|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-517 |
1.57e-111 |
|
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: 341.75 E-value: 1.57e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:COG0028 61 ARATGKPGVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDvlypyfmVQKEMVPAKPPKGLVGRVvswylenylanlfagawepQPEgplpldiPQA 161
Cdd:COG0028 141 LRRAFRIATSGRPGPVVLDIPKD-------VQAAEAEEEPAPPELRGY-------------------RPR-------PAP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLtPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAAL 234
Cdd:COG0028 188 DPEAIEEAAELLAAAKRPVILAGGGARR-AGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREEMLLNsdifWKPQEAVQGDVGSFVLKLVEGLQGQTWA-PDWV 312
Cdd:COG0028 267 AEADLVLAVGARFDDRVTGNwDEFAPDAKIIHIDIDPAEIGKN----YPVDLPIVGDAKAVLAALLEALEPRADDrAAWL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 313 EELREADRQKEQTFREKAAmpvaqHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVG 392
Cdd:COG0028 343 ARIAAWRAEYLAAYAADDG-----PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACGLAYTDYHKA 471
Cdd:COG0028 418 LPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKL 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 768000693 472 AMGLGARGLLLsrENEDQVVKVLHDAQQQcrdGHPVVVNILIGRTD 517
Cdd:COG0028 498 AEAFGAKGERV--ETPEELEAALEEALAS---DGPALIDVRVDPEE 538
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
2-512 |
2.60e-89 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 284.31 E-value: 2.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK05858 62 AKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPyfMVQKEMVPAKPPkglvgrvvswylenylanlfagawePQPEGPLPldipqa 161
Cdd:PRK05858 142 VDQALQAAVTPHRGPVFVDFPMDHAFS--MADDDGRPGALT-------------------------ELPAGPTP------ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSAdKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIV 241
Cdd:PRK05858 189 DPDALARAAGLLAEAQRPVIMAGTDVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 242 LAGTVCDFRLSYGRVLSHSSKIIIVnrnREEMLLNSDIfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREAD-- 319
Cdd:PRK05858 268 VVGVPMDFRLGFGVFGGTAQLVHVD---DAPPQRAHHR--PVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAEta 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 320 -RQKEQTFREKAAMPvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALG 398
Cdd:PRK05858 343 aRARDAAELADDRDP----IHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 399 AKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWtqiSREQVPS---LGSNVACGLA-YTDYHKAAMG 474
Cdd:PRK05858 419 ARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRA 495
|
490 500 510
....*....|....*....|....*....|....*....
gi 768000693 475 LGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNIL 512
Cdd:PRK05858 496 LGGHGELVTVPAE------LGPALERAFAsGVPYLVNVL 528
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
340-513 |
1.27e-70 |
|
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: 223.18 E-value: 1.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 340 PVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPS--LGSNVACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSygLGLPVTTLLPDTRYDLVAEAFGGKGELV--TTPEELKPALKRA 158
|
170
....*....|....*.
gi 768000693 498 QQQcrdGHPVVVNILI 513
Cdd:cd02004 159 LAS---GKPALINVII 171
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
4-461 |
1.06e-50 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 182.49 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 4 LSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTL---LQnRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK09259 69 LTQKPGVCLTVSAPGFLNGLTALANATTNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVLypyfmvQKEMVPAKPPKGLVgRVVSwylenylanlfagawepqpegPLPLDIPq 160
Cdd:PRK09259 148 GVARAIRTAVSGRPGGVYLDLPAKVL------AQTMDADEALTSLV-KVVD---------------------PAPAQLP- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 161 aSPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVI 240
Cdd:PRK09259 199 -APEAVDRALDLLKKAKRPLIILGKGAAYAQADEQ-IREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 241 VLAGTVCDFRLSYGR--VLSHSSKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQTWAP--DWVEELR 316
Cdd:PRK09259 277 LLVGARLNWLLSHGKgkTWGADKKFIQIDIEPQEIDSNRPI----AAPVVGDIGSVMQALLAGLKQNTFKApaEWLDALA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 317 EADRQKEQTFREK--AAMPVAQHLNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAG 394
Cdd:PRK09259 353 ERKEKNAAKMAEKlsTDTQPMNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMG 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000693 395 FALGAKLC--RPdaeVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGwtqISR--EQVPSLGSNVAC 461
Cdd:PRK09259 432 YAIAAAVEtgKP---VVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSP 496
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
2-477 |
2.51e-47 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 172.47 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGG--AASTLLQNRGALQAV-DQLSLFRPLCKFCVSVRRVRDI 78
Cdd:PRK07524 59 ARVSGKPGVCFIITGPGMTNIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 79 VPTLRAAMAAAQSGTPGPVFVELPVDVlypyfMVQKEMVPAKPPKGLVGRvvswylenylanlfagawepqpegplpldi 158
Cdd:PRK07524 139 PEVLARAFAVFDSARPRPVHIEIPLDV-----LAAPADHLLPAPPTRPAR------------------------------ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRS-----AA 233
Cdd:PRK07524 184 PGPAPAALAQAAERLAAARRPLILAGGGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 LKKADVIVLAGTV---CDFRLSY-GRVLSHSSKIII------VNRNREemllnsdifwkPQEAVQGDVGSFVLKLVEGLQ 303
Cdd:PRK07524 261 IAEADVVLAVGTElgeTDYDVYFdGGFPLPGELIRIdidpdqLARNYP-----------PALALVGDARAALEALLARLP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 304 GQTWAPDWVEELREADRQKEqtfREKAAMPVAQHlnpVQVLQLVEETLPDNsILVVDGGDFVGTAAHLVQPRGPLRWLD- 382
Cdd:PRK07524 330 GQAAAADWGAARVAALRQAL---RAEWDPLTAAQ---VALLDTILAALPDA-IFVGDSTQPVYAGNLYFDADAPRRWFNa 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACG 462
Cdd:PRK07524 403 STGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVD 482
|
490
....*....|....*
gi 768000693 463 LAYTDYHKAAMGLGA 477
Cdd:PRK07524 483 PYTPDFIALARAFGC 497
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
2-513 |
8.73e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 169.16 E-value: 8.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06276 58 ARASGKVGVCVATSGPGATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPkglvgrvvswyLENYLANLFagawepqpegplpldipqA 161
Cdd:PRK06276 138 FRAAFEIAKTGRPGPVHIDLPKDVQEGELDLEKYPIPAKID-----------LPGYKPTTF------------------G 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAAL 234
Cdd:PRK06276 189 HPLQIKKAAELIAEAERPVILAGGGVIISGASEE-LIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGtvCDF--RLSyGRVLSHS--SKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQTWAPD 310
Cdd:PRK06276 268 TESDVLIAIG--CRFsdRTT-GDISSFApnAKIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 311 --WVEELREadrqkeqtfREKAAMPVA----QHLNPVQVLQLVEETLPD-----NSILVVDGGDFVGTAAHLVQPRGPLR 379
Cdd:PRK06276 341 seWLERVKK---------LKKESIPRMdfddKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHFFKTSAPRS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV------GNDAGWTQI---SRE 450
Cdd:PRK06276 412 FISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIfdnrtlGMVYQWQNLyygKRQ 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000693 451 QVPSLGSNvacglayTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAqqqCRDGHPVVVNILI 513
Cdd:PRK06276 492 SEVHLGET-------PDFVKLAESYGVKADRV--EKPDEIKEALKEA---IKSGEPYLLDIII 542
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
2-515 |
9.08e-45 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 166.33 E-value: 9.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK07525 63 TRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTpGPVFVELPVDvlYPYFMVQKEMvpakppkglvgrvvswylenylanlfagawePQPegpLPLDIPQA 161
Cdd:PRK07525 143 LNRVFDKAKRES-GPAQINIPRD--YFYGVIDVEI-------------------------------PQP---VRLERGAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLH---IRENRSAA----L 234
Cdd:PRK07525 186 GEQSLAEAAELLSEAKFPVILSGAGVVLS-DAIEECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTvcdfRLSYGRVLSH--------SSKIIIVNRNREEMLLNsdifwKPQE-AVQGDVGSFVLKLVEGLQGQ 305
Cdd:PRK07525 265 AKADVVLALGT----RLNPFGTLPQygidywpkDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVARELLARLAER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 306 TWAP---------------DWVEELREADRQKEQ---TFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGT 367
Cdd:PRK07525 336 LAGDagreerkaliaaeksAWEQELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 368 AAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQI 447
Cdd:PRK07525 416 ANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAE 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 448 SREQVPSLGSN-VACGL-AYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 515
Cdd:PRK07525 496 KKNQVDFYNNRfVGTELdNNVSYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
2-441 |
2.48e-43 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 161.81 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK08527 61 ARASGKVGVAIVTSGPGFTNAVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDV-------LYPyfmVQKEMVPAKPpkglvgrvvswyleNYLANlfagawepqpegpl 154
Cdd:PRK08527 141 LKEAFYIARSGRPGPVHIDIPKDVtatlgefEYP---KEISLKTYKP--------------TYKGN-------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 155 pldipqasPQQVQRCVEILSRAKRPLMVLGSQALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIR 227
Cdd:PRK08527 190 --------SRQIKKAAEAIKEAKKPLFYLGGGAILS-NASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 228 ENRSAALKKADVIVLAGTVCDFRLSyGRV--LSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQ 303
Cdd:PRK08527 261 YAANMAMSECDLLISLGARFDDRVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 304 G---QTWAPdWVEELREADRQKEQTFREKAAMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRW 380
Cdd:PRK08527 334 EenpTTYKE-WREILKRYNELHPLSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQL 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000693 381 LDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK08527 408 ATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-479 |
1.91e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 159.22 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MA----RLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVr 76
Cdd:PRK08322 53 MAatygRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 77 DIVPTL-RAAMAAAQSGTPGPVFVELPVDVlypyfmvqkemvpakppkglvgrvvswylenylanlfagAWEPQPEGPLP 155
Cdd:PRK08322 132 DNIPEVvREAFRLAEEERPGAVHLELPEDI---------------------------------------AAEETDGKPLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 156 LD---IPQASPQQVQRCVEILSRAKRPLMVLGSQAlLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHP-------LH 225
Cdd:PRK08322 173 RSysrRPYASPKAIERAAEAIQAAKNPLILIGAGA-NRKTASKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 226 IRENRSAALKKADVIVLAG-TVCDFrlSYGRVLSHSSKIII-VNRNREEMllnsDIFWKPQEAVQGDVGSFVLKLVEGL- 302
Cdd:PRK08322 252 QGDYVHCAIEHADLIINVGhDVIEK--PPFFMNPNGDKKVIhINFLPAEV----DPVYFPQVEVVGDIANSLWQLKERLa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 303 QGQTWAPDWVEELREADRQKEQTFREKAAMPVAqhlnPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLD 382
Cdd:PRK08322 326 DQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK----PQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNvaCG 462
Cdd:PRK08322 402 DNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFED--FG 479
|
490
....*....|....*....
gi 768000693 463 LAYT--DYHKAAMGLGARG 479
Cdd:PRK08322 480 LDFGnpDFVKYAESYGAKG 498
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-515 |
1.42e-40 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 154.16 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06048 65 ARATGKVGVCVATSGPGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVlypyfmVQKEMVPAKPPKglvgrvVSwyLENYlanlfagawEPQPEGplpldipqa 161
Cdd:PRK06048 145 IKEAFHIASTGRPGPVLIDLPKDV------TTAEIDFDYPDK------VE--LRGY---------KPTYKG--------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAvETLGVPCFLGGMARGLLGRNHPLHI-------RENRSAAL 234
Cdd:PRK06048 193 NPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELA-ETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTVCDFRLSyGRVLSHS--SKIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKLVEGLQGQTWAPdWV 312
Cdd:PRK06048 272 QESDLIIAVGARFDDRVT-GKLASFApnAKIIHIDIDPAEISKNV----KVDVPIVGDAKQVLKSLIKYVQYCDRKE-WL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 313 EELREADRQKEQTFREKAAMpvaqhLNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVG 392
Cdd:PRK06048 346 DKINQWKKEYPLKYKEREDV-----IKPQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA------GWTQISREQVPSlgsnVACGLAYT 466
Cdd:PRK06048 420 FPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDKRYS----HTCIKGSV 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 768000693 467 DYHKAAMGLGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNILIGR 515
Cdd:PRK06048 496 DFVKLAEAYGALGLRVEKPSE------VRPAIEEAVAsDRPVVIDFIVEC 539
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-480 |
1.90e-40 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 153.97 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06725 72 ARASGKVGVVFATSGPGATNLVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDvlypyfmVQKEmvpakppkglvgRVVSWYLEnylaNLFAGAWEPQpegplpldiPQA 161
Cdd:PRK06725 152 VQEAFYIAESGRPGPVLIDIPKD-------VQNE------------KVTSFYNE----VVEIPGYKPE---------PRP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAAL 234
Cdd:PRK06725 200 DSMKLREVAKAISKAKRPLLYIGG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTVCDFRLSyGRV--LSHSSKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSfVLKLVEGLQGQTWAPDWV 312
Cdd:PRK06725 279 TECDLLLALGVRFDDRVT-GKLelFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKK-ALHMLLHMSIHTQTDEWL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 313 EELREADRQKEQTFREKAAMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVG 392
Cdd:PRK06725 353 QKVKTWKEEYPLSYKQKESE-----LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA------GWTQI---SREQVPSLGSnvacgl 463
Cdd:PRK06725 428 FPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS------ 501
|
490
....*....|....*..
gi 768000693 464 ayTDYHKAAMGLGARGL 480
Cdd:PRK06725 502 --PDFVKVAEAYGVKGL 516
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
2-479 |
5.07e-38 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 146.69 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGG--AASTLLQNRGALQAV-DQLSLFRPLCKFCVSVRRVRDI 78
Cdd:PRK08266 63 ARSTGRPGVCSVVPGPGVLNAGAALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 79 VPTLRAAMAAAQSGTPGPVFVELPVDVLypyfmvqkemvpakppkGLVGRVvswylenylanlfagawEPQPEGPlPLDI 158
Cdd:PRK08266 143 PALVAEAFQQMLSGRPRPVALEMPWDVF-----------------GQRAPV-----------------AAAPPLR-PAPP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIreNRSAA---LK 235
Cdd:PRK08266 188 PAPDPDAIAAAAALIAAAKNPMIFVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLGL--NFAAAyelWP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 236 KADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREEMllnsdIFWKPQEAVQGDVGSFVLKLVEGLQGQ-TWAPDWVEE 314
Cdd:PRK08266 263 QTDVVIGIGSRLELPTFRWPWRPDGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAgSKRPSRRAE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 315 LREAdrqkeqtfreKAAmpVAQHLNPVQ----VLQLVEETLPDNSIlVVDGGDFVGTAAHLVQP-RGPLRWLDPGAFGTL 389
Cdd:PRK08266 338 LREL----------KAA--ARQRIQAVQpqasYLRAIREALPDDGI-FVDELSQVGFASWFAFPvYAPRTFVTCGYQGTL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 390 GVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSL-GSNVACGLAYTDY 468
Cdd:PRK08266 405 GYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDF 484
|
490
....*....|.
gi 768000693 469 HKAAMGLGARG 479
Cdd:PRK08266 485 VKLAESFGVAA 495
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-434 |
7.57e-37 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 143.79 E-value: 7.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06965 79 ARATGKVGVALVTSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDvlypyfmVQKEMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqa 161
Cdd:PRK06965 159 VKKAFYIARTGRPGPVVVDIPKD-------VSKTPCEYEYPKSVEMR----------------SYNPVTKG--------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADkLRAAVETLGVPCF-----LGGMAR------GLLGrnhpLHIRENR 230
Cdd:PRK06965 207 HSGQIRKAVSLLLSAKRPYIYTGGGVILANASRE-LRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 231 SAALKKADVIVLAGTVCDFRL--SYGRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQT 306
Cdd:PRK06965 282 NMAMQHCDVLIAIGARFDDRVigNPAHFASRPRKIIHIDIDPSSIskRVKVDI------PIVGDVKEVLKELIEQLQTAE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 307 WAPD------W---VEELREADRQKEQTFREKaampvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGP 377
Cdd:PRK06965 356 HGPDadalaqWwkqIEGWRSRDCLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEP 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 768000693 378 LRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK06965 428 RRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPV 484
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
1-515 |
2.30e-36 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 142.26 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSG--TVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAAstllqNRGaLQAVD----QLSLFRPLCKFCVSVRR 74
Cdd:PRK06154 73 YARATSgeRVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGY-----PRG-STDVApnfeSLRNYRHITKWCEQVTL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 75 VRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYpyfmvqkEMVPAKPpkglvgrvvswylENYlanlfagawepqpeGPL 154
Cdd:PRK06154 147 PDEVPELMRRAFTRLRNGRPGPVVLELPVDVLA-------EELDELP-------------LDH--------------RPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 155 PLDIPQASPQQVQRCVEILSRAKRPLMVLGsQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAA- 233
Cdd:PRK06154 193 RRSRPGADPVEVVEAAALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 ------LKKADVIVLAGtvCDF-RLSYGRVLSHSSKIIIVNRNREEmlLNSDIFWKpqEAVQGDVGSFVLKLVEGLQG-- 304
Cdd:PRK06154 272 atvahfLREADVLFGIG--CSLtRSYYGLPMPEGKTIIHSTLDDAD--LNKDYPID--HGLVGDAALVLKQMIEELRRrv 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 305 ------------------QTWAPDWVEELREADRQkeqtfrekaampvaqhLNPVQVLQLVEETL-PDNSILVVDGGDFV 365
Cdd:PRK06154 346 gpdrgraqqvaaeieavrAAWLAKWMPKLTSDSTP----------------INPYRVVWELQHAVdIKTVIITHDAGSPR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 366 GTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND---A 442
Cdd:PRK06154 410 DQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNfsmG 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000693 443 GWTQISREQVPSLGSNVACGlaytDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 515
Cdd:PRK06154 490 GYDKVMPVSTTKYRATDISG----DYAAIARALGGYGERV--EDPEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
2-515 |
1.11e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 140.96 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK07418 80 ARATGKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPYFmvqkEMVPAKP----PKGlvgrvvswylenylanlfagaWEPQPEGplpld 157
Cdd:PRK07418 160 VAEAFHIASSGRPGPVLIDIPKDVGQEEF----DYVPVEPgsvkPPG---------------------YRPTVKG----- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 158 ipqaSPQQVQRCVEILSRAKRPLMVLGSQAlLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENR 230
Cdd:PRK07418 210 ----NPRQINAALKLIEEAERPLLYVGGGA-ISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 231 SAALKKADVIVLAGTVCDFRLSyGRVLSHSS--KII---I----VNRNReemllnsdifwKPQEAVQGDVGSFVLKLVEG 301
Cdd:PRK07418 285 NFAVTECDLLIAVGARFDDRVT-GKLDEFASraKVIhidIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLER 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 302 LQGQTWAP---DWVEELreadrqkeQTFREKAAMPVAQH---LNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHLVQpR 375
Cdd:PRK07418 353 SLEPTTPPrtqAWLERI--------NRWKQDYPLVVPPYegeIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAQFLR-N 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 376 GPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQISREQVPSL 455
Cdd:PRK07418 423 GPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQWQESF 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768000693 456 ------GSNVACGLAytDYHKAAMGLGARGLLLSRENEdqvvkvLHDAQQQC--RDGhPVVVNILIGR 515
Cdd:PRK07418 502 ygerysASNMEPGMP--DFVKLAEAFGVKGMVISERDQ------LKDAIAEAlaHDG-PVLIDVHVRR 560
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-442 |
2.59e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 139.07 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK08155 70 MARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVlypyfmvqkemvpakppkglvgrvvswylenYLANLFAGAWePQPEGPLPldIPQ 160
Cdd:PRK08155 150 VISDAFRIAQSGRPGPVWIDIPKDV-------------------------------QTAVIELEAL-PAPAEKDA--APA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 161 ASPQQVQRCVEILSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAA 233
Cdd:PRK08155 196 FDEESIRDAAAMINAAKRPVLYLGG-GVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 LKKADVIVLAGTVCDFRlSYGRVLSH--SSKIIIVNRNREEMllnsDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWApDW 311
Cdd:PRK08155 275 LQEADLLIVLGARFDDR-AIGKTEQFcpNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQPRA-EW 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 312 VEelREADRQKEQTFrekaAMPVAQH-LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLG 390
Cdd:PRK08155 349 HQ--LVADLQREFPC----PIPKADDpLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMG 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 768000693 391 VGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGNDA 442
Cdd:PRK08155 423 FGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-447 |
8.42e-35 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 137.70 E-value: 8.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSP-ILLLGGAASTLLQnRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK08199 66 GKLTGRPGICFVTRGPGATNASIGVHTAFQDSTPmILFVGQVARDFRE-REAFQEIDYRRMFGPMAKWVAEIDDAARIPE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVLYpyfmvQKEMVPAKPPkglvGRVVswylenylanlfagawEPQPegplpldipq 160
Cdd:PRK08199 145 LVSRAFHVATSGRPGPVVLALPEDVLS-----ETAEVPDAPP----YRRV----------------AAAP---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 161 aSPQQVQRCVEILSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRE-----NRS--AA 233
Cdd:PRK08199 190 -GAADLARLAELLARAERPLVILGG-SGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDlglgiNPAlaAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 LKKADVIVLAGTvcdfRLsyGRVLSHSSKIIIVNRNReEMLLNSDI-------FWKPQEAVQGDVGSFVLKL--VEGLQG 304
Cdd:PRK08199 268 IREADLVLAVGT----RL--GEVTTQGYTLLDIPVPR-QTLVHVHPdaeelgrVYRPDLAIVADPAAFAAALaaLEPPAS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 305 QTWApDWVEELREADRQkeqtfrEKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPG 384
Cdd:PRK08199 341 PAWA-EWTAAAHADYLA------WSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATWLHRFFRFRRYRTQLAPT 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000693 385 AfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQI 447
Cdd:PRK08199 414 S-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-444 |
1.07e-34 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 137.04 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAAST--LLQNRGAL-QAVDQLSLFRPLCKFCVSVRRVRDI 78
Cdd:PRK07064 61 ARVSGGLGVALTSTGTGAGNAAGALVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 79 VPTLRAAMAAAQSGTPGPVFVELPVDVLYpyfmvqkemvpakppkglvgRVVSWylenylanlfagawePQPEGPLPLDI 158
Cdd:PRK07064 141 LATIREAVRVALTAPTGPVSVEIPIDIQA--------------------AEIEL---------------PDDLAPVHVAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpTSADKLRAAVEtLGVPCFLGGMARGLLGRNHPLHIRE-NRSAA---- 233
Cdd:PRK07064 186 PEPDAAAVAELAERLAAARRPLLWLGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAveal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 LKKADVIVLAGTvcdfRLSYGRVLSHSSKI------IIVNRNREEMLLNSDIFwkpqeaVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK07064 262 YKTCDLLLVVGS----RLRGNETLKYSLALprplirVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 308 A-PDWVEELREADRQKEQTFRekaampvaQHLNPVQVL-QLVEETLPDNSILVVDGGDFVGTAAH-LVQPRGPLRWLDPG 384
Cdd:PRK07064 332 VdPAFAADLRAAREAAVADLR--------KGLGPYAKLvDALRAALPRDGNWVRDVTISNSTWGNrLLPIFEPRANVHAL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 385 AfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGW 444
Cdd:PRK07064 404 G-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
2-497 |
1.57e-34 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 137.20 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFcvsVRRVRD---I 78
Cdd:PRK06112 69 ARVSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 79 VPTLRAAMAAAQSGTPGPVFVELPVDVLypyfmvqkeMVPAKPPkglvGRVVSwylenylANLfaGAWepqpegplPLDI 158
Cdd:PRK06112 146 DDYVDQAFTAATSGRPGPVVLLLPADLL---------TAAAAAP----AAPRS-------NSL--GHF--------PLDR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------------- 224
Cdd:PRK06112 196 TVPAPQRLAEAASLLAQAQRPVVVAGGGVHIS-GASAALAALQSLAGLPVATTNMGKGAVDETHPLslgvvgslmgprsp 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 225 --HIREnrsaALKKADVIVLAGTvcdfRLSYG-----RVLSHSSKIII-------VNRNREEMLLNSDifwkPQEAVQGd 290
Cdd:PRK06112 275 grHLRD----LVREADVVLLVGT----RTNQNgtdswSLYPEQAQYIHidvdgeeVGRNYEALRLVGD----ARLTLAA- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 291 vgsfvLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPV---AQHLNPVQVLQLVEETLPDNSILVVDGG-DFVG 366
Cdd:PRK06112 342 -----LTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVAlsdASPIRPERIMAELQAVLTGDTIVVADASySSIW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 367 TAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA--GW 444
Cdd:PRK06112 417 VANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 768000693 445 tQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGllLSRENEDQVVKVLHDA 497
Cdd:PRK06112 497 -QKHAETVKFGTHTDACHFAAVDHAAIARACGCDG--VRVEDPAELAQALAAA 546
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
2-103 |
2.90e-34 |
|
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: 126.49 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:cd07035 54 ARATGKPGVVLVTSGPGLTNAVTGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEA 133
|
90 100
....*....|....*....|..
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPV 103
Cdd:cd07035 134 LRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-520 |
1.09e-33 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 134.21 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK08617 61 IGRLTGKPGVVLVTSGPGVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVLypyfmvqKEMVPAKPPKGLvgrvvswylenylanlfagawEPQPEGPlpldipq 160
Cdd:PRK08617 141 VLANAFRAAESGRPGAAFVSLPQDVV-------DAPVTSKAIAPL---------------------SKPKLGP------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 161 ASPQQVQRCVEILSRAKRPLMVLGSQAlLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHplhirENRSAA------- 233
Cdd:PRK08617 186 ASPEDINYLAELIKNAKLPVLLLGMRA-SSPEVTAAIRRLLERTNLPVVETFQAAGVISREL-----EDHFFGrvglfrn 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 ------LKKADVIVLAGtvcdfrlsYGRV--------LSHSSKIIIVNRNREEMllnsDIFWKPQEAVQGDVGSFVLKLV 299
Cdd:PRK08617 260 qpgdelLKKADLVITIG--------YDPIeyeprnwnSEGDATIIHIDVLPAEI----DNYYQPERELIGDIAATLDLLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 300 EGLQGQTWAPDWVEELreADRQKEQTFREKAAMPVAQHL-NPVQVLQLVEETLPDNSILVVDGGDF-VGTAAHL--VQPR 375
Cdd:PRK08617 328 EKLDGLSLSPQSLEIL--EELRAQLEELAERPARLEEGAvHPLRIIRALQDIVTDDTTVTVDVGSHyIWMARYFrsYEPR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 376 GPLrwldpgaFG----TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQ 451
Cdd:PRK08617 406 HLL-------FSngmqTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQE 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000693 452 VPSLGSNVACGLAYTDYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrDGhPVVVNILIgrtDFRD 520
Cdd:PRK08617 479 EMKYGRSSGVDFGPVDFVKYAESFGAKG--LRVTSPDELEPVLREALAT--DG-PVVIDIPV---DYSD 539
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-441 |
1.36e-33 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 134.18 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK07282 68 AKSTGKLGVAVVTSGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVlypyfmvqkemvpakppkglVGRVVSWYLEnylanlfagawepqPEGPLPLDIPQA 161
Cdd:PRK07282 148 ITEAVHIATTGRPGPVVIDLPKDV--------------------SALETDFIYD--------------PEVNLPSYQPTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQ--QVQRCVEILSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSA 232
Cdd:PRK07282 194 EPNdmQIKKILKQLSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 233 ALKKADVIVLAGTVCDFRL-SYGRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTWAP 309
Cdd:PRK07282 273 AMTEADFMINIGSRFDDRLtGNPKTFAKNAKVAHIDIDPAEIgkIIKTDI------PVVGDAKKALQMLLAEPTVHNNTE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 310 DWVEELREaDRQKEQTFREKAAMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTL 389
Cdd:PRK07282 347 KWIEKVTK-DKNRVRSYDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTM 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 768000693 390 GVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK07282 421 GFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNN 472
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
2-515 |
7.28e-33 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 132.41 E-value: 7.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK07789 89 AQATGRVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLypyfmvQKEMVpakppkglvgrvvswylenylanlFAgaWEPQPEGPLPLDIPQA 161
Cdd:PRK07789 169 IAEAFHIASTGRPGPVLVDIPKDAL------QAQTT------------------------FS--WPPRMDLPGYRPVTKP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHPLHI-------RENRSAAL 234
Cdd:PRK07789 217 HGKQIREAAKLIAAARRPVLYVGGGVIRAEASAE-LRELAELTGIPVVTTLMARGAFPDSHPQHLgmpgmhgTVAAVAAL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTVCDFRLSyGRVLSHS--SKIIIVN-------RNREemllnSDIFwkpqeaVQGDVGSFVLKLVEGLQGQ 305
Cdd:PRK07789 296 QRSDLLIALGARFDDRVT-GKLDSFApdAKVIHADidpaeigKNRH-----ADVP------IVGDVKEVIAELIAALRAE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 306 TWA---PD---WVEELREADRQKEQTFREkaamPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLR 379
Cdd:PRK07789 364 HAAggkPDltaWWAYLDGWRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRT 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGNDA-----GWTQISREQVP 453
Cdd:PRK07789 440 WLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINNGNlgmvrQWQTLFYEERY 519
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000693 454 SlGSNVACGLAYT-DYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQcrDGHPVVVNILIGR 515
Cdd:PRK07789 520 S-NTDLHTHSHRIpDFVKLAEAYGCVGLRCEREED--VDAVIEKARAI--NDRPVVIDFVVGK 577
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
2-479 |
4.15e-32 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 129.96 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06456 63 ARASGVPGVCTATSGPGTTNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPyfMVQKEMVPAKPpkglvgrvvswYLENYlanlfagawepqpeGPLPLDIpqa 161
Cdd:PRK06456 143 IKNAFYIATTGRPGPVVIDIPRDIFYE--KMEEIKWPEKP-----------LVKGY--------------RDFPTRI--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAvETLGVPCFLGGMARGLLGRNHPLHI-------RENRSAAL 234
Cdd:PRK06456 193 DRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTVCDFRL--SYGRVLSHSSKIIIVNRNREEmllnSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPD-- 310
Cdd:PRK06456 272 LESDAMLVVGARFSDRTftSYDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIILRELIKAITELGQKRDrs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 311 -WVEELREADRQKEQTFREKAAmpvaQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTL 389
Cdd:PRK06456 348 aWLKRVKEYKEYYSQFYYTEEN----GKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTM 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 390 GVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVgNDAGWTQISREQVPSLGSNVACGLAY---T 466
Cdd:PRK06456 424 GFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVRQVQDLFFGKRIVGVDYgpsP 502
|
490
....*....|...
gi 768000693 467 DYHKAAMGLGARG 479
Cdd:PRK06456 503 DFVKLAEAFGALG 515
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
2-442 |
8.62e-32 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 129.09 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06466 62 ARATGKTGVVLVTSGPGATNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPyfmvqKEMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqa 161
Cdd:PRK06466 142 IKKAFYIAQSGRPGPVVVDIPKDMTNP-----AEKFEYEYPKKVKLR----------------SYSPAVRG--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPTSAdKLRAAVETLGVPCF-----LGGMAR------GLLGrnhpLHIRENR 230
Cdd:PRK06466 192 HSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASA-LLTELAHLLNLPVTntlmgLGGFPGtdrqflGMLG----MHGTYEA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 231 SAALKKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK06466 267 NMAMHHADVILAVGARFDDRVTNGpAKFCPNAKIIHIDIDPASIskTIKADI------PIVGPVESVLTEMLAILKEIGE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 308 APD------WVEELREAdRQKEQTFREKAAMPVAqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWL 381
Cdd:PRK06466 341 KPDkealaaWWKQIDEW-RGRHGLFPYDKGDGGI--IKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWI 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000693 382 DPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 442
Cdd:PRK06466 418 NSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
2-434 |
1.25e-31 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 128.40 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK08979 62 ARATGKVGVVLVTSGPGATNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPYFmvqkeMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqa 161
Cdd:PRK08979 142 IKKAFYIASTGRPGPVVIDLPKDCLNPAI-----LHPYEYPESIKMR----------------SYNPTTSG--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSQALLtpTSADK-LRAAVETLGVPCFLGGMARGLLGRNHP-------LHIRENRSAA 233
Cdd:PRK08979 192 HKGQIKRGLQALLAAKKPVLYVGGGAII--SGADKqILQLAEKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 LKKADVIVLAGTVCDFRLSygrvlshsskiiivnRNREEMLLNSDIFW---KP---QEAVQGD---VGSF------VLKL 298
Cdd:PRK08979 270 MHNADLIFGIGVRFDDRTT---------------NNLEKYCPNATILHidiDPssiSKTVRVDipiVGSAdkvldsMLAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 299 VEGLQGQ-------TWAPDwVEELREADRQKEQTFREKaampvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHL 371
Cdd:PRK08979 335 LDESGETndeaaiaSWWNE-IEVWRSRNCLAYDKSSER--------IKPQQVIETLYKLTNGDAYVASDVGQHQMFAALY 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000693 372 VQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK08979 406 YPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
2-106 |
1.75e-31 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 119.26 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQA-VDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:pfam02776 57 ARATGKPGVVLVTSGPGATNALTGLANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPE 136
|
90 100
....*....|....*....|....*.
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVL 106
Cdd:pfam02776 137 VLRRAFRAALSGRPGPVYLEIPLDVL 162
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
1-434 |
3.69e-31 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 126.92 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK08978 57 YARATGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDvlypyfmVQKEMVPAKPPkglvgrvvswylenylanlfagawePQPegplPLDIPQ 160
Cdd:PRK08978 137 IMAEAFEIASSGRPGPVLVDIPKD-------IQLAEGELEPH-------------------------LTT----VENEPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 161 ASPQQVQRCVEILSRAKRPLMVLG-----SQALltptsaDKLRAAVETLGVP--CFLGGMarGLLGRNHP-----LHIRE 228
Cdd:PRK08978 181 FPAAELEQARALLAQAKKPVLYVGggvgmAGAV------PALREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 229 NRSA--ALKKADVIVLAGTVCDFRLSyGRVLSHSS--KIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGL 302
Cdd:PRK08978 253 TKAAnlAVQECDLLIAVGARFDDRVT-GKLNTFAPhaKVIHLDIDPAEInkLRQAHV------ALQGDLNALLPALQQPL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 303 QGQTWApDWVEELREadrqkEQTFREKAAmpvAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLD 382
Cdd:PRK08978 326 NIDAWR-QHCAQLRA-----EHAWRYDHP---GEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFIT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 768000693 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK08978 397 SSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPV 448
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-437 |
7.87e-31 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 126.12 E-value: 7.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK07979 61 LARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVLYPYFmvqkeMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipq 160
Cdd:PRK07979 141 VLKKAFWLAASGRPGPVVVDLPKDILNPAN-----KLPYVWPESVSMR----------------SYNPTTQG-------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 161 aSPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHP-------LHIRENRSAA 233
Cdd:PRK07979 192 -HKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQ-LKELVEKLNLPVVSSLMGLGAFPATHRqslgmlgMHGTYEANMT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 234 LKKADVIVLAGTVCDFRLSYGRVLSHSSKIII---VNRNREEMLLNSDIfwkpqeAVQGDvGSFVLKLVEGLQGQTWAPD 310
Cdd:PRK07979 270 MHNADVIFAVGVRFDDRTTNNLAKYCPNATVLhidIDPTSISKTVTADI------PIVGD-ARQVLEQMLELLSQESAHQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 311 WVEELREADRQKEQtFREKAAM---PVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFG 387
Cdd:PRK07979 343 PLDEIRDWWQQIEQ-WRARQCLkydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLG 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768000693 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMAL 437
Cdd:PRK07979 422 TMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
360-511 |
8.95e-31 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 116.92 E-value: 8.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 360 DGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVG 439
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768000693 440 NDAGWTQISREQVPSLGSNVAC----GLAYTDYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrdGHPVVVNI 511
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGpsgkILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-441 |
3.77e-30 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 124.26 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK06882 62 ARSTGKVGCVLVTSGPGATNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPST 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMvpakpPKGLvgrvvswYLENYLANLfagawepqpegplpldipQA 161
Cdd:PRK06882 142 IKKAFYIASTGRPGPVVIDIPKDMVNPANKFTYEY-----PEEV-------SLRSYNPTV------------------QG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQQVQRCVEILSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCF-----LGGMAR------GLLGrnhpLHIRENR 230
Cdd:PRK06882 192 HKGQIKKALKALLVAKKPVLFVGG-GVITAECSEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 231 SAALKKADVIVLAGTVCDFRLS--YGRVLSHsSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEG--LQGQT 306
Cdd:PRK06882 267 NNAMHESDLILGIGVRFDDRTTnnLAKYCPN-AKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEEnlAKSQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 307 WAPDWVEELREADRQKEQTFREKAAMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAF 386
Cdd:PRK06882 346 DLTAWWQQINEWKAKKCLEFDRTSDV-----IKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGA 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 768000693 387 GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06882 421 GTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
2-441 |
1.77e-29 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 122.15 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PLN02470 71 AKASGKVGVCIATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVlypyfmvQKEM-VPA-KPPKGLVGrvvswylenYLANLfagawePQPegplpldiP 159
Cdd:PLN02470 151 IREAFFLASSGRPGPVLVDIPKDI-------QQQLaVPNwNQPMKLPG---------YLSRL------PKP--------P 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 160 QASpqQVQRCVEILSRAKRPLMVLGSQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRE-------NRSA 232
Cdd:PLN02470 201 EKS--QLEQIVRLISESKRPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 233 ALKKADVIVLAGTVCDFRLSyGRVLSHSS--KIIIVNRNREEMLLNSdifwKPQEAVQGDVgSFVLKLVEGL--QGQTWA 308
Cdd:PLN02470 276 AVDSADLLLAFGVRFDDRVT-GKLEAFASraSIVHIDIDPAEIGKNK----QPHVSVCADV-KLALQGLNKLleERKAKR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 309 PDWVEELREADRQKEQ---TFREKAAMPVAQHlnpvqVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGA 385
Cdd:PLN02470 350 PDFSAWRAELDEQKEKfplSYPTFGDAIPPQY-----AIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGG 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 768000693 386 FGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PLN02470 425 LGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-487 |
8.75e-28 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 117.17 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK07710 73 ARISGKPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDvlypyfMVQKEmvpakppkglvgrvvswylenylanlfaGAWEPQPEGPLPLDIPQA 161
Cdd:PRK07710 153 IKEAFHIATTGRPGPVLIDIPKD------MVVEE----------------------------GEFCYDVQMDLPGYQPNY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SPQ--QVQRCVEILSRAKRPLMVLGSQALLTPTSaDKLRAAVETLGVPcflggMARGLLG-----RNHPL-------HIR 227
Cdd:PRK07710 199 EPNllQIRKLVQAVSVAKKPVILAGAGVLHAKAS-KELTSYAEQQEIP-----VVHTLLGlggfpADHPLflgmagmHGT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 228 ENRSAALKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREEMLLNSDIfwKPQEAVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK07710 273 YTANMALYECDLLINIGARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQEGKKEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 308 APDWVEELREADRQKEQTFREKAampvaQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFG 387
Cdd:PRK07710 350 HHEWLSLLKNWKEKYPLSYKRNS-----ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG------WTQISREQVPSlGSNVAC 461
Cdd:PRK07710 425 TMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEAlgmvrqWQEEFYNQRYS-HSLLSC 503
|
490 500
....*....|....*....|....*.
gi 768000693 462 glaYTDYHKAAMGLGARGLLLSRENE 487
Cdd:PRK07710 504 ---QPDFVKLAEAYGIKGVRIDDELE 526
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
2-434 |
1.83e-27 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 116.35 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK09107 69 ARSTGKPGVVLVTSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDVLYpyfmvqkemvpAK----PPKGLVGRVvswylenylanlfagAWEPQPEGplpld 157
Cdd:PRK09107 149 IHEAFHVATSGRPGPVVVDIPKDVQF-----------ATgtytPPQKAPVHV---------------SYQPKVKG----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 158 ipqaSPQQVQRCVEILSRAKRPLMVLGSQALLT-PTSADKLRAAVETLGVP--CFLGGMAR---------GLLGrnhpLH 225
Cdd:PRK09107 198 ----DAEAITEAVELLANAKRPVIYSGGGVINSgPEASRLLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 226 IRENRSAALKKADVIVLAGTVCDFRLSyGRVLS---HSSKIII------VNRNreemlLNSDIfwkpqeAVQGDVGSFVL 296
Cdd:PRK09107 270 GTYEANMAMHDCDVMLCVGARFDDRIT-GRLDAfspNSKKIHIdidpssINKN-----VRVDV------PIIGDVGHVLE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 297 KLVEGLQGQTWAPD------WVEELREADRQKEQTFREKAAMPVAQHlnpvQVLQLVEETLPDNSILVVDGGDFVGTAAH 370
Cdd:PRK09107 338 DMLRLWKARGKKPDkealadWWGQIARWRARNSLAYTPSDDVIMPQY----AIQRLYELTKGRDTYITTEVGQHQMWAAQ 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768000693 371 LVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK09107 414 FFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
2-513 |
1.79e-26 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 113.26 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:CHL00099 71 ARSTGKVGVCFATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAQSGTPGPVFVELPVDV---LYPYFMVqkemVPAKPPKGLVGrvvswylenylanlfagaWEPqpegplpldI 158
Cdd:CHL00099 151 VAEAFYIAKHGRPGPVLIDIPKDVgleKFDYYPP----EPGNTIIKILG------------------CRP---------I 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIrenrsaalkkaD 238
Cdd:CHL00099 200 YKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS-DAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCL-----------G 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 239 VIVLAGTV--------CDFRLSYG-----RV------LSHSSKIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKLV 299
Cdd:CHL00099 268 MLGMHGTAyanfavseCDLLIALGarfddRVtgkldeFACNAQVIHIDIDPAEIGKNR----IPQVAIVGDVKKVLQELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 300 EGLQGQTWAPDwvEELREADRQKEQTFREKAAMPVAQH---LNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHL--VQP 374
Cdd:CHL00099 344 ELLKNSPNLLE--SEQTQAWRERINRWRKEYPLLIPKPstsLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlkCKP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 375 RgplRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQISRE-QVP 453
Cdd:CHL00099 421 R---KWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN-KWQGMVRQwQQA 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000693 454 SLG-----SNVACGLAytDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQcrDGhPVVVNILI 513
Cdd:CHL00099 497 FYGeryshSNMEEGAP--DFVKLAEAYGIKGLRI--KSRKDLKSSLKEALDY--DG-PVLIDCQV 554
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
2-444 |
1.79e-26 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 113.17 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLlqNRGAL-----------QAVDQLSLFRPLCKFCV 70
Cdd:PRK08327 70 ALVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 71 SVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLypyfmVQKemvpakppkglVGRVvswylenylanlfagawEPQP 150
Cdd:PRK08327 148 EIRRGDQIGEVVARAIQIAMSEPKGPVYLTLPREVL-----AEE-----------VPEV-----------------KADA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 151 EGPLPLDIPQASPQQVQRCVEILSRAKRPLmVLGSQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENR 230
Cdd:PRK08327 195 GRQMAPAPPAPDPEDIARAAEMLAAAERPV-IITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 231 SAALKKADVIVLAGTVCDFRLSYGRvLSHSSKIIIVNrnreEMLLNSDI-FWK-PQE-AVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK08327 274 RADLAEADLVLVVDSDVPWIPKKIR-PDADARVIQID----VDPLKSRIpLWGfPCDlCIQADTSTALDQLEERLKSLAS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 308 APDWVEELREADRQKEQTFREKAAMPVAQHL------NPVQVLQLVEETLPDNSILVVDGGdFVGTAAHLvqpRGPLRWL 381
Cdd:PRK08327 349 AERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPGSYF 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768000693 382 DPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFV--RHKIPVMALVGNDAGW 444
Cdd:PRK08327 425 GDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
342-513 |
5.56e-26 |
|
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: 104.26 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 342 QVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 422 IEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQq 500
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRV--EDPEDLEAALAEALA- 157
|
170
....*....|...
gi 768000693 501 cRDGhPVVVNILI 513
Cdd:cd00568 158 -AGG-PALIEVKT 168
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
6-515 |
3.02e-25 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 109.68 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 6 GTVGVAAVTAGPGLTNTVTAVKNAqMAQS-PILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRA 84
Cdd:PRK11269 67 GNIGVCIGTSGPAGTDMITGLYSA-SADSiPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 85 AMAAAQSGTPGPVFVELPVDvlypyfmVQKEMVpakppkglvgrvvswylenylanlfagAWEPQPEGPLPLDIPQASPQ 164
Cdd:PRK11269 146 AFHLMRSGRPGPVLIDLPFD-------VQVAEI---------------------------EFDPDTYEPLPVYKPAATRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 165 QVQRCVEILSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL----------HIRENrsAAL 234
Cdd:PRK11269 192 QIEKALEMLNAAERPLIVAGG-GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 235 KKADVIVLAGTVCDFRlsygrvlsHSSKIIIVNRNREemLLNSDI-------FWKPQEAVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK11269 269 LASDFVLGIGNRWANR--------HTGSVEVYTKGRK--FVHVDIeptqigrVFGPDLGIVSDAKAALELLVEVAREWKA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 308 A------PDWVEELREadrqkeqtfrEKAAMPVAQH-----LNPVQVLQLVEETLPDNSILV-------VDGGDFVgtaa 369
Cdd:PRK11269 339 AgrlpdrSAWVADCQE----------RKRTLLRKTHfdnvpIKPQRVYEEMNKAFGRDTCYVstiglsqIAAAQFL---- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 370 HLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISR 449
Cdd:PRK11269 405 HVYKPR---HWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQ 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000693 450 EQVPsLGSNVACGLAY------------TDYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 515
Cdd:PRK11269 482 AQRA-FDMDYCVQLAFeninspelngygVDHVKVAEGLGCKAIRVFKPED--IAPALEQAKALMAEFRvPVVVEVILER 557
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
338-516 |
2.57e-24 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 100.28 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 338 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 418 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSN-VACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHD 496
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
|
170 180
....*....|....*....|
gi 768000693 497 AQQQCRDGHPVVVNILIGRT 516
Cdd:cd02013 162 AIAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
338-513 |
5.76e-23 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 96.06 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 338 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 418 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
|
170
....*....|....*.
gi 768000693 498 QQQcrDGhPVVVNILI 513
Cdd:cd02014 160 LAA--DG-PVVIDVVT 172
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
2-513 |
1.22e-20 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 95.45 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKF---CVSVRRVRDI 78
Cdd:PRK08611 63 AKLTGKIGVCLSIGGPGAIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYnhqIMSAENLPEI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 79 VPT-LRAAMAAAqsgtpGPVFVELPVDVLypyfmvqKEMVPAKPpkglvgrvvswyleNYLANLFAgawepqpegplpLD 157
Cdd:PRK08611 143 VNQaIRTAYEKK-----GVAVLTIPDDLP-------AQKIKDTT--------------NKTVDTFR------------PT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 158 IPQASPQQVQRCVEILSRAKRPLMVLGsqaLLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL------HIRENRS 231
Cdd:PRK08611 185 VPSPKPKDIKKAAKLINKAKKPVILAG---LGAKHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYslgnlgKIGTKPA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 232 -AALKKADVIVLAGTvcDFrlSYGRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLqgqtwa 308
Cdd:PRK08611 262 yEAMQEADLLIMVGT--NY--PYVDYLPKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALHQLTENI------ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 309 pDWVEELR--EADRQKEQTFREKAAMPVAQHLNPV---QVLQLVEETLPDNSILVVD-GGDFVGTAAHL-VQPRGPL--- 378
Cdd:PRK08611 326 -KHVEDRRflEACQENMAKWWKWMEEDENNASTPIkpeRVMAAIQKIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiis 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 379 RWLdpgafGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSN 458
Cdd:PRK08611 405 SWL-----GTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 768000693 459 VACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRdghPVVVNILI 513
Cdd:PRK08611 480 YAIDLSDMDYAKFAEACGGKGYRV--EKAEELDPAFEEALAQDK---PVIIDVYV 529
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
166-298 |
3.98e-19 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 83.77 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 166 VQRCVEILSRAKRPLMVLGSQALLtPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKAD 238
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRR-SGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768000693 239 VIVLAGTVCDFRLSYGRVLSHSS--KIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKL 298
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPdaKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
2-517 |
9.97e-18 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 85.98 E-value: 9.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALqaV----------DQLSLFRPLCkfCVS 71
Cdd:COG3961 63 ARVNG-LGALVTTYGVGELSAINGIAGAYAERVPVVHIVGAPGTRAQRRGPL--LhhtlgdgdfdHFLRMFEEVT--VAQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 72 VR-----------RVrdivptLRAAMAAAQsgtpgPVFVELPVDVlypyfmVQKEMVPakppkglvgrvvswylenylan 140
Cdd:COG3961 138 AVltpenaaaeidRV------LAAALREKR-----PVYIELPRDV------ADAPIEP---------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 141 lfagawepqPEGPLPLDIPQASPQQVQRCV----EILSRAKRPLMVLGSQAL---LTptsaDKLRAAVETLGVPCFLGGM 213
Cdd:COG3961 179 ---------PEAPLPLPPPASDPAALAAAVaaaaERLAKAKRPVILAGVEVHrfgLQ----EELLALAEKTGIPVATTLL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 214 ARGLLGRNHPLHI--------RENRSAALKKADVIVLAGTV-CDFrlsygrvlshsskiiivnrnreemllNSDIF--WK 282
Cdd:COG3961 246 GKSVLDESHPQFIgtyagaasSPEVREYVENADCVLCLGVVfTDT--------------------------NTGGFtaQL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 283 PQEAVQgDVGSFVLKLveglqGQTWAP-----DWVEELREADRQKEQTFREKAAMPVAQHLNPVQVL------QLVEETL 351
Cdd:COG3961 300 DPERTI-DIQPDSVRV-----GGHIYPgvslaDFLEALAELLKKRSAPLPAPAPPPPPPPAAPDAPLtqdrlwQRLQAFL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 352 PDNSILVVDGGD--FVGTAAHLvqPRGpLRWLDPGAFGTLG--VGAgfALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTF 427
Cdd:COG3961 374 DPGDIVVADTGTslFGAADLRL--PEG-ATFIAQPLWGSIGytLPA--ALGAALAAPDRRVILLVGDGAFQLTAQELSTM 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 428 VRHKIPVMALVGNDAGWTqISReqvpslgsnVACGL--AYTD-----YHKAAMGLGARGLLLSR-ENEDQVVKVLHDAQQ 499
Cdd:COG3961 449 LRYGLKPIIFVLNNDGYT-IER---------AIHGPdgPYNDianwdYAKLPEAFGGGNALGFRvTTEGELEEALAAAEA 518
|
570
....*....|....*...
gi 768000693 500 QCRdgHPVVVNILIGRTD 517
Cdd:COG3961 519 NTD--RLTLIEVVLDKMD 534
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
2-487 |
3.97e-17 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 84.11 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPlckfcVSVRRVRDIVP- 80
Cdd:PRK06457 59 AKITGKPSACMGTSGPGSIHLLNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDD-----VAVFNQILINPe 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 ----TLRAAMAAAQSgTPGPVFVELPVDVLypyfmvqkemvpakppkglvgRVVSWYLENYlanlfagaWEPQPEGPLPL 156
Cdd:PRK06457 134 naeyIIRRAIREAIS-KRGVAHINLPVDIL---------------------RKSSEYKGSK--------NTEVGKVKYSI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 157 DIPQASpqqvqrcvEILSRAKRPLMVLGSQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHP--------LHIRE 228
Cdd:PRK06457 184 DFSRAK--------ELIKESEKPVLLIGGGTR---GLGKEINRFAEKIGAPIIYTLNGKGILPDLDPkvmggiglLGTKP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 229 NRSAaLKKADVIVLAGTVcdfrLSYGRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFV-LKLVEglqgq 305
Cdd:PRK06457 253 SIEA-MDKADLLIMLGTS----FPYVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLnIDIEE----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 306 twAPDWVEElrEADRQKEQTFR--EKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDP 383
Cdd:PRK06457 317 --KSDKFYE--ELKGKKEDWLDsiSKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 384 GAFGTLGVGAGFALGAKLCR-PDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQ----VPSLGSN 458
Cdd:PRK06457 393 AWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEWGVD 472
|
490 500
....*....|....*....|....*....
gi 768000693 459 vacgLAYTDYHKAAMGLGARGLLLSRENE 487
Cdd:PRK06457 473 ----LYNPDFTKIAESIGFKGFRLEEPKE 497
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
338-440 |
7.58e-15 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the 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. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 72.92 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 338 LNPVQVLQLVEETLPDNSILVVDggdfVGT----AAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFG 413
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTD----VGQhqmwAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDG 76
|
90 100
....*....|....*....|....*..
gi 768000693 414 DGAFGYSLIEFDTFVRHKIPVMALVGN 440
Cdd:cd02015 77 DGSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
340-520 |
3.67e-14 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 70.78 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 340 PVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQ 499
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRI--ESADDLLPVLERALA 158
|
170 180
....*....|....*....|.
gi 768000693 500 QcrDGhPVVVNILIgrtDFRD 520
Cdd:cd02010 159 A--DG-VHVIDCPV---DYSE 173
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
11-484 |
5.79e-14 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 74.22 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 11 AAVTAGPGLTNTVTAVKNaqmaQSPILLLGGA-ASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAA 89
Cdd:PRK07092 81 SAAGVGNAMGNLFTAFKN----HTPLVITAGQqARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 90 QSGTPGPVFVELPVDvlypyfmvqKEMVPAKPpkgLVGRVVSwylenylanlFAGAwepqpegplpldipqASPQQVQRC 169
Cdd:PRK07092 157 MQPPRGPVFVSIPYD---------DWDQPAEP---LPARTVS----------SAVR---------------PDPAALARL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 170 VEILSRAKRPLMVLGSQALLTPTSADKLRAAvETLGVPCFLGGMA-RGLLGRNHPLH------IRENRSAALKKADVIVL 242
Cdd:PRK07092 200 GDALDAARRPALVVGPAVDRAGAWDDAVRLA-ERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 243 AGTVCdFRL---SYGRVLSHSSKIIIVNRNREEMLlnsdifWKPQ-EAVQGDVGSFVLKLVEGL-QGQTWAPDWVEELRE 317
Cdd:PRK07092 279 IGAPV-FTYhveGPGPHLPEGAELVQLTDDPGEAA------WAPMgDAIVGDIRLALRDLLALLpPSARPAPPARPMPPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 318 ADRQKEqtfrekaAMPVAQhlnpvqVLQLVEETLPDNSILVVDGGDFVGTaahlVQPRgpLRWLDPGAF-----GTLGVG 392
Cdd:PRK07092 352 APAPGE-------PLSVAF------VLQTLAALRPADAIVVEEAPSTRPA----MQEH--LPMRRQGSFytmasGGLGYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQIsREQVPSLGSNVACGLAY--TDYHK 470
Cdd:PRK07092 413 LPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGAL-RWFAPVFGVRDVPGLDLpgLDFVA 491
|
490
....*....|....
gi 768000693 471 AAMGLGARGLLLSR 484
Cdd:PRK07092 492 LARGYGCEAVRVSD 505
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
338-513 |
1.08e-13 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 69.16 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 338 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 418 GYSLIEFDTFVRHKIPVMALVGNDAGWtQISREQVPSLGSNVACGLAY---------TDYHKAAMGLGARGLLLSRENEd 488
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVETPEE- 157
|
170 180
....*....|....*....|....*.
gi 768000693 489 qvvkvLHDAQQQC-RDGHPVVVNILI 513
Cdd:cd02002 158 -----LDEALREAlAEGGPALIEVVV 178
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
345-517 |
1.84e-12 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 66.02 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 345 QLVEETLPDNSILVVDGGDFVGTAAHLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEF 424
Cdd:cd02005 9 QQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 425 DTFVRHKIPVMALVGNDAGWT---QISREQVPslgsnvacglaYTD-----YHKAAMGLGARGLLLSR--ENEDQVVKVL 494
Cdd:cd02005 88 STMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFrvKTEGELDEAL 156
|
170 180
....*....|....*....|...
gi 768000693 495 HDAQQQCrdGHPVVVNILIGRTD 517
Cdd:cd02005 157 KDALFNR--DKLSLIEVILPKDD 177
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
2-105 |
1.32e-11 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) 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. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 62.95 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRR---VRDI 78
Cdd:cd07039 58 AKLTGKLGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPEL 137
|
90 100
....*....|....*....|....*...
gi 768000693 79 VPT-LRAAMAaaqsgTPGPVFVELPVDV 105
Cdd:cd07039 138 LDRaIRTAIA-----KRGVAVLILPGDV 160
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
2-476 |
7.87e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 64.51 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPIL-LLGGAASTLLQNRGALQAvDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK12474 63 GRIAGKPAVTLLHLGPGLANGLANLHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRWVHRSASAGAVDS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVlypyfmvqkemvpakppkglvgrvvswylenylanlfagAWEPQPEGPLPL-DIP 159
Cdd:PRK12474 142 DVARAVQAAQSAPGGIATLIMPADV---------------------------------------AWNEAAYAAQPLrGIG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 160 QA--SPQQVQRCVEILSRAKRPLMVLGSQALLTP--TSADKLRAAVetlGVPCFLGGMA-RGLLGRNH-PL----HIREN 229
Cdd:PRK12474 183 PApvAAETVERIAALLRNGKKSALLLRGSALRGAplEAAGRIQAKT---GVRLYCDTFApRIERGAGRvPIeripYFHEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 230 RSAALKKADVIVLAGT---VCDFrlSY----GRVLSHSSKIIIVNRNREEmllnsdifwkpqeavqgdvgsfvlkLVEGL 302
Cdd:PRK12474 260 ITAFLKDVEQLVLVGAkppVSFF--AYpgkpSWGAPPGCEIVYLAQPDED-------------------------LAQAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 303 QgqtwapDWVEELREADRQKEQTFREKAAMPVAQhLNPVQVLQLVEETLPDNSIlVVDGGDFVGTAAHLVQPRGPLRWLD 382
Cdd:PRK12474 313 Q------DLADAVDAPAEPAARTPLALPALPKGA-LNSLGVAQLIAHRTPDQAI-YADEALTSGLFFDMSYDRARPHTHL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG----WTQISREQVPSLGSN 458
Cdd:PRK12474 385 PLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSyailNGELQRVGAQGAGRN 464
|
490 500
....*....|....*....|..
gi 768000693 459 VACGLAY----TDYHKAAMGLG 476
Cdd:PRK12474 465 ALSMLDLhnpeLNWMKIAEGLG 486
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
2-417 |
2.80e-10 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 62.62 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAastllQNRGAL-----QAVDQLSLFR----PLCKFCVSV 72
Cdd:PRK08273 62 AKFTGEVGVCLATSGPGAIHLLNGLYDAKLDHVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 73 RRVRDIVP-TLRAAMAaaqsgTPGPVFVELPVDVlypyfmvQKEmvPAKPPKGLVGRVVSwylenylanlfaGAWEPQPE 151
Cdd:PRK08273 137 EQLRHLVDrAVRTALA-----ERTVTAVILPNDV-------QEL--EYEPPPHAHGTVHS------------GVGYTRPR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 152 gPLPldipqaSPQQVQRCVEILSRAKRPLMVLGSQALltpTSADKLRAAVETLGvpcflGGMARGLLGRnhplhirenrs 231
Cdd:PRK08273 191 -VVP------YDEDLRRAAEVLNAGRKVAILVGAGAL---GATDEVIAVAERLG-----AGVAKALLGK----------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 232 AALKK-----ADVIVLAGTvcdfRLSYgRVLSHSSKIIIVNRNreemllnsdiF----WKPQE----AVQGDVGSFVLKL 298
Cdd:PRK08273 245 AALPDdlpwvTGSIGLLGT----KPSY-ELMRECDTLLMVGSS----------FpyseFLPKEgqarGVQIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 299 ---VE-GLQGQTWA------------PD--WVEELREADRQKEQTFREKAAMPvAQHLNPVQVLQLVEETLPDNSILVVD 360
Cdd:PRK08273 310 rypMEvNLVGDAAEtlrallpllerkKDrsWRERIEKWVARWWETLEARAMVP-ADPVNPQRVFWELSPRLPDNAILTAD 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 768000693 361 GGDFVG-TAAHLVQPRGPLRWLDpGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:PRK08273 389 SGSCANwYARDLRMRRGMMASLS-GTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAM 445
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
1-103 |
1.26e-08 |
|
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: 53.89 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:cd06586 54 YARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPA 132
|
90 100
....*....|....*....|....
gi 768000693 81 T-LRAAMAAAQSgtPGPVFVELPV 103
Cdd:cd06586 133 GiDHAIRTAYAS--QGPVVVRLPR 154
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
2-438 |
1.48e-07 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 54.08 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPIL-LLGGAASTLLQNRGALQAvDQLSLFRPLCKFCVSVRRVRDIVP 80
Cdd:PRK07586 59 ARMAGKPAATLLHLGPGLANGLANLHNARRARTPIVnIVGDHATYHRKYDAPLTS-DIEALARPVSGWVRRSESAADVAA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 81 TLRAAMAAAQSGTPGPVFVELPVDVlypyfmvqkemvpakppkglvgrvvswylenylanlfagAWEP--QPEGPLPL-D 157
Cdd:PRK07586 138 DAAAAVAAARGAPGQVATLILPADV---------------------------------------AWSEggPPAPPPPApA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 158 IPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVET---LGVPCFLGGMARGllgRNHPLHIR-----EN 229
Cdd:PRK07586 179 PAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATgarLLAETFPARMERG---AGRPAVERlpyfaEQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 230 RSAALKKADVIVLAGT---VCDFrlSYgrvlshsskiiivnRNREEMLlnsdifwKPQEAVqgdvgsfVLKLVEGLQGQT 306
Cdd:PRK07586 256 ALAQLAGVRHLVLVGAkapVAFF--AY--------------PGKPSRL-------VPEGCE-------VHTLAGPGEDAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 307 WAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDF-VGTAAHLVQPRgPLRWLD-PG 384
Cdd:PRK07586 306 AALEALADALGAKPAAPPLAAPARPPLPTGALTPEAIAQVIAALLPENAIVVDESITSgRGFFPATAGAA-PHDWLTlTG 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768000693 385 afGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV 438
Cdd:PRK07586 385 --GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVI 436
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
370-515 |
7.58e-06 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 46.89 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 370 HLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAgWTQISR 449
Cdd:cd02006 43 HVYKPR---HWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIR 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768000693 450 EQVPSLGSNVACGLAY------------TDYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 515
Cdd:cd02006 119 QAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPEE--LAAAFEQAKKLMAEHRvPVVVEAILER 195
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
342-511 |
1.99e-04 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 42.68 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 342 QVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd02003 3 EVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 422 IEFDTFVRHKIPVMALVGNDAGWTQISREQVpSLGS---------------NVACGLAYTDYHKAAMGLGARglLLSREN 486
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQE-STGSgsfgtefrdrdqesgQLDGALLPVDFAANARSLGAR--VEKVKT 159
|
170 180
....*....|....*....|....*
gi 768000693 487 EDQVVKVLHDAQQQCRdghPVVVNI 511
Cdd:cd02003 160 IEELKAALAKAKASDR---TTVIVI 181
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
160-221 |
3.02e-04 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 41.47 E-value: 3.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768000693 160 QASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVP-CFLGGMARGLLGRN 221
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
1-102 |
6.72e-04 |
|
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: 40.56 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVR------R 74
Cdd:cd07037 54 LAKASGRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddD 133
|
90 100
....*....|....*....|....*...
gi 768000693 75 VRDIVPTLRAAMAAAQSGTPGPVFVELP 102
Cdd:cd07037 134 LWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
2-442 |
1.08e-03 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 41.51 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT 81
Cdd:PRK09124 61 AQLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 82 LRAAMAAAqSGTPGPVFVELPVDVLYpyfmvqkEMVPAKPPkglvgrvVSWYlenylanlfagawepqpEGPLPLDIPQA 161
Cdd:PRK09124 141 LAIAMRKA-ILNRGVAVVVLPGDVAL-------KPAPERAT-------PHWY-----------------HAPQPVVTPAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 162 SpqQVQRCVEILSRAKRPLMVLGSQallTPTSADKLRAAVETLGVPC---------------FLGGMArGLLGRNHPLHi 226
Cdd:PRK09124 189 E--ELRKLAALLNGSSNITLLCGSG---CAGAHDELVALAETLKAPIvhalrgkehveydnpYDVGMT-GLIGFSSGYH- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 227 renrsaALKKADVIVLAGTvcDFrlSYGRVLSHSSKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQT 306
Cdd:PRK09124 262 ------AMMNCDTLLMLGT--DF--PYRQFYPTDAKIIQIDINPGSLGRRSPV----DLGLVGDVKATLAALLPLLEEKT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 307 wAPDWVEELREADRQKEQTFREKA-AMPVAQHLNPVQVLQLVEETLPDNSILVVDggdfVGT----AAHLVQPRGPLRWL 381
Cdd:PRK09124 328 -DRKFLDKALEHYRKARKGLDDLAvPSDGGKPIHPQYLARQISEFAADDAIFTCD----VGTptvwAARYLKMNGKRRLL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768000693 382 DPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 442
Cdd:PRK09124 403 GSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
2-102 |
3.12e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 40.61 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768000693 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVP- 80
Cdd:PLN02980 359 ARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPa 438
|
90 100
....*....|....*....|....*..
gi 768000693 81 -----TLRAAMAAAQSGTPGPVFVELP 102
Cdd:PLN02980 439 rmvltTLDSAVHWATSSPCGPVHINCP 465
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
389-415 |
4.92e-03 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 39.02 E-value: 4.92e-03
10 20
....*....|....*....|....*..
gi 768000693 389 LGVGAGFALGAKLCRPDAEVWCLFGDG 415
Cdd:cd02012 111 LSVAVGMALAEKLLGFDYRVYVLLGDG 137
|
|
| |
