|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
76-1687 |
0e+00 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 2428.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 76 EVGEVGDRDLPVDVSFTRRLPPVLTLGDGLAALRRAGEEVKACPPAAAaSGVIRFEVLVPPSTKALKWLCTQFKRSSLFP 155
Cdd:PLN02980 1 ELEVNLDDDLVVEVCITRTLPPALTLELGLESLKEAVNELKLNPPASS-SGVLRFQVAVPPSAKALKWFCSQPTSSDVFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 156 QFYLSRKQTTDSSIQL------EISGAGSAICF-HGSSRVDNGFDLISRYLSFNSHLIRAYGSVGVKYDKELLSLEERIG 228
Cdd:PLN02980 80 VFFLSKETTEPSYKSLyvkrphGVFGIGNAICFvHSSSLDSNGHSMIRRYLSSESAMVTAYGFMDINFNKESSSVNSKAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 229 SFYFFIPQVELSEFDGYSMLSSTIVWDDSVSHTFEDSVCLFESCFSQIWSSYDSSATICYENMVTSYIGESRMSESRNTQ 308
Cdd:PLN02980 160 SFYFFVPQIELDEHEEVSILSATLAWDDSLSYTFEQAISSYESSIYQVSSHFWPTAEDHWFKLLKSSLAKASVEEIHPAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 309 LVYLDAEFLAVIDGKAVTEKENCPTSDQSFVRFSPQFLFCANMdlCLQSNKIESFIRRCSNINLAWASFIVEEFVRLGFT 388
Cdd:PLN02980 240 LVYMGFFTLSGRDQAAVKELKSIQSSCQFHCRLSPDVVFSSNM--LDHEGEVSNFLKDYANINAVWASLIIEECTRLGLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 389 YFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPSVVEASQDFVPLILLT 468
Cdd:PLN02980 318 YFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 469 ADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDHIYARMVLTTVDSAAYYAMQAPQGPVHINCAFREPLDYGYQDW 548
Cdd:PLN02980 398 ADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPARMVLTTLDSAVHWATSSPCGPVHINCPFREPLDGSPTNW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 549 SVDCLKGLDKWFINREPYTRYLGMKMVSALGNYSCSVREVLEIVKNANQGLLLVGAIHTEDDIWAVTLLARHLSWPIAAD 628
Cdd:PLN02980 478 MSSCLKGLDMWMSNAEPFTKYIQMQSSKADGDTTGQITEVLEVIQEAKRGLLLIGAIHTEDDIWAALLLAKHLMWPVVAD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 629 VLSGLRMRKVQKSIPGLDKSICFIDHIDQILLSESVKSWKTPDVIVQIGSRITSKRVGTYLESCSPSSYILIDAHPCRHD 708
Cdd:PLN02980 558 ILSGLRLRKLFKSFPEFELNILFVDHLDHALLSDSVRNWIQFDVVIQIGSRITSKRVSQMLEKCFPFSYILVDKHPCRHD 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 709 PSHVVTHRIQATITEFAASLCQCNFQTKTSRWSDILMVLNSAVSQEIMFQVHSECSLTEPYVAHVIGEALYGDATMFIGN 788
Cdd:PLN02980 638 PSHLVTHRVQSNIVQFADCLLKAQFPRRRSKWHGHLQALDGMVAQEISFQIHAESSLTEPYVAHVISEALTSDSALFIGN 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 789 SMVIRDLDMFGKGWIDHSTNANNAMMHHFPGFLGAPVAGNRGASGIDGLLSTSIGFAIGSNKHVFCVIGDISFLHDTNGL 868
Cdd:PLN02980 718 SMAIRDADMYGCSSENYSSRIVDMMLSAELPCQWIQVAGNRGASGIDGLLSTAIGFAVGCNKRVLCVVGDISFLHDTNGL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 869 SLLNQRTQRKPMTVIVINNHGGAIFSLLPVAKTASLQILEKFFYTLHDISISKLCAA----------------------- 925
Cdd:PLN02980 798 SILSQRIARKPMTILVINNHGGAIFSLLPIAKRTEPRVLNQYFYTSHDISIENLCLAhgvrhlhvgtkseledalftsqv 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 926 -------------------HRIISMFTDHSATMHLAYLLGGPYCKDGVNGFSVGRIHAAEYMFYRIQLAAPRTSGISE-S 985
Cdd:PLN02980 878 eqmdcvvevessidanaafHSTLRKFACQAAEHALGILSESSCLHSIIDGVFLCKISGMEYSLYRIQLCAPPTSASVDfS 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 986 SFFHEGFILKLCVGDSIVGFGEVAPIEIHEEDLLDVEEQLRFLFHRMKDAELD-VVPLLRGSFSNWIWTTLGIPPSSVFP 1064
Cdd:PLN02980 958 QFHREGFILSLSLEDGSVGFGEVAPLEIHEEDLLDVEEQLRFLLHVIKGAKISfMLPLLKGSFSSWIWSELGIPPSSIFP 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1065 SVKCGLEMAILNLLESQRIDRSYGIFTGSNVVEYNQSSTANIQICALVDSCGTPMDVTLAVVKLVAEGFTTVKLKVGRRE 1144
Cdd:PLN02980 1038 SVRCGLEMAILNAIAVRHGSSLLNILDPYQKDENGSEQSHSVQICALLDSNGSPLEVAYVARKLVEEGFSAIKLKVGRRV 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1145 NPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPVDSVNDIIKFCENSGLPVALDETIDNL 1224
Cdd:PLN02980 1118 SPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDEDDLIKFCEETGLPVALDETIDKF 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1225 TGDVIPKLHQFSHPGIVALVIKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESSVGLATYIQFAHYVDRQNDITSRIKN 1304
Cdd:PLN02980 1198 EECPLRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYIQFASYLEMQNAKASREMN 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1305 RGSCGNVAHGLGTYQWLREDVSDQKLKIHAPPLGDGIRASAEDAHGYLQHLVINDKKIERTYSEEKLRSYFIQVDGDNFS 1384
Cdd:PLN02980 1278 KGTCPSVAHGLGTYRWLKEDVTMNPLGIFRSPYSGFIEASVADASRNLQKFQINNDVIVRTFKEEQVRTYELRVDVDGFS 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1385 YQVKLQEGGDCTHEKVILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILQHDVENSNQISFSVQSVADLLLK 1464
Cdd:PLN02980 1358 CLIKVHEVGQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSKIQNHAKETQTEPTLSVELVADLLYK 1437
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1465 LIRNITDGAVVVVGYSMGARIALHMALNQNHKvnfstlyllclflyfydsnavplrqISGAVIISGSPGLRDEASKRRRS 1544
Cdd:PLN02980 1438 LIEHITPGKVTLVGYSMGARIALYMALRFSDK-------------------------IEGAVIISGSPGLKDEVARKIRS 1492
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1545 AIDRSRAHFLSSCGLENFLETWYSAKMWASLREHPKFDSLVRTRMKHNNIKALSKVLADSSIGTQKSLWEDLKHLKSPLL 1624
Cdd:PLN02980 1493 AKDDSRARMLIDHGLEIFLENWYSGELWKSLRNHPHFNKIVASRLLHKDVPSLAKLLSDLSIGRQPSLWEDLKQCDTPLL 1572
|
1610 1620 1630 1640 1650 1660
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443056271 1625 IVAGEKDPKFKEISQQMCREIRKHKDRESDG---LCEMIIIPDSGHAVHVENPLPLVRAIRKFLVR 1687
Cdd:PLN02980 1573 LVVGEKDVKFKQIAQKMYREIGKSKESGNDKgkeIIEIVEIPNCGHAVHLENPLPVIRALRKFLTR 1638
|
|
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
368-928 |
0e+00 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 554.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 368 SNINLAWASFIVEEFVRLGFTYFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAV 447
Cdd:COG1165 3 KNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGTAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 448 SNLLPSVVEASQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDHI-YARMVLTTVDSAAYYAMQA 526
Cdd:COG1165 83 ANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPdALRYLRRTINRALAAALGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 527 PQGPVHINCAFREPLdygYQDwsVDCLKGLDKwfinREPYTRYLGMKMVSALGnyscSVREVLEIVKNANQGLLLVGAIH 606
Cdd:COG1165 163 PPGPVHINVPFREPL---YPD--PDEEDPLAA----GGPWIRVTPPEPAPSPE----ALAQLADELERAKRGLIVAGPLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 607 T-EDDIWAVTLLARHLSWPIAADVLSGLRmrkvqksipgldkSICFIDHIDQILLSESVKSWKTPDVIVQIGSRITSKRV 685
Cdd:COG1165 230 PpEELAEALAALAEALGWPVLADPLSNLR-------------HPNVISTYDLLLRNPEFAELLQPDLVIRFGGPPVSKRL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 686 GTYLESCSPSSYILIDAHPCRHDPSHVVTHRIQATITEFAASLCQcNFQTKTSRWSDILMVLNSAVSQEIMfQVHSECSL 765
Cdd:COG1165 297 KQFLRRHPPAEHWVVDPSGEWRDPFHSLTRVIEADPEAFLEALAE-RLPPADSAWLARWLAAEQKARAAID-EYLAEDPL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 766 TEPYVAHVIGEALYGDATMFIGNSMVIRDLDMFGkgwidhstnannammhhFPGFLGAPVAGNRGASGIDGLLSTSIGFA 845
Cdd:COG1165 375 SEGAVARRLLEALPEGSTLFVGNSMPVRDLDLFA-----------------RPLPKGVRVYANRGASGIDGTVSTALGAA 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 846 IGSNKHVFCVIGDISFLHDTNGlsLLNQRTQRKPMTVIVINNHGGAIFSLLPVAKTAslQILEKFFYTLHDISISKLCAA 925
Cdd:COG1165 438 LASGKPTVLLTGDLSFLHDLNG--LLLLYELPPNLTIVVVNNDGGGIFSMLPGAKFE--PEFERFFGTPHGLDFEHLAAM 513
|
...
gi 1443056271 926 HRI 928
Cdd:COG1165 514 YGL 516
|
|
| menD |
TIGR00173 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought ... |
374-847 |
5.32e-146 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought until recently to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695). 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 272941 [Multi-domain] Cd Length: 432 Bit Score: 456.29 E-value: 5.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 374 WASFIVEEFVRLGFTYFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPS 453
Cdd:TIGR00173 1 WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTSGTAVANLLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 454 VVEASQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDHIYARMVLTTVDSAAYYAMQAPQGPVHI 533
Cdd:TIGR00173 81 VIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEPLAYLRSTVDRALAQAQGAPPGPVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 534 NCAFREPLDygyqdwSVDCLKGLDKWFinREPYTRYLgmkmVSALGNYSCSVREVLEIVKNANQGLLLVGAIHTEDDIWA 613
Cdd:TIGR00173 161 NVPFREPLY------PDPLLQPLQPWL--RSGVPTIS----TGPPVLDPESLQELWDRLRQAKRGLIIAGPLAGAEDAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 614 VTLLARHLSWPIAADVLSGLRmrkvQKSIPGLdksicfIDHIDQILLSESVKSWKTPDVIVQIGSRITSKRVGTYLEScS 693
Cdd:TIGR00173 229 LAALAEALGWPLLADPLSGLR----GGPHPLV------IDHYDLLLANAELREELQPDLVIRFGGPPVSKRLRQWLAR-A 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 694 PSSYILIDAHPCRHDPSHVVTHRIQATITEFAASLCQCnFQTKTSRWSDILMVLNSAVsQEIMFQVHSECSLTEPYVAHV 773
Cdd:TIGR00173 298 PAEYWVVDPRPGWLDPFHHATTRLEASPAAFAEALAGL-LKNPAAAWLDRWLEAEAKA-RAALREVLAEEPLSELSLARA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443056271 774 IGEALYGDATMFIGNSMVIRDLDMFGKgwidhstnannammhhfPGFLGAPVAGNRGASGIDGLLSTSIGFAIG 847
Cdd:TIGR00173 376 LSQLLPDGSALFVGNSMPIRDLDTFSS-----------------PPDKPIRVFANRGASGIDGTLSTALGIAAA 432
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
378-537 |
2.05e-79 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 258.97 E-value: 2.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 378 IVEEFVRLGFTYFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPSVVEA 457
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 458 SQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDHIYARMVLTTVDSAAYYAMQAPQGPVHINCAF 537
Cdd:cd07037 83 YYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
1399-1685 |
1.15e-57 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 200.13 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1399 KVILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILQHDVENsnqiSFsVQSVADLLLKLIRNITDGAVVVVG 1478
Cdd:TIGR03695 3 PVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSSQSPSDIERY----DF-EEAAQLLLATLLDQLGIEPFFLVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1479 YSMGARIALHMALNQNHKVnfstlyllclflyfydsnavplrqiSGAVIISGSPGLRDEASKRRRSAIDRSRAHFLSSCG 1558
Cdd:TIGR03695 78 YSMGGRIALYYALQYPERV-------------------------QGLILESGSPGLQTEEERAARRQNDEQLAQRFEQEG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1559 LENFLETWYSAKMWASLREHPKF--DSLVRTRmKHNNIKALSKVLADSSIGTQKSLWEDLKHLKSPLLIVAGEKDPKFKE 1636
Cdd:TIGR03695 133 LEAFLDDWYQQPLFASQKNLPPEqrQALRAER-LANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQ 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1443056271 1637 ISQQMCREIRKHKdresdglceMIIIPDSGHAVHVENPLPLVRAIRKFL 1685
Cdd:TIGR03695 212 IAKEMQKLIPNLT---------LHIIPNAGHNIHLENPEAFAKILLAFL 251
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
765-926 |
3.23e-48 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 170.08 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 765 LTEPYVAHVIGEALYGDATMFIGNSMVIRDLDMFGKgwidhstnannammhhfPGFLGAPVAGNRGASGIDGLLSTSIGF 844
Cdd:cd02009 1 LTEPALARALPDHLPEGSQLFVGNSMPIRDLDLFAL-----------------PSDKTVRVFANRGASGIDGTLSTALGI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 845 AIGSNKHVFCVIGDISFLHDTNGLSLLNQrtQRKPMTVIVINNHGGAIFSLLPVAKTASlqILEKFFYTLHDISISKLCA 924
Cdd:cd02009 64 ALATDKPTVLLTGDLSFLHDLNGLLLGKQ--EPLNLTIVVINNNGGGIFSLLPQASFED--EFERLFGTPQGLDFEHLAK 139
|
..
gi 1443056271 925 AH 926
Cdd:cd02009 140 AY 141
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
970-1289 |
1.01e-39 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 148.95 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 970 YRIQLAAP-RTSGISESSFfhEGFILKLCVGDSIVGFGEVAPIeiheedlldveeqlrflfhrmkdaeldvvpllrgsfs 1048
Cdd:cd03320 6 YSLPLSRPlGTSRGRLTRR--RGLLLRLEDLTGPVGWGEIAPL------------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1049 nwiwttlgippssvfpSVKCGLEMAILNLLesqridrsygiftgsNVVEYNQSSTANIQICALVdsCGTPMDVTLAVVKL 1128
Cdd:cd03320 47 ----------------PLAFGIESALANLE---------------ALLVGFTRPRNRIPVNALL--PAGDAAALGEAKAA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1129 VAEGFTTVKLKVGRRENpAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPVdSVNDIIKFC 1208
Cdd:cd03320 94 YGGGYRTVKLKVGATSF-EEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPL-PPDDLAELR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1209 E-NSGLPVALDETIDNLTGDviPKLHQFSHPGivALVIKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESSVGLATYIQ 1287
Cdd:cd03320 172 RlAAGVPIALDESLRRLDDP--LALAAAGALG--ALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAH 247
|
..
gi 1443056271 1288 FA 1289
Cdd:cd03320 248 LA 249
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
970-1290 |
1.33e-39 |
|
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441050 [Multi-domain] Cd Length: 325 Bit Score: 150.41 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 970 YRIQLaaPRTSGI---SESSFFHEGFILKLCVGDSiVGFGEVAP-IEIHEEDLLDVEEQLRFLFHRMKDAELdvvpllrg 1045
Cdd:COG1441 7 YRYSI--PMDAGVilrNQRLKTRDGLLVRLQEGGR-EGWGEIAPlPGFSQETLEQAEQQALAWLQRWLAGDL-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1046 sfsnwiwttlgIPPSSVFPSVKCGLEMAILNLlesqridrsYGIFtgsnvveynqSSTANIQICALvdsC-GTPMDvtLA 1124
Cdd:COG1441 76 -----------LDEKSLLPSVAFGLSCALAEL---------EGEL----------PEAANYRAAPL---CsGDPDE--LI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1125 VVKLVAEGFTTVKLKVGRREnPAEDAAVIQKVREIVGyKINIRADANRKWTYEQAIDFGSRVK---GLCLQYIEEPVDSV 1201
Cdd:COG1441 121 ARLNQMPGEKVAKVKVGLYE-AVRDGMVVNLLLEAIP-DLRLRLDANRSWTLDKAVQFAKYVNpehRSRIAFLEEPCKTP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1202 NDIIKFCENSGLPVALDETI--DNLTgDVIPklhqfshPGIVALVIKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESS 1279
Cdd:COG1441 199 EESREFARETGIAIAWDESVrePDFR-VEAE-------PGVAAIVIKPTLVGSLQRCRQLIEQAHQLGLQAVISSSIESS 270
|
330
....*....|.
gi 1443056271 1280 VGLATYIQFAH 1290
Cdd:COG1441 271 LGLTQLARLAA 281
|
|
| PLN02786 |
PLN02786 |
isochorismate synthase |
66-279 |
1.39e-36 |
|
isochorismate synthase
Pssm-ID: 178383 [Multi-domain] Cd Length: 533 Bit Score: 146.85 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 66 RRAGIVIDVDevGEVGDRDLPVDVSFTRRLPPVLTLGDGLAALRRAGEEVKACPPAAAaSGVIRFEVLVPPSTKALKWLC 145
Cdd:PLN02786 12 RKTSCSQSMN--GCQGDPKVPVGTVETRTLPAVLSPADATERLISAVSELKSQPPPFS-SGILRLQVPIPQQIGAIDWLH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 146 TQFKrssLFPQFYLSRKQTT-----------------DSSIQLEISGAGSAICFHGSSRVD-NGFDLISRYLSFNSHLIR 207
Cdd:PLN02786 89 AQNE---LLPRCFFSRRSDTgdrpdllldssngngngSDHNLVSVAGVGSAVFFRDLDPFShDDWRSIKRFLSSKSPLIR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443056271 208 AYGsvGVKYDKEL-LSLE-ERIGSFYFFIPQVELSEFDGYSMLSSTIVWDDSVSHTFEDSVCLFESCFSQIWSS 279
Cdd:PLN02786 166 AYG--AIRFDPNGkISVEwEPFGSFYFIVPQVEFNELGGSSMLAATIAWDDALSWTWENAIEALQETMLQVSSV 237
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
1403-1685 |
6.26e-33 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 128.42 E-value: 6.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1403 FLHGFLGTSEDWVPMMKALsPSARVIAVDLPGHGESEILQhdVENSNQISfsvqsvaDLLLKLIRNITDGAVVVVGYSMG 1482
Cdd:PRK11126 7 FLHGLLGSGQDWQPVGEAL-PDYPRLYIDLPGHGGSAAIS--VDGFADVS-------RLLSQTLQSYNILPYWLVGYSLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1483 ARIALHMALNQNHkvnfstlyllclflyfydsnavplRQISGAVIISGSPGLRDEASKRRRSAIDRSRAHFLSSCGLENF 1562
Cdd:PRK11126 77 GRIAMYYACQGLA------------------------GGLCGLIVEGGNPGLQNAEERQARWQNDRQWAQRFRQEPLEQV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1563 LETWYSAKMWASLrEHPKFDSLVRTRmKHNNIKALSKVLADSSIGTQKSLWEDLKHLKSPLLIVAGEKDPKFKEISQQMC 1642
Cdd:PRK11126 133 LADWYQQPVFASL-NAEQRQQLVAKR-SNNNGAAVAAMLEATSLAKQPDLRPALQALTFPFYYLCGERDSKFQALAQQLA 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1443056271 1643 REIRkhkdresdglcemiIIPDSGHAVHVENPLPLVRAIRKFL 1685
Cdd:PRK11126 211 LPLH--------------VIPNAGHNAHRENPAAFAASLAQIL 239
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
990-1296 |
4.03e-32 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 128.39 E-value: 4.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 990 EGFILKLCVGdSIVGFGEVAPIE-IHEEDLLDVEEQLRFLFHRmkdaeldvvpllrgsfsnwiWTTLGI-PPSSVFPSVK 1067
Cdd:TIGR01927 22 EGLIVRLTDE-GRTGWGEIAPLPgFGTETLAEALDFCRALIEE--------------------ITRGDIeAIDDQLPSVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1068 CGLEMAILNLLESQRIdrsygiftgsnvveynqsSTANIQICALVDScGTPMDVTLAVVKlvAEGFTTVKLKVGRREnPA 1147
Cdd:TIGR01927 81 FGFESALIELESGDEL------------------PPASNYYVALLPA-GDPALLLLRSAK--AEGFRTFKWKVGVGE-LA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1148 EDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVK---GLCLQYIEEPVDSVNDIIKFCENSGLPVALDETIDNL 1224
Cdd:TIGR01927 139 REGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDpnlRGRIAFLEEPLPDADEMSAFSEATGTAIALDESLWEL 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443056271 1225 tgdviPKLHQFSHPGI-VALVIKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESSVGLATYIQFAHYVDRQN 1296
Cdd:TIGR01927 219 -----PQLADEYGPGWrGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLSPDP 286
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1372-1687 |
9.97e-32 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 124.34 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1372 RSYFIQVDGDNFSYQVKLQEGgdctheKVILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILQHDvensnqi 1451
Cdd:COG0596 3 TPRFVTVDGVRLHYREAGPDG------PPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1452 sFSVQSVADLLLKLIRNITDGAVVVVGYSMGARIALHMALNQNHKVnfstlyllclflyfydsnavplrqiSGAVIISgs 1531
Cdd:COG0596 70 -YTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV-------------------------AGLVLVD-- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1532 pglrdeaskrrrSAIDRSRAHFlsscglenfletwysakmwaslrehpkfdslvrtRMKHNNIKALSKVLADSsigTQKS 1611
Cdd:COG0596 122 ------------EVLAALAEPL----------------------------------RRPGLAPEALAALLRAL---ARTD 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443056271 1612 LWEDLKHLKSPLLIVAGEKDPKFK-EISQQMCREIRKhkdresdglCEMIIIPDSGHAVHVENPLPLVRAIRKFLVR 1687
Cdd:COG0596 153 LRERLARITVPTLVIWGEKDPIVPpALARRLAELLPN---------AELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
969-1289 |
1.36e-31 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 128.02 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 969 FYRIQLAAPRTSGISESSFFH-EGFILKLCVGDSIVGFGEVAPIEIHEEDLLD-VEEQLRflfhrmkdaeldvvPLLRG- 1045
Cdd:COG4948 8 VYPVRLPLKRPFTISRGTRTErDVVLVRVETDDGITGWGEAVPGGTGAEAVAAaLEEALA--------------PLLIGr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1046 SFSNW--IWTTLGiPPSSVFPSVKCGLEMAILNLLesqridrsyGIFTGSNVVEY-NQSSTANIQICALVDScGTPMDVT 1122
Cdd:COG4948 74 DPLDIeaLWQRLY-RALPGNPAAKAAVDMALWDLL---------GKALGVPVYQLlGGKVRDRVPVYATLGI-DTPEEMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1123 LAVVKLVAEGFTTVKLKVGRReNPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV--DS 1200
Cdd:COG4948 143 EEAREAVARGFRALKLKVGGP-DPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLpaED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1201 VNDIIKFCENSGLPVALDETIDNLTGdvIPKLHQfsHPGIVALVIKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESSV 1280
Cdd:COG4948 222 LEGLAELRRATPVPIAADESLTSRAD--FRRLIE--AGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGI 297
|
....*....
gi 1443056271 1281 GLATYIQFA 1289
Cdd:COG4948 298 GLAAALHLA 306
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
1116-1289 |
1.80e-26 |
|
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 110.51 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1116 GTPMDVTLAVVKLVAEGFTTVKLKVGRreNPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIE 1195
Cdd:cd03315 84 GEPAEVAEEARRALEAGFRTFKLKVGR--DPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1196 EPV--DSVNDIIKFCENSGLPVALDETIDNLtGDVIPKLHQfshPGIVALVIKPSVVGGFETAAYIAKWAHMHDKMAVIS 1273
Cdd:cd03315 162 QPLpaDDLEGRAALARATDTPIMADESAFTP-HDAFRELAL---GAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVG 237
|
170
....*....|....*.
gi 1443056271 1274 STYESSVGLATYIQFA 1289
Cdd:cd03315 238 SMIESGLGTLANAHLA 253
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
378-534 |
4.70e-25 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 103.47 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 378 IVEEFVRLGFTYFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPSVVEA 457
Cdd:pfam02776 5 LADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGLANA 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443056271 458 SQDFVPLILLTADRPPELQDVGANQA-INQVNHFGSFVRHFFSLPPPDDhiyarmVLTTVDSAAYYAMQAPQGPVHIN 534
Cdd:pfam02776 85 YVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADE------IPEVLRRAFRAALSGRPGPVYLE 156
|
|
| TPP_enzyme_M_2 |
pfam16582 |
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine ... |
553-786 |
8.39e-25 |
|
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine pyrophosphate in sequences not captured by pfam00205. This enzyme is necessary for the first step of the biosynthesis of menaquinone, or vitamin K2, an important cofactor in electron transport in bacteria.
Pssm-ID: 435442 Cd Length: 207 Bit Score: 103.93 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 553 LKGLDKWFINREPYTRYlgmkmvsalgnyscsVREVLEIVKNAN-------QGLLLVGAIhTEDDIWAVTLLARHLSWPI 625
Cdd:pfam16582 3 LAPLGDWLQQNKPWLRY---------------QAQQLEVPTHDDwdfwrqkKGVIVAGRL-SAEEGMQLAAWAQKLGWPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 626 AADVLSGlrmrkVQKSIPgldksicfidHIDQILLSESVKS-WKTPDVIVQIGSRITSKRVGTYLESCSPSSYILIDAHP 704
Cdd:pfam16582 67 LTDVQSQ-----TGQPLP----------YADLWLANPTAREeLAQADIVIQFGGRLTSKRLLQFLAACKPHEYWLVDPLP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 705 CRHDPSHVVTHRIQATITEFaaslCQCNFQTKTSRWSDILMVLNSAVSQEIMFQVHSEcsLTEPYVAHVIGEALYGDATM 784
Cdd:pfam16582 132 GRLDPAHHRGRRFVASVGEW----LRAHPPLRQAPWALELLALSEFLASFIEQQVGGE--FGEAQLAHRIAALLPDQGQL 205
|
..
gi 1443056271 785 FI 786
Cdd:pfam16582 206 FI 207
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
378-534 |
9.09e-25 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 102.22 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 378 IVEEFVRLGFTYFCIAPGSRSSPLaLSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPSVVEA 457
Cdd:cd07035 3 LVEALKAEGVDHVFGVPGGAILPL-LDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLANA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443056271 458 SQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDhiyarmVLTTVDSAAYYAMQAPQGPVHIN 534
Cdd:cd07035 82 YLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEE------IPEALRRAFRIALSGRPGPVALD 152
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
1121-1289 |
1.19e-23 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 101.10 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1121 VTLAVVKLVAEGFTTVKLKVGRREnPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV-- 1198
Cdd:pfam13378 3 AAEARRAVEARGFRAFKLKVGGPD-PEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVpp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1199 DSVNDIIKFCENSGLPVALDETIDNltgdvipkLHQF----SHPGIVALVIKPSVVGGFETAAYIAKWAHMHDkMAVISS 1274
Cdd:pfam13378 82 DDLEGLARLRRATPVPIATGESLYS--------REDFrrllEAGAVDIVQPDVTRVGGITEALKIAALAEAFG-VPVAPH 152
|
170
....*....|....*
gi 1443056271 1275 TYESSVGLATYIQFA 1289
Cdd:pfam13378 153 SGGGPIGLAASLHLA 167
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
990-1290 |
1.87e-23 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 103.38 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 990 EGFILKLCVGDSiVGFGEVAPI-EIHEEDLLDVEEQLRFLFHRMKDAELDvvpllrgsfsnwiwttlgiPPSSVFPSVKC 1068
Cdd:PRK05105 28 DGLVVQLREGER-EGWGEIAPLpGFSQETLEEAQEALLAWLNNWLAGDCD-------------------DELSQYPSVAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1069 GLEMAILNL---LESQRIDRSygiftgsnvveynqsstanIQICAlvdscGTPMDVTLAVVKLvaEGFTTVKLKVGRREn 1145
Cdd:PRK05105 88 GLSCALAELagtLPQAANYRT-------------------APLCY-----GDPDELILKLADM--PGEKVAKVKVGLYE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1146 PAEDAAVIQKVREIVGyKINIRADANRKWTYEQAIDFGSRVKGLC---LQYIEEPVDSVNDIIKFCENSGLPVALDETId 1222
Cdd:PRK05105 141 AVRDGMLVNLLLEAIP-DLKLRLDANRGWTLEKAQQFAKYVPPDYrhrIAFLEEPCKTPDDSRAFARATGIAIAWDESL- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443056271 1223 NLTGdvipklHQFS-HPGIVALVIKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESSVGLATYIQFAH 1290
Cdd:PRK05105 219 REPD------FQFEaEPGVRAIVIKPTLTGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLAA 281
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
375-892 |
2.01e-22 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 103.70 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 375 ASFIVEEFVRLGFTY-FCIaPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPS 453
Cdd:COG0028 6 ADALVEALEAEGVETvFGV-PGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 454 VVEASQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDhiyarmVLTTVDSAAYYAMQAPQGPVHI 533
Cdd:COG0028 85 LADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPED------LPEVLRRAFRIATSGRPGPVVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 534 NCafrePLDYGYQDWSVdclkgldkwfinrEPYTRYLGMKMVSALGNYScSVREVLEIVKNANQGLLLVGA-IHTEDDIW 612
Cdd:COG0028 159 DI----PKDVQAAEAEE-------------EPAPPELRGYRPRPAPDPE-AIEEAAELLAAAKRPVILAGGgARRAGAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 613 AVTLLARHLSWPIAADVlsglrMRKVqkSIPGLDKsiCFIDHIDQILLSESVKSWKTPDVIVQIGSRITSKRVGTYLESC 692
Cdd:COG0028 221 ELRALAERLGAPVVTTL-----MGKG--AFPEDHP--LYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 693 SPSSYILIDAHPCRHDPSHVVTHRIQATITEFAASLCQcNFQTKTSRWSDILMVLNSAVSQEIMFQVHSECSLTEPYVAH 772
Cdd:COG0028 292 PDAKIIHIDIDPAEIGKNYPVDLPIVGDAKAVLAALLE-ALEPRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 773 VIGEALYGDATMFIGnsmvirdldmfgkgwidhSTNANNAMMHHFP-----GFLGAPVAGNRGASgidglLSTSIGFAIG 847
Cdd:COG0028 371 ALREALPDDAIVVTD------------------VGQHQMWAARYLRfrrprRFLTSGGLGTMGYG-----LPAAIGAKLA 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1443056271 848 -SNKHVFCVIGDISFLHdtNGLSLLNQRTQRKPMTVIVINNHG-GAI 892
Cdd:COG0028 428 rPDRPVVAITGDGGFQM--NLQELATAVRYGLPVKVVVLNNGGlGMV 472
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
970-1293 |
7.76e-22 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 98.41 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 970 YRIQLAAPRTsgISESSFFH-EGFILKLCVgDSIVGFGEVAPIE-IHEEDLLDVEEQLRflfhrmkdaelDVVPLLRGSF 1047
Cdd:cd03319 7 ERLPLKRPFT--IARGSRTEaENVIVEIEL-DGITGYGEAAPTPrVTGETVESVLAALK-----------SVRPALIGGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1048 SNW--IWTTLG--IPPssvFPSVKCGLEMAILNLlESQRIDRS---YGIFTGSNVVEynqssTAnIQIcalvdSCGTPMD 1120
Cdd:cd03319 73 PRLekLLEALQelLPG---NGAARAAVDIALWDL-EAKLLGLPlyqLWGGGAPRPLE-----TD-YTI-----SIDTPEA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1121 VTLAVVKLVAEGFTTVKLKVGRreNPAEDAAVIQKVREIVGyKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV-- 1198
Cdd:cd03319 138 MAAAAKKAAKRGFPLLKIKLGG--DLEDDIERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVpa 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1199 DSVNDIIKFCENSGLPVALDETIDNLtGDViPKLHQfshPGIVALV-IKPSVVGGFETAAYIAKWAHMHDKMAVISSTYE 1277
Cdd:cd03319 215 GDDDGLAYLRDKSPLPIMADESCFSA-ADA-ARLAG---GGAYDGInIKLMKTGGLTEALRIADLARAAGLKVMVGCMVE 289
|
330 340
....*....|....*....|
gi 1443056271 1278 SSVGLATYIQFA----HYVD 1293
Cdd:cd03319 290 SSLSIAAAAHLAaakaDFVD 309
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
1399-1674 |
7.73e-20 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 90.64 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1399 KVILFLHGFLGTSEDWVPMMKALSPS-ARVIAVDLPGHGESEILqhdvenSNQISFSVQSVADLLLKLIRNITDGAVVVV 1477
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRP------KAQDDYRTDDLAEDLEYILEALGLEKVNLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1478 GYSMGARIALHMALNQNHKVnfstlyllclflyfydsnavplrqiSGAVIISG--SPGLRDEASKRRRSAIDRSRAHFLS 1555
Cdd:pfam00561 75 GHSMGGLIALAYAAKYPDRV-------------------------KALVLLGAldPPHELDEADRFILALFPGFFDGFVA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1556 SCGLENFLETWYSAKMWASLREHPKFdsLVRTRMKhnNIKALSKVLADSSIGTQKSLWEDLKH---------LKSPLLIV 1626
Cdd:pfam00561 130 DFAPNPLGRLVAKLLALLLLRLRLLK--ALPLLNK--RFPSGDYALAKSLVTGALLFIETWSTelrakflgrLDEPTLII 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1443056271 1627 AGEKDPKFKEisqQMCREIRKHKDREsdglcEMIIIPDSGHAVHVENP 1674
Cdd:pfam00561 206 WGDQDPLVPP---QALEKLAQLFPNA-----RLVVIPDAGHFAFLEGP 245
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
1109-1297 |
1.66e-19 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 89.31 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1109 CALVDSCGTPMDVTLAVvklvaegfttvKLKVGRRENPAEDA--AVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRV 1186
Cdd:cd00308 49 MALWDLAAKALGVPLAE-----------LLGGGSRDRVPAYGsiERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1187 KGLCLQYIEEPVDSVN--DIIKFCENSGLPVALDEtidnLTGDVIPKLHQFSHPGIVALVIKPSVVGGFETAAYIAKWAH 1264
Cdd:cd00308 118 EKYGLAWIEEPCAPDDleGYAALRRRTGIPIAADE----SVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAE 193
|
170 180 190
....*....|....*....|....*....|....*
gi 1443056271 1265 MHDKMAVISSTYESSVGLA--TYIQFAHYVDRQND 1297
Cdd:cd00308 194 AFGIRVMVHGTLESSIGTAaaLHLAAALPNDRAIE 228
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
378-537 |
5.09e-19 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 85.47 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 378 IVEEFVRLGFTYFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSrKPAIVITSSGTAVSNLLPSVVEA 457
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAG-GPPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 458 SQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLppPDDHIYARMVLTtvdsaAYYAMQAPQGPVHINCAF 537
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISS--PSPAELPAGIDH-----AIRTAYASQGPVVVRLPR 154
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
1123-1198 |
4.91e-18 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 80.79 E-value: 4.91e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443056271 1123 LAVVKLVAEGFTTVKLKVGRreNPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV 1198
Cdd:smart00922 7 AARRAVAEAGFRAVKVKVGG--GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
1117-1289 |
1.70e-17 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 86.13 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1117 TPMDVTLAVVKLVAEGFTTVKLKVGR----RENPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQ 1192
Cdd:cd03316 139 SPEELAEEAKRAVAEGFTAVKLKVGGpdsgGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1193 YIEEPV--DSVNDIIKFCENSGLPVALDETIDNltgdvipkLHQFSHP---GIVAlVIKPSV--VGGFETAAYIAKWAHM 1265
Cdd:cd03316 219 WFEEPVppDDLEGLARLRQATSVPIAAGENLYT--------RWEFRDLleaGAVD-IIQPDVtkVGGITEAKKIAALAEA 289
|
170 180
....*....|....*....|....
gi 1443056271 1266 HDkMAVISSTYESSVGLATYIQFA 1289
Cdd:cd03316 290 HG-VRVAPHGAGGPIGLAASLHLA 312
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
990-1327 |
9.58e-17 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 83.14 E-value: 9.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 990 EGFILKLCVGDSIVGFGEVAPI-EIHEEDLldvEEQLRF---LFHRMKDAELdvvpllrgsfsnwiwttLGIPPSsvFPS 1065
Cdd:PRK02714 29 EGIILRLTDETGKIGWGEIAPLpWFGSETL---EEALAFcqqLPGEITPEQI-----------------FSIPDA--LPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1066 VKCGLEMAILNLLESQridrsygiftgsNVVEYNqsstaNIQICALVDSCGTPMDvtlAVVKLVAEGFTTVKLKVGRrEN 1145
Cdd:PRK02714 87 CQFGFESALENESGSR------------SNVTLN-----PLSYSALLPAGEAALQ---QWQTLWQQGYRTFKWKIGV-DP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1146 PAEDAAVIQKVREIVGYKINIRADANRKWTYEQA---IDFGSRVKGLCLQYIEEP--VDSVNDIIKFCENSGLPVALDET 1220
Cdd:PRK02714 146 LEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPlpPDQFDEMLQLSQDYQTPIALDES 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1221 IDNLTGdvIPKLHQFSHPGIvaLVIKPSVVGGFETaayIAKWAHMHDKMAVISSTYESSVGLATYIQFAHYVDRqndits 1300
Cdd:PRK02714 226 VANLAQ--LQQCYQQGWRGI--FVIKPAIAGSPSR---LRQFCQQHPLDAVFSSVFETAIGRKAALALAAELSR------ 292
|
330 340
....*....|....*....|....*..
gi 1443056271 1301 riKNRgscgnvAHGLGTYQWLREDVSD 1327
Cdd:PRK02714 293 --PDR------ALGFGVTHWFSDEEED 311
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1372-1685 |
4.02e-15 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 76.19 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1372 RSYFIQVDGDNFSYQVKLQEGGdctHEKVILFLHGFLGTSEDWVPMMKALSPS-ARVIAVDLPGHGESEILQHDVEnsnq 1450
Cdd:COG2267 5 LVTLPTRDGLRLRGRRWRPAGS---PRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1451 iSFSvQSVADL--LLKLIRNITDGAVVVVGYSMGARIALHMALNQNHKVNfstlyllclflyfydsnavplrqisgAVII 1528
Cdd:COG2267 78 -SFD-DYVDDLraALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVA--------------------------GLVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1529 SGSPGLRDEaskrrrsaidrsrahflsscglenflETWYSAKMWASLRehpkfdslvrtrmkhnnikalskvladssigt 1608
Cdd:COG2267 130 LAPAYRADP--------------------------LLGPSARWLRALR-------------------------------- 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443056271 1609 qksLWEDLKHLKSPLLIVAGEKDPKF-KEISQQMCREIRKHKdresdglcEMIIIPDSGHAVHVENPLPLV-RAIRKFL 1685
Cdd:COG2267 152 ---LAEALARIDVPVLVLHGGADRVVpPEAARRLAARLSPDV--------ELVLLPGARHELLNEPAREEVlAAILAWL 219
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
1118-1327 |
4.28e-15 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 78.47 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1118 PMDVTLAVV------KLVAE--GFTTVKLKVG-RRENPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDfgsRVKG 1188
Cdd:PRK02901 80 PVNATVPAVdaaqvpEVLARfpGCRTAKVKVAePGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVA---AARA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1189 LC----LQYIEEPVDSVNDIIKFCENSGLPVALDETIDNLtgdvipklhqfSHPGIVA-------LVIKPSVVGGFETAA 1257
Cdd:PRK02901 157 LDadgpLEYVEQPCATVEELAELRRRVGVPIAADESIRRA-----------EDPLRVAragaadvAVLKVAPLGGVRAAL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1258 YIAKWAHMHdkmAVISSTYESSVGLATYIQFAHYVDRQNDitsriknrgscgnvAHGLGTYQWLREDVSD 1327
Cdd:PRK02901 226 DIAEQIGLP---VVVSSALDTSVGIAAGLALAAALPELDH--------------ACGLATGGLFEEDVAD 278
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
1398-1685 |
6.79e-14 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 73.44 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1398 EKVILFLHGFLGTSEDWVPMMKALSPS-ARVIAVDLPGHGESEilqhdvENSNQISFS--VQSVADLLLKLiRNITDgAV 1474
Cdd:COG1647 15 RKGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSP------EDLLKTTWEdwLEDVEEAYEIL-KAGYD-KV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1475 VVVGYSMGARIALHMALNqnhkvnfstlyllclflyfydsnavpLRQISGAVIIsgSPGLRdeaskrrrsaIDRSRAHFL 1554
Cdd:COG1647 87 IVIGLSMGGLLALLLAAR--------------------------YPDVAGLVLL--SPALK----------IDDPSAPLL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1555 SScgLENFLETWysaKMWASLREHPKFDSLVRTRMKHNNIKALSKVLADssigtqksLWEDLKHLKSPLLIVAGEKDPKF 1634
Cdd:COG1647 129 PL--LKYLARSL---RGIGSDIEDPEVAEYAYDRTPLRALAELQRLIRE--------VRRDLPKITAPTLIIQSRKDEVV 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1443056271 1635 K-EISQQMCREIR-KHKdresdglcEMIIIPDSGHAVHVENPLPLV-RAIRKFL 1685
Cdd:COG1647 196 PpESARYIYERLGsPDK--------ELVWLEDSGHVITLDKDREEVaEEILDFL 241
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
1401-1680 |
9.14e-13 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 69.42 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1401 ILFLHGFlgtSEDWVPMMKALSPSARVIAVDLPGHGESEILQHDVENsnqisfsVQSVADLLLKLIRnitDGAVVVVGYS 1480
Cdd:pfam12697 1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLAD-------LADLAALLDELGA---ARPVVLVGHS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1481 MGARIALHMAlnqnhkvnfstlyllclflyfydsnavPLRQISGAVIisGSPGLRDEASKRRRSAIDRSRAHFLSscgle 1560
Cdd:pfam12697 68 LGGAVALAAA---------------------------AAALVVGVLV--APLAAPPGLLAALLALLARLGAALAA----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1561 nflETWYSAKMWAslrehpkfDSLVRTRMKHNNIKALSKVLADSSIGTQKSLWEDLKHLKSPLLIVAGEkDPKFKEISQQ 1640
Cdd:pfam12697 114 ---PAWLAAESLA--------RGFLDDLPADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEE-DRLVPELAQR 181
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1443056271 1641 MCREIRKhkdresdglCEMIIIPDSGHAVHvENPLPLVRA 1680
Cdd:pfam12697 182 LLAALAG---------ARLVVLPGAGHLPL-DDPEEVAEA 211
|
|
| bchO_mg_che_rel |
TIGR03056 |
putative magnesium chelatase accessory protein; Members of this family belong to the alpha ... |
1400-1685 |
1.51e-12 |
|
putative magnesium chelatase accessory protein; Members of this family belong to the alpha/beta fold family hydrolases (pfam00561). Members are found in bacterial genomes if and only if they encoded for anoxygenic photosynthetic systems similar to that of Rhodobacter capsulatus and other alpha-Proteobacteria. Members often are encoded in the same operon as subunits of the protoporphyrin IX magnesium chelatase, and were once designated BchO. No literature supports a role as an actual subunit of magnesium chelatase, but an accessory role is possible, as suggested by placement by its probable hydrolase activity. [Energy metabolism, Photosynthesis]
Pssm-ID: 132100 Cd Length: 278 Bit Score: 69.92 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1400 VILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILQhdvensnQISFSVQSVADLLLKLIRNITDGAVVVVGY 1479
Cdd:TIGR03056 30 LLLLLHGTGASTHSWRDLMPPLARSFRVVAPDLPGHGFTRAPF-------RFRFTLPSMAEDLSALCAAEGLSPDGVIGH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1480 SMGARIALHMALNqnhkvnfstLYLLCLFLYFYDSNAVPLRQISGAVIISGSPGL-----------RDEASKRRRSAIDR 1548
Cdd:TIGR03056 103 SAGAAIALRLALD---------GPVTPRMVVGINAALMPFEGMAGTLFPYMARVLacnpftppmmsRGAADQQRVERLIR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1549 SRAHFLSSCGLenfleTWYSAKMwaslREHPKFDSLVRTrMKHNNIKALSKvladssigtqkslweDLKHLKSPLLIVAG 1628
Cdd:TIGR03056 174 DTGSLLDKAGM-----TYYGRLI----RSPAHVDGALSM-MAQWDLAPLNR---------------DLPRITIPLHLIAG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443056271 1629 EKDPKFK-EISQQMCREIRKHKDRESDGLcemiiipdsGHAVHVENPLPLVRAIRKFL 1685
Cdd:TIGR03056 229 EEDKAVPpDESKRAATRVPTATLHVVPGG---------GHLVHEEQADGVVGLILQAA 277
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1375-1497 |
1.53e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 68.05 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1375 FIQVDGDNFSYqVKLQEGGDCThekvILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEilqHDVENSNqISFS 1454
Cdd:PRK14875 113 KARIGGRTVRY-LRLGEGDGTP----VVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASS---KAVGAGS-LDEL 183
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1443056271 1455 VQSVADLLLKLirNItdGAVVVVGYSMGARIALHMALNQNHKV 1497
Cdd:PRK14875 184 AAAVLAFLDAL--GI--ERAHLVGHSMGGAVALRLAARAPQRV 222
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
1129-1205 |
1.99e-09 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 61.59 E-value: 1.99e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443056271 1129 VAEGFTTVKLKVGRreNPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPVdSVNDII 1205
Cdd:cd03324 208 LAQGFTHFKLKVGA--DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPT-SPDDIL 281
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
1400-1497 |
4.33e-08 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 55.30 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1400 VILFLHGFLGTSEDWVPMMKALS-PSARVIAVD---LPGHGE----SEILQHDVENSNQISFSVQSVADLLLKLI--RNI 1469
Cdd:COG0400 7 LVVLLHGYGGDEEDLLPLAPELAlPGAAVLAPRapvPEGPGGrawfDLSFLEGREDEEGLAAAAEALAAFIDELEarYGI 86
|
90 100
....*....|....*....|....*...
gi 1443056271 1470 TDGAVVVVGYSMGARIALHMALNQNHKV 1497
Cdd:COG0400 87 DPERIVLAGFSQGAAMALSLALRRPELL 114
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
1399-1497 |
4.47e-08 |
|
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273783 [Multi-domain] Cd Length: 245 Bit Score: 55.98 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1399 KVILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESeilqhdvenSNQISFSVQSVADLLLKLirniTDGAVVVVG 1478
Cdd:TIGR01738 5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRS---------RGFGPLSLADMAEAIAAQ----APDPAIWLG 71
|
90
....*....|....*....
gi 1443056271 1479 YSMGARIALHMALNQNHKV 1497
Cdd:TIGR01738 72 WSLGGLVALHIAATHPDRV 90
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
1067-1289 |
5.35e-08 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 56.94 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1067 KCGLEMAILNLLEsQRIDRSYGIFTGSNVVEynqsstaNIQICALVDSCGTPMDVTLAVVKLVAEGFTTVKLKVGRREnP 1146
Cdd:cd03318 101 KAAIEMALLDAQG-RRLGLPVSELLGGRVRD-------SLPVAWTLASGDTERDIAEAEEMLEAGRHRRFKLKMGARP-P 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1147 AEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV--DSVNDIIKFCENSGLPVALDETIDNL 1224
Cdd:cd03318 172 ADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVprENLDGLARLRSRNRVPIMADESVSGP 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443056271 1225 TgDVIpklhQFSHPGIVALV-IKPSVVGGFETAAYIAKWAHMHDKMAVISSTYESSVGLATYIQFA 1289
Cdd:cd03318 252 A-DAF----ELARRGAADVFsLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLF 312
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
1400-1687 |
5.80e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 55.41 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1400 VILFLHGFLGTSED-WVPMMKALspsAR----VIAVDLPGHGESE--ILQHDVENsnqisfsVQSVADLLLKliRNITDG 1472
Cdd:COG1506 25 VVVYVHGGPGSRDDsFLPLAQAL---ASrgyaVLAPDYRGYGESAgdWGGDEVDD-------VLAAIDYLAA--RPYVDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1473 A-VVVVGYSMGARIALHMALNQNhkvnfstlyllclflyfydsnavplRQISGAVIISGSPGLRDEASKRRrsaidrsra 1551
Cdd:COG1506 93 DrIGIYGHSYGGYMALLAAARHP-------------------------DRFKAAVALAGVSDLRSYYGTTR--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1552 hflsscglenfletWYSAKMWASLREHPKFdslvrtRMKHNNIKALSKvladssigtqkslwedlkhLKSPLLIVAGEKD 1631
Cdd:COG1506 139 --------------EYTERLMGGPWEDPEA------YAARSPLAYADK-------------------LKTPLLLIHGEAD 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1443056271 1632 P--KFKEiSQQMCREIRKHKDResdglCEMIIIPDSGHAVHVENPLPLVRAIRKFLVR 1687
Cdd:COG1506 180 DrvPPEQ-AERLYEALKKAGKP-----VELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1126-1198 |
2.82e-07 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 54.80 E-value: 2.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443056271 1126 VKLVAEGFTTVKLKVGRrENPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV 1198
Cdd:cd03321 150 VTAAEEGFHAVKTKIGY-PTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPT 221
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
1129-1200 |
3.37e-07 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 54.34 E-value: 3.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443056271 1129 VAEGFTTVKLKVGRreNPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPVDS 1200
Cdd:cd03328 150 VAQGIPRVKMKIGR--DPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSS 219
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1401-1499 |
3.57e-07 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 52.78 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1401 ILF-LHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILQHDVEnsnqisfsvqSVADLLLKLIRNI-TDGAVVVVG 1478
Cdd:pfam00975 2 PLFcFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIE----------ALADEYAEALRQIqPEGPYALFG 71
|
90 100
....*....|....*....|....
gi 1443056271 1479 YSMGARIALHMAL---NQNHKVNF 1499
Cdd:pfam00975 72 HSMGGMLAFEVARrleRQGEAVRS 95
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1416-1491 |
9.02e-07 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 51.78 E-value: 9.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443056271 1416 PMMKALSPSARVIAVDLPGHGE--SEILQHDVEnsnqisfsvqSVADLLLKLIRNITDGAVVVVGYSMGARIALHMAL 1491
Cdd:COG3208 24 PWAAALPPDIEVLAVQLPGRGDrlGEPPLTSLE----------ELADDLAEELAPLLDRPFALFGHSMGALLAFELAR 91
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1387-1499 |
5.79e-06 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 51.24 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1387 VKLQEGGDctheKVILFL-HGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILQHDVEnsnqisfsvqSVADLLLKL 1465
Cdd:COG3319 593 VPLRAGGS----GPPLFCvHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPASVE----------EMAARYVEA 658
|
90 100 110
....*....|....*....|....*....|....*...
gi 1443056271 1466 IRNIT-DGAVVVVGYSMGARIALHMA---LNQNHKVNF 1499
Cdd:COG3319 659 IRAVQpEGPYHLLGWSFGGLVAYEMArqlEAQGEEVAL 696
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
375-534 |
7.55e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 50.86 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 375 ASFIVEEFVRLGFTYFCIAPGSRSSPL--ALSASV---HPLTTciscyDERSLGFHALGYGRGSRKPAIVITSSGTAVSN 449
Cdd:PRK08155 16 AELIVRLLERQGIRIVTGIPGGAILPLydALSQSTqirHILAR-----HEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 450 LLPSVVEASQDFVPLILLTADRPPELqdVGANqAINQVNHFGsfvrhfFSLPPPDDHIYARMV--LTTVDSAAY-YAMQA 526
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQVPASM--IGTD-AFQEVDTYG------ISIPITKHNYLVRDIeeLPQVISDAFrIAQSG 161
|
....*...
gi 1443056271 527 PQGPVHIN 534
Cdd:PRK08155 162 RPGPVWID 169
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
1401-1488 |
7.68e-06 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 46.36 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1401 ILFLHGFLGTSEDWVPMMKAL-SPSARVIAVDLPGHgeseilqhdvensnqiSFSVQSVADLLLKLIRNI--TDGA--VV 1475
Cdd:COG1075 8 VVLVHGLGGSAASWAPLAPRLrAAGYPVYALNYPST----------------NGSIEDSAEQLAAFVDAVlaATGAekVD 71
|
90
....*....|....*.
gi 1443056271 1476 VVGYSMG---ARIALH 1488
Cdd:COG1075 72 LVGHSMGglvARYYLK 87
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
1399-1687 |
8.06e-06 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 49.14 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1399 KVILFLHGFLGTSEDWVPMMKALspsAR----VIAVDLPGHGESE--------ILQHDVENsnqisfsvqsVADLLLKLi 1466
Cdd:COG1073 38 PAVVVAHGNGGVKEQRALYAQRL---AElgfnVLAFDYRGYGESEgepreegsPERRDARA----------AVDYLRTL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1467 RNITDGAVVVVGYSMGARIALHMALNqnhkvnfstlyllclflyfydsnavpLRQISGAVIISGSPGLRDEASKRRRSAi 1546
Cdd:COG1073 104 PGVDPERIGLLGISLGGGYALNAAAT--------------------------DPRVKAVILDSPFTSLEDLAAQRAKEA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1547 drsrahflsscglenfletwYSAKM-WASLREHPKFDSLVRTRMkhNNIKAlskvladssigtqkslwedLKHLKSPLLI 1625
Cdd:COG1073 157 --------------------RGAYLpGVPYLPNVRLASLLNDEF--DPLAK-------------------IEKISRPLLF 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443056271 1626 VAGEKDPKfkeISQQMCREI--RKHKDResdglcEMIIIPDSGHA-VHVENPLPLVRAIRKFLVR 1687
Cdd:COG1073 196 IHGEKDEA---VPFYMSEDLyeAAAEPK------ELLIVPGAGHVdLYDRPEEEYFDKLAEFFKK 251
|
|
| Pancreat_lipase_like |
cd00707 |
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain ... |
1396-1498 |
2.08e-05 |
|
Pancreatic lipase-like enzymes. Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.
Pssm-ID: 238363 [Multi-domain] Cd Length: 275 Bit Score: 48.39 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1396 THEKVILFLHGFLGTSED-WV-PMMKAL--SPSARVIAVD-LPGhgeSEILQHD-VENSNQISfsvQSVADLLLKLIRNI 1469
Cdd:cd00707 34 PSRPTRFIIHGWTSSGEEsWIsDLRKAYlsRGDYNVIVVDwGRG---ANPNYPQaVNNTRVVG---AELAKFLDFLVDNT 107
|
90 100 110
....*....|....*....|....*....|...
gi 1443056271 1470 tdGA----VVVVGYSMGARIALHMALNQNHKVN 1498
Cdd:cd00707 108 --GLslenVHLIGHSLGAHVAGFAGKRLNGKLG 138
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
1124-1216 |
2.41e-05 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 48.86 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1124 AVVKLvAE------GFTTVKLKVGRREnPAEDAAVIQKVRE-IVGYKIniRADANRKWTYEQAIDFGSRVKGLcLQYIEE 1196
Cdd:cd03323 171 GVVRL-ARaaidryGFKSFKLKGGVLP-GEEEIEAVKALAEaFPGARL--RLDPNGAWSLETAIRLAKELEGV-LAYLED 245
|
90 100
....*....|....*....|
gi 1443056271 1197 PVDSVNDIIKFCENSGLPVA 1216
Cdd:cd03323 246 PCGGREGMAEFRRATGLPLA 265
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
372-740 |
3.80e-05 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 48.37 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 372 LAWASFIVEEFVRLGFTYFCIAPGSrsSPLALSASVHPLTTC--ISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSN 449
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGG--SVLDIYDAIHTLGGIehVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 450 LLPSVVEASQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDhiyarmVLTTVDSAAYYAMQAPQG 529
Cdd:PRK06882 82 AITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAED------IPSTIKKAFYIASTGRPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 530 PVHIncafrepldygyqDWSVDCLKGLDKWFINrepYTRYLGMKMVS-ALGNYSCSVREVLEIVKNANQGLLLV-GAIHT 607
Cdd:PRK06882 156 PVVI-------------DIPKDMVNPANKFTYE---YPEEVSLRSYNpTVQGHKGQIKKALKALLVAKKPVLFVgGGVIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 608 EDDIWAVTLLARHLSWPIAADvLSGLrmrkvqKSIPGLDKSicFIDHIDQILLSESVKSWKTPDVIVQIGSRITSKRVGT 687
Cdd:PRK06882 220 AECSEQLTQFAQKLNLPVTSS-LMGL------GAYPSTDKQ--FLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNN 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 688 YLESCSPSSYILIDAHPC---RHDPSHV-VTHRIQATITEFAASLCQCNF---QTKTSRW 740
Cdd:PRK06882 291 LAKYCPNAKVIHIDIDPTsisKNVPAYIpIVGSAKNVLEEFLSLLEEENLaksQTDLTAW 350
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
372-534 |
7.23e-05 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 47.51 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 372 LAWASFIVEEFVRLGFTYFCIAPGSrsSPLALSASVHPLTTC--ISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSN 449
Cdd:PRK08979 4 LSGASMIVRSLIDEGVKHIFGYPGG--SVLDIYDALHEKSGIehILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 450 LLPSVVEASQDFVPLILLTADRPPELQDVGANQAINQVNHFGSFVRHFFSLPPPDDhiyarmVLTTVDSAAYYAMQAPQG 529
Cdd:PRK08979 82 TITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAED------IPEIIKKAFYIASTGRPG 155
|
....*
gi 1443056271 530 PVHIN 534
Cdd:PRK08979 156 PVVID 160
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
375-472 |
3.03e-04 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 45.50 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 375 ASFIVEEFVRLGFTYFCIAPGSRSSPLALSASVHPLTTCISCYDERSLGFHALGYGRGSRKPAIVITSSGTAVSNLLPSV 454
Cdd:PLN02470 16 ADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGL 95
|
90
....*....|....*...
gi 1443056271 455 VEASQDFVPLILLTADRP 472
Cdd:PLN02470 96 ADALLDSVPLVAITGQVP 113
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
832-889 |
3.52e-04 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 42.57 E-value: 3.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443056271 832 SGIDGLLSTSIGFAIG-----SNKHVFCVIGDISFLHDTNGLSLLNQRtqRKPMTVIVINNHG 889
Cdd:pfam02775 24 SGGLGTMGYGLPAAIGaklarPDRPVVAIAGDGGFQMNLQELATAVRY--NLPITVVVLNNGG 84
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
1126-1271 |
4.44e-04 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239443 [Multi-domain] Cd Length: 341 Bit Score: 44.63 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1126 VKLVAEGFTTVKLKVGrrENPAEDAAVIQK-------VREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPV 1198
Cdd:cd03327 129 KEYLKEGYRGMKMRFG--YGPSDGHAGLRKnvelvraIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1199 --DSVNDIIKFCENSGLPVALDEtidnltgdvipklHQFSHPGIVAL-------VIKPSV--VGGFETAAYIAKWAHMHD 1267
Cdd:cd03327 207 ipDDIEGYAELKKATGIPISTGE-------------HEYTVYGFKRLlegravdILQPDVnwVGGITELKKIAALAEAYG 273
|
....
gi 1443056271 1268 KMAV 1271
Cdd:cd03327 274 VPVV 277
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
1375-1497 |
5.27e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 43.83 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1375 FIQVDGDNFSYqVKLQEGgdctheKVILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEILqhdvensnQISFS 1454
Cdd:PRK03592 11 RVEVLGSRMAY-IETGEG------DPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKP--------DIDYT 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1443056271 1455 VQSVADLLLKLI--RNITDgaVVVVGYSMGARIALHMALNQNHKV 1497
Cdd:PRK03592 76 FADHARYLDAWFdaLGLDD--VVLVGHDWGSALGFDWAARHPDRV 118
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
815-887 |
1.12e-03 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 41.88 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 815 HHFPG-----FLGApvagNRGASGIDGLLS--TSIGFAIG-----SNKHVFCVIGDISFLHdtNGLS-LLNQRTQRKPMT 881
Cdd:cd02008 27 SIVSGdigcyTLGA----LPPLNAIDTCTCmgASIGVAIGmakasEDKKVVAVIGDSTFFH--SGILgLINAVYNKANIT 100
|
....*.
gi 1443056271 882 VIVINN 887
Cdd:cd02008 101 VVILDN 106
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
770-892 |
1.30e-03 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 41.47 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 770 VAHVIGEALYGDATMFIGnsmvirdldmfgkgwidhSTNANNAMMHHFPgflgAPVAGNRGASGIDGLLSTSIGFAIGS- 848
Cdd:cd00568 2 VLAALRAALPEDAIVVND------------------AGNSAYWAYRYLP----LRRGRRFLTSTGFGAMGYGLPAAIGAa 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1443056271 849 ----NKHVFCVIGDISFLHdtNGLSLLNQRTQRKPMTVIVINNHG-GAI 892
Cdd:cd00568 60 laapDRPVVCIAGDGGFMM--TGQELATAVRYGLPVIVVVFNNGGyGTI 106
|
|
| Abhydrolase_2 |
pfam02230 |
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ... |
1397-1496 |
1.50e-03 |
|
Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.
Pssm-ID: 396693 [Multi-domain] Cd Length: 217 Bit Score: 41.98 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1397 HEKVILFLHGfLGTS--------EDWVPM--MKALSPSARVIAVDLPGHGESEI---LQHDVENSNQISFSVQSVADLLL 1463
Cdd:pfam02230 13 AQATVIFLHG-LGDSghgwadaaKTEAPLpnIKFIFPHGPEIPVTLNGGMRMPAwfdLVGLSPNAKEDEAGIKNSAETIE 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 1443056271 1464 KLIRN-----ITDGAVVVVGYSMGARIALHMALNQNHK 1496
Cdd:pfam02230 92 ELIDAeqkkgIPSSRIIIGGFSQGAMLALYSALTLPLP 129
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
832-889 |
1.56e-03 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 41.36 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443056271 832 SGIDGLLSTSIGFAIGS-----NKHVFCVIGDISFlhdtnGLSLLNQRT---QRKPMTVIVINNHG 889
Cdd:cd02004 44 AGTFGTLGVGLGYAIAAalarpDKRVVLVEGDGAF-----GFSGMELETavrYNLPIVVVVGNNGG 104
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
375-468 |
1.63e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 43.03 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 375 ASFIVEEFVRLGFTYFCIAPGSRSSPL--ALSAS--VHPLTTciscyDERSLGFHALGYGRGSRKPAIVITSSGTAVSNL 450
Cdd:PRK06725 18 AGHVIQCLKKLGVTTVFGYPGGAILPVydALYESglKHILTR-----HEQAAIHAAEGYARASGKVGVVFATSGPGATNL 92
|
90
....*....|....*...
gi 1443056271 451 LPSVVEASQDFVPLILLT 468
Cdd:PRK06725 93 VTGLADAYMDSIPLVVIT 110
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
1397-1672 |
1.72e-03 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 41.82 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1397 HEKVILFLHGFLGTSEDWVPMMKALS-PSARVIAVDLPGHGESEILQHDVEnsnqiSFSvQSVADL--LLKLIRNITDGA 1473
Cdd:pfam12146 3 PRAVVVLVHGLGEHSGRYAHLADALAaQGFAVYAYDHRGHGRSDGKRGHVP-----SFD-DYVDDLdtFVDKIREEHPGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1474 -VVVVGYSMGARIALHMALNQNHKVNfstlyllclflyfydsnavplrqisgAVIISgSPGLRDEASKRRRsaIDRSRAH 1552
Cdd:pfam12146 77 pLFLLGHSMGGLIAALYALRYPDKVD--------------------------GLILS-APALKIKPYLAPP--ILKLLAK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1553 FLSSCgLENFLETWYSAKMWAS-----LREHPKfDSLVRTRMKHNnikalskvLADSSIGTQKSLWEDLKHLKSPLLIVA 1627
Cdd:pfam12146 128 LLGKL-FPRLRVPNNLLPDSLSrdpevVAAYAA-DPLVHGGISAR--------TLYELLDAGERLLRRAAAITVPLLLLH 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1628 GEKDPkfkeI-----SQQMCREIrKHKDresdglCEMIIIPDSGHAVHVE 1672
Cdd:pfam12146 198 GGADR----VvdpagSREFYERA-GSTD------KTLKLYPGLYHELLNE 236
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
1381-1497 |
2.05e-03 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 41.93 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1381 DNFSYQVKLQegGDCThekvILFLHGFLGTSEDWVPMMKALSPSARVIAVDLPGHGESEilqhdvensnqiSFSVQSVAD 1460
Cdd:PRK10349 2 NNIWWQTKGQ--GNVH----LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR------------GFGALSLAD 63
|
90 100 110
....*....|....*....|....*....|....*..
gi 1443056271 1461 LLLKLIRNITDGAvVVVGYSMGARIALHMALNQNHKV 1497
Cdd:PRK10349 64 MAEAVLQQAPDKA-IWLGWSLGGLVASQIALTHPERV 99
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
375-541 |
2.87e-03 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 42.29 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 375 ASFIVEEFVRLGFTYFCIAPGSRSSPL-----ALSASVHPLTTCISCYDErSLGFH-ALGYGRGSRKPAIVI--TSSGTA 446
Cdd:PRK08327 10 AELFLELLKELGVDYIFINSGTDYPPIieakaRARAAGRPLPEFVICPHE-IVAISmAHGYALVTGKPQAVMvhVDVGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 447 vsNLLPSVVEASQDFVPLiLLTADRPPELQDvGANQAINQVNHF-------GSFVRHF----FSLPppddhiYARMVLTT 515
Cdd:PRK08327 89 --NALGGVHNAARSRIPV-LVFAGRSPYTEE-GELGSRNTRIHWtqemrdqGGLVREYvkwdYEIR------RGDQIGEV 158
|
170 180
....*....|....*....|....*.
gi 1443056271 516 VDSAAYYAMQAPQGPVHINCAfREPL 541
Cdd:PRK08327 159 VARAIQIAMSEPKGPVYLTLP-REVL 183
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
1400-1492 |
4.85e-03 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 40.99 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1400 VILFLHGFLGTSEDWVPMMKA------------LSPsarVIAVDLPGHGESEILQHDVENSNQISFsvqsVADLLLKLIR 1467
Cdd:COG2382 114 VLYLLDGGGGDEQDWFDQGRLptildnliaagkIPP---MIVVMPDGGDGGDRGTEGPGNDAFERF----LAEELIPFVE 186
|
90 100 110
....*....|....*....|....*....|
gi 1443056271 1468 N----ITDGA-VVVVGYSMGARIALHMALN 1492
Cdd:COG2382 187 KnyrvSADPEhRAIAGLSMGGLAALYAALR 216
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
1129-1199 |
5.07e-03 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239442 [Multi-domain] Cd Length: 385 Bit Score: 41.23 E-value: 5.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443056271 1129 VAEGFTTVKLKVGRrENPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPVD 1199
Cdd:cd03326 172 LDRGYTVVKIKIGG-APLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGD 241
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
1400-1490 |
5.51e-03 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 40.33 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1400 VILFLHGFLGTSEDWVPMMKALspsAR----VIAVDLPGHGESEILQHDVENSNQISFSVQSVADLL-----LKLIRNIT 1470
Cdd:COG0412 31 GVVVLHEIFGLNPHIRDVARRL---AAagyvVLAPDLYGRGGPGDDPDEARALMGALDPELLAADLRaaldwLKAQPEVD 107
|
90 100
....*....|....*....|
gi 1443056271 1471 DGAVVVVGYSMGARIALHMA 1490
Cdd:COG0412 108 AGRVGVVGFCFGGGLALLAA 127
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
1127-1222 |
5.73e-03 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 40.84 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1127 KLVAEGFTTVKLKVGRRENPAEDAAVIQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKGLCLQYIEEPVD--SVNDI 1204
Cdd:cd03329 153 ECKALGYRAIKLHPWGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLReaSISSY 232
|
90
....*....|....*...
gi 1443056271 1205 IKFCENSGLPVALDETID 1222
Cdd:cd03329 233 RWLAEKLDIPILGTEHSR 250
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
426-533 |
6.01e-03 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 41.13 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 426 ALGYGRGSRKPAIVITSSGTAVSNLLPSVVEASQDFVPLILLTA--DRPPELQDVGA-NQAINQVNHFGSFVRHFFSLPP 502
Cdd:PRK07064 57 ADAHARVSGGLGVALTSTGTGAGNAAGALVEALTAGTPLLHITGqiETPYLDQDLGYiHEAPDQLTMLRAVSKAAFRVRS 136
|
90 100 110
....*....|....*....|....*....|.
gi 1443056271 503 PDDhiyarmVLTTVDSAAYYAMQAPQGPVHI 533
Cdd:PRK07064 137 AET------ALATIREAVRVALTAPTGPVSV 161
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
1116-1219 |
7.61e-03 |
|
D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239441 [Multi-domain] Cd Length: 352 Bit Score: 40.39 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443056271 1116 GTPMDVTLAVVKLVAEGFTTVKL----KVGRRENPAE-DAAV--IQKVREIVGYKINIRADANRKWTYEQAIDFGSRVKG 1188
Cdd:cd03325 122 DRPSDVAEAARARREAGFTAVKMnateELQWIDTSKKvDAAVerVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEP 201
|
90 100 110
....*....|....*....|....*....|...
gi 1443056271 1189 LCLQYIEEPV--DSVNDIIKFCENSGLPVALDE 1219
Cdd:cd03325 202 YRLLFIEEPVlpENVEALAEIAARTTIPIATGE 234
|
|
| |
