|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
3-554 |
2.25e-144 |
|
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: 427.65 E-value: 2.25e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 3 EIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLN 82
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDALRR-QSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEI 162
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDIWDKKINIDENNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNAR 242
Cdd:COG0028 161 PKDVQAAEAEEEPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 243 GICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGFN-LTPSESIVVISNDPSsELRPSYYET--IKA 319
Cdd:COG0028 241 GAFPEDHPLYLGMLGMHG-TPAANEALAEADLVLAVGARFDDRVTGNWDeFAPDAKIIHIDIDPA-EIGKNYPVDlpIVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 320 DPLVFLKELVNQLKRDTKNKkinDQWKKEIEKYKNDWDNLIKQTlkrkyRDAVNPALFFSKLNDALKRNRIIIGGQGTHV 399
Cdd:COG0028 319 DAKAVLAALLEALEPRADDR---AAWLARIAAWRAEYLAAYAAD-----DGPIKPQRVIAALREALPDDAIVVTDVGQHQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 400 LYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNSYR 479
Cdd:COG0028 391 MWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLG 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505044757 480 VLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLITSRDDMPP--TNTEM 554
Cdd:COG0028 471 MVRQWQELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALAsDGPALIDVRVDPEENPPgaTLDEM 548
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
4-549 |
8.01e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 248.52 E-value: 8.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 4 IKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEykNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNS 83
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYD--SDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 84 LTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYV----ESPDVFVEKFEKAMIdlfyGNPKPVV 159
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIkkpeEIPEIFRAAFEIAKT----GRPGPVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 160 LEIPEDIWDKKINIDENNFPN----ISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYI 235
Cdd:PRK06276 155 IDLPKDVQEGELDLEKYPIPAkidlPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 236 LTTGNARGICEEDHPRCIGRVGYGGGSLyADNALKSTDYLLVFGEGFDDITT---YGFnlTPSESIVVISNDPSsELRps 312
Cdd:PRK06276 235 CTTLMGKGAFPEDHPLALGMVGMHGTKA-ANYSVTESDVLIAIGCRFSDRTTgdiSSF--APNAKIIHIDIDPA-EIG-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 313 yyETIKAD-PLV-----FLKELVNQLKRdtKNKKINDQWKKEIEKYKndwdnliKQTLKR-KYRDA-VNPALFFSKLNDA 384
Cdd:PRK06276 309 --KNVRVDvPIVgdaknVLRDLLAELMK--KEIKNKSEWLERVKKLK-------KESIPRmDFDDKpIKPQRVIKELMEV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 385 LK-----RNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQ 459
Cdd:PRK06276 378 LReidpsKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 460 TIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNN-PDFAKLAESFGIRGIKISRDEEIDNSIKE-ILANGPIV 537
Cdd:PRK06276 458 TIAEYDIPVVICIFDNRTLGMVYQWQNLYYGKRQSEVHLGEtPDFVKLAESYGVKADRVEKPDEIKEALKEaIKSGEPYL 537
|
570
....*....|..
gi 505044757 538 VDLITSRDDMPP 549
Cdd:PRK06276 538 LDIIIDPAEALP 549
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-546 |
1.87e-73 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 244.30 E-value: 1.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 1 MVEIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYeyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGF 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELY--DSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 81 LNSLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVES----PDVFVEKFEKAMIdlfyGNPK 156
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDakdlPRIIKEAFHIAST----GRPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 157 PVVLEIPEDIWDKKINIDENNFPNI-SYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYI 235
Cdd:PRK06048 159 PVLIDLPKDVTTAEIDFDYPDKVELrGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 236 LTTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGF-NLTPSESIVVISNDPSsELRpsyy 314
Cdd:PRK06048 239 TTTLMGIGAIPTEHPLSLGMLGMHG-TKYANYAIQESDLIIAVGARFDDRVTGKLaSFAPNAKIIHIDIDPA-EIS---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 315 ETIKAD-PLV-----FLKELVNQLKRDTK---NKKINdQWKKEIE-KYKNDwdnlikqtlkrkyRDAVNPALFFSKLNDA 384
Cdd:PRK06048 313 KNVKVDvPIVgdakqVLKSLIKYVQYCDRkewLDKIN-QWKKEYPlKYKER-------------EDVIKPQYVIEQIYEL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 385 LKrNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDE 464
Cdd:PRK06048 379 CP-DAIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 465 NLDVKIIIVNdNSY--RVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILANG-PIVVDLI 541
Cdd:PRK06048 458 DIPVIVAILN-NGYlgMVRQWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDrPVVIDFI 536
|
....*
gi 505044757 542 TSRDD 546
Cdd:PRK06048 537 VECEE 541
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
9-546 |
2.10e-69 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 234.21 E-value: 2.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 9 ALARGLINLGIKRIYGVIGTTVLNFYDALY--EYKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:CHL00099 15 ALIDSLVRHGVKHIFGYPGGAILPIYDELYawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALnLYHYYV-----ESPDVFVEKFEKAMidlfYGNPKPVVLE 161
Cdd:CHL00099 95 IATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPI-VKHSYVvrdarDISRIVAEAFYIAK----HGRPGPVLID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 162 IPEDIWDKKIN----IDENNFPNI-SYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYIL 236
Cdd:CHL00099 170 IPKDVGLEKFDyyppEPGNTIIKIlGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 237 TTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGFNLTPSESIVV-ISNDPS--SELRPSY 313
Cdd:CHL00099 250 TTLMGKGIFDEDHPLCLGMLGMHG-TAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIhIDIDPAeiGKNRIPQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 314 YeTIKADPLVFLKELVNQLKRDTkNKKINDQ---WKKEIEKYKNDWDNLIKQTlkrkyRDAVNPALFFSKLNDaLKRNRI 390
Cdd:CHL00099 329 V-AIVGDVKKVLQELLELLKNSP-NLLESEQtqaWRERINRWRKEYPLLIPKP-----STSLSPQEVINEISQ-LAPDAY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 391 IIGGQGTHVLYTYDYMKVYEfGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKI 470
Cdd:CHL00099 401 FTTDVGQHQMWAAQFLKCKP-RKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 471 IIVNDN------SYRVLYLKQLINKSNRIYGTelnnPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLITS 543
Cdd:CHL00099 480 IIINNKwqgmvrQWQQAFYGERYSHSNMEEGA----PDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDyDGPVLIDCQVI 555
|
...
gi 505044757 544 RDD 546
Cdd:CHL00099 556 EDE 558
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
3-558 |
4.25e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 229.99 E-value: 4.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 3 EIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLN 82
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYK-QNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESpdvfVEKFEKAMIDLFY----GNPKPV 158
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKS----IEELPRILKEAFYiarsGRPGPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 159 VLEIPEDI--------WDKKINIdennfpnISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEI 230
Cdd:PRK08527 157 HIDIPKDVtatlgefeYPKEISL-------KTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 231 TDSYILTTGNARGICEEDHPRCIGRVGYGGGslYADN-ALKSTDYLLVFGEGFDD-ITTYGFNLTPSESIVVISNDPSS- 307
Cdd:PRK08527 230 TGIPAVETLMARGVLRSDDPLLLGMLGMHGS--YAANmAMSECDLLISLGARFDDrVTGKLSEFAKHAKIIHVDIDPSSi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 308 -ELRPSYYeTIKADPLVFLKELVNQLKrDTKNKKINdQWKKEIEKYK-------NDWDNLIKqtlkrkyrdavnPALFFS 379
Cdd:PRK08527 308 sKIVNADY-PIVGDLKNVLKEMLEELK-EENPTTYK-EWREILKRYNelhplsyEDSDEVLK------------PQWVIE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 380 KLNDALKRNRIIIGGQGTHVLYTYDYmkvYEFG---GFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIE 456
Cdd:PRK08527 373 RVGELLGDDAIISTDVGQHQMWVAQF---YPFNyprQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 457 ALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELN-NPDFAKLAESFGIRGIKISRDEEIDNSIKEILANGP 535
Cdd:PRK08527 450 ELMTAVEYKIPVINIILNNNFLGMVRQWQTFFYEERYSETDLStQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDK 529
|
570 580
....*....|....*....|....
gi 505044757 536 I-VVDLITSRddmpptnTEMVLKM 558
Cdd:PRK08527 530 VaLIDVKIDR-------FENVLPM 546
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
18-550 |
1.20e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 223.95 E-value: 1.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 18 GIKRIYGVIGTTVLNFYDALYEY--KNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGLGIAMKDRS 95
Cdd:PRK06456 16 GVKVIFGIPGLSNMQIYDAFVEDlaNGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGLITAYWDSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 96 RLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPEDIWDKKIniDE 175
Cdd:PRK06456 96 PVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPRDIFYEKM--EE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 176 NNFPNISYEK-----EENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNARGICEEDHP 250
Cdd:PRK06456 174 IKWPEKPLVKgyrdfPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFPGKTAIPHDHP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 251 RCIGRVGYGGGSLYADNALKStDYLLVFGEGFDD--ITTYGFNLTPSESIVVISNDPSSELRPSYYET-IKADPLVFLKE 327
Cdd:PRK06456 254 LYFGPMGYYGRAEASMAALES-DAMLVVGARFSDrtFTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVgIYGNAKIILRE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 328 LVNQLkRDTKNKKINDQWKKEIEKYKNDWDNLIKQTLKRKYRdavnPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMK 407
Cdd:PRK06456 333 LIKAI-TELGQKRDRSAWLKRVKEYKEYYSQFYYTEENGKLK----PWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 408 VYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVkIIIVNDNsyRVLYL---K 484
Cdd:PRK06456 408 VLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPV-ISVIFDN--RTLGLvrqV 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505044757 485 QLINKSNRIYGTEL-NNPDFAKLAESFGIRGIKISRDEEIDNSIKE-ILANGPIVVDLITSRDDMP-PT 550
Cdd:PRK06456 485 QDLFFGKRIVGVDYgPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSaIKEDIPAVIRVPVDKEELAlPT 553
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-557 |
5.23e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 222.15 E-value: 5.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 3 EIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEykNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLN 82
Cdd:PRK06725 14 EVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE--SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESpdvfVEKFEKAMIDLFY----GNPKPV 158
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRD----VNQLSRIVQEAFYiaesGRPGPV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 159 VLEIPEDIWDKKINIDENNFPNI-SYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILT 237
Cdd:PRK06725 168 LIDIPKDVQNEKVTSFYNEVVEIpGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 238 TGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGFNL-TPSESIVVISNDPSSelrpsYYET 316
Cdd:PRK06725 248 TLMGLGAYPPGDPLFLGMLGMHG-TYAANMAVTECDLLLALGVRFDDRVTGKLELfSPHSKKVHIDIDPSE-----FHKN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 317 IKAD-PLVF-LKELVNQLKRDTKNKKiNDQWKKEIEKYKNDWDNLIKQTlkrkyRDAVNPALFFSKLNDALKRNRIIIGG 394
Cdd:PRK06725 322 VAVEyPVVGdVKKALHMLLHMSIHTQ-TDEWLQKVKTWKEEYPLSYKQK-----ESELKPQHVINLVSELTNGEAIVTTE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 395 QGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVN 474
Cdd:PRK06725 396 VGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIIN 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 475 DNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILAN-GPIVVDLITSRDD-----MP 548
Cdd:PRK06725 476 NKFLGMVRQWQEMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHeGPVVVDFCVEEGEnvfpmVP 555
|
570
....*....|.
gi 505044757 549 PT--NTEMVLK 557
Cdd:PRK06725 556 PNkgNNEMIMK 566
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
1-555 |
5.76e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 219.31 E-value: 5.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 1 MVEIKL------SEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKENVAISAADAEYRTTKKPAAAVV 74
Cdd:PRK07282 1 MEKISLespksgSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEG-IRHILARHEQGALHEAEGYAKSTGKLGVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 75 HAGGGFLNSLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYV----ESPDVFVEKFEKAMIdl 150
Cdd:PRK07282 80 TSGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIretaDIPRIITEAVHIATT-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 151 fyGNPKPVVLEIPEDIWDKK---INIDENNFPniSYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYEL 227
Cdd:PRK07282 158 --GRPGPVVIDLPKDVSALEtdfIYDPEVNLP--SYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 228 SEITDSYILTTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTyGFNLTPSESIVV--ISNDP 305
Cdd:PRK07282 234 AERYQIPVVTTLLGQGTIATSHPLFLGMGGMHG-SYAANIAMTEADFMINIGSRFDDRLT-GNPKTFAKNAKVahIDIDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 306 SsELRpsyyETIKAD-PLVF-LKELVNQLKRDTKNKKINDQWKKEIEKYKNdwdnliKQTLKRKYRDAVNPALFFSKLND 383
Cdd:PRK07282 312 A-EIG----KIIKTDiPVVGdAKKALQMLLAEPTVHNNTEKWIEKVTKDKN------RVRSYDKKERVVQPQAVIERIGE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 384 ALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKD 463
Cdd:PRK07282 381 LTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 464 ENLDVKIIIVNDNSYRVLYLKQLI----NKSNRIYGTElnnPDFAKLAESFGIRGIKISRDEEIDNSIKEILANGPIVVD 539
Cdd:PRK07282 461 YKVPIKVVMLNNHSLGMVRQWQESfyegRTSESVFDTL---PDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDVPMLIE 537
|
570 580
....*....|....*....|...
gi 505044757 540 LITSRDD----MPPT---NTEMV 555
Cdd:PRK07282 538 VDISRKEhvlpMVPAgksNHEML 560
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
7-532 |
7.27e-62 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 213.53 E-value: 7.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHE-KSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPEDI 166
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 167 WDKKINIDEnNFPNI----SYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNAR 242
Cdd:PRK08979 166 LNPAILHPY-EYPESikmrSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 243 GICEEDHPRCIGRVGYGGgsLY-ADNALKSTDylLVFGEG--FDDITTYGFN-LTPSESIVVISNDPSselrpSYYETIK 318
Cdd:PRK08979 245 GAFPGTHKNSLGMLGMHG--RYeANMAMHNAD--LIFGIGvrFDDRTTNNLEkYCPNATILHIDIDPS-----SISKTVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 319 AD-PLV-----FLKELVNQL--KRDTKNKKINDQWKKEIEKYKNdwdnliKQTLK-RKYRDAVNPALFFSKLNDALKRNR 389
Cdd:PRK08979 316 VDiPIVgsadkVLDSMLALLdeSGETNDEAAIASWWNEIEVWRS------RNCLAyDKSSERIKPQQVIETLYKLTNGDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 390 IIIGGQGTHVLYTYDYmkvYEFGG---FMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENL 466
Cdd:PRK08979 390 YVASDVGQHQMFAALY---YPFDKprrWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505044757 467 DVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNN-PDFAKLAESFGIRGIKISRDEEIDNSIKEILA 532
Cdd:PRK08979 467 PVKIINLNNRFLGMVKQWQDMIYQGRHSHSYMDSvPDFAKIAEAYGHVGIRISDPDELESGLEKALA 533
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
8-532 |
1.88e-61 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 212.68 E-value: 1.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:PRK06466 8 EMLVRALRDEGVEYIYGYPGGAVLHIYDALFK-QDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 88 GIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAmidlFY----GNPKPVVLEIP 163
Cdd:PRK06466 87 ATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKA----FYiaqsGRPGPVVVDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 164 ED----------IWDKKINIDennfpniSYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDS 233
Cdd:PRK06466 163 KDmtnpaekfeyEYPKKVKLR-------SYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 234 YILTTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGF-NLTPSESIVVISNDPSSelrps 312
Cdd:PRK06466 236 PVTNTLMGLGGFPGTDRQFLGMLGMHG-TYEANMAMHHADVILAVGARFDDRVTNGPaKFCPNAKIIHIDIDPAS----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 313 YYETIKAD-PLV-----FLKELVNQLKRDTK--NKKINDQWKKEIE---------KYKNDWDNLIKqtlkrkyrdavnPA 375
Cdd:PRK06466 310 ISKTIKADiPIVgpvesVLTEMLAILKEIGEkpDKEALAAWWKQIDewrgrhglfPYDKGDGGIIK------------PQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 376 LFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSI 455
Cdd:PRK06466 378 QVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNI 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505044757 456 EALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNN-PDFAKLAESFGIRGIKISRDEEIDNSIKEILA 532
Cdd:PRK06466 458 QELSTCLQYGLPVKIINLNNGALGMVRQWQDMQYEGRHSHSYMESlPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFA 535
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-548 |
3.18e-60 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 209.09 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 1 MVEIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGF 80
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 81 LNSLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAmIDLFYGNPKPVVL 160
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQA-IRTAYEKKGVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 161 EIPEDIWDKKINIDENNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSneVNFENSRSYIYELSEITDSYILTTGN 240
Cdd:PRK08611 160 TIPDDLPAQKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAG--LGAKHAKEELLAFAEKAKIPIIHTLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 241 ARGICEEDHPRCIGRVGYgGGSLYADNALKSTDYLLVFGegfddiTTYGF-NLTPSE-SIVVISNDPSS-ELRPSYYETI 317
Cdd:PRK08611 238 AKGIIPDDHPYSLGNLGK-IGTKPAYEAMQEADLLIMVG------TNYPYvDYLPKKaKAIQIDTDPANiGKRYPVNVGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 318 KADPLVFLKELVNQLKRDTKNKKIN------DQWKKEIEKYKNDWDNLIKqtlkrkyrdavnPALFFSKLNDALKRNRII 391
Cdd:PRK08611 311 VGDAKKALHQLTENIKHVEDRRFLEacqenmAKWWKWMEEDENNASTPIK------------PERVMAAIQKIADDDAVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 392 IGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKII 471
Cdd:PRK08611 379 SVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505044757 472 IVNDNSYRVLYLKQLInKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKE-ILANGPIVVDLITSRDDMP 548
Cdd:PRK08611 459 VLNNQQLAFIKYEQQA-AGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEaLAQDKPVIIDVYVDPNAAP 535
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-555 |
1.20e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 202.97 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALY--EYKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PRK07418 23 YALMDSLKRHGVKHIFGYPGGAILPIYDELYkaEAEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNLVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPD----VFVEKFEKAMIdlfyGNPKPVVLE 161
Cdd:PRK07418 103 GIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSdmarIVAEAFHIASS----GRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 162 IPEDIWDKKIN---IDENNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTT 238
Cdd:PRK07418 179 IPKDVGQEEFDyvpVEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 239 GNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGFN-LTPSESIVVISNDPSsEL----RPSY 313
Cdd:PRK07418 259 LMGKGAFDEHHPLSVGMLGMHG-TAYANFAVTECDLLIAVGARFDDRVTGKLDeFASRAKVIHIDIDPA-EVgknrRPDV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 314 yeTIKADPLVFLKELVNQLKRDTKNKKiNDQWKKEIEKYKNDWDNLIKQtlkrkYRDAVNPALFFSKLNDaLKRNRIIIG 393
Cdd:PRK07418 337 --PIVGDVRKVLVKLLERSLEPTTPPR-TQAWLERINRWKQDYPLVVPP-----YEGEIYPQEVLLAVRD-LAPDAYYTT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 394 GQGTHVLYTYDYMKVyefG--GFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKII 471
Cdd:PRK07418 408 DVGQHQMWAAQFLRN---GprRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 472 IVNDN------SYRVLYLKQLINKSNRIYGTelnnPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLITSR 544
Cdd:PRK07418 485 IINNGwqgmvrQWQESFYGERYSASNMEPGM----PDFVKLAEAFGVKGMVISERDQLKDAIAEALAhDGPVLIDVHVRR 560
|
570
....*....|....*...
gi 505044757 545 DD-----MPP--TNTEMV 555
Cdd:PRK07418 561 DEncypmVPPgkSNAQMV 578
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
8-559 |
4.20e-56 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 197.41 E-value: 4.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARglinLGIKRIYGVIGTTVLNFYDALYEykNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:PRK08978 9 HALRA----QGVDTVFGYPGGAIMPVYDALYD--GGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 88 GIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVES----PDVFVEKFEKAMidlfYGNPKPVVLEIP 163
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSleelPEIMAEAFEIAS----SGRPGPVLVDIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 164 EDiwdkkINIDENNFPNI--SYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNA 241
Cdd:PRK08978 159 KD-----IQLAEGELEPHltTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 242 RGICEEDHPRCIGRVGYGGGSlyADN-ALKSTDYLLVFGEGFDDITTYGFN-LTPSESIVVISNDPS--SELRPSYYeTI 317
Cdd:PRK08978 234 LGAVEADHPYYLGMLGMHGTK--AANlAVQECDLLIAVGARFDDRVTGKLNtFAPHAKVIHLDIDPAeiNKLRQAHV-AL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 318 KADplvfLKELVNQLkrdTKNKKInDQWKKEIekykndwdnlikQTLKRKYR-------DAVNPALFFSKLNDALKRNRI 390
Cdd:PRK08978 311 QGD----LNALLPAL---QQPLNI-DAWRQHC------------AQLRAEHAwrydhpgEAIYAPALLKQLSDRKPADTV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 391 IIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKI 470
Cdd:PRK08978 371 VTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 471 IIVnDNSyRVLYLKQ----LINKsnRIYGTELN-NPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLITSR 544
Cdd:PRK08978 451 VLL-DNQ-RLGMVRQwqqlFFDE--RYSETDLSdNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNsEGPYLLHVSIDE 526
|
570 580
....*....|....*....|..
gi 505044757 545 DD-----MPP--TNTEMVLKMD 559
Cdd:PRK08978 527 LEnvwplVPPgaSNSEMLEKLS 548
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-546 |
1.27e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 196.90 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 6 LSEALARGlinlGIKRIYGVIGTTVLNFYDALYeyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PRK07710 22 LIEALEKE----GVEVIFGYPGGAVLPLYDALY--DCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYV----ESPDVFVEKFEKAMIdlfyGNPKPVVLE 161
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVrkasDLPRIIKEAFHIATT----GRPGPVLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 162 IPEDIWDKKINID---ENNFPniSYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTT 238
Cdd:PRK07710 172 IPKDMVVEEGEFCydvQMDLP--GYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 239 GNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGFN-LTPSESIVVISNDPSsELRPSYYETI 317
Cdd:PRK07710 250 LLGLGGFPADHPLFLGMAGMHG-TYTANMALYECDLLINIGARFDDRVTGNLAyFAKEATVAHIDIDPA-EIGKNVPTEI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 318 K--ADPLVFLKELVNQlkrdtKNKKIN-DQWKKEIEKYKNDWDNLIKQTlkrkyRDAVNPALFFSKLNDALKRNRIIIGG 394
Cdd:PRK07710 328 PivADAKQALQVLLQQ-----EGKKENhHEWLSLLKNWKEKYPLSYKRN-----SESIKPQKAIEMLYEITKGEAIVTTD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 395 QGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVN 474
Cdd:PRK07710 398 VGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILN 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505044757 475 DNSYRVLYLKQLINKSNRiYGTEL--NNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLITSRDD 546
Cdd:PRK07710 478 NEALGMVRQWQEEFYNQR-YSHSLlsCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIElQEPVVIDCRVLQSE 551
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
7-539 |
4.95e-54 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 193.00 E-value: 4.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK09107 14 AEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQ-QDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESpdvfVEKFEKAMIDLFY----GNPKPVVLEI 162
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKD----VNDLARVIHEAFHvatsGRPGPVVVDI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDI------WDKKINIDENnfpnISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEV---NFENSRsYIYELSEITDS 233
Cdd:PRK09107 169 PKDVqfatgtYTPPQKAPVH----VSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVinsGPEASR-LLRELVELTGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 234 YILTTGNARGICEEDHPRCIGRVGYGGgsLY-ADNALKSTDYLLVFGEGFDD-ITTYGFNLTPSESIVVISNDPSSelrp 311
Cdd:PRK09107 244 PITSTLMGLGAYPASGKNWLGMLGMHG--TYeANMAMHDCDVMLCVGARFDDrITGRLDAFSPNSKKIHIDIDPSS---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 312 sYYETIKAD-PLV-----FLKELVNQLKRDTK--NKKINDQWKKEIEKYKNdwdnliKQTLK-RKYRDAVNPALFFSKLN 382
Cdd:PRK09107 318 -INKNVRVDvPIIgdvghVLEDMLRLWKARGKkpDKEALADWWGQIARWRA------RNSLAyTPSDDVIMPQYAIQRLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 383 DALK-RNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTI 461
Cdd:PRK09107 391 ELTKgRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 462 KDENLDVKIIIVNdNSY--RVLYLKQLI--NKSNRIYGTELnnPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPI 536
Cdd:PRK09107 471 VQYNLPVKIFILN-NQYmgMVRQWQQLLhgNRLSHSYTEAM--PDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDvDKPV 547
|
...
gi 505044757 537 VVD 539
Cdd:PRK09107 548 IFD 550
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
3-529 |
4.78e-53 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 190.01 E-value: 4.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 3 EIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLN 82
Cdd:PRK06965 20 DSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYK-QDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEI 162
Cdd:PRK06965 99 AVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDIWDKKInidENNFPNI----SYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTT 238
Cdd:PRK06965 179 PKDVSKTPC---EYEYPKSvemrSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 239 GNARGICEEDHPRCIGRVGYgGGSLYADNALKSTDYLLVFGEGFDD--ITTYGFNLTPSESIVVISNDPSselrpSYYET 316
Cdd:PRK06965 256 LMGLGAYPASDKKFLGMLGM-HGTYEANMAMQHCDVLIAIGARFDDrvIGNPAHFASRPRKIIHIDIDPS-----SISKR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 317 IKAD-PLV-----FLKELVNQLKRDTKNKKIN--DQWKKEIEKYKNdwdnliKQTLKRKYRDAV-NPALFFSKLNDALKR 387
Cdd:PRK06965 330 VKVDiPIVgdvkeVLKELIEQLQTAEHGPDADalAQWWKQIEGWRS------RDCLKYDRESEIiKPQYVVEKLWELTDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 388 NRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLD 467
Cdd:PRK06965 404 DAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTP 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505044757 468 VKIIIVNDNSYRVLYLKQLINKSNRIYGTELNN-PDFAKLAESFGIRGIKISRDEEIDNSIKE 529
Cdd:PRK06965 484 VKIISLNNRYLGMVRQWQEIEYSKRYSHSYMDAlPDFVKLAEAYGHVGMRIEKTSDVEPALRE 546
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
6-549 |
5.27e-53 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 189.27 E-value: 5.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 6 LSEALARGLINLGIKRIYGVIGTTVLNFYDALYeyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PRK06457 4 VAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIR--KSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFygNPKPVV-LEIPE 164
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAI--SKRGVAhINLPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 165 DIWDKKINIDennfPNISYEKEENVNEEDVKRVKEEILKSNKPLILV-------SNEVNfensrsyiyELSEITDSYILT 237
Cdd:PRK06457 160 DILRKSSEYK----GSKNTEVGKVKYSIDFSRAKELIKESEKPVLLIgggtrglGKEIN---------RFAEKIGAPIIY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 238 TGNARGICEEDHPRCIGRVGYGGGSLYADnALKSTDYLLVFGEGFdditTYGFNLTPSESIVVISNDPSSelrpsYYETI 317
Cdd:PRK06457 227 TLNGKGILPDLDPKVMGGIGLLGTKPSIE-AMDKADLLIMLGTSF----PYVNFLNKSAKVIQVDIDNSN-----IGKRL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 318 KAD-PLVFLKELVNQLKRDTKNKKI-------NDQWKKEIEKYKNDWDNLIKqtlkrkyrdavnPALFFSKLNDALKRNR 389
Cdd:PRK06457 297 DVDlSYPIPVAEFLNIDIEEKSDKFyeelkgkKEDWLDSISKQENSLDKPMK------------PQRVAYIVSQKCKKDA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 390 IIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKI-SNPDREVIAIIGDGEALMSIEALQTIKDENLDV 468
Cdd:PRK06457 365 VIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFaVENKRQVISFVGDGGFTMTMMELITAKKYDLPV 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 469 KIIIVNDNSYRVLYLKQLINKSNRiYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEIL-ANGPIVVDLITSRDD- 546
Cdd:PRK06457 445 KIIIYNNSKLGMIKFEQEVMGYPE-WGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLnTKGPAVLDAIVDPNEr 523
|
....
gi 505044757 547 -MPP 549
Cdd:PRK06457 524 pMPP 527
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
8-548 |
8.87e-53 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 188.30 E-value: 8.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:PRK08266 8 EAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGAAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 88 GIAMKDRSRLLLITGSVKRRL--KNTDSWLEV-DQ----EGLSKALNLYHYYVESPDVFVEKFEKAMidlfYGNPKPVVL 160
Cdd:PRK08266 88 LTAYGCNSPVLCLTGQIPSALigKGRGHLHEMpDQlatlRSFTKWAERIEHPSEAPALVAEAFQQML----SGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 161 EIPEDIWDKKIniDENNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILV-------SNEVNfensrsyiyELSEITDS 233
Cdd:PRK08266 164 EMPWDVFGQRA--PVAAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVgggaagaGEEIR---------ELAEMLQA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 234 YILTTGNARGICEEDHPrcigrvgYGGGSLYADNALKSTDYLLVFGEGFDDITTYGFNLTPSESIVVISNDPSSELRPSY 313
Cdd:PRK08266 233 PVVAFRSGRGIVSDRHP-------LGLNFAAAYELWPQTDVVIGIGSRLELPTFRWPWRPDGLKVIRIDIDPTEMRRLKP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 314 YETIKADPLVFLKELVNQLKRdtKNKKINDQwKKEIEKYKNDWDNLIkqtlkrkyrDAVNPALFFSK-LNDALKRNRIII 392
Cdd:PRK08266 306 DVAIVADAKAGTAALLDALSK--AGSKRPSR-RAELRELKAAARQRI---------QAVQPQASYLRaIREALPDDGIFV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 393 GgQGTHVLYTYDY-MKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKII 471
Cdd:PRK08266 374 D-ELSQVGFASWFaFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505044757 472 IVNDNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILANG-PIVVDLITSRDDMP 548
Cdd:PRK08266 453 VFNNNAYGNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGgPVLIEVPVPRGSEA 530
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-541 |
2.25e-52 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 188.02 E-value: 2.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 6 LSEALARGlinlGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PLN02470 19 LVEALERE----GVDTVFAYPGGASMEIHQALTR-SNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYV----ESPDVFVEKFEKAMidlfYGNPKPVVLE 161
Cdd:PLN02470 94 GLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVmdveDIPRVIREAFFLAS----SGRPGPVLVD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 162 IPEDI--------WDKKINIdennfPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNevNFENSRSYIYELSEITDS 233
Cdd:PLN02470 170 IPKDIqqqlavpnWNQPMKL-----PGYLSRLPKPPEKSQLEQIVRLISESKRPVVYVGG--GCLNSSEELREFVELTGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 234 YILTTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITTYGFNLTPSE-SIVVISNDPSsEL--- 309
Cdd:PLN02470 243 PVASTLMGLGAFPASDELSLQMLGMHG-TVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRaSIVHIDIDPA-EIgkn 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 310 -RPsyYETIKADPLVFLKELvNQLKRDTKNKKIN-DQWKKEIEKYKNDWDNLIKQtlkrkYRDAVNPALFFSKLNDALKR 387
Cdd:PLN02470 321 kQP--HVSVCADVKLALQGL-NKLLEERKAKRPDfSAWRAELDEQKEKFPLSYPT-----FGDAIPPQYAIQVLDELTDG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 388 NRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLD 467
Cdd:PLN02470 393 NAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 468 VKIIIVNDNsyrvlYLKQLINKSNRIYG-----TELNN--------PDFAKLAESFGIRGIKISRDEEIDNSIKEIL-AN 533
Cdd:PLN02470 473 VKIMVLNNQ-----HLGMVVQWEDRFYKanrahTYLGDpdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLdTP 547
|
....*...
gi 505044757 534 GPIVVDLI 541
Cdd:PLN02470 548 GPYLLDVI 555
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-532 |
5.80e-52 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 186.66 E-value: 5.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 1 MVEIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGF 80
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGG-IEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 81 LNSLTGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVL 160
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 161 EIPEDI----------WDKKINIDENNfPNISYEKEEnvneedVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEI 230
Cdd:PRK06882 160 DIPKDMvnpankftyeYPEEVSLRSYN-PTVQGHKGQ------IKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 231 TDSYILTTGNARGICEEDHPRCIGRVGYgGGSLYADNALKSTDYLLVFGEGFDDITTYGF-NLTPSESIVVISNDPSsel 309
Cdd:PRK06882 233 LNLPVTSSLMGLGAYPSTDKQFLGMLGM-HGTYEANNAMHESDLILGIGVRFDDRTTNNLaKYCPNAKVIHIDIDPT--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 310 rpSYYETIKAD-PLV-----FLKELVNQLKRD--TKNKKINDQWKKEIEKYKndwdnlIKQTLK-RKYRDAVNPALFFSK 380
Cdd:PRK06882 309 --SISKNVPAYiPIVgsaknVLEEFLSLLEEEnlAKSQTDLTAWWQQINEWK------AKKCLEfDRTSDVIKPQQVVEA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 381 LNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQT 460
Cdd:PRK06882 381 IYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELST 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505044757 461 IKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNN-PDFAKLAESFGIRGIKISRDEEIDNSIKEILA 532
Cdd:PRK06882 461 AKQYDIPVVIVSLNNRFLGMVKQWQDLIYSGRHSQVYMNSlPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFS 533
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
377-542 |
1.55e-50 |
|
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: 171.28 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 377 FFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIE 456
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 457 ALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGP 535
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAaGGP 161
|
....*..
gi 505044757 536 IVVDLIT 542
Cdd:cd00568 162 ALIEVKT 168
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
7-555 |
2.14e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 179.52 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKnEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK08155 16 AELIVRLLERQGIRIVTGIPGGAILPLYDALSQST-QIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYV----ESPDVFVEKFEKAMidlfYGNPKPVVLEI 162
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVrdieELPQVISDAFRIAQ----SGRPGPVWIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDIWDKKINIDENNFPNISyEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNAR 242
Cdd:PRK08155 171 PKDVQTAVIELEALPAPAEK-DAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 243 GICEEDHPRCIGRVGYGGGSlYADNALKSTDYLLVFGEGFDDIT---TYGFnlTPSESIVVISNDPS--SELRPSYYeTI 317
Cdd:PRK08155 250 GMLPKAHPLSLGMLGMHGAR-STNYILQEADLLIVLGARFDDRAigkTEQF--CPNAKIIHVDIDRAelGKIKQPHV-AI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 318 KADPLVFLKELVNQLKRDTKNkkindQWKKEIEKYKNDWDNLIKQTlkrkyRDAVNPALFFSKLNDALKRNRIIIGGQGT 397
Cdd:PRK08155 326 QADVDDVLAQLLPLVEAQPRA-----EWHQLVADLQREFPCPIPKA-----DDPLSHYGLINAVAACVDDNAIITTDVGQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 398 HVLYTydyMKVYEFGG---FMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVN 474
Cdd:PRK08155 396 HQMWT---AQAYPLNRprqWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 475 DNSYRVLYLKQLINKSNRIYGTEL-NNPDFAKLAESFGIRGIKISRDEEIDNSIKEILAN-GPIvvdLITSRDDM----- 547
Cdd:PRK08155 473 NEALGLVHQQQSLFYGQRVFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRpGPA---LIHVRIDAeekvy 549
|
570
....*....|...
gi 505044757 548 ---PP--TNTEMV 555
Cdd:PRK08155 550 pmvPPgaANTEMI 562
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
7-532 |
2.10e-48 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 176.96 E-value: 2.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGG-IDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPEDI 166
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 167 ----------WDKKINIDENNfPNISYEKEEnvneedVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYIL 236
Cdd:PRK07979 166 lnpanklpyvWPESVSMRSYN-PTTQGHKGQ------IKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 237 TTGNARGICEEDHPRCIGRVGYgGGSLYADNALKSTDYLLVFGEGFDDITTYgfNLT---PSESIVVISNDPSselrpSY 313
Cdd:PRK07979 239 SSLMGLGAFPATHRQSLGMLGM-HGTYEANMTMHNADVIFAVGVRFDDRTTN--NLAkycPNATVLHIDIDPT-----SI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 314 YETIKAD-PLV-----FLKELVNQLKRDTKNKKIND--QWKKEIEKYKNdwdnliKQTLK-RKYRDAVNPALFFSKLNDA 384
Cdd:PRK07979 311 SKTVTADiPIVgdarqVLEQMLELLSQESAHQPLDEirDWWQQIEQWRA------RQCLKyDTHSEKIKPQAVIETLWRL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 385 LKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDE 464
Cdd:PRK07979 385 TKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQY 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505044757 465 NLDVKIIIVNDNsyrvlYLKQLINKSNRIYGTELNN------PDFAKLAESFGIRGIKISRDEEIDNSIKEILA 532
Cdd:PRK07979 465 ELPVLVLNLNNR-----YLGMVKQWQDMIYSGRHSQsymqslPDFVRLAEAYGHVGIQISHPDELESKLSEALE 533
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
7-547 |
6.37e-47 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 173.63 E-value: 6.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKnEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK07789 34 AQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDST-KVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPD----VFVEKFEKAMIdlfyGNPKPVVLEI 162
Cdd:PRK07789 113 IADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADdiprVIAEAFHIAST----GRPGPVLVDI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDI--------WDKKINIdennfPniSYEkeeNVNEEDVKRVKEE---ILKSNKPLILVSNEVNFENSRSYIYELSEIT 231
Cdd:PRK07789 189 PKDAlqaqttfsWPPRMDL-----P--GYR---PVTKPHGKQIREAaklIAAARRPVLYVGGGVIRAEASAELRELAELT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 232 DSYILTTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDD-ITTYGFNLTPSESIVVISNDPS--SE 308
Cdd:PRK07789 259 GIPVVTTLMARGAFPDSHPQHLGMPGMHG-TVAAVAALQRSDLLIALGARFDDrVTGKLDSFAPDAKVIHADIDPAeiGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 309 LRpsyyetiKAD-PLV-----FLKELVNQLKRDTKNKKIND--QWKKEIekykNDWdnliKQTLKRKYRD----AVNPAL 376
Cdd:PRK07789 338 NR-------HADvPIVgdvkeVIAELIAALRAEHAAGGKPDltAWWAYL----DGW----RETYPLGYDEpsdgSLAPQY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 377 FFSKLNDALKRNRIIIGGQGTHVLYTYDYMKvYE-------FGGfmaatnLGSMGFALPAAIGAKISNPDREVIAIIGDG 449
Cdd:PRK07789 403 VIERLGEIAGPDAIYVAGVGQHQMWAAQFID-YEkprtwlnSGG------LGTMGYAVPAAMGAKVGRPDKEVWAIDGDG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 450 EALMSIEALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNN-----PDFAKLAESFGIRGIKISRDEEID 524
Cdd:PRK07789 476 CFQMTNQELATCAIEGIPIKVALINNGNLGMVRQWQTLFYEERYSNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVD 555
|
570 580
....*....|....*....|....*
gi 505044757 525 NSIKEILA--NGPIVVDLITSRDDM 547
Cdd:PRK07789 556 AVIEKARAinDRPVVIDFVVGKDAM 580
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
8-552 |
2.82e-45 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 167.74 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:PRK08199 12 QILVDALRANGVERVFCVPGESYLAVLDALHD-ETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASIGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 88 GIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQE----GLSKalnlyhYYVESPDV-----FVEK-FEKAMidlfYGNPKP 157
Cdd:PRK08199 91 HTAFQDSTPMILFVGQVARDFREREAFQEIDYRrmfgPMAK------WVAEIDDAaripeLVSRaFHVAT----SGRPGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 158 VVLEIPEDIWDkkiniDENNFPNISYEK--EENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYI 235
Cdd:PRK08199 161 VVLALPEDVLS-----ETAEVPDAPPYRrvAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 236 LTTGNARGICEEDHPRCIGRVGYGggslyADNAL----KSTDYLLVFGEGFDDITTYGFNL----TPSESIVVISNDPSs 307
Cdd:PRK08199 236 ACAFRRQDLFDNRHPNYAGDLGLG-----INPALaariREADLVLAVGTRLGEVTTQGYTLldipVPRQTLVHVHPDAE- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 308 ELRPSYYET--IKADPLVFLKELvnqLKRDTKNKKINDQWKKEIEKYKNDWdnlikqTLKRKYRDAVNPALFFSKLNDAL 385
Cdd:PRK08199 310 ELGRVYRPDlaIVADPAAFAAAL---AALEPPASPAWAEWTAAAHADYLAW------SAPLPGPGAVQLGEVMAWLRERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 386 KRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNlGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDEN 465
Cdd:PRK08199 381 PADAIITNGAGNYATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 466 LDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILANG-PIVVDLITSR 544
Cdd:PRK08199 460 LPIIVIVVNNGMYGTIRMHQEREYPGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGkPALIEIRIDP 539
|
....*...
gi 505044757 545 DDMPPTNT 552
Cdd:PRK08199 540 EAITPTAT 547
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-174 |
1.63e-43 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 152.39 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 6 LSEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPG-IRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDsWL--EVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIP 163
Cdd:pfam02776 80 GLANAYVDSVPLLVISGQRPRSLVGRG-ALqqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIP 158
|
170
....*....|.
gi 505044757 164 EDIWDKKINID 174
Cdd:pfam02776 159 LDVLLEEVDED 169
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
10-549 |
1.65e-43 |
|
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: 162.64 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 10 LARGLINLGIKRIYGVIGTTVLNFYDALYEYKnEIKQITVRKENVAISAADAeYRTTKKPAAAVVHAGGGFLNSLTGLGI 89
Cdd:COG3961 11 LLDRLAELGIRHIFGVPGDYNLPFLDAIEAHP-GIRWVGCCNELNAGYAADG-YARVNGLGALVTTYGVGELSAINGIAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 90 AMKDRSRLLLITGSVKRRLKNTDSwlevdqeglskalnLYH-------YyvespDVFVEKFEK--------------AMI 148
Cdd:COG3961 89 AYAERVPVVHIVGAPGTRAQRRGP--------------LLHhtlgdgdF-----DHFLRMFEEvtvaqavltpenaaAEI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 149 D------LFYGnpKPVVLEIPEDIWDKKINIDENNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRS 222
Cdd:COG3961 150 DrvlaaaLREK--RPVYIELPRDVADAPIEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 223 YIYELSEITDSYILTTGNARGICEEDHPRCIGrvGYGG--GSLYADNALKSTDYLLVFGEGFDDITTYGF--NLTPSESI 298
Cdd:COG3961 228 ELLALAEKTGIPVATTLLGKSVLDESHPQFIG--TYAGaaSSPEVREYVENADCVLCLGVVFTDTNTGGFtaQLDPERTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 299 VVISNdpSSELRPSYYETikadplVFLKELVNQLKRdtKNKKINDQW---KKEIEKYKNDWDNLIKQtlkrkyrdavnpA 375
Cdd:COG3961 306 DIQPD--SVRVGGHIYPG------VSLADFLEALAE--LLKKRSAPLpapAPPPPPPPAAPDAPLTQ------------D 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 376 LFFSKLNDALKRNRIIIGGQGTHVLYTYDyMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSI 455
Cdd:COG3961 364 RLWQRLQAFLDPGDIVVADTGTSLFGAAD-LRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 456 EALQTIKDENLDVKIIIVNDNSYRVlylKQLINKSNRIYgTELNNPDFAKLAESFG---IRGIKISRDEEIDNSIKEILA 532
Cdd:COG3961 443 QELSTMLRYGLKPIIFVLNNDGYTI---ERAIHGPDGPY-NDIANWDYAKLPEAFGggnALGFRVTTEGELEEALAAAEA 518
|
570
....*....|....*....
gi 505044757 533 N--GPIVVDLITSRDDMPP 549
Cdd:COG3961 519 NtdRLTLIEVVLDKMDAPP 537
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
396-539 |
1.95e-43 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 151.58 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 396 GTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVND 475
Cdd:pfam02775 3 GCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNN 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505044757 476 NSYRVLYLKQLINKSNRIYGTE---LNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVD 539
Cdd:pfam02775 83 GGYGMTRGQQTPFGGGRYSGPSgkiLPPVDFAKLAEAYGAKGARVESPEELEEALKEALEhDGPALID 150
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
374-558 |
4.30e-43 |
|
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: 151.88 E-value: 4.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 374 PALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALM 453
Cdd:cd02015 3 PQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 454 SIEALQTIKDENLDVKIIIVNdNSY--RVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEIL 531
Cdd:cd02015 83 NIQELATAAQYNLPVKIVILN-NGSlgMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEAL 161
|
170 180
....*....|....*....|....*...
gi 505044757 532 AN-GPIVVDLITSRDdmpptntEMVLKM 558
Cdd:cd02015 162 ASdGPVLLDVLVDPE-------ENVLPM 182
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-164 |
6.83e-41 |
|
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: 144.98 E-value: 6.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEykNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR--SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505044757 88 GIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPE 164
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
5-539 |
1.88e-40 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 154.22 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 5 KLSEALARGLINLGIKRIYGVIGTTVLNFYDALYeyKNEIKQITVRKENVAISAADAEYRTTKKpaAAVVHA--GGGFLN 82
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALR--DSSIKLILTRHEQGAAFMAATYGRLTGK--AGVCLStlGPGATN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITGSV--KRrlkntdSWLE----VDQEGLSKALNLYHYYVESPD----VFVEKFEKAMIDlfy 152
Cdd:PRK08322 78 LVTGVAYAQLGGMPMVAITGQKpiKR------SKQGsfqiVDVVAMMAPLTKWTRQIVSPDnipeVVREAFRLAEEE--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 153 gNPKPVVLEIPEDIwdKKINIDENNFPnISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITD 232
Cdd:PRK08322 149 -RPGAVHLELPEDI--AAEETDGKPLP-RSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 233 SYILTTGNARGICEEDHPRCIGRVGYGGGSlYADNALKSTDylLVFGEGFDDITTYGFNLTPSESIVVIS-NDPSSELRP 311
Cdd:PRK08322 225 IPFFTTQMGKGVIPETHPLSLGTAGLSQGD-YVHCAIEHAD--LIINVGHDVIEKPPFFMNPNGDKKVIHiNFLPAEVDP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 312 SYYETIK-----ADPLVFLKELV--NQLKRDTKNKKINDQWKKEIEKYKNDwdnlikqtlkrkYRDAVNPALFFSKLNDA 384
Cdd:PRK08322 302 VYFPQVEvvgdiANSLWQLKERLadQPHWDFPRFLKIREAIEAHLEEGADD------------DRFPMKPQRIVADLRKV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 385 LKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDE 464
Cdd:PRK08322 370 MPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRL 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505044757 465 NLDVKIIIVNDNSYRVLYLKQlINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVD 539
Cdd:PRK08322 450 GLPLVVLILNDNAYGMIRWKQ-ENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAqPGVHVID 524
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
8-552 |
7.89e-40 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 152.45 E-value: 7.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGK-IRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 88 GIAMKDRSRLLLITGSVKRRLKNTDSWL--EV-DQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPE 164
Cdd:PRK07064 86 VEALTAGTPLLHITGQIETPYLDQDLGYihEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 165 DIWDKKINIDENNFPniSYEKEENVNEEDVKRVKEEILKSNKPLILVSNevnfeNSRSYIYELSEITDS--YILTTGNAR 242
Cdd:PRK07064 166 DIQAAEIELPDDLAP--VHVAVPEPDAAAVAELAERLAAARRPLLWLGG-----GARHAGAEVKRLVDLgfGVVTSTQGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 243 GICEEDHPRCIGRVGyggGSLYADNALKSTDYLLVFGEGFDDITTYGFNLTPSESIVVISNDPSSELR--PSYYeTIKAD 320
Cdd:PRK07064 239 GVVPEDHPASLGAFN---NSAAVEALYKTCDLLLVVGSRLRGNETLKYSLALPRPLIRVDADAAADGRgyPNDL-FVHGD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 321 PLVFLKELVNQLKrdtKNKKINDQWKKEIEKykndwdnlIKQTLKRKYRDAVNP-ALFFSKLNDALKRNRII-----IGG 394
Cdd:PRK07064 315 AARVLARLADRLE---GRLSVDPAFAADLRA--------AREAAVADLRKGLGPyAKLVDALRAALPRDGNWvrdvtISN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 395 Q--GTHVLYTYD-YMKVYEFGGfmaatnlgSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKII 471
Cdd:PRK07064 384 StwGNRLLPIFEpRANVHALGG--------GIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 472 IVNDNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLitsrdDM--- 547
Cdd:PRK07064 456 LMNDGGYGVIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAkEGPVLVEV-----DMlsi 530
|
570
....*....|....
gi 505044757 548 ---------PPTNT 552
Cdd:PRK07064 531 gpfaaafagPPVKK 544
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
372-549 |
1.20e-39 |
|
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: 142.28 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 372 VNPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYefGGFMAAT--NLGSMGFALPAAIGAKISNPDREVIAIIGDG 449
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMN--GKQRFILsgLLATMGNGLPGAIAAKLAYPDRQVIALSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 450 EALMSIEALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRiYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKE 529
Cdd:cd02014 80 GFAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPE-FGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDE 158
|
170 180
....*....|....*....|.
gi 505044757 530 ILA-NGPIVVDLITSRdDMPP 549
Cdd:cd02014 159 ALAaDGPVVIDVVTDP-NEPP 178
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
373-542 |
1.65e-34 |
|
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: 128.48 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 373 NPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNlGSMGFALPAAIGAKISNPDREVIAIIGDGEAL 452
Cdd:cd02002 2 TPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 453 MSIEALQTIKDENLDVKIIIVNDNSYRVL--YLKQL---INKSNRIYGTELNNP--DFAKLAESFGIRGIKISRDEEIDN 525
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYGALrsFLKRVgpeGPGENAPDGLDLLDPgiDFAAIAKAFGVEAERVETPEELDE 160
|
170
....*....|....*...
gi 505044757 526 SIKEILA-NGPIVVDLIT 542
Cdd:cd02002 161 ALREALAeGGPALIEVVV 178
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
7-533 |
2.02e-31 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 128.19 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNEIKQ----ITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLN 82
Cdd:PRK08327 10 AELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGRPlpefVICPHEIVAISMAHGYALVTGKPQAVMVHVDVGTAN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITG----SVKRRLKNTDS---WL-EV-DQEGLSKALNLYHYYVESPDVFVEKFEKAMiDLFYG 153
Cdd:PRK08327 90 ALGGVHNAARSRIPVLVFAGrspyTEEGELGSRNTrihWTqEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAI-QIAMS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 154 NPK-PVVLEIPEDIWDKKIN---IDENNFPNISyekEENVNEEDVKRVKEEILKSNKPLILVS----NEVNFEnsrsyiy 225
Cdd:PRK08327 169 EPKgPVYLTLPREVLAEEVPevkADAGRQMAPA---PPAPDPEDIARAAEMLAAAERPVIITWragrTAEGFA------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 226 ELSEITDSYILTTGNARGI---CEEDHPRcigRVGYGGGSLYADnalksTDYLLVFGEGFDDITTygfNLTPSES--IVV 300
Cdd:PRK08327 239 SLRRLAEELAIPVVEYAGEvvnYPSDHPL---HLGPDPRADLAE-----ADLVLVVDSDVPWIPK---KIRPDADarVIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 301 ISNDPSSELRPSYY----ETIKADPLVFLKELVNQLKRDTKN-KKINDQWKKEIEKYKNDWDNLIKQTL-KRKYRDAVNP 374
Cdd:PRK08327 308 IDVDPLKSRIPLWGfpcdLCIQADTSTALDQLEERLKSLASAeRRRARRRRAAVRELRIRQEAAKRAEIeRLKDRGPITP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 375 ALFFSKLNDALKRNRIIIggqgTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMS 454
Cdd:PRK08327 388 AYLSYCLGEVADEYDAIV----TEYPFVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 455 I--EALQTIKDENLDVKIIIVNDNSY-------RVLYLKQLINKSNRIYGTELN-NPDFAKLAESFGIRGIKISRDEEID 524
Cdd:PRK08327 464 VpeAAHWVAERYGLPVLVVVFNNGGWlavkeavLEVYPEGYAARKGTFPGTDFDpRPDFAKIAEAFGGYGERVEDPEELK 543
|
....*....
gi 505044757 525 NSIKEILAN 533
Cdd:PRK08327 544 GALRRALAA 552
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
8-539 |
2.65e-30 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 124.97 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEykNEIKQITVRKE-NVAISAAdAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK08617 9 DLVVDSLINQGVKYVFGIPGAKIDRVFDALED--SGPELIVTRHEqNAAFMAA-AIGRLTGKPGVVLVTSGPGVSNLATG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKR--RLKNTDSWLevDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPE 164
Cdd:PRK08617 86 LVTATAEGDPVVAIGGQVKRadRLKRTHQSM--DNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 165 DIWDKKINIDenNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILV----SNEvnfENSRSyIYELSEITDSYILTTGN 240
Cdd:PRK08617 164 DVVDAPVTSK--AIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLgmraSSP---EVTAA-IRRLLERTNLPVVETFQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 241 ARGICEEDH-PRCIGRVGygggsLY----ADNALKSTDylLVFGEGFDDITtY---GFNLTPSESIVVISNDPSSElrPS 312
Cdd:PRK08617 238 AAGVISRELeDHFFGRVG-----LFrnqpGDELLKKAD--LVITIGYDPIE-YeprNWNSEGDATIIHIDVLPAEI--DN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 313 YYETIK------ADPLVFLKELVNQLKRDTKNKKINDQWKKEIEKykndwDNLIKQTLKRkyrDAVNPALFFSKLNDALK 386
Cdd:PRK08617 308 YYQPEReligdiAATLDLLAEKLDGLSLSPQSLEILEELRAQLEE-----LAERPARLEE---GAVHPLRIIRALQDIVT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 387 RNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENL 466
Cdd:PRK08617 380 DDTTVTVDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKL 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505044757 467 DVKIIIVNDNSYRVLYLKQlINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVD 539
Cdd:PRK08617 460 NIVHIIWNDGHYNMVEFQE-EMKYGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALAtDGPVVID 532
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
7-533 |
1.12e-29 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 123.18 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTvlnFYDALYEY-KNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PRK07525 9 SEAFVETLQAHGITHAFGIIGSA---FMDASDLFpPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESP----DVFVEKFEKAmidlfYGNPKPVVLE 161
Cdd:PRK07525 86 AVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPsrmaEVLNRVFDKA-----KRESGPAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 162 IPEDIWDKKINIDennFPNIS-YEK----EENVNEedvkrvKEEILKSNK-PLILVSNEVNFENSRSYIYELSEITDSYI 235
Cdd:PRK07525 161 IPRDYFYGVIDVE---IPQPVrLERgaggEQSLAE------AAELLSEAKfPVILSGAGVVLSDAIEECKALAERLDAPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 236 LTTGNARGICEEDHPRCIGRVGYGGgSLYADNALKSTDYLLVFGEGFDDITT---YGFNLTPSES-IVVISNDPSS-ELR 310
Cdd:PRK07525 232 ACGYLHNDAFPGSHPLWVGPLGYNG-SKAAMELIAKADVVLALGTRLNPFGTlpqYGIDYWPKDAkIIQVDINPDRiGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 311 PSYYETIKADPLVFLKELVNQLKRDTKNKKINDQWKKEIEKYKNDWD---------------NLIKQTLKRKyRDAVNPA 375
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAERLAGDAGREERKALIAAEKSAWEqelsswdhedddpgtDWNEEARARK-PDYMHPR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 376 LFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSI 455
Cdd:PRK07525 390 QALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISM 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505044757 456 EALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTEL-NNPDFAKLAESFGIRGIKISRDEEIDNSIKEILAN 533
Cdd:PRK07525 470 NEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELdNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDA 548
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
8-540 |
1.15e-29 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 122.78 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEYKneIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGL 87
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPGVHTVELYRGLAGSG--IRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 88 GIAMKDRSRLLLITgSVKRR--LKNTDSWL-EV-DQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIP 163
Cdd:PRK07524 84 GQAYADSIPMLVIS-SVNRRasLGKGRGKLhELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 164 EDIWDKKINIDENNFPNISYEKEENvnEEDVKRVKEEILKSNKPLILVSN---EVNFEnsrsyIYELSEITDSYILTTGN 240
Cdd:PRK07524 163 LDVLAAPADHLLPAPPTRPARPGPA--PAALAQAAERLAAARRPLILAGGgalAAAAA-----LRALAERLDAPVALTIN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 241 ARGICEEDHPRCIGrvgyGGGSLYADNALKS--------------TDYLLVFGEGFDdittygfnlTPSESIVvISNDPS 306
Cdd:PRK07524 236 AKGLLPAGHPLLLG----ASQSLPAVRALIAeadvvlavgtelgeTDYDVYFDGGFP---------LPGELIR-IDIDPD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 307 SELRPSYYE-TIKADPLVFLKELVNQLKrdtkNKKINDQW--------KKEIEkykNDWDnlikqTLKRKYRDavnpalF 377
Cdd:PRK07524 302 QLARNYPPAlALVGDARAALEALLARLP----GQAAAADWgaarvaalRQALR---AEWD-----PLTAAQVA------L 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 378 FSKLNDALKRNRIIigGQGTHVLYTYDYmkVYEF----GGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALM 453
Cdd:PRK07524 364 LDTILAALPDAIFV--GDSTQPVYAGNL--YFDAdaprRWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQF 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 454 SIEALQTIKDENLDVKIIIVNDNSYRVLYlKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA- 532
Cdd:PRK07524 440 TLPELASAVEADLPLIVLLWNNDGYGEIR-RYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFAr 518
|
....*...
gi 505044757 533 NGPIVVDL 540
Cdd:PRK07524 519 PGPTLIEV 526
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
6-550 |
2.14e-29 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 122.40 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 6 LSEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKnEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PRK09124 5 VADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMG-TIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAM---IdlfyGNPKPVVLEI 162
Cdd:PRK09124 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMrkaI----LNRGVAVVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDIWDKKInidENNFPNISYEKEENV---NEEDVKRVKEEILKSNKPLILVSNEVnfENSRSYIYELSEITDSYILTTG 239
Cdd:PRK09124 160 PGDVALKPA---PERATPHWYHAPQPVvtpAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 240 NARGICEEDHPRCIGRVGY-GGGSLYAdnALKSTDYLLVFGEGFdditTYGFNLTPSESIVVISNDPSS---------EL 309
Cdd:PRK09124 235 RGKEHVEYDNPYDVGMTGLiGFSSGYH--AMMNCDTLLMLGTDF----PYRQFYPTDAKIIQIDINPGSlgrrspvdlGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 310 RPSYYETIKAdplvflkeLVNQLKRDTKNKKInDQWKKEIEKYKNDWDNLIKQTLKRKyrdAVNPALFFSKLNDALKRNR 389
Cdd:PRK09124 309 VGDVKATLAA--------LLPLLEEKTDRKFL-DKALEHYRKARKGLDDLAVPSDGGK---PIHPQYLARQISEFAADDA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 390 IIIGGQGTHVLYTYDYMKVYE----FGGFmaatNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDEN 465
Cdd:PRK09124 377 IFTCDVGTPTVWAARYLKMNGkrrlLGSF----NHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 466 LDVKIIIVNdNSyrVLYLKQLINKSNRI--YGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLIT 542
Cdd:PRK09124 453 LPVKIVVFN-NS--VLGFVAMEMKAGGYltDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAhDGPALVDVVT 529
|
570
....*....|
gi 505044757 543 SRDD--MPPT 550
Cdd:PRK09124 530 AKQElaMPPQ 539
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
374-539 |
5.14e-29 |
|
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: 113.15 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 374 PALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALM 453
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 454 SIEALQTIKDENLDVKIIIVNDNSYRVLYLKQLiNKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA- 532
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQE-KEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAa 159
|
....*..
gi 505044757 533 NGPIVVD 539
Cdd:cd02010 160 DGVHVID 166
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
5-545 |
5.45e-28 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 117.99 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 5 KLSEALARGLINLGIKRIygvIGTTVLNFYDAlyEYKNEIKQITVRKENVAISAADAEYRTT--KKPAAAVVHAGGGFLN 82
Cdd:PRK06154 21 KVAEAVAEILKEEGVELL---FGFPVNELFDA--AAAAGIRPVIARTERVAVHMADGYARATsgERVGVFAVQYGPGAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 83 SLTGLGIAMKDRSRLLLITGSVKRRLKNTDSwlevdqeGLSKALNLYHY--YVES---PDVFVEKFEKAMIDLFYGNPKP 157
Cdd:PRK06154 96 AFGGVAQAYGDSVPVLFLPTGYPRGSTDVAP-------NFESLRNYRHItkWCEQvtlPDEVPELMRRAFTRLRNGRPGP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 158 VVLEIPEDIWDKKINIDENNFPNiSYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILT 237
Cdd:PRK06154 169 VVLELPVDVLAEELDELPLDHRP-SRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 238 TGNARGICEEDHPRCIGRvgyGGGSLYA--DNALKSTDYLLVFGEGFDDiTTYGFNLTPSESIVVISNDPSsELRPSYY- 314
Cdd:PRK06154 248 TLNGKSAFPEDHPLALGS---GGRARPAtvAHFLREADVLFGIGCSLTR-SYYGLPMPEGKTIIHSTLDDA-DLNKDYPi 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 315 -ETIKADPLVFLKELVNQLKRD-TKNKKINDQWKKEIEKYKNDWdnLIKQTLKRKYRDA-VNPALFFSKLNDALKRNRII 391
Cdd:PRK06154 323 dHGLVGDAALVLKQMIEELRRRvGPDRGRAQQVAAEIEAVRAAW--LAKWMPKLTSDSTpINPYRVVWELQHAVDIKTVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 392 IggqgthvlyTYD----------YMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTI 461
Cdd:PRK06154 401 I---------THDagsprdqlspFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 462 KDENLDVKIIIVNDNSYRVlYLKQLINKSNRiYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEIL----ANGPIV 537
Cdd:PRK06154 472 VRERIPILTILLNNFSMGG-YDKVMPVSTTK-YRATDISGDYAAIARALGGYGERVEDPEMLVPALLRALrkvkEGTPAL 549
|
....*...
gi 505044757 538 VDLITSRD 545
Cdd:PRK06154 550 LEVITSEE 557
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
374-543 |
3.21e-26 |
|
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: 104.92 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 374 PALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALM 453
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 454 SIEALQTIKDENLDVKIIIVNDNS-YRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA 532
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGwYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 505044757 533 NG-PIVVDLITS 543
Cdd:cd02004 161 SGkPALINVIID 172
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
377-550 |
4.25e-25 |
|
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: 102.23 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 377 FFSKLNDALKRNRIIIGGQGThVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIE 456
Cdd:cd02005 7 LWQQVQNFLKPNDILVAETGT-SWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 457 ALQTIKDENLDVKIIIVNDNSYRVLylkQLINKSNRIYgTELNNPDFAKLAESFG----IRGIKISRDEEIDNSIKEILA 532
Cdd:cd02005 86 ELSTMIRYGLNPIIFLINNDGYTIE---RAIHGPEASY-NDIANWNYTKLPEVFGggggGLSFRVKTEGELDEALKDALF 161
|
170 180
....*....|....*....|
gi 505044757 533 N--GPIVVDLITSRDDMPPT 550
Cdd:cd02005 162 NrdKLSLIEVILPKDDAPEA 181
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
5-170 |
7.78e-24 |
|
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: 98.01 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 5 KLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSL 84
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRR-EGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 85 TGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMiDLFYGNPKPVVLEIPE 164
Cdd:cd07039 80 NGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAI-RTAIAKRGVAVLILPG 158
|
....*.
gi 505044757 165 DIWDKK 170
Cdd:cd07039 159 DVQDAP 164
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
6-556 |
2.88e-23 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 103.91 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 6 LSEALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLT 85
Cdd:PRK06546 5 VAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGG-IEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 86 GLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPdvfvEKFEKAM---IDLFYGNPKPVVLEI 162
Cdd:PRK06546 84 GLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSA----EQAPRVLhsaIQHAVAGGGVSVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 163 PEDIWDKKInidENNFPNISYEKEENV---NEEDVKRVKEEILKSNKPLILVSNEVnfENSRSYIYELSEITDSYIlttG 239
Cdd:PRK06546 160 PGDIADEPA---PEGFAPSVISPRRPTvvpDPAEVRALADAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPV---G 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 240 NA-RG--ICEEDHPRCIGR---VGYGGgslyADNALKSTDYLLVFGEGFdditTYGfNLTPSESIVVISNDPSSELRPSY 313
Cdd:PRK06546 232 HSlRGkeWIQYDNPFDVGMsglLGYGA----AHEAMHEADLLILLGTDF----PYD-QFLPDVRTAQVDIDPEHLGRRTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 314 YE-TIKADPLVFLKELVNQLKRDTKN-------KKINDQWKKEIEKYkndwdnlikqTLKRKYRDAVNPALFFSKLNDAL 385
Cdd:PRK06546 303 VDlAVHGDVAETIRALLPLVKEKTDRrfldrmlKKHARKLEKVVGAY----------TRKVEKHTPIHPEYVASILDELA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 386 KRNRIIIGGQGTHVLYTYDYM----KVYEFGGFMAatnlGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTI 461
Cdd:PRK06546 373 ADDAVFTVDTGMCNVWAARYItpngRRRVIGSFRH----GSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 462 KDENLDVKIIIVNDNSYRVLYLKQLINKSNRiYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDL 540
Cdd:PRK06546 449 KLYDLPVKVVVFNNSTLGMVKLEMLVDGLPD-FGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAhPGPALVDV 527
|
570
....*....|....*....
gi 505044757 541 ITSRD--DMPPTNT-EMVL 556
Cdd:PRK06546 528 VTDPNalSIPPTITgEQVK 546
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
370-542 |
5.87e-23 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 102.34 E-value: 5.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 370 DAVNPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGF--MAAtnlGSMGFALPAAIGAKISNPDREVIAIIG 447
Cdd:PRK07092 357 EPLSVAFVLQTLAALRPADAIVVEEAPSTRPAMQEHLPMRRQGSFytMAS---GGLGYGLPAAVGVALAQPGRRVIGLIG 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 448 DGEALMSIEALQTIKDENLDVKIIIVNDNSYRVL-YLKQLINKSNrIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNS 526
Cdd:PRK07092 434 DGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALrWFAPVFGVRD-VPGLDLPGLDFVALARGYGCEAVRVSDAAELADA 512
|
170
....*....|....*..
gi 505044757 527 IKEILA-NGPIVVDLIT 542
Cdd:PRK07092 513 LARALAaDGPVLVEVEV 529
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
370-532 |
9.96e-23 |
|
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: 96.04 E-value: 9.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 370 DAVNPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDG 449
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 450 EALMSIEALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEIDNSIKE 529
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESESFAKIAEACGAKGITVDKPEDVGPALQK 161
|
...
gi 505044757 530 ILA 532
Cdd:cd02013 162 AIA 164
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
18-475 |
1.30e-21 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 98.25 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 18 GIKRIYGVIGTTVLNFYDALYeyKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGLGIAMKDRSRL 97
Cdd:PRK05858 19 GVDTMFTLSGGHLFPLYDGAR--EEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 98 LLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPEDIWDKKINIDENN 177
Cdd:PRK05858 97 VVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHAFSMADDDGRP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 178 FPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNARGICEEDHPRCIGRVg 257
Cdd:PRK05858 177 GALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRA- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 258 ygggslyADNALKSTDYLLVFGEGFDdiTTYGFNLTPSESIVVISNDPSSELrpSYYETIKADPLVFLKELVNQLKRDTK 337
Cdd:PRK05858 256 -------RGKALGEADVVLVVGVPMD--FRLGFGVFGGTAQLVHVDDAPPQR--AHHRPVAAGLYGDLSAILSALAGAGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 338 NKKINDQWKKEI---EKYKNDWDnlikQTLKRKYRDAVNPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGF 414
Cdd:PRK05858 325 DRTDHQGWIEELrtaETAARARD----AAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCW 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505044757 415 MAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVND 475
Cdd:PRK05858 401 LDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNN 461
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-554 |
3.27e-21 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 97.36 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 1 MVEIKLSEALARGLINLGIKRIYGVIGTTVLNFYDALYEyKNEIKQITVRKENVAISAADAEYRTTK-KPAAAVVHAGGG 79
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRK-HGGIRHILARHVEGASHMAEGYTRATAgNIGVCIGTSGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 80 FLNSLTGLGIAMKDRSRLLLITGSVKR-RLKNTDsWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPV 158
Cdd:PRK11269 80 GTDMITGLYSASADSIPILCITGQAPRaRLHKED-FQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 159 VLEIPEDIWDKKINIDENNFPNISYEKEEnVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTT 238
Cdd:PRK11269 159 LIDLPFDVQVAEIEFDPDTYEPLPVYKPA-ATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 239 GNARGICEEDHPRCIGRVGYGGGSLYADNALKSTDYLLVFGEGFDD-----ITTYgfnlTPSESIVVISNDPSSELR--- 310
Cdd:PRK11269 238 LMGWGAIPDDHPLMAGMVGLQTSHRYGNATLLASDFVLGIGNRWANrhtgsVEVY----TKGRKFVHVDIEPTQIGRvfg 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 311 PSYyeTIKADPLVFLKELVNQLKRDTKNKKIND--QWKKEIEKykndwdnlIKQTLKRK--YRDA-VNPALFFSKLNDAL 385
Cdd:PRK11269 314 PDL--GIVSDAKAALELLVEVAREWKAAGRLPDrsAWVADCQE--------RKRTLLRKthFDNVpIKPQRVYEEMNKAF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 386 KRNRI---------IIGGQgthvlytydYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIE 456
Cdd:PRK11269 384 GRDTCyvstiglsqIAAAQ---------FLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 457 ALQTIKDENLDVKIIIVNdNSYRvlylkQLINKSNRIYGT---------ELNNP-------DFAKLAESFGIRGIKISRD 520
Cdd:PRK11269 455 ELAVGAQFNLPYIHVLVN-NAYL-----GLIRQAQRAFDMdycvqlafeNINSPelngygvDHVKVAEGLGCKAIRVFKP 528
|
570 580 590
....*....|....*....|....*....|....*....
gi 505044757 521 EEIDNSIKEILA-----NGPIVVDLITSRDdmppTNTEM 554
Cdd:PRK11269 529 EDIAPALEQAKAlmaefRVPVVVEVILERV----TNISM 563
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
7-549 |
3.17e-19 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 91.36 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYG-VIGTTVLNFYDALyeyknEIKQITVRKENVAISAADAEYRTTKKPAaaVVHAGGGFLNSL- 84
Cdd:PRK06112 17 AHAIARALKRHGVEQIFGqSLPSALFLAAEAI-----GIRQIAYRTENAGGAMADGYARVSGKVA--VVTAQNGPAATLl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 85 -TGLGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIP 163
Cdd:PRK06112 90 vAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 164 EDIWDKKIN----IDENNFPNISYEKEENVnEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTG 239
Cdd:PRK06112 170 ADLLTAAAAapaaPRSNSLGHFPLDRTVPA-PQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 240 NARGICEEDHPRCIGRVGYGGG----SLYADNALKSTDYLLVFGEGFDDITTYGFNLTPSESIVV-ISNDPSSELRPsyY 314
Cdd:PRK06112 249 MGKGAVDETHPLSLGVVGSLMGprspGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIhIDVDGEEVGRN--Y 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 315 ETIK-----ADPLVFLKE---LVNQLKRDTKNKKINDQWKKEIEKYKNDwdnlikqtlKRKYRDA----VNPALFFSKLN 382
Cdd:PRK06112 327 EALRlvgdaRLTLAALTDalrGRDLAARAGRRAALEPAIAAGREAHRED---------SAPVALSdaspIRPERIMAELQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 383 DALKRNRIIIGGQGTHVLYTYDYMKVYEFGG-FMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTI 461
Cdd:PRK06112 398 AVLTGDTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 462 KDENLDVKIIIVNDNsyrvlYLKQLINKSNRIYGTELNNPDF-----AKLAESFGIRGIKISRDEEIDNSIKEILAN-GP 535
Cdd:PRK06112 478 RRMGVPVTIVVLNNG-----ILGFQKHAETVKFGTHTDACHFaavdhAAIARACGCDGVRVEDPAELAQALAAAMAApGP 552
|
570
....*....|....
gi 505044757 536 IVVDLITSRDDMPP 549
Cdd:PRK06112 553 TLIEVITDPSAFPP 566
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
421-540 |
1.39e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 85.67 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 421 GSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNSYRVLYLKQLIN-------KSNRI 493
Cdd:PRK07586 385 GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVgagnpgpRALDM 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 505044757 494 ygTELNNP--DFAKLAESFGIRGIKISRDEEIDNSIKEILAN-GPIVVDL 540
Cdd:PRK07586 465 --LDLDDPdlDWVALAEGMGVPARRVTTAEEFADALAAALAEpGPHLIEA 512
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
325-549 |
3.15e-17 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 84.96 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 325 LKELVNQLKRDTknkkiNDQWKKEIEKYKNDWDnlikQTLKRKYR---DAVNPALFFSKLNDALKRNRIIIGGQGTHVLY 401
Cdd:PRK08273 325 LRALLPLLERKK-----DRSWRERIEKWVARWW----ETLEARAMvpaDPVNPQRVFWELSPRLPDNAILTADSGSCANW 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 402 TYDYMKVYefGGFMAAT--NLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMS-IEALQTI-------KDENLdvkII 471
Cdd:PRK08273 396 YARDLRMR--RGMMASLsgTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVakywrqwSDPRL---IV 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 472 IVNDNS--------YRVLYLKQLINKSNRIygtelnnPDF--AKLAESFGIRGIKISRDEEIDNSIKEIL-ANGPIVVDL 540
Cdd:PRK08273 471 LVLNNRdlnqvtweQRVMEGDPKFEASQDL-------PDVpyARFAELLGLKGIRVDDPEQLGAAWDEALaADRPVVLEV 543
|
....*....
gi 505044757 541 ITSRdDMPP 549
Cdd:PRK08273 544 KTDP-NVPP 551
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
194-328 |
5.84e-17 |
|
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: 77.60 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 194 VKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNARGICEEDHPRCIGRVGYgGGSLYADNALKSTD 273
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGM-HGTPAANEALEEAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 505044757 274 YLLVFGEGFDDITTYGFNLT--PSESIVVISNDPsSELRPSY--YETIKADPLVFLKEL 328
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEfaPDAKIIHIDIDP-AEIGKNYpvDVPIVGDAKETLEAL 137
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
18-539 |
1.79e-14 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 76.18 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 18 GIKRIYGVIGTTVLNFydALYEYKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTGLGIAMKDRSRL 97
Cdd:PRK09259 24 GIDTIYGVVGIPITDL--ARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANATTNCFPM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 98 LLITGSVKRR---LKNTDsWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPEDIWDKKINID 174
Cdd:PRK09259 102 IMISGSSEREivdLQQGD-YEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLAQTMDAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 175 ENN---FPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRSYIYELSEITDSYILTTGNARGICEEDHPR 251
Cdd:PRK09259 181 EALtslVKVVDPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 252 CIGrvgyGGGSLyadnALKSTD----------YLLVFGEGfddiTTYGfnltPSESIVVISNDPsSEL---RPsyyetIK 318
Cdd:PRK09259 261 SAA----AARSL----ALANADvvllvgarlnWLLSHGKG----KTWG----ADKKFIQIDIEP-QEIdsnRP-----IA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 319 AdPLV-----FLKELVNQLKRDTknKKINDQWKKEIEKYKNdwDNLIKqtLKRKYRDAVNPALFFSKL---NDALKRNR- 389
Cdd:PRK09259 319 A-PVVgdigsVMQALLAGLKQNT--FKAPAEWLDALAERKE--KNAAK--MAEKLSTDTQPMNFYNALgaiRDVLKENPd 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 390 IIIGGQGTHVL-YTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNpDREVIAIIGD---GEALMSIEalqTIKDEN 465
Cdd:PRK09259 392 IYLVNEGANTLdLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVET-GKPVVAIEGDsafGFSGMEVE---TICRYN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 466 LDVKIIIVNDNS-YRvlylkqlinksnriyGTELNNPDFA--------------KLAESFGIRGIKISRDEEIDNSIKEI 530
Cdd:PRK09259 468 LPVTVVIFNNGGiYR---------------GDDVNLSGAGdpsptvlvhharydKMMEAFGGVGYNVTTPDELRHALTEA 532
|
570
....*....|
gi 505044757 531 LANG-PIVVD 539
Cdd:PRK09259 533 IASGkPTLIN 542
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
7-541 |
2.40e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 75.68 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 7 SEALARGLINLGIKRIYGVIGTTVLNFYDALyEYKNEIKQITVRKENVAISAADAEYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:PRK12474 8 ADSVVDTLLNCGVEVCFANPGTSEMHFVAAL-DRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWLEVDQEGLSKALNLYHYYVESPDVFVEKFEKAMIDLFYGNPKPVVLEIPEDI 166
Cdd:PRK12474 87 LHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPADV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 167 -WdkkiNIDENNFPNISYEKEENVNEEDVKRVKEEILKSNKPLILVSNEVNFENSRsyiyelsEITDSYILTTGnARGIC 245
Cdd:PRK12474 167 aW----NEAAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRGSALRGAPL-------EAAGRIQAKTG-VRLYC 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 246 EEDHPRC---IGRVGYGGGSLYADNA---LKSTDYLLVFGEgfddittygfnlTPSESIVVISNDPSSELRPSYYETIKA 319
Cdd:PRK12474 235 DTFAPRIergAGRVPIERIPYFHEQItafLKDVEQLVLVGA------------KPPVSFFAYPGKPSWGAPPGCEIVYLA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 320 DPLvflKELVNQLkrdtknkkindQWKKEIEKYKNDWDNLIKQTLkrkyrdavnPALFFSKLNdALKRNRIIIGGQGTHV 399
Cdd:PRK12474 303 QPD---EDLAQAL-----------QDLADAVDAPAEPAARTPLAL---------PALPKGALN-SLGVAQLIAHRTPDQA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 400 LYTYD-------YMKVYEFGGFMAATNL--GSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKI 470
Cdd:PRK12474 359 IYADEaltsglfFDMSYDRARPHTHLPLtgGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTV 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505044757 471 IIVNDNSYRVLYLK-QLINKS----NRIYGTELNNP--DFAKLAESFGIRGIKISRDEEIDNSIKEILAN-GPIVVDLI 541
Cdd:PRK12474 439 VIFANRSYAILNGElQRVGAQgagrNALSMLDLHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQrGPRLIEAM 517
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
423-540 |
9.08e-14 |
|
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: 70.41 E-value: 9.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 423 MGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNSYRVL--------------YLKQLIN 488
Cdd:cd02003 50 MGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCInnlqestgsgsfgtEFRDRDQ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 505044757 489 KSNRIYGtELNNPDFAKLAESFGIRGIKISRDEEIDNSIKEILAN-GPIVVDL 540
Cdd:cd02003 130 ESGQLDG-ALLPVDFAANARSLGARVEKVKTIEELKAALAKAKASdRTTVIVI 181
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
420-552 |
1.55e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 61.00 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 420 LGSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNSYRVLYLKQLINKSNRIygteln 499
Cdd:PRK06163 56 LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTV------ 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 505044757 500 npDFAKLAESFGIRGIKISRDEE-IDNSIKEILA-NGPIvvdLITSR-DDMPPTNT 552
Cdd:PRK06163 130 --DVVAIARGAGLENSHWAADEAhFEALVDQALSgPGPS---FIAVRiDDKPGVGT 180
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
372-554 |
2.21e-10 |
|
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: 60.37 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 372 VNPALFFSKLNDALKRNRIIIGGQGTHVLYTYDYMKVYEFGGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEA 451
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 452 LMSIEALQTIKDENLDVKIIIVNdNSYRvlylkQLINKSNRIYGTE---------LNNP-------DFAKLAESFGIRGI 515
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVN-NAYL-----GLIRQAQRAFDMDyqvnlafenINSSelggygvDHVKVAEGLGCKAI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505044757 516 KISRDEEIDNSIKEILA-----NGPIVVDLITSRddmpPTNTEM 554
Cdd:cd02006 162 RVTKPEELAAAFEQAKKlmaehRVPVVVEAILER----VTNISM 201
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
420-554 |
1.04e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 54.99 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 420 LGSMGFALPAAIGAKISNPdREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNSyrvlylkqlinksnrIYGTELN 499
Cdd:cd03372 41 LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATIAAEKPKNLIIVVLDNG---------------AYGSTGN 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505044757 500 NP-------DFAKLAESFGIRGI-KISRDEEIDNSIKEILAnGPIVVDLITSRDDMPPTNTEM 554
Cdd:cd03372 105 QPthagkktDLEAVAKACGLDNVaTVASEEAFEKAVEQALD-GPSFIHVKIKPGNTDVPNIPR 166
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
402-495 |
4.75e-08 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 53.30 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 402 TYDYMKVYEFGGfmaatnlgSMGFALPAAIGAKISNPDREVIAIIGDGEALmSI---EALQTIKdENLDVKIIIVNdnsy 478
Cdd:cd03375 40 LPYYFNTYGFHT--------LHGRALAVATGVKLANPDLTVIVVSGDGDLA-AIggnHFIHAAR-RNIDITVIVHN---- 105
|
90
....*....|....*..
gi 505044757 479 rvlylkqlinksNRIYG 495
Cdd:cd03375 106 ------------NQIYG 110
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
426-476 |
5.44e-08 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 55.79 E-value: 5.44e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 505044757 426 ALPAAIGAKISNPDREVIAIIGDGeAL---MSIEALQTIKDENLDVkIIIVNDN 476
Cdd:COG1154 124 ALGMAVARDLKGEDRKVVAVIGDG-ALtggMAFEALNNAGHLKKDL-IVILNDN 175
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
424-495 |
1.19e-07 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 53.31 E-value: 1.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505044757 424 GFALPAAIGAKISNPDREVIAIIGDGEAL---MS--IEALQtikdENLDVKIIIVNdnsyrvlylkqlinksNRIYG 495
Cdd:PRK11867 72 GRALAIATGLKLANPDLTVIVVTGDGDALaigGNhfIHALR----RNIDITYILFN----------------NQIYG 128
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
421-476 |
1.42e-06 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 48.85 E-value: 1.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 505044757 421 GSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDN 476
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIHIVLNN 103
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
8-115 |
2.42e-06 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) 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, for many the active sites lie between PP and PYR domains on different subunits. 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. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 47.49 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 8 EALARGLINLGIKRIYGVIGTTVLNFYDALYEYKNeIKQITVRKE-NVAIsAADAeYRTTKKPAAAVVHAGGGFLNSLTG 86
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPG-LRWVGNCNElNAGY-AADG-YARVKGLGALVTTYGVGELSALNG 77
|
90 100
....*....|....*....|....*....
gi 505044757 87 LGIAMKDRSRLLLITGSVKRRLKNTDSWL 115
Cdd:cd07038 78 IAGAYAEHVPVVHIVGAPSTKAQASGLLL 106
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
422-542 |
3.19e-06 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 47.93 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 422 SMGFALPAAIGAKISNPDREVIAIIGDGeAL---MSIEALQTIKDENLDVkIIIVNDNsyrvlylKQLINKSNriyGTEL 498
Cdd:cd02007 80 SISAALGMAVARDLKGKKRKVIAVIGDG-ALtggMAFEALNNAGYLKSNM-IVILNDN-------EMSISPNV---GTPG 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 505044757 499 NnpdfakLAESFGIR------GIKISRDEEIDNSIKEIlaNGPIVVDLIT 542
Cdd:cd02007 148 N------LFEELGFRyigpvdGHNIEALIKVLKEVKDL--KGPVLLHVVT 189
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
377-538 |
5.91e-06 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 46.89 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 377 FFSKLNDALKRNRIIIGGQGTHVLYTYDymkvyefgGFMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGEALMS-I 455
Cdd:cd02008 15 SFYALRKAFKKDSIVSGDIGCYTLGALP--------PLNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSgI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 456 EALQTIKDENLDVKIIIVnDNSYRVLYLKQLINKSNRIYGTELNNPDFAKLAESFGIRGIKISRDEEID---NSIKEILA 532
Cdd:cd02008 87 LGLINAVYNKANITVVIL-DNRTTAMTGGQPHPGTGKTLTEPTTVIDIEALVRAIGVKRVVVVDPYDLKairEELKEALA 165
|
....*..
gi 505044757 533 N-GPIVV 538
Cdd:cd02008 166 VpGVSVI 172
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
402-495 |
6.31e-06 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 47.83 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 402 TYDYMKVYefgGFMAAtnlgsMGFALPAAIGAKISNPDREVIAIIGDGeALMSI---EALQTIKdENLDVKIIIVNdnsy 478
Cdd:COG1013 53 APGYFNVP---GFHTL-----HGRAAAVATGIKLANPDLTVIVFGGDG-DTYDIggnHLIHAAR-RNEDITYIVYD---- 118
|
90
....*....|....*..
gi 505044757 479 rvlylkqlinksNRIYG 495
Cdd:COG1013 119 ------------NEIYG 123
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
426-476 |
6.40e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 48.92 E-value: 6.40e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 505044757 426 ALPAAIGAKISN-PDREVIAIIGDGeAL---MSIEALQTIKDENLDVkIIIVNDN 476
Cdd:PRK05444 126 ALGMAKARDLKGgEDRKVVAVIGDG-ALtggMAFEALNNAGDLKSDL-IVILNDN 178
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
414-476 |
8.89e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 48.57 E-value: 8.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505044757 414 FMAATNLGSMGFALPAAIGAKISNPDREVIAIIGDGE--ALMSIEALQTIKDENLDVkIIIVNDN 476
Cdd:PRK12571 116 FGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSltAGMAYEALNNAGAADRRL-IVILNDN 179
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
424-495 |
9.10e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 47.57 E-value: 9.10e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505044757 424 GFALPAAIGAKISNPDREVIAIIGDGEaLMSIEALQTIK--DENLDVKIIIVNdnsyrvlylkqlinksNRIYG 495
Cdd:PRK05778 73 GRAIAFATGAKLANPDLEVIVVGGDGD-LASIGGGHFIHagRRNIDITVIVEN----------------NGIYG 129
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
421-552 |
2.86e-05 |
|
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
Pssm-ID: 274508 [Multi-domain] Cd Length: 361 Bit Score: 46.58 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 421 GSMGFALPAAIGAKISNPDREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNSyrvlylkqlINKSNRIYGTELNN 500
Cdd:TIGR03297 221 GSMGHASQIALGLALARPDQRVVCLDGDGAALMHMGGLATIGTQGPANLIHVLFNNG---------AHDSVGGQPTVSQH 291
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 505044757 501 PDFAKLAESFGIRGI-KISRDEEIDNSIKEIL-ANGPIVVDL---ITSRDDMP-PTNT 552
Cdd:TIGR03297 292 LDFAQIAKACGYAKVyEVSTLEELETALTAASsANGPRLIEVkvrPGSRADLGrPTTS 349
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
430-543 |
9.25e-04 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 40.27 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 430 AIGAKISNPDReVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDNS---YRVLYLKQLINKSNRIYGTeLNNPDFAKL 506
Cdd:cd02009 60 ALGIALATDKP-TVLLTGDLSFLHDLNGLLLGKQEPLNLTIVVINNNGggiFSLLPQASFEDEFERLFGT-PQGLDFEHL 137
|
90 100 110
....*....|....*....|....*....|....*...
gi 505044757 507 AESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDLITS 543
Cdd:cd02009 138 AKAYGLEYRRVSSLDELEQALESALAqDGPHVIEVKTD 175
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
420-540 |
1.17e-03 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 39.78 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 420 LGSMGFALPAAIGAKISNPdREVIAIIGDGEALMSIEALQTIKDENLDVKIIIVNDnsyrvlylkqlinksNRIYGTELN 499
Cdd:cd02001 41 LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTPLNLILVVLD---------------NRAYGSTGG 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505044757 500 NP------DFAKLAESFGIRGIKISRDEEIDNSIKEILA-NGPIVVDL 540
Cdd:cd02001 105 QPtpssnvNLEAWAAACGYLVLSAPLLGGLGSEFAGLLAtTGPTLLHA 152
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
424-478 |
2.21e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 40.10 E-value: 2.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505044757 424 GFALPAAIGAKISNPDREVIAIIGDGEALmSIEALQTIKD--ENLDVKIIIVNDNSY 478
Cdd:PRK09628 71 GRAVAYATGIKLANPDKHVIVVSGDGDGL-AIGGNHTIHGcrRNIDLNFILINNFIY 126
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
404-478 |
2.33e-03 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 40.12 E-value: 2.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505044757 404 DYMKVYEFGGFMaatnlgsmGFALPAAIGAKISNPDREVIAIIGDGEAL-MSIEALQTIKDENLDVKIIIVNDNSY 478
Cdd:PRK11866 50 EFLNTYGIHGIH--------GRVLPIATGVKWANPKLTVIGYGGDGDGYgIGLGHLPHAARRNVDITYIVSNNQVY 117
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
421-529 |
6.40e-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: 38.64 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505044757 421 GSMGFALPAAIG----AKISNPDREVIAIIGDGEaLM---SIEALQTIKDENLDvKIIIVNDNsyrvlylkqlinksNR- 492
Cdd:cd02012 105 GSLGQGLSVAVGmalaEKLLGFDYRVYVLLGDGE-LQegsVWEAASFAGHYKLD-NLIAIVDS--------------NRi 168
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505044757 493 -IYGT---ELNNPDFAKLAESFGIRGIKISRD--EEIDNSIKE 529
Cdd:cd02012 169 qIDGPtddILFTEDLAKKFEAFGWNVIEVDGHdvEEILAALEE 211
|
|
| XFP_N |
pfam09364 |
XFP N-terminal domain; Bacterial enzyme splits fructose-6-P and/or xylulose-5-P with the aid ... |
421-451 |
6.90e-03 |
|
XFP N-terminal domain; Bacterial enzyme splits fructose-6-P and/or xylulose-5-P with the aid of inorganic phosphate into either acetyl-P and erythrose-4-P and/or acetyl-P and glyeraldehyde-3-P EC:4.1.2.9, EC:4.1.2.22. This family is distantly related to transketolases e.g. pfam02779.
Pssm-ID: 401348 Cd Length: 364 Bit Score: 38.98 E-value: 6.90e-03
10 20 30
....*....|....*....|....*....|.
gi 505044757 421 GSMGFALPAAIGAKISNPDREVIAIIGDGEA 451
Cdd:pfam09364 140 GELGYALSHAYGAVLDNPDLIVPCVVGDGEA 170
|
|
| TPP_PK |
cd02011 |
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK ... |
421-451 |
7.54e-03 |
|
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK catalyzes the conversion of D-xylulose 5-phosphate and phosphate to acetyl phosphate, D-glyceraldehyde-3-phosphate and H2O. This enzyme requires divalent magnesium ions and TPP for activity.
Pssm-ID: 238969 [Multi-domain] Cd Length: 227 Bit Score: 38.08 E-value: 7.54e-03
10 20 30
....*....|....*....|....*....|.
gi 505044757 421 GSMGFALPAAIGAKISNPDREVIAIIGDGEA 451
Cdd:cd02011 62 GELGYSLSHAYGAVFDNPDLIVACVVGDGEA 92
|
|
| PRK05261 |
PRK05261 |
phosphoketolase; |
421-451 |
8.10e-03 |
|
phosphoketolase;
Pssm-ID: 235379 [Multi-domain] Cd Length: 785 Bit Score: 39.02 E-value: 8.10e-03
10 20 30
....*....|....*....|....*....|.
gi 505044757 421 GSMGFALPAAIGAKISNPDREVIAIIGDGEA 451
Cdd:PRK05261 142 GELGYSLSHAYGAAFDNPDLIVACVVGDGEA 172
|
|
| |
