------FADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 615 TGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaK 694
Cdd:TIGR02638 157 NKRKFVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGG-K 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 695 DPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRRY 774
Cdd:TIGR02638 236 DLEAREQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNA---------------EFTGEKY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 775 AEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADflakVDELAVEAFDDQCTGANPRYPLISELK 854
Cdd:TIGR02638 301 REIAKAMGVKTEGMSDEEARDAAVEAVKTLSKRVGIPEGLSELGVKEED----IPALAEAALADVCTGGNPRETTVEEIE 376
|
..
gi 520910047 855 EV 856
Cdd:TIGR02638 377 EL 378
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
456-857 |
2.10e-77 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 256.35 E-value: 2.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 456 KLPKSIYFRRGSLPVaLGDL---EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVttFYEVEADPTLSIVKKGAEQMR 532
Cdd:cd08196 4 YQPVKIIFGEGILKE-LPDIikeLGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 533 SFQPDVILALGGGSPMDAAKIMWVMYEHPEthfeelamrfmDIRKRIYKFPKMGQKA-ELVCITTTSGTGSEVTPFAVVT 611
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDG-----------SIEDYLEGKKKIPKKGlPLIAIPTTAGTGSEVTPVAVLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 612 DDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYAN 691
Cdd:cd08196 150 DKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 692 GaKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKQTAFSQYdrpqar 771
Cdd:cd08196 230 P-NDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQ------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 772 rryaevadhLGLSQPGDrTAQKIerllgwlEELKLALDIPASIQAAGVNEADflakVDELAVEAFDDQCTGANPRYPLIS 851
Cdd:cd08196 303 ---------LGFKDAEE-LADKI-------EELKKRIGLRTRLSELGITEED----LEEIVEESFHPNRANNNPVEVTKE 361
|
....*.
gi 520910047 852 ELKEVL 857
Cdd:cd08196 362 DLEKLL 367
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
458-857 |
7.08e-74 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 247.03 E-value: 7.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGSLpVALGDL--EGKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFyEVEADPTLSIVKKGAEQMRSFQ 535
Cdd:cd08183 1 PPRIVFGRGSL-QELGELaaELGKRALLVTGRSSLRSGRLARLLEALEAAGIEVALF-SVSGEPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 PDVILALGGGSPMDAAKIMWVMYEHPEThfeelAMRFMDIrkrIYKFPKMGQK-AELVCITTTSGTGSEVTPFAVVTDDQ 614
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGS-----VLDYLEV---VGKGRPLTEPpLPFIAIPTTAGTGSEVTKNAVLSSPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 615 TGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGAk 694
Cdd:cd08183 151 HGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGE- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 695 DPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkQTAFSQYDRPQARRRY 774
Cdd:cd08183 230 DLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANL------RALREREPDSPALARY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 775 AEVADHLGlsqpGDRTAQkIERLLGWLEELKLALDIPaSIQAAGVNEADFlakvDELAVEAFDDQCTGANPRYPLISELK 854
Cdd:cd08183 304 RELAGILT----GDPDAA-AEDGVEWLEELCEELGIP-RLSEYGLTEEDF----PEIVEKARGSSSMKGNPIELSDEELL 373
|
...
gi 520910047 855 EVL 857
Cdd:cd08183 374 EIL 376
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
457-861 |
1.65e-71 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 241.36 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGS---LPVALGDLegKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRS 533
Cdd:cd08191 3 SPSRLLFGPGArraLGRVAARL--GSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 534 FQPDVILALGGGSPMDAAKIMWVMYEH---PETHFEELAMRfmdirkriykfpkmGQKAELVCITTTSGTGSEVTPFAVV 610
Cdd:cd08191 81 FDPDVVIGLGGGSNMDLAKVVALLLAHggdPRDYYGEDRVP--------------GPVLPLIAVPTTAGTGSEVTPVAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 611 TDDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAY---------------VSVLANEYSDGQAL 675
Cdd:cd08191 147 TDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYtardfppfprldpdpVYVGKNPLTDLLAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 676 QALKLLKEYLPSSYANGAkDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNandn 755
Cdd:cd08191 227 EAIRLIGRHLPRAVRDGD-DLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 756 ptkqtafsqydRPQARRRYAEVADHLGLsQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEA 835
Cdd:cd08191 302 -----------RPARAAELAEIARALGV-TTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADL----PGLAEKA 365
|
410 420
....*....|....*....|....*..
gi 520910047 836 FDDQ-CTGANPRYPLISELKEVLLASY 861
Cdd:cd08191 366 LSVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
461-830 |
1.34e-69 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 235.20 E-value: 1.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 461 IYFRRGSLPVaLGDL---EGKKRAFLVTDRFLFNNGYADEVVSLLkAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPD 537
Cdd:cd08182 4 IIFGPGALAE-LKDLlggLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 538 VILALGGGSPMDAAKIMWVMYEHPETHFEELAmrfmDIRKRIYKfpkmgQKAELVCITTTSGTGSEVTPFAVVTDDQTGA 617
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGENLLLLR----TGEKAPEE-----NALPLIAIPTTAGTGSEVTPFATIWDEAEGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 618 KYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPsSYANGAKDPI 697
Cdd:cd08182 153 KYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLP-LLLENLPNLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 698 AREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafSQYDRPQARRRYAEV 777
Cdd:cd08182 232 AREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNA----------GADDECDDDPRGREI 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 520910047 778 ADHLGLSQPGDrTAQKIERLLgwleelkLALDIPASIQAAGVNEADFLAKVDE 830
Cdd:cd08182 302 LLALGASDPAE-AAERLRALL-------ESLGLPTRLSEYGVTAEDLEALAAS 346
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
460-861 |
4.49e-68 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 232.44 E-value: 4.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 460 SIYFRRGSLPVALGDLE--GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPD 537
Cdd:cd08190 3 NIRFGPGATRELGMDLKrlGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 538 VILALGGGSPMDAAKIMWVMYEHPETHFEelamrfmDIRKRIYK-FPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQTG 616
Cdd:cd08190 83 AFVAVGGGSVIDTAKAANLYATHPGDFLD-------YVNAPIGKgKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 617 AKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVL------------------ANEYSDGQALQAL 678
Cdd:cd08190 156 VKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPISDVWAEKAI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 679 KLLKEYLPSSYANGaKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGA-------------EFHLPHGLANSLLMA 745
Cdd:cd08190 236 ELIGKYLRRAVNDG-DDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgypvdHPHVPHGLSVALTAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 746 NVVRYNANDNPtkqtafsqydrpqarRRYAEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADfl 825
Cdd:cd08190 315 AVFRFTAPACP---------------ERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDD-- 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 520910047 826 akVDELAVEAFDDQ-CTGANPRYPLISELKEVLLASY 861
Cdd:cd08190 378 --IPALVEGTLPQQrLLKLNPRPVTEEDLEEIFEDAL 412
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
462-856 |
2.95e-67 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 229.50 E-value: 2.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 462 YFRRGSLPVALGDLE--GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVI 539
Cdd:PRK10624 12 YFGRGAIGALTDEVKrrGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 540 LALGGGSPMDAAKIMWVMYEHPEthfeelamrFMDIRKRIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDDQTGAKY 619
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNPE---------FADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 620 PLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANgakDPIAR 699
Cdd:PRK10624 163 VCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG---DKEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 700 EKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRRYAEVAD 779
Cdd:PRK10624 240 EGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA---------------DFTGEKYRDIAR 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520910047 780 HLGLSQPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADflakVDELAVEAFDDQCTGANPRYPLISELKEV 856
Cdd:PRK10624 305 AMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEED----IPALAQAAFDDVCTGGNPREATLEDIVEL 377
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
456-758 |
1.48e-60 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 210.13 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 456 KLPKSIYFRRGSLPV------ALGdlegkKRAFLVTDRF-LFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGA 528
Cdd:cd08181 2 YMPTKVYFGKNCVEKhadelaALG-----KKALIVTGKHsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 529 EQMRSFQPDVILALGGGSPMDAAKIMWVMYEHPEtHFEELamrfmdirkriYKFPKMGQKAELVCITTTSGTGSEVTPFA 608
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAANKD-GDEDL-----------FQNGKYNPPLPIVAIPTTAGTGSEVTPYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 609 VVTDDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPsS 688
Cdd:cd08181 145 ILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLP-N 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 689 YANGAKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTK 758
Cdd:cd08181 224 LLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEK 293
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-405 |
6.51e-56 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 197.45 E-value: 6.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 14 ARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESG--MGIVEDKVIKNHFASEYIYNKYKDEKTCGILEE 91
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGkpIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 92 DDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVldaaVAAGAPKDIIGWID 171
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELL----QEAGLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 172 QPSVELSNALMKHEGIALILATGGPGMVKAAY----SSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCA 247
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMkaaaENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 248 SEQAVIVMDEVYDEVKERFAThkahvlskadadkvrkvllidgalnakivgqpatkiaemagVKVPADTkilvgegigev 327
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT-----------------------------------------VLVDVDP----------- 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520910047 328 syDDEFAHEKLS-PTLGMFRASSFENAVDQAVKmveiGGIGHTSGLYTDqdvNADRIRYFGDRLKTARILVNIPTTHGG 405
Cdd:cd06534 265 --DMPIAQEEIFgPVLPVIRFKDEEEAIALAND----TEYGLTAGVFTR---DLNRALRVAERLRAGTVYINDSSIGVG 334
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
477-845 |
1.23e-53 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 191.71 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 477 GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWV 556
Cdd:PRK09860 30 GFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 557 myehpethfeeLAMRFMDIRKriYKFPKMGQKAEL--VCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVD 634
Cdd:PRK09860 110 -----------VAANGGDIRD--YEGVDRSAKPQLpmIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVND 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 635 ANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGAkDPIAREKVHNAATIAGVAFA 714
Cdd:PRK09860 177 SSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGS-NAKAREAMAYAQFLAGMAFN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 715 NAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANdnptkqtafsqydrpQARRRYAEVADHLGLSQPGDRTAQKI 794
Cdd:PRK09860 256 NASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK---------------VAAARLRDCAAAMGVNVTGKNDAEGA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 520910047 795 ERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANP 845
Cdd:PRK09860 321 EACINAIRELAKKVDIPAGLRDLNVKEEDF----AVLATNALKDACGFTNP 367
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
477-860 |
1.06e-52 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 189.47 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 477 GKKRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWV 556
Cdd:PRK15454 48 GLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 557 MYEHPETHFEELAMRfMDIRKRIykfpkmgqkaELVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVDAN 636
Cdd:PRK15454 128 LVTNPDSTLAEMSET-SVLQPRL----------PLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 637 LVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGaKDPIAREKVHNAATIAGVAFANA 716
Cdd:PRK15454 197 LTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYG-HDLAARESMLLASCMAGMAFSSA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 717 FLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNandnptkqtafsqydRPQARRRYAEVADHLGLSQPGDRTAqkier 796
Cdd:PRK15454 276 GLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFN---------------RMVCRERFSQIGRALRTKKSDDRDA----- 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520910047 797 lLGWLEELKLALDIPASIQAAGVNEADFLAkvdeLAVEAFDDQCTGANPRYPLISELKEVLLAS 860
Cdd:PRK15454 336 -INAVSELIAEVGIGKRLGDVGATSAHYGA----WAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
461-855 |
2.40e-48 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 176.47 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 461 IYFRRGSLPvALGDL--EGKKRAFLVTDR-FLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPD 537
Cdd:cd08187 10 IIFGKGAIE-ELGEEikKYGKKVLLVYGGgSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 538 VILALGGGSPMDAAKI--MWVMYEHPethFEElamrFMDIRKRIYKFPKMGqkaelvCITTTSGTGSEVTPFAVVTDDQT 615
Cdd:cd08187 89 FILAVGGGSVIDAAKAiaAGAKYDGD---VWD----FFTGKAPPEKALPVG------TVLTLAATGSEMNGGAVITNEET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVS-VLANEYSDGQALQALKLLKEYLPSSYANGaK 694
Cdd:cd08187 156 KEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLAEGLLRTVIENGPKALKDP-D 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 695 DPIAREKVHNAATIAgvafANAFLGV-------CHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKqtaFSQYdr 767
Cdd:cd08187 235 DYEARANLMWAATLA----LNGLLGAgrggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPER---FAQF-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 768 pqARRryaeVadhLGLSQPGD--RTAQK-IERLLGWLEELKLaldiPASIQAAGVNEADFlakvDELAveafdDQCTGAN 844
Cdd:cd08187 306 --ARR----V---FGIDPGGDdeETALEgIEALEEFFKSIGL----PTTLSELGIDEEDI----EEMA-----EKAVRGG 363
|
410
....*....|.
gi 520910047 845 PRYPLISELKE 855
Cdd:cd08187 364 GLGGGFKPLTR 374
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
477-857 |
5.51e-45 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 166.65 E-value: 5.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 477 GKKRAFLVTDRFLFNNgyADEVVSLLKAQG-MEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMW 555
Cdd:cd08192 22 GASRVFIVTSKSLATK--TDVIKRLEEALGdRHVGVFSGVRQHTPREDVLEAARAVREAGADLLVSLGGGSPIDAAKAVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 556 VMYEHPETHFEELAMRFMDIRKRIYkfpKMGQKAELVCITTT-SgtGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVD 634
Cdd:cd08192 100 LALAEDVTDVDQLDALEDGKRIDPN---VTGPTLPHIAIPTTlS--GAEFTAGAGATDDDTGHKQGFAHPELGPDAVILD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 635 ANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPsSYANGAKDPIAREKVHNAATIAGVAFA 714
Cdd:cd08192 175 PELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLP-RSKADPEDLEARLKCQLAAWLSLFGLG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 715 NAF-LGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKqtafsqydrpQARRRYAEVADHLGLSQPGDRTAQK 793
Cdd:cd08192 254 SGVpMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAER----------QRLIARALGLVTGGLGREAADAADA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520910047 794 IERLLgwleelkLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPRyPLIS--ELKEVL 857
Cdd:cd08192 324 IDALI-------RELGLPRTLRDVGVGRDQL----EKIAENALTDVWCRTNPR-PITDkdDVLEIL 377
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
477-750 |
1.29e-40 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 153.96 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 477 GKKRAFLVTDRFLFN-NGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMW 555
Cdd:cd08186 22 GIDKVIIVTGRSSYKkSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 556 VMYEHPETHFEELamrfmdirkriYKFPKMGQKA-ELVCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVD 634
Cdd:cd08186 102 VLLAYGGKTARDL-----------YGFRFAPERAlPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPLYAIDD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 635 ANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANgAKDPIAREKVHNAATIAGVAFA 714
Cdd:cd08186 171 PRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALAN-PKDLEARYWLLYASMIAGIAID 249
|
250 260 270
....*....|....*....|....*....|....*..
gi 520910047 715 NAFLGVCHSMAHKI-GAEFHLPHGLANSLLMANVVRY 750
Cdd:cd08186 250 NGLLHLTHALEHPLsGLKPELPHGLGLALLGPAVVKY 286
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
458-859 |
2.26e-40 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 153.54 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGS---LPVALGDLeGKKRAFLVTDRFLfnnGYADEVVSLLKAQ--GMEVTTFYEVEADPTLSIVKKGAEQMR 532
Cdd:cd14866 5 PLRLFSGRGAlarLGRELDRL-GARRALVVCGSSV---GANPDLMDPVRAAlgDRLAGVFDGVRPHSPLETVEAAAEALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 533 SFQPDVILALGGGSPMDAAKIMWVMYEHPEThFEELAMRFMDirKRIYKFPKMGQ-KAELVCITTTSGTGSEVTPFAVvT 611
Cdd:cd14866 81 EADADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAE--DGLMVSPRLDApKLPIFVVPTTPTTADVKAGSAV-T 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 612 DDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSsyAN 691
Cdd:cd14866 157 DPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPR--LA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 692 GAKDPIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQAR 771
Cdd:cd14866 235 DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA---------------PATD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 772 RRYAEVADHLGLsqPGDRTAQKIERLLGWLEELKLALDIPASIQAAGVNEADFlakvDELAVEAFDDQCTGANPR-YPLI 850
Cdd:cd14866 300 GRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDL----PAIAEAAMDDWFMDNNPRpVPTA 373
|
....*....
gi 520910047 851 SELKEVLLA 859
Cdd:cd14866 374 EELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
461-832 |
2.24e-36 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 141.75 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 461 IYFRRGSLPvALGDL--EGKKRAFLVTDR-FLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPD 537
Cdd:COG1979 12 IIFGKGQIA-KLGEEipKYGKKVLLVYGGgSIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 538 VILALGGGSPMDAAK-I-MWVMYEHPethfeelamrfmdirkrIYKFPKMGQKAE----LVCITTTSGTGSEVTPFAVVT 611
Cdd:COG1979 91 FILAVGGGSVIDGAKaIaAGAKYDGD-----------------PWDILTGKAPVEkalpLGTVLTLPATGSEMNSGSVIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 612 DDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLAN-EYSDGQALQALKLLKEYLPSSYA 690
Cdd:COG1979 154 NEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDaPLQDRFAEGLLRTLIEEGPKALK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 691 NGaKDPIAREKVHNAATIAgvafANAFLGV-------CHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKqtaFS 763
Cdd:COG1979 234 DP-EDYDARANLMWAATLA----LNGLIGAgvpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEK---FA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910047 764 QYdrpqARRryaeVadhLGLSQPGDR-TAQK-IERLLGWLEElklaLDIPASIQAAGVNEADFlakvDELA 832
Cdd:COG1979 306 QY----AER----V---WGITEGDDEeRALEgIEATEEFFES----LGLPTRLSEYGIDEEDI----EEMA 357
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
456-861 |
2.75e-34 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 135.51 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 456 KLPKSIYFRRGSLpVALGDLEGK--KRAFLVTDRFLFNNGYADEVVSLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRS 533
Cdd:cd14864 2 KIPPNIVFGADSL-ERIGEEVKEygSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 534 FQPDVILALGGGSPMDAAKIMWVMYEHPethfeelamrfMDIRKRIYKFPKMGQKAELVCITTTSGTGSEVTPFAVVTDD 613
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVAILANND-----------GGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 614 QTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGA 693
Cdd:cd14864 150 RSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 694 KDPiAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRR 773
Cdd:cd14864 230 NTP-AEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAA---------------TSAPDK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 774 YAEVADHLGLSQPGDRTAQKIERLLGWLEELKLALDIPASiqaagVNEADFLAKVDELAVEAFDDQCTGANPRYPLISEL 853
Cdd:cd14864 294 YAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTR-----LKDLDLASSLEQLAAIAEDAPKLNGLPRSMSSDDI 368
|
....*...
gi 520910047 854 KEVLLASY 861
Cdd:cd14864 369 FDILKAAF 376
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
519-757 |
9.17e-32 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 128.10 E-value: 9.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 519 PTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWVMYEHPethFEELAMRFMDIRKriykfpkmgqKAELVCITTTS 598
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISP---VLDLFDGKIPLIK----------EKELIIVPTTC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 599 GTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQAL 678
Cdd:cd14860 129 GTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 679 KLLKEylpsSYANGAKD-PIAREKVHN----AATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAN 753
Cdd:cd14860 209 EMILE----GYQEIAEKgEEARFPLLGdfliASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQE 284
|
....
gi 520910047 754 DNPT 757
Cdd:cd14860 285 KNPD 288
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
458-846 |
3.30e-26 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 110.67 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGSLPVALGDLE--GKKRAFLVTDRFlfNNGYADEVVSLLKaqGMEVTTFYEVEADPTLSIVKKGAEQMRSFQ 535
Cdd:cd08177 1 PQRVVFGAGTLAELAEELErlGARRALVLSTPR--QRALAERVAALLG--DRVAGVFDGAVMHVPVEVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 PDVILALGGGSPMDAAKImwvmyehpethfeeLAMRfmdirkriykfpkmgQKAELVCITTTSgTGSEVTPFAVVTDDqt 615
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKA--------------IALR---------------TGLPIVAVPTTY-AGSEMTPIWGETED-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 616 GAKYPLADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSSYANGAkD 695
Cdd:cd08177 125 GVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPS-D 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 696 PIAREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNAndnptkqtafsqydrPQARRRYA 775
Cdd:cd08177 204 LEARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA---------------PAAPDAMA 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910047 776 EVADHLGLSQPGDRtaqkierllgwLEELKLALDIPASIQAAGVNEADfLAKVDELAVEAfddqcTGANPR 846
Cdd:cd08177 269 RLARALGGGDAAGG-----------LYDLARRLGAPTSLRDLGMPEDD-IDRAADLALAN-----PYPNPR 322
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
458-765 |
5.91e-24 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 102.44 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 458 PKSIYFRRGslpvALGDLE-----GKKRAFLVTDRFLfNNGYADEVVSLLKAqGMEVTTFYEVEADPTLSIVKKGAEQMR 532
Cdd:cd07766 1 PTRIVFGEG----AIAKLGeikrrGFDRALVVSDEGV-VKGVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 533 SFQPDVILALGGGSPMDAAKIMWVMyehpethfeelamrfmdirkriykfpkMGQKAELVCITTTSGTGSEVTPFAVVTD 612
Cdd:cd07766 75 AAEADAVIAVGGGSTLDTAKAVAAL---------------------------LNRGIPFIIVPTTASTDSEVSPKSVITD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 613 DQTGAKYplADYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEayvsvlaneysdgqalqalkllkeylpssyang 692
Cdd:cd07766 128 KGGKNKQ--VGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------- 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520910047 693 akdpiaREKVHNAATIAGVAFANA-FLGVCHSMAHKIGAEFHLPHGLANSLLMANVVRYNANDNPTKQTAFSQY 765
Cdd:cd07766 173 ------LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAV 240
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
463-744 |
1.12e-23 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 103.50 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 463 FRRGSLpVALGDLEGKKR------AFLVTDRFLFNNGYADevvsLLKAQGMEVTTFYEVEADPTLSIVKKGAEQMRSFQ- 535
Cdd:cd08184 6 FGRGSF-DQLGELLAERRksnndyVVFFIDDVFKGKPLLD----RLPLQNGDLLIFVDTTDEPKTDQIDALRAQIRAENd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 536 --PDVILALGGGSPMDAAKIMWVMYEHPE--THFE--ELAMRfmdirKRIYKfpkmgqkaelVCITTTSGTGSEVTPFAV 609
Cdd:cd08184 81 klPAAVVGIGGGSTMDIAKAVSNMLTNPGsaADYQgwDLVKN-----PGIYK----------IGVPTLSGTGAEASRTAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 610 VTDdqTGAKYPL-ADYELtPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLANEYSDGQALQALKLLKEYLPSS 688
Cdd:cd08184 146 LTG--PEKKLGInSDYTV-FDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLSD 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 520910047 689 YANGAKDpiaREKVHNAATIAGVAFANAFLGVCHSMAHKIGAEFHLPHGLANSLLM 744
Cdd:cd08184 223 DMMSPEN---REKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVF 275
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
10-405 |
1.64e-22 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 101.52 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 10 DALVARVKAAQAEFATYSQEQVDKIFRAAS--LAANQARIplAQQAVAESGMGIVE-----DKVIKN-HFASEYIYNKYK 81
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLAdlLEERREEL--AALETLETGKPIEEalgevARAADTfRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 82 DEktcgILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAavaaG 161
Cdd:cd07078 79 EV----IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA----G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 162 APKDIIGWIDQPSVELSNALMKHEGIALILATGGPG----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMS 237
Cdd:cd07078 151 LPPGVLNVVTGDGDEVGAALASHPRVDKISFTGSTAvgkaIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 238 KTFDNGVVCASEQAVIVMDEVYDEVKERF-ATHKAHVLSKADADKVRKVLLIDGALNAKIVGQPATKIAEMAgvKVPADT 316
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLvERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGA--KLLCGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 317 KILVGEG--------IGEVSYDDEFAHEKL-SPTLGMFRASSFENAVDQAVKMVeiggIGHTSGLYTDqdvNADRIRYFG 387
Cdd:cd07078 309 KRLEGGKgyfvpptvLTDVDPDMPIAQEEIfGPVLPVIPFKDEEEAIELANDTE----YGLAAGVFTR---DLERALRVA 381
|
410
....*....|....*...
gi 520910047 388 DRLKTARILVNIPTTHGG 405
Cdd:cd07078 382 ERLEAGTVWINDYSVGAE 399
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
1-408 |
1.34e-20 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 96.06 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 1 MPVTNLAELDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMGIVE-----DKVIKN-HFASE 74
Cdd:pfam00171 23 VPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEargevDRAIDVlRYYAG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 75 YIyNKYKDEktcgILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNStndAAKLVl 154
Cdd:pfam00171 103 LA-RRLDGE----TLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLT---ALLLA- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 155 DAAVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPG----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRA 230
Cdd:pfam00171 174 ELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvgrhIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 231 VASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATHKAH---------------VLSKADADKVRKvlLIDGALN-- 293
Cdd:pfam00171 254 VEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKlkvgdpldpdtdmgpLISKAQLERVLK--YVEDAKEeg 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 294 AKIV-GQPATKIaemAGVKVPAdTkILVGegigeVSYDDEFAHEKL-SPTLGMFRASSFENAVDQA--VKMveiggiGHT 369
Cdd:pfam00171 332 AKLLtGGEAGLD---NGYFVEP-T-VLAN-----VTPDMRIAQEEIfGPVLSVIRFKDEEEAIEIAndTEY------GLA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 520910047 370 SGLYTDqdvNADRIRYFGDRLKTARILVNIPTT-------HGGIGD 408
Cdd:pfam00171 396 AGVFTS---DLERALRVARRLEAGMVWINDYTTgdadglpFGGFKQ 438
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
2-408 |
1.39e-19 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 92.88 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 2 PVTNLAELDALVARVKAAQAEFATYS-QEQVDKIFRAASL-AANQARipLAQQAVAESGMGIVE-----DKVIKN--HFA 72
Cdd:COG1012 38 PAATAEDVDAAVAAARAAFPAWAATPpAERAAILLRAADLlEERREE--LAALLTLETGKPLAEargevDRAADFlrYYA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 73 SEYiyNKYKDEKtcgILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNStndAAKL 152
Cdd:COG1012 116 GEA--RRLYGET---IPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLS---ALLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 153 VlDAAVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPG----MVKAAYSSGKPAIGVGAGNVPVVIDETADIK 228
Cdd:COG1012 188 A-ELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAvgrrIAAAAAENLKRVTLELGGKNPAIVLDDADLD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 229 RAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATH-KAHVL--------------SKADADKVRKvlLIDGALN 293
Cdd:COG1012 267 AAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAaKALKVgdpldpgtdmgpliSEAQLERVLA--YIEDAVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 294 --AKIVgqpatkiaemAGVKVPADTK-------ILVGegigeVSYDDEFAHEKL-SPTLGMFRASSFENAVDQA--VKMv 361
Cdd:COG1012 345 egAELL----------TGGRRPDGEGgyfveptVLAD-----VTPDMRIAREEIfGPVLSVIPFDDEEEAIALAndTEY- 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 520910047 362 eiggiGHTSGLYTDqdvNADRIRYFGDRLKTARILVNIPTT-------HGGIGD 408
Cdd:COG1012 409 -----GLAASVFTR---DLARARRVARRLEAGMVWINDGTTgavpqapFGGVKQ 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
1-357 |
6.23e-18 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 87.49 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 1 MPVTNLAELDALVARVKAAQAEF-ATYSQEQVDKIFRAASLAANQARIpLAQQAVAESGMGIVE-----DKVIKN-HFAS 73
Cdd:cd07094 15 VPADDRADAEEALATARAGAENRrALPPHERMAILERAADLLKKRAEE-FAKIIACEGGKPIKDarvevDRAIDTlRLAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 74 EYIYNKYKDEKTCGILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLV 153
Cdd:cd07094 94 EEAERIRGEEIPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 154 LDaavaAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGM---VKAAYSSGKPAIGVGaGNVPVVIDETADIKRA 230
Cdd:cd07094 174 VE----AGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVgeaLRANAGGKRIALELG-GNAPVIVDRDADLDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 231 VASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFA---------------THKAHVLSKADADKVRKVL--------- 286
Cdd:cd07094 249 IEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVaavkklkvgdpldedTDVGPLISEEAAERVERWVeeaveagar 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910047 287 LIDGALNAKIVGQPATKiaemagVKVPADTKILvgegigevsyddefAHEKLSPTLGMFRASSFENAVDQA 357
Cdd:cd07094 329 LLCGGERDGALFKPTVL------EDVPRDTKLS--------------TEETFGPVVPIIRYDDFEEAIRIA 379
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-398 |
1.78e-17 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 86.17 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 1 MPVTNLAELDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGMgIVEDKVIKNHFASEYI-Y-- 77
Cdd:cd07088 29 VPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK-TLSLARVEVEFTADYIdYma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 78 -NKYKDEKTcgILEEDDSMGTMTIA-EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVld 155
Cdd:cd07088 108 eWARRIEGE--IIPSDRPNENIFIFkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELV-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 156 aaVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRA 230
Cdd:cd07088 184 --DEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEagqkiMEAAAENITKVSLELG-GKAPAIVMKDADLDLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 231 VASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATHKAHVlskadadKVRKVLLIDGALNAKIVGQPATKIAEM--- 307
Cdd:cd07088 261 VKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAV-------KVGDPFDAATDMGPLVNEAALDKVEEMver 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 308 ---AGVKVPADTKILVGEG--------IGEVSYDDEFAHEKL-SPTLGMFRASSFENAVDQAVKMVeiggIGHTSGLYTD 375
Cdd:cd07088 334 aveAGATLLTGGKRPEGEKgyfyeptvLTNVRQDMEIVQEEIfGPVLPVVKFSSLDEAIELANDSE----YGLTSYIYTE 409
|
410 420
....*....|....*....|...
gi 520910047 376 qdvNADRIRYFGDRLKTARILVN 398
Cdd:cd07088 410 ---NLNTAMRATNELEFGETYIN 429
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
103-379 |
5.13e-14 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 75.16 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAavaaGAPKDIIGWIDQPSVELSNALM 182
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGRGETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 183 KHEGIALILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDE 257
Cdd:PRK10090 147 GNPKVAMVSMTGSVSagekiMAAAAKNITKVCLELG-GKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 258 VYDEVKERFATHKAHVLS--KADADKVRKVLLIDGALNAKIVGQPATKIAEmaGVKVPADTKILVGEG-------IGEVS 328
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFgnPAERNDIAMGPLINAAALERVEQKVARAVEE--GARVALGGKAVEGKGyyypptlLLDVR 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 520910047 329 YDDEFAHEK-LSPTLGMfraSSFeNAVDQAVKMVEIGGIGHTSGLYTdQDVN 379
Cdd:PRK10090 304 QEMSIMHEEtFGPVLPV---VAF-DTLEEAIAMANDSDYGLTSSIYT-QNLN 350
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
98-280 |
6.60e-14 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 74.94 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAavaaGAPKDIIGWIDQPSVEL 177
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEA----GLPKGALNVVTGSGETV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATGGPGMVKA-AYSSG--KPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07149 194 GDALVTDPRVRMISFTGSPAVGEAiARKAGlkKVTLELG-SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFV 272
|
170 180
....*....|....*....|....*...
gi 520910047 255 MDEVYDEVKERF--ATHKAHVLSKADAD 280
Cdd:cd07149 273 HEDIYDEFLERFvaATKKLVVGDPLDED 300
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
98-266 |
8.57e-14 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 74.69 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAavaaGAPKDIIGWIDQPSVEL 177
Cdd:cd07145 118 FTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEA----GLPPGVINVVTGYGSEV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKtFDN-GVVCASEQAV 252
Cdd:cd07145 194 GDEIVTNPKVNMISFTGstavGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGR-FENaGQVCNAVKRI 272
|
170
....*....|....
gi 520910047 253 IVMDEVYDEVKERF 266
Cdd:cd07145 273 LVEEEVYDKFLKLL 286
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
99-408 |
1.42e-13 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 73.93 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRaknsTNDAAKLVLDAAVAAGAPKDIIGWIDQPSVELS 178
Cdd:cd07146 116 TLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEK----TPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 NALMKHEGIALILATGGPGMVK--AAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07146 192 DELITHPDVDLVTFTGGVAVGKaiAATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 257 EVYDEVKERFATHKAH---------------VLSKADADKVRKVllIDGALN--AKIVGQPATKIAEMAGV---KVPADT 316
Cdd:cd07146 272 SVADEFVDLLVEKSAAlvvgdpmdpatdmgtVIDEEAAIQIENR--VEEAIAqgARVLLGNQRQGALYAPTvldHVPPDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 317 KILVGEGIGevsyddefaheklsPTLGMFRASSFenavDQAVKMVEIGGIGHTSGLYTDqdvNADRIRYFGDRLKTARIL 396
Cdd:cd07146 350 ELVTEETFG--------------PVAPVIRVKDL----DEAIAISNSTAYGLSSGVCTN---DLDTIKRLVERLDVGTVN 408
|
330
....*....|....*....
gi 520910047 397 VN-IP------TTHGGIGD 408
Cdd:cd07146 409 VNeVPgfrselSPFGGVKD 427
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-401 |
3.64e-13 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 72.77 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 2 PVTNLAELDALVARVKAAQAEFATYSQ-EQVDKIFRAASLAAnQARIPLAQQAVAESGMGIVEDK--VIKNHFASEYIYN 78
Cdd:cd07131 32 PLSTASDVDAAVEAAREAFPEWRKVPApRRAEYLFRAAELLK-KRKEELARLVTREMGKPLAEGRgdVQEAIDMAQYAAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 79 K----YKDEKTCGILEEDdsmgTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVL 154
Cdd:cd07131 111 EgrrlFGETVPSELPNKD----AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 155 DAavaaGAPKDIIGWIDQPSVELSNALMKHEGIALILATG----GPGMVKAAYSSGKP-AIGVGAGNvPVVIDETADIKR 229
Cdd:cd07131 187 EA----GLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGstevGERIGETCARPNKRvALEMGGKN-PIIVMDDADLDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 230 AVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERF--ATHKAHVLSKADADKVRKVLLIDGALNaKIVGQpaTKIAEM 307
Cdd:cd07131 262 ALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFveRAKRLRVGDGLDEETDMGPLINEAQLE-KVLNY--NEIGKE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 308 AGVKVPADTKILVGEGIGE-----------VSYDDEFAHEKL-SPTLGMFRASSFEnavdQAVKMVEIGGIGHTSGLYTd 375
Cdd:cd07131 339 EGATLLLGGERLTGGGYEKgyfveptvftdVTPDMRIAQEEIfGPVVALIEVSSLE----EAIEIANDTEYGLSSAIYT- 413
|
410 420
....*....|....*....|....*.
gi 520910047 376 QDVNadRIRYFGDRLKTARILVNIPT 401
Cdd:cd07131 414 EDVN--KAFRARRDLEAGITYVNAPT 437
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
492-748 |
1.43e-12 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 70.21 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 492 NGYADEVVSLLKaqGMEVTTFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAKIMWVMYEHPETH--FEELA 569
Cdd:PRK15138 44 TGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 570 MRFMDIRKRIykfpKMGqkaelvCITTTSGTGSEVTPFAVVTDDQTGAKYPLADYELTPNMAIVDANLVMNMPKSLTAFG 649
Cdd:PRK15138 122 TGGKEIKSAI----PMG------SVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 650 GYDAVVHALEAYVSVLAN-----EYSDGQALQAL----KLLKEylPSSYAngakdpiAREKVHNAATIAGVAFANAflGV 720
Cdd:PRK15138 192 VVDAFVHTVEQYVTYPVDakiqdRFAEGILLTLIeegpKALKE--PENYD-------VRANVMWAATQALNGLIGA--GV 260
|
250 260
....*....|....*....|....*....
gi 520910047 721 CHSMA-HKIGAEFHLPHGLANSLLMANVV 748
Cdd:PRK15138 261 PQDWAtHMLGHELTAMHGLDHAQTLAIVL 289
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
10-408 |
3.07e-12 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 69.67 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 10 DALVArVKAAQAEFATYSQ---EQVDKIFRAASlAANQARIP-LAQQAVAESGmGIVEDKVIKNHFASEYIYN------K 79
Cdd:cd07150 22 DAERA-IAAAYDAFPAWAAttpSERERILLKAA-EIMERRADdLIDLLIDEGG-STYGKAWFETTFTPELLRAaagecrR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 80 YKDEktcgiLEEDDSMGT--MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVldaa 157
Cdd:cd07150 99 VRGE-----TLPSDSPGTvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIM---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 158 VAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATG----GPGM-VKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVA 232
Cdd:cd07150 170 EEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGstavGREIaEKAGRHLKKITLELG-GKNPLIVLADADLDYAVR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 233 SVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFA--THKAHVLSKADADKVRKVlLIDGALNAKIVGQPATKIAEMAgv 310
Cdd:cd07150 249 AAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVarASKLKVGDPRDPDTVIGP-LISPRQVERIKRQVEDAVAKGA-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 311 kvpadtKILVGEG----------IGEVSYD-DEFAHEKLSPTLGMFRASSFEnavdQAVKMVEIGGIGHTSGLYTDqdvN 379
Cdd:cd07150 326 ------KLLTGGKydgnfyqptvLTDVTPDmRIFREETFGPVTSVIPAKDAE----EALELANDTEYGLSAAILTN---D 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 520910047 380 ADRIRYFGDRLKTARILVNIPTTH-------GGIGD 408
Cdd:cd07150 393 LQRAFKLAERLESGMVHINDPTILdeahvpfGGVKA 428
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
92-268 |
1.97e-11 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 67.08 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 92 DDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIGwid 171
Cdd:cd07115 106 RGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTG--- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 172 qPSVELSNALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVC 246
Cdd:cd07115 183 -FGEVAGAALVEHPDVDKITFTGSTAvgrkiMQGAAGNLKRVSLELG-GKSANIVFADADLDAAVRAAATGIFYNQGQMC 260
|
170 180
....*....|....*....|..
gi 520910047 247 ASEQAVIVMDEVYDEVKERFAT 268
Cdd:cd07115 261 TAGSRLLVHESIYDEFLERFTS 282
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
92-403 |
2.40e-11 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 66.89 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 92 DDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNStndAAKLVlDAAVAAGAPKDIIGWID 171
Cdd:cd07097 124 RPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPAS---AWALV-EILEEAGLPAGVFNLVM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 172 QPSVELSNALMKHEGIALILATGGPGMVKAAYSSgkpAIGVGA-------GNVPVVIDETADIKRAVASVLMSKTFDNGV 244
Cdd:cd07097 200 GSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA---AAARGArvqlemgGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 245 VCASEQAVIVMDEVYDEVKERFathkahvlskadADKVRKvLLIDGALNAKIVGQPATKIAEMA--------GVKVPADT 316
Cdd:cd07097 277 RCTASSRLIVTEGIHDRFVEAL------------VERTKA-LKVGDALDEGVDIGPVVSERQLEkdlryieiARSEGAKL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 317 ----KILVGEGIG---------EVSYDDEFAHEKL-SPTLGMFRASSFenavDQAVKMVEIGGIGHTSGLYTDqdvNADR 382
Cdd:cd07097 344 vyggERLKRPDEGyylapalfaGVTNDMRIAREEIfGPVAAVIRVRDY----DEALAIANDTEFGLSAGIVTT---SLKH 416
|
330 340
....*....|....*....|.
gi 520910047 383 IRYFGDRLKTARILVNIPTTH 403
Cdd:cd07097 417 ATHFKRRVEAGVVMVNLPTAG 437
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
21-398 |
4.85e-11 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 66.17 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 21 AEFATYSQEQVDKIFRAASLAANQ--ARIPLAQQAVAESGMGIVEDK--VIKNHFASE----YIYNKYKDEKTCGILEED 92
Cdd:cd07151 24 AEIPAASKEDVDEAYRAAAAAQKEwaATLPQERAEILEKAAQILEERrdEIVEWLIREsgstRIKANIEWGAAMAITREA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 93 DSM-GTMT---------------IAEPVGIICGIVPTTNPTSTAIfKSLI-SLKTRNGIIFSPhprAKNSTNDAAKLVLD 155
Cdd:cd07151 104 ATFpLRMEgrilpsdvpgkenrvYREPLGVVGVISPWNFPLHLSM-RSVApALALGNAVVLKP---ASDTPITGGLLLAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 156 AAVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGP--GMVKAAYSSG---KPAIGVGaGNVPVVIDETADIKRA 230
Cdd:cd07151 180 IFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTpvGRHIGELAGRhlkKVALELG-GNNPFVVLEDADIDAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 231 VASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFAthkAHVLSKADADKVRKVLLIDGALNAKIVGQPATKI--AEMA 308
Cdd:cd07151 259 VNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFV---ERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIeqAVEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 309 GVKV----PADTKILVGEGIGEVSYDDEFAHEKL-SPTLGMFRASSFENAVDQAvKMVEIG--GIGHTSGLytdqdvnaD 381
Cdd:cd07151 336 GATLlvggEAEGNVLEPTVLSDVTNDMEIAREEIfGPVAPIIKADDEEEALELA-NDTEYGlsGAVFTSDL--------E 406
|
410
....*....|....*..
gi 520910047 382 RIRYFGDRLKTARILVN 398
Cdd:cd07151 407 RGVQFARRIDAGMTHIN 423
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
102-265 |
1.41e-10 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 64.63 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNStndaAKLVLDAAVAAGAPKDIIGWIdQPSVELSNAL 181
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT----ALLLAEILTEAGLPDGVFNVV-QGGGETGQLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDE 257
Cdd:cd07090 190 CEHPDVAKVSFTGsvptGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269
|
....*...
gi 520910047 258 VYDEVKER 265
Cdd:cd07090 270 IKDEFTER 277
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
454-737 |
7.83e-10 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 61.72 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 454 WHKLPKSIYFRRG---SLPVALGDLegKKRAFLVTDRFLFNNgYADEVVSLLKAQGMEVTtFYEVEADPTLSIVKKGAEQ 530
Cdd:COG0371 2 VIILPRRYVQGEGaldELGEYLADL--GKRALIITGPTALKA-AGDRLEESLEDAGIEVE-VEVFGGECSEEEIERLAEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 531 MRSFQPDVILALGGGSPMDAAKImwvmyehpethfeeLAMRfmdirkriykfpkmgQKAELVCITTTSGTGSEVTPFAVV 610
Cdd:COG0371 78 AKEQGADVIIGVGGGKALDTAKA--------------VAYR---------------LGLPVVSVPTIASTDAPASPLSVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 611 TDDQTGAKYPLAdYELTPNMAIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSVLAN-----EYSDGQALQALKLLKEYL 685
Cdd:COG0371 129 YTEDGAFDGYSF-LAKNPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDWSLAHrdlagEYYTEAAVALARLCAETL 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520910047 686 pSSYANGAKDPIAREKVHNA------ATI--AGVAFANAF----LGVCHSMAH---KIGAEFHLPHG 737
Cdd:COG0371 208 -LEYGEAAIKAVEAGVVTPAlervveANLllSGLAMGIGSsrpgSGAAHAIHNgltALPETHHALHG 273
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
102-357 |
6.05e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 59.54 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTstAIFKSLIS--LKTRNGIIFSPhprAKNSTNDAAKLVlDAAVAAGAPKDIIGWIDQPSVELSN 179
Cdd:cd07124 165 RPLGVGAVISPWNFPL--AILAGMTTaaLVTGNTVVLKP---AEDTPVIAAKLV-EILEEAGLPPGVVNFLPGPGEEVGD 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 180 ALMKHEGIALILATG---------------GPGMVKAayssgKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGV 244
Cdd:cd07124 239 YLVEHPDVRFIAFTGsrevglriyeraakvQPGQKWL-----KRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQ 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 245 VCASEQAVIVMDEVYDEVKERF-----------ATHKAH----VLSKADADKVRKVLLIdgalnakivGQPATKIAemAG 309
Cdd:cd07124 314 KCSACSRVIVHESVYDEFLERLvertkalkvgdPEDPEVymgpVIDKGARDRIRRYIEI---------GKSEGRLL--LG 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 520910047 310 VKVPADTKilvgEG-------IGEVSYDDEFAHEKL-SPTLGMFRASSFENAVDQA 357
Cdd:cd07124 383 GEVLELAA----EGyfvqptiFADVPPDHRLAQEEIfGPVLAVIKAKDFDEALEIA 434
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
132-408 |
9.46e-09 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 58.44 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 132 NGIIFSPHPRAKNStndaAKLVLDAAVAAGAPKDIIGWIdQPSVELSNALMKHEGIALILATGGP--GMVKAAYSSGKP- 208
Cdd:cd07095 126 NTVVFKPSELTPAV----AELMVELWEEAGLPPGVLNLV-QGGRETGEALAAHEGIDGLLFTGSAatGLLLHRQFAGRPg 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 209 ---AIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD-EVYDEVKERF-ATHKAHVLSKADADKVR 283
Cdd:cd07095 201 kilALEMG-GNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPDgAVGDAFLERLvEAAKRLRIGAPDAEPPF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 284 KVLLIDGALNAKIVGQPATKIAE-----MAGVKVPADTKiLVGEGIGEVSYDDEFAHEKL-SPTLGMFRASSFenavDQA 357
Cdd:cd07095 280 MGPLIIAAAAARYLLAQQDLLALggeplLAMERLVAGTA-FLSPGIIDVTDAADVPDEEIfGPLLQVYRYDDF----DEA 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 520910047 358 VKMVEIGGIGHTSGLYTDqdvNADRIRYFGDRLKTARILVNIPTT-------HGGIGD 408
Cdd:cd07095 355 IALANATRFGLSAGLLSD---DEALFERFLARIRAGIVNWNRPTTgasstapFGGVGL 409
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
77-266 |
6.36e-08 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 56.00 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 77 YNKYKDEKTCGILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDa 156
Cdd:cd07143 118 YGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPE- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 157 avaAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAV 231
Cdd:cd07143 197 ---AGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLvgrkvMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAV 273
|
170 180 190
....*....|....*....|....*....|....*
gi 520910047 232 ASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERF 266
Cdd:cd07143 274 VWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRF 308
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
8-272 |
6.84e-08 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 56.00 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 8 ELDALVARVKAAQAEFATYSQEQVDKIFRAAS--LAANQARIplAQQAVAESGmgivedkviknhfaSEYIYNKYKDEKT 85
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAeiLEERRDEI--ADWLIRESG--------------STRPKAAFEVGAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 86 CGILEEDDSM--------------GTMTIA--EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDA 149
Cdd:cd07104 65 IAILREAAGLprrpegeilpsdvpGKESMVrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 150 -AKLVldaaVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGM-----VKAAYSSGKPAIGVGaGNVPVVIDE 223
Cdd:cd07104 145 iAEIF----EEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVgrhigELAGRHLKKVALELG-GNNPLIVLD 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 520910047 224 TADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATHKAH 272
Cdd:cd07104 220 DADLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKA 268
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
99-268 |
9.49e-08 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 55.53 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIGwidqpSVELS 178
Cdd:cd07113 138 TRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-----KGAVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 NALMKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07113 213 AQLISHPDVAKVSFTGsvatGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYV 292
|
170
....*....|....
gi 520910047 255 MDEVYDEVKERFAT 268
Cdd:cd07113 293 HRSKFDELVTKLKQ 306
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
99-284 |
1.20e-07 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 55.19 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIGWIDQPSVels 178
Cdd:cd07142 137 TLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGA--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 nALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVI 253
Cdd:cd07142 214 -AIASHMDVDKVAFTGSTEvgkiiMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTF 292
|
170 180 190
....*....|....*....|....*....|.
gi 520910047 254 VMDEVYDEVKERfatHKAHVLSKADADKVRK 284
Cdd:cd07142 293 VHESIYDEFVEK---AKARALKRVVGDPFRK 320
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
102-398 |
1.22e-07 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 55.38 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKD----IIGWIDQpsvel 177
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHDPDlvqlVTCLPET----- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATGGPG---MV-KAAYSSGKPAIGVGAGNVPVVIDETADIKrAVASVLMSKTFDN-GVVCASEQAV 252
Cdd:cd07098 194 AEALTSHPVIDHITFIGSPPvgkKVmAAAAESLTPVVLELGGKDPAIVLDDADLD-QIASIIMRGTFQSsGQNCIGIERV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 253 IVMDEVYDEVKERFAThkahvlsKADADKVRKVLLIDGALNAKIVGQPATKIAEMAGVKVPADTKILVGeG--------- 323
Cdd:cd07098 273 IVHEKIYDKLLEILTD-------RVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAG-Gkryphpeyp 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 324 ---------IGEVSYDDEFAHEKL-SPTLGMFRASSfenaVDQAVKMVEIGGIGHTSGLYTDqdvNADRIRYFGDRLKTA 393
Cdd:cd07098 345 qghyfpptlLVDVTPDMKIAQEEVfGPVMVVMKASD----DEEAVEIANSTEYGLGASVFGK---DIKRARRIASQLETG 417
|
....*
gi 520910047 394 RILVN 398
Cdd:cd07098 418 MVAIN 422
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
102-267 |
1.29e-07 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 55.03 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTndaakLVLDAAVAAGAPKDIIGWIDQPSVELSNAL 181
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT-----LLLAELAAEVLPPGVVNVVCGGGASAGDAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDE 257
Cdd:cd07092 192 VAHPRVRMVSLTGsvrtGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHES 271
|
170
....*....|
gi 520910047 258 VYDEVKERFA 267
Cdd:cd07092 272 VYDEFVAALV 281
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-267 |
1.78e-07 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 54.46 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 2 PVTNLAELDALVARVKAAQAEFATYSQEQVDKIFR--AASLAANQ---ARI-------PLAQqAVAESGMGIvedKVIKn 69
Cdd:cd07106 14 PVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLaiADAIEANAeelARLltleqgkPLAE-AQFEVGGAV---AWLR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 70 HFASeyiyNKYKDEktcgILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTnda 149
Cdd:cd07106 89 YTAS----LDLPDE----VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 150 AKLV--LDAAVAAGAPKDIIGwidqpSVELSNALMKHEGIALILATG----GPGMVKAAYSSGKPA---IGvgaGNVPVV 220
Cdd:cd07106 158 LKLGelAQEVLPPGVLNVVSG-----GDELGPALTSHPDIRKISFTGstatGKKVMASAAKTLKRVtleLG---GNDAAI 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 520910047 221 IDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFA 267
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALV 276
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-267 |
1.94e-07 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 54.62 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 10 DALVArVKAAQAEF------ATYSQEQVDKIFR-AASLAANQARipLAQQAVAESGMGIVEDK----VIKNHFasEYiYN 78
Cdd:cd07119 36 DAKRA-IAAARRAFdsgewpHLPAQERAALLFRiADKIREDAEE--LARLETLNTGKTLRESEididDVANCF--RY-YA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 79 KYKDEKTCGILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDaav 158
Cdd:cd07119 110 GLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 159 aAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDEtADIKRAVAS 233
Cdd:cd07119 187 -AGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTAtgrsiMRAAAGNVKKVALELGGKNPNIVFAD-ADFETAVDQ 264
|
250 260 270
....*....|....*....|....*....|....
gi 520910047 234 VLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFA 267
Cdd:cd07119 265 ALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALA 298
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
102-295 |
2.32e-07 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 54.32 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPraknSTNDAAKLVLDAAVAAGAPKDIIGWIDQPSvELSNAL 181
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAE----YTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATGGPGMVKA-----AYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMD 256
Cdd:cd07111 221 ANHPGVDKVAFTGSTEVGRAlrratAGTGKKLSLELG-GKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQE 299
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 520910047 257 EVYDEVKERFATHKAHVLSKADADKVrkvllID-GALNAK 295
Cdd:cd07111 300 SVAEELIRKLKERMSHLRVGDPLDKA-----IDmGAIVDP 334
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
102-315 |
2.45e-07 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 54.28 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhpraKNSTNDAAKLVLDAAVAAGAPKDIIGWIDQPSVELSNAL 181
Cdd:cd07110 119 EPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP----SELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDE 257
Cdd:cd07110 195 AAHPGIDKISFTGstatGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHES 274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520910047 258 VYDEVKERFATH-KAHVLSKADADKVRKVLLIDGALNAKIVGQPATKIAEMA----GVKVPAD 315
Cdd:cd07110 275 IADAFLERLATAaEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGArllcGGRRPAH 337
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
102-297 |
3.07e-07 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 54.11 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhpraknSTNDA--AKLVLDAAVAAGAPKDIIGWIDQPSVELSN 179
Cdd:cd07082 140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP------ATQGVllGIPLAEAFHDAGFPKGVVNVVTGRGREIGD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 180 ALMKHEGIALILATGGPG----MVKAAysSGKPAI-GVGAGNVPVVIDEtADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07082 214 PLVTHGRIDVISFTGSTEvgnrLKKQH--PMKRLVlELGGKDPAIVLPD-ADLELAAKEIVKGALSYSGQRCTAIKRVLV 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 255 MDEVYDEVKERFATHKAH---------------VLSKADADKVRKvlLIDGALN--AKIV 297
Cdd:cd07082 291 HESVADELVELLKEEVAKlkvgmpwdngvditpLIDPKSADFVEG--LIDDAVAkgATVL 348
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
16-342 |
3.09e-07 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 54.00 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 16 VKAAQAEFATYSQeqVDKIFRAASL-------AANQARipLAQQAVAESGMGIVEDKVIKNHFASEYIynKY------KD 82
Cdd:cd07117 44 VKAAQEAFKTWRK--TTVAERANILnkiadiiDENKEL--LAMVETLDNGKPIRETRAVDIPLAADHF--RYfagvirAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 83 EKTCGILEEDdsmgTMTIA--EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhprakNSTNDAAKLVLDAAVAA 160
Cdd:cd07117 118 EGSANMIDED----TLSIVlrEPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKP-----SSTTSLSLLELAKIIQD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 161 GAPKDIIGWIDQPSVELSNALMKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLM 236
Cdd:cd07117 189 VLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGstevGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 237 SKTFDNGVVCASEQAVIVMDEVYDEVKERFAthkahvlSKADADKVRKVLLIDGALNAKIVGQPATKIAEMAGVKVPADT 316
Cdd:cd07117 269 GILFNQGQVCCAGSRIFVQEGIYDEFVAKLK-------EKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGA 341
|
330 340
....*....|....*....|....*..
gi 520910047 317 KILV-GEGIGEVSYDDEFAhekLSPTL 342
Cdd:cd07117 342 KILTgGHRLTENGLDKGFF---IEPTL 365
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-272 |
6.54e-07 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 52.98 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLvldaAVAAGAPKDIIGWIDQPSVEL 177
Cdd:PRK09847 152 MIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGL----AKEAGLPDGVLNVVTGFGHEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAG--NVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQA 251
Cdd:PRK09847 228 GQALSRHNDIDAIAFTGstrtGKQLLKDAGDSNMKRVWLEAGgkSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180
....*....|....*....|.
gi 520910047 252 VIVMDEVYDEVKERFATHKAH 272
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQN 328
|
|
| proA |
PRK00197 |
gamma-glutamyl phosphate reductase; Provisional |
128-239 |
1.13e-06 |
|
gamma-glutamyl phosphate reductase; Provisional
Pssm-ID: 234685 Cd Length: 417 Bit Score: 51.99 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 128 LKTRNGIIFsphpR----AKNStNDA-AKLVLDAAVAAGAPKDIIGWIDQPSVELSNALMKHEG-IALILATGGPGMVKA 201
Cdd:PRK00197 138 LKSGNAVIL----RggseAIHS-NRAlVAVIQEALEEAGLPADAVQLVETTDRAAVGELLKLDGyVDVIIPRGGAGLIRR 212
|
90 100 110
....*....|....*....|....*....|....*....
gi 520910047 202 AYSSGK-PAIGVGAGNVPVVIDETADIKRAVASVLMSKT 239
Cdd:PRK00197 213 VVENATvPVIEHGDGICHIYVDESADLDKALKIVLNAKT 251
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-385 |
1.16e-06 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 51.81 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPT--------------STAIFKslislktrnGIIFSPHpraknstndAAKLVLDAAVAAGAP 163
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVilgtraiayplaagNTVVLK---------ASELSPR---------THWLIGRVFHEAGLP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 164 KDIIGWI-----DQPSVelSNALMKHEGIALILATG----GPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASV 234
Cdd:cd07105 155 KGVLNVVthspeDAPEV--VEALIAHPAVRKVNFTGstrvGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 235 LMSKTFDNGVVCASEQAVIVMDEVYDEVKERFA---------THKAHVL-SKADADKVRKvlLIDGALN--AKIV-GQPA 301
Cdd:cd07105 233 LFGAFLNSGQICMSTERIIVHESIADEFVEKLKaaaeklfagPVVLGSLvSAAAADRVKE--LVDDALSkgAKLVvGGLA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 302 TKiaEMAGVKVPA--------DTKIlvgegigevsYDDE-FAheklsPTLGMFRASSfenaVDQAVKMVEIGGIGHTSGL 372
Cdd:cd07105 311 DE--SPSGTSMPPtildnvtpDMDI----------YSEEsFG-----PVVSIIRVKD----EEEAVRIANDSEYGLSAAV 369
|
330
....*....|....*...
gi 520910047 373 YTdQDVN-----ADRIRY 385
Cdd:cd07105 370 FT-RDLAralavAKRIES 386
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
98-267 |
2.39e-06 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 51.23 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLvldaAVAAGAPKDIIGWIDQPSVEL 177
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAEL----ALQAGIPPGVLNVVMGDAPEI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAV 252
Cdd:PLN02278 231 GDALLASPKVRKITFTGSTAvgkklMAGAAATVKRVSLELG-GNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRI 309
|
170
....*....|....*
gi 520910047 253 IVMDEVYDEVKERFA 267
Cdd:PLN02278 310 LVQEGIYDKFAEAFS 324
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
91-357 |
2.61e-06 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 51.01 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 91 EDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLdaavAAGAPKDIIGWI 170
Cdd:cd07114 107 DKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAE----EAGFPPGVVNVV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 171 DQPSVELSNALMKHEGIALILATGGP----GMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMsktfdnGVVC 246
Cdd:cd07114 183 TGFGPETGEALVEHPLVAKIAFTGGTetgrHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVA------GIFA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 247 ASEQA------VIVMDEVYDEVKERFA---------------THKAHVLSKADADKVRKVLLIDGALNAKIV--GQPATK 303
Cdd:cd07114 257 AAGQTcvagsrLLVQRSIYDEFVERLVararairvgdpldpeTQMGPLATERQLEKVERYVARAREEGARVLtgGERPSG 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 520910047 304 IAEMAGVKVPAdtKILVGegigeVSYDDEFAHEKL-SPTLGMFRASSFENAVDQA 357
Cdd:cd07114 337 ADLGAGYFFEP--TILAD-----VTNDMRIAQEEVfGPVLSVIPFDDEEEAIALA 384
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
2-267 |
4.00e-06 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 50.44 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 2 PVTNLAELDALVARVKAAQAEFA-TYSQEQVDKIFRAASLAANQARiPLAQQAVAESGMGI-----VEDKVIKNHF---- 71
Cdd:cd07108 14 PRSRAADVDRAVAAAKAAFPEWAaTPARERGKLLARIADALEARSE-ELARLLALETGNALrtqarPEAAVLADLFryfg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 72 --ASEYiynkyKDEktcgILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFsphprakNSTNDA 149
Cdd:cd07108 93 glAGEL-----KGE----TLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL-------KAAEDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 150 --AKLVLDAAVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPGMVKAAY-SSGKPAIGVG---AGNVPVVIDE 223
Cdd:cd07108 157 plAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYrAAADRLIPVSlelGGKSPMIVFP 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 520910047 224 TADIKRAVASVLMSKTFD-NGVVCASEQAVIVMDEVYDEVKERFA 267
Cdd:cd07108 237 DADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLV 281
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
99-271 |
5.10e-06 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 50.20 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLvldaAVAAGAPKDIIGWIDQPSVELS 178
Cdd:PLN02766 154 TLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHL----AKLAGVPDGVINVVTGFGPTAG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 NALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVI 253
Cdd:PLN02766 230 AAIASHMDVDKVSFTGSTEvgrkiMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVY 309
|
170
....*....|....*...
gi 520910047 254 VMDEVYDEVKERfATHKA 271
Cdd:PLN02766 310 VQEGIYDEFVKK-LVEKA 326
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
100-268 |
6.32e-06 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 49.64 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 100 IAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAvaagaPKDIIGWIdQPSVELSN 179
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYL-----DPSYVRVI-EGGVEVTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 180 ALMKHEgIALILATGGP--GMV--KAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV- 254
Cdd:PTZ00381 180 ELLKEP-FDHIFFTGSPrvGKLvmQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVh 258
|
170
....*....|....*..
gi 520910047 255 ---MDEVYDEVKERFAT 268
Cdd:PTZ00381 259 rsiKDKFIEALKEAIKE 275
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
103-280 |
3.01e-05 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 47.69 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhpraKNSTNDAAKLVLDAAVAAGAPKDIIGWIDQPSVELSNALM 182
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP----DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 183 KHEGIALILATGGPGMVKAAySSGKPAIGVGA---GNVPVVIDETADIKRAVASVLMSkTFDN-GVVCASEQAVIVMDEV 258
Cdd:cd07101 194 DNADYVMFTGSTATGRVVAE-RAGRRLIGCSLelgGKNPMIVLEDADLDKAAAGAVRA-CFSNaGQLCVSIERIYVHESV 271
|
170 180
....*....|....*....|..
gi 520910047 259 YDEVKERFATHKAHVLSKADAD 280
Cdd:cd07101 272 YDEFVRRFVARTRALRLGAALD 293
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
457-554 |
3.23e-05 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 47.16 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 457 LPKSIYFRRGSL---PVALGDLEGKKRAFLVTDRFLFNNgYADEVVSLLKAQGMEVTTFYEVEADpTLSIVKKGAEQMRS 533
Cdd:cd08173 1 LPRNVVVGHGAInkiGEVLKKLLLGKRALIITGPNTYKI-AGKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKE 78
|
90 100
....*....|....*....|.
gi 520910047 534 FQPDVILALGGGSPMDAAKIM 554
Cdd:cd08173 79 SKADFIIGVGGGKVIDVAKYA 99
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
2-273 |
3.94e-05 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 47.24 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 2 PVTNLAELDALVArvkAAQAEFATYSQeQVDKIFRAASLAANQARI-----PLAQQAVAESGMGIV-----EDKVIKNHF 71
Cdd:cd07089 14 PDAGAADVDAAIA---AARRAFDTGDW-STDAEERARCLRQLHEALearkeELRALLVAEVGAPVMtaramQVDGPIGHL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 72 --ASEYIyNKYKDEKTcgiLEEDDSMGTMTIA----EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRakns 145
Cdd:cd07089 90 ryFADLA-DSFPWEFD---LPVPALRGGPGRRvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 146 TNDAAKLVLDAAVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGAGNVPVV 220
Cdd:cd07089 162 TPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAvgrriMAQAAATLKRVLLELGGKSANIV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 520910047 221 IDEtADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATHKAHV 273
Cdd:cd07089 242 LDD-ADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEAL 293
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
103-430 |
3.96e-05 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 47.23 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIgwidQPSVELSNALM 182
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPEDVTLI----NGDGKTMQALL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 183 KHEGIALILATGGPGMVKAAYSSGKPA-IGVGAGNV-PVVIDETADIKRAVA-SVLMSKTFDNGVVCASEQAVIVMDE-- 257
Cdd:cd07084 176 LHPNPKMVLFTGSSRVAEKLALDAKQArIYLELAGFnWKVLGPDAQAVDYVAwQCVQDMTACSGQKCTAQSMLFVPENws 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 258 ---VYDEVKERFATHKahvlskaDADKVRKVLLIDGALnAKIVGQPatkiaEMAGVKVPADTKILVGEGIGE-------- 326
Cdd:cd07084 256 ktpLVEKLKALLARRK-------LEDLLLGPVQTFTTL-AMIAHME-----NLLGSVLLFSGKELKNHSIPSiygacvas 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 327 ---VSYDDEFAHEKL--SPTLGMFrASSFENAVDQAVKMVEIGGIGH---TSGLYTDQDVNADRIryfGDRLKTARILVN 398
Cdd:cd07084 323 alfVPIDEILKTYELvtEEIFGPF-AIVVEYKKDQLALVLELLERMHgslTAAIYSNDPIFLQEL---IGNLWVAGRTYA 398
|
330 340 350
....*....|....*....|....*....|....
gi 520910047 399 IPTTHGGI--GDLYNFNVAPSlTLGCGSWGGNSI 430
Cdd:cd07084 399 ILRGRTGVapNQNHGGGPAAD-PRGAGIGGPEAI 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
102-267 |
4.26e-05 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 47.18 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNStndaAKLVLDAAVAAGAPKDIIgwidqpSV-----E 176
Cdd:cd07139 136 EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLD----AYLLAEAAEEAGLPPGVV------NVvpadrE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 177 LSNALMKHEGIALILATGGpgmvKAAyssGKpAIGVGAGNV------------PVVIDETADIKRAVASVLMSKTFDNGV 244
Cdd:cd07139 206 VGEYLVRHPGVDKVSFTGS----TAA---GR-RIAAVCGERlarvtlelggksAAIVLDDADLDAAVPGLVPASLMNNGQ 277
|
170 180
....*....|....*....|...
gi 520910047 245 VCASEQAVIVMDEVYDEVKERFA 267
Cdd:cd07139 278 VCVALTRILVPRSRYDEVVEALA 300
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
97-274 |
6.52e-05 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 46.43 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 97 TMTIAEPVGIiCG-IVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAavaaGAPKDIIGWIDQPSV 175
Cdd:cd07091 135 AYTRREPIGV-CGqIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEA----GFPPGVVNIVPGFGP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 176 ELSNALMKHEGIALI-----LATGGPGMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQ 250
Cdd:cd07091 210 TAGAAISSHMDVDKIaftgsTAVGRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGS 289
|
170 180
....*....|....*....|....*
gi 520910047 251 AVIVMDEVYDEVKERF-ATHKAHVL 274
Cdd:cd07091 290 RIFVQESIYDEFVEKFkARAEKRVV 314
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
92-398 |
6.88e-05 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 46.18 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 92 DDSMGtMTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIGWid 171
Cdd:cd07118 109 DDMLG-LVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGY-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 172 qpSVELSNALMKHEGIALILATGGPGMvkaayssGKPAIGVGAGNV-----------PVVIDETADIKRAVASVLMSKTF 240
Cdd:cd07118 186 --GATVGQAMTEHPDVDMVSFTGSTRV-------GKAIAAAAARNLkkvslelggknPQIVFADADLDAAADAVVFGVYF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 241 DNGVVCASEQAVIVMDEVYDEVKERFATHKAHVLSKADADKVRKV-LLIDGALNAKIVGQPATKIAEMAGVKVPADtKIL 319
Cdd:cd07118 257 NAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVgAIINEAQLAKITDYVDAGRAEGATLLLGGE-RLA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 320 VGEG-------IGEVSYDDEFAHEKL-SPTLGMFRassFENaVDQAVKMVEIGGIGHTSGLYTDqdvNADRIRYFGDRLK 391
Cdd:cd07118 336 SAAGlfyqptiFTDVTPDMAIAREEIfGPVLSVLT---FDT-VDEAIALANDTVYGLSAGVWSK---DIDTALTVARRIR 408
|
....*..
gi 520910047 392 TARILVN 398
Cdd:cd07118 409 AGTVWVN 415
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
479-552 |
7.69e-05 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 45.87 E-value: 7.69e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520910047 479 KRAFLVTDRFLFNNgYADEVVSLLKAQGMEVTtFYEVEADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAK 552
Cdd:cd08170 23 KKALVIADPFVLDL-VGERLEESLEKAGLEVV-FEVFGGECSREEIERLAAIARANGADVVIGIGGGKTIDTAK 94
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
149-267 |
9.21e-05 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 45.89 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 149 AAKLVlDAAVAAGAPKDIIGWIDQPSVELSNALMKHEGIALILATG----GPGMVKAAYSSGKPAI---GvgaGNVPVVI 221
Cdd:cd07103 160 ALALA-ELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGstavGKLLMAQAADTVKRVSlelG---GNAPFIV 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 520910047 222 DETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFA 267
Cdd:cd07103 236 FDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLV 281
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
106-384 |
1.61e-04 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 45.16 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 106 IICGIVPTTNpTSTAIFKSLIslkTRNGIIFSPHPRA---KNSTNDAAKLVLdaaVAAGAPKDIIGWI-DQPSVELSNAL 181
Cdd:cd07127 200 IGCSTFPTWN-GYPGLFASLA---TGNPVIVKPHPAAilpLAITVQVAREVL---AEAGFDPNLVTLAaDTPEEPIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATGGP--GMVKAAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV----- 254
Cdd:cd07127 273 ATRPEVRIIDFTGSNafGDWLEANARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgi 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 255 --MDEV--YDEVKERFAThkahVLSKADADKVRKVLLIdGALNAKIVGQPATKIAEMAGVKVPAD-------------TK 317
Cdd:cd07127 353 qtDDGRksFDEVAADLAA----AIDGLLADPARAAALL-GAIQSPDTLARIAEARQLGEVLLASEavahpefpdarvrTP 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520910047 318 ILVGegiGEVSYDDEFAHEKLSPTLGMFRASSFENAVDQAVKMV-EIGGIghTSGLY-TDQDVnADRIR 384
Cdd:cd07127 428 LLLK---LDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVrEHGAM--TVGVYsTDPEV-VERVQ 490
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
102-261 |
1.81e-04 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 44.90 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPH---PRAknstndAAKLVlDAAVAAGAPKDIIGWIdQPSVELS 178
Cdd:cd07099 118 RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSevtPLV------GELLA-EAWAAAGPPQGVLQVV-TGDGATG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 NALMKhEGIALILATGGPG-----MVKAAySSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVI 253
Cdd:cd07099 190 AALID-AGVDKVAFTGSVAtgrkvMAAAA-ERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVY 267
|
....*...
gi 520910047 254 VMDEVYDE 261
Cdd:cd07099 268 VHESVYDE 275
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
2-274 |
1.84e-04 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 44.93 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 2 PVTNLAELDALVARVKAAQAEFATYS-QEQVDKIFRA-ASLAANQARI----------PLAQQAVAESGMgivEDKVikN 69
Cdd:cd07102 13 PLASLEAVRAALERARAAQKGWRAVPlEERKAIVTRAvELLAANTDEIaeeltwqmgrPIAQAGGEIRGM---LERA--R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 70 HFASeyIYNKYKDEKtcgILEEDDSMGTMTIAEPVGIICGIVPTTNPTSTAIfKSLI-SLKTRNGIIFSPHPRaknsTND 148
Cdd:cd07102 88 YMIS--IAEEALADI---RVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAV-NAVIpALLAGNAVILKHSPQ----TPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 149 AAKLVLDAAVAAGAPKDIIGWIdQPSVELSNALMKHEGIALILATGG-PGMVKAAYSSGKPAIGVG---AGNVPVVIDET 224
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVL-HLSHETSAALIADPRIDHVSFTGSvAGGRAIQRAAAGRFIKVGlelGGKDPAYVRPD 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 520910047 225 ADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERF-ATHKAHVL 274
Cdd:cd07102 237 ADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFvAVVKGYKL 287
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
174-273 |
2.34e-04 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 44.54 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 174 SVELSNALMKHEGIALILATGGPG---MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQ 250
Cdd:cd07147 189 SRDDADLLVTDERIKLLSFTGSPAvgwDLKARAGKKKVVLELG-GNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQ 267
|
90 100
....*....|....*....|...
gi 520910047 251 AVIVMDEVYDEVKERFATHKAHV 273
Cdd:cd07147 268 RVLVHRSVYDEFKSRLVARVKAL 290
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
180-267 |
2.93e-04 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 44.48 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 180 ALMKHEGIALILATGGPG-----MVKAAYSSGKPAIGVGaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07093 190 ALVAHPDVDLISFTGETAtgrtiMRAAAPNLKPVSLELG-GKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268
|
90
....*....|...
gi 520910047 255 MDEVYDEVKERFA 267
Cdd:cd07093 269 QRSIYDEFLERFV 281
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
99-267 |
4.01e-04 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 43.76 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhprAKNSTNDAAKLVlDAAVAAGAPKDIIGWIDQPSVELS 178
Cdd:cd07109 113 TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKP---AEDAPLTALRLA-ELAEEAGLPAGALNVVTGLGAEAG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 NALMKHEGIALILATGGPGMVKA-AYSSGKPAIGVG---AGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:cd07109 189 AALVAHPGVDHISFTGSVETGIAvMRAAAENVVPVTlelGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLV 268
|
170
....*....|...
gi 520910047 255 MDEVYDEVKERFA 267
Cdd:cd07109 269 HRSIYDEVLERLV 281
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
154-342 |
4.09e-04 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 43.75 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 154 LDAAVAAG----------AP------KDIIGWIDQPS--------VELSNALMK----HegialILATGGPG-----MVK 200
Cdd:cd07134 121 LVSAIAAGntailkpselTPhtsaviAKIIREAFDEDevavfegdAEVAQALLElpfdH-----IFFTGSPAvgkivMAA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 201 AA--YSSGKPAIGvgaGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATHKAHVLSKAD 278
Cdd:cd07134 196 AAkhLASVTLELG---GKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDA 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910047 279 ADKVRKVLlidgalnAKIVGQPAT-KIAEMAGVKVPADTKILVGegiGEVSYDDEFahekLSPTL 342
Cdd:cd07134 273 ARKASPDL-------ARIVNDRHFdRLKGLLDDAVAKGAKVEFG---GQFDAAQRY----IAPTV 323
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-268 |
4.34e-04 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 43.72 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 99 TIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhprAKNSTNDAAKLVlDAAVAAGAPKDIIGWIdQPSVELS 178
Cdd:PRK13252 138 TRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKP---SEVTPLTALKLA-EIYTEAGLPDGVFNVV-QGDGRVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 179 NALMKHEGIALILATGGPGMVK----AAYSSGKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIV 254
Cdd:PRK13252 213 AWLTEHPDIAKVSFTGGVPTGKkvmaAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFV 292
|
170
....*....|....
gi 520910047 255 MDEVYDEVKERFAT 268
Cdd:PRK13252 293 QKSIKAAFEARLLE 306
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
3-272 |
4.39e-04 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 43.82 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 3 VTNLAELDALVARVKAAQAEFATYSQEQVDKIFRAASLAANQARIPLAQQAVAESGmGIVEdkviKNHFASEYIYNKYKD 82
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRP----KAGFEVGAAIGELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 83 EKTCGILEEDD----SMGTMTIAE--PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDA 156
Cdd:cd07152 84 AAGLPTQPQGEilpsAPGRLSLARrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARLFEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 157 AvaaGAPKDII----GwidqpSVELSNALMKHEGIALILATGGPGM-----VKAAYSSGKPAIGVGAGNVPVVIDEtADI 227
Cdd:cd07152 164 A---GLPAGVLhvlpG-----GADAGEALVEDPNVAMISFTGSTAVgrkvgEAAGRHLKKVSLELGGKNALIVLDD-ADL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 520910047 228 KRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATHKAH 272
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKH 279
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
479-742 |
4.53e-04 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 43.29 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 479 KRAFLVTDRFlfnngyADEVVS-----LLKAQGmeVTTFYEV-EADPTLSIVKKGAEQMRSFQPDVILALGGGSPMDAAK 552
Cdd:cd08550 23 KKALIIGGKT------ALEAVGeklekSLEEAG--IDYEVEVfGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 553 ImwvmyehpethfeelamrfmdirkriykfpkMGQKAELVCIT--TTSGTGSEVTPFAVVTDDQtGAKYPLADYELTPNM 630
Cdd:cd08550 95 A-------------------------------VADRLGLPVVTvpTIAATCAAWSALSVLYDEE-GEFLGYSLLKRSPDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 631 AIVDANLVMNMPKSLTAFGGYDAVVHALEAYVSvLANEYSDG-------QALQALKLLKEylpssYANGAKDPIAREKVH 703
Cdd:cd08550 143 VLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPS-SRGGPDDLalqaavqLAKLAYDLLLE-----YGVQAVEDVRQGKVT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 520910047 704 NAatIAGVAFANAFL-GVCHSMAhkiGAEFH--LPHGLANSL 742
Cdd:cd08550 217 PA--LEDVVDAIILLaGLVGSLG---GGGCRtaAAHAIHNGL 253
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
215-269 |
1.02e-03 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 42.45 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 520910047 215 GNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERFATH 269
Cdd:cd07100 207 GSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEA 261
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
98-403 |
1.08e-03 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 42.36 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAavaagAPKDIIGWIDQPSVEL 177
Cdd:cd07107 111 YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREV-----LPPGVFNILPGDGATA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATG----GPGMVKAAYSSGKP-AIGVGAGNvPVVIDETADIKRAVASVLMSKTFD-NGVVCASEQA 251
Cdd:cd07107 186 GAALVRHPDVKRIALIGsvptGRAIMRAAAEGIKHvTLELGGKN-ALIVFPDADPEAAADAAVAGMNFTwCGQSCGSTSR 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 252 VIVMDEVYDEVKERFATH-KAHVLSKADADKVRKVLLIDGALNAKIVGQPATKIAE----MAGVKVPADTKILVGEGIGE 326
Cdd:cd07107 265 LFVHESIYDEVLARVVERvAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREgarlVTGGGRPEGPALEGGFYVEP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 327 VSYDDEFAHEKLS------PTLGMFRASSFENAVDQaVKMVEiggIGHTSGLYTDQDVNADRIryfGDRLKTARILVNIP 400
Cdd:cd07107 345 TVFADVTPGMRIAreeifgPVLSVLRWRDEAEMVAQ-ANGVE---YGLTAAIWTNDISQAHRT---ARRVEAGYVWINGS 417
|
...
gi 520910047 401 TTH 403
Cdd:cd07107 418 SRH 420
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
454-553 |
1.16e-03 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 42.19 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 454 WHKLPKSIYFRRG---SLPVALGDLEGKKRAFLVTDRfLFNNGYADEVVSLLKAQGmEVTTFyEVEaDPTLSIVKKGAEQ 530
Cdd:PRK00843 7 WIQLPRDVVVGHGvldDIGDVCSDLKLTGRALIVTGP-TTKKIAGDRVEENLEDAG-DVEVV-IVD-EATMEEVEKVEEK 82
|
90 100
....*....|....*....|...
gi 520910047 531 MRSFQPDVILALGGGSPMDAAKI 553
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAKL 105
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
102-266 |
1.38e-03 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 42.23 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhprAKNSTNDAAKLVlDAAVAAGAPKDIIGWIDQPSVELSNAL 181
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKP---ASDTPVIAAKFV-EVLEEAGLPAGVVNFVPGSGSEVGDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATGG---------------PGMVKAayssgKPAIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVC 246
Cdd:PRK03137 246 VDHPKTRFITFTGSrevglriyeraakvqPGQIWL-----KRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
170 180
....*....|....*....|
gi 520910047 247 ASEQAVIVMDEVYDEVKERF 266
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKV 340
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
103-266 |
1.42e-03 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 42.16 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 103 PVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNStndaAKLVLDAAVAAGAPKDIIGWIDQPSVELSNALm 182
Cdd:PRK13968 126 PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGC----AQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 183 KHEGIALILATGGpgmVKAAYSSGKPAigvGA----------GNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAV 252
Cdd:PRK13968 201 NDSRIAAVTVTGS---VRAGAAIGAQA---GAalkkcvlelgGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRF 274
|
170
....*....|....
gi 520910047 253 IVMDEVYDEVKERF 266
Cdd:PRK13968 275 IIEEGIASAFTERF 288
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
102-265 |
2.50e-03 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 41.43 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 102 EPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPhprAKNSTNDAAKLVlDAAVAAGAPKDIIGWIDQPSVELSNAL 181
Cdd:cd07112 123 EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP---AEQSPLTALRLA-ELALEAGLPAGVLNVVPGFGHTAGEAL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 182 MKHEGIALILATGGPG-----MVKAAYSSGKP-AIGVGAGNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVM 255
Cdd:cd07112 199 GLHMDVDALAFTGSTEvgrrfLEYSGQSNLKRvWLECGGKSPNIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVH 278
|
170
....*....|
gi 520910047 256 DEVYDEVKER 265
Cdd:cd07112 279 ESIKDEFLEK 288
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
98-407 |
4.05e-03 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 40.59 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 98 MTIAEPVGIICGIVPTTNPTSTAIFKSLISLKTRNGIIFSPHPRAKNSTNDAAKLVLDAAVAAGAPKDIIGWIdQPSVEL 177
Cdd:PLN02315 149 MEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSF-CGGAEI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 178 SNALMKHEGIALILATGGPG---MVKAAYSS--GKPAIGVGAGNVPVVIDEtADIKRAVASVLMSKTFDNGVVCASEQAV 252
Cdd:PLN02315 228 GEAIAKDTRIPLVSFTGSSKvglMVQQTVNArfGKCLLELSGNNAIIVMDD-ADIQLAVRSVLFAAVGTAGQRCTTCRRL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 253 IVMDEVYDEVKERFATHKAHVLSkadADKVRKVLLIdGALNAkivgqPATKIAEMAGVKVPADT--KILVG------EG- 323
Cdd:PLN02315 307 LLHESIYDDVLEQLLTVYKQVKI---GDPLEKGTLL-GPLHT-----PESKKNFEKGIEIIKSQggKILTGgsaiesEGn 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 324 -----IGEVSYDDEFAHEKL-SPTLGMFRASSFENAVDQAVKMVEiggiGHTSGLYTDQDVNAdrIRYFGDRLKTARIL- 396
Cdd:PLN02315 378 fvqptIVEISPDADVVKEELfGPVLYVMKFKTLEEAIEINNSVPQ----GLSSSIFTRNPETI--FKWIGPLGSDCGIVn 451
|
330
....*....|.
gi 520910047 397 VNIPTTHGGIG 407
Cdd:PLN02315 452 VNIPTNGAEIG 462
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
215-286 |
8.03e-03 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 39.51 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 215 GNVPVVIDETADIKRAVASVLMSKTFDNGVVCASEQAVIVMDEVYDEVKERF--------------ATHKAHVLSKADAD 280
Cdd:cd07135 217 GKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELkkvldefypgganaSPDYTRIVNPRHFN 296
|
....*.
gi 520910047 281 KVRKVL 286
Cdd:cd07135 297 RLKSLL 302
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
460-545 |
9.89e-03 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 39.35 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910047 460 SIYFRRGSLPVALGDLEGKK--RAFLVTDRFLFNNgYADEVVSLLKAQGMEVTTFyEVEADP---TLSIVKKGAEQM--- 531
Cdd:cd08195 3 PILIGSGLLDKLGELLELKKgsKVVIVTDENVAKL-YGELLLKSLEAAGFKVEVI-VIPAGEkskSLETVERIYDFLlea 80
|
90
....*....|....*..
gi 520910047 532 ---RSfqpDVILALGGG 545
Cdd:cd08195 81 gldRD---SLLIALGGG 94
|
|
| |
