|
Name |
Accession |
Description |
Interval |
E-value |
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
28-622 |
2.12e-146 |
|
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: 435.36 E-value: 2.12e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLyspsVESAGLRWVGTCNELNAAYAADGYSRySNKIGCLITTYGVGELSA 107
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAI----EAHPGIRWVGCCNELNAGYAADGYAR-VNGLGALVTTYGVGELSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGvAKSIDSRSSnfsDRNLHHlvpQLHDSNFkgpNHkvYHDMVKdRVACSVAYLeDIETACDQ 187
Cdd:COG3961 83 INGIAGAYAERVPVVHIVG-APGTRAQRR---GPLLHH---TLGDGDF---DH--FLRMFE-EVTVAQAVL-TPENAAAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 188 VDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQqdcivyPSENQLSDIINKITSWIYSSKTPAILGDVLTDR 267
Cdd:COG3961 149 IDRVLAAALREKRPVYIELPRDVADAPIEPPEAPLPLPPPA------SDPAALAAAVAAAAERLAKAKRPVILAGVEVHR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 268 YGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPn 347
Cdd:COG3961 223 FGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDP- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 348 AKIIQFHPNYIRLvdtrqgNEQMFKGINFAPILKELykridvSKLSLQYDSNVTQYTNETMRLEDPTNGQssiITQVHLQ 427
Cdd:COG3961 302 ERTIDIQPDSVRV------GGHIYPGVSLADFLEAL------AELLKKRSAPLPAPAPPPPPPPAAPDAP---LTQDRLW 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 428 KTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHsnahinggnvkedykpRLI 507
Cdd:COG3961 367 QRLQAFLDPGDIVVADTGTSLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDR----------------RVI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 508 LFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGK-YTNSTLIQcp 586
Cdd:COG3961 431 LLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYNDIANWDYAKLPEAFGGGNALgFRVTTEGE-- 508
|
570 580 590
....*....|....*....|....*....|....*.
gi 1806636768 587 skLALKLEELKnsNKRSGIELLEVKLGELDFPEQLK 622
Cdd:COG3961 509 --LEEALAAAE--ANTDRLTLIEVVLDKMDAPPLLK 540
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
29-208 |
5.82e-76 |
|
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: 239.70 E-value: 5.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRYsNKIGCLITTYGVGELSAL 108
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIE----ENPGLRWVGNCNELNAGYAADGYARV-KGLGALVTTYGVGELSAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVGVAksidSRSSNFSDRNLHHLVPqlhdsnfkGPNHKVYHDMVKDrVACSVAYLEDIETACDQV 188
Cdd:cd07038 76 NGIAGAYAEHVPVVHIVGAP----STKAQASGLLLHHTLG--------DGDFDVFLKMFEE-ITCAAARLTDPENAAEEI 142
|
170 180
....*....|....*....|
gi 1806636768 189 DNVIRDIYKYSKPGYIFVPA 208
Cdd:cd07038 143 DRVLRTALRESRPVYIEIPR 162
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
421-622 |
3.96e-75 |
|
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: 238.20 E-value: 3.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 421 ITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHsnahinggnvke 500
Cdd:cd02005 2 LTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDR------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 501 dykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGkytns 580
Cdd:cd02005 70 ----RVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGGG----- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1806636768 581 tliqCPSKLALKLEELKN-----SNKRSGIELLEVKLGELDFPEQLK 622
Cdd:cd02005 141 ----GLSFRVKTEGELDEalkdaLFNRDKLSLIEVILPKDDAPEALK 183
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
18-576 |
2.25e-58 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 206.09 E-value: 2.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 18 VSNRSATIpfGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLyspsVESAGLRWVGTCNELNAAYAADGYSRySNKIGCLI 97
Cdd:PLN02573 11 VSSSDATL--GRHLARRLVEIGVTDVFSVPGDFNLTLLDHL----IAEPGLNLIGCCNELNAGYAADGYAR-ARGVGACV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 98 TTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRssnfSDRNLHHLVpQLHDsnFkGPNHKVYHDmvkdrVACSVAY 177
Cdd:PLN02573 84 VTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDYG----TNRILHHTI-GLPD--F-SQELRCFQT-----VTCYQAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 178 LEDIETACDQVDNVIRDIYKYSKPGYIfvpadfadmSVTCdNLVNVPRIS-QQDCIVYPSENQLSDIIN------KITSW 250
Cdd:PLN02573 151 INNLEDAHELIDTAISTALKESKPVYI---------SVSC-NLAAIPHPTfSREPVPFFLTPRLSNKMSleaaveAAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 251 IYSSKTPAILGDVLTDRYGVSNFLNKLICKTGiWNFStVM--GKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHF 328
Cdd:PLN02573 221 LNKAVKPVLVGGPKLRVAKACKAFVELADASG-YPVA-VMpsAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 329 GVDINEINNGHYTFTYKPNaKIIQFHPNYIRLvdtrqGNEQMFKGINFAPILKELYKRIdvsklslqyDSNVTQYTN-ET 407
Cdd:PLN02573 299 GPIFNDYSSVGYSLLLKKE-KAIIVQPDRVTI-----GNGPAFGCVLMKDFLEALAKRV---------KKNTTAYENyKR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 408 MRL---EDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIA 484
Cdd:PLN02573 364 IFVpegEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 485 MQDHsnahinggnvkedykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIM-GPtrsYNDVMSWKW 563
Cdd:PLN02573 444 APDK----------------RVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVEIHdGP---YNVIKNWNY 504
|
570
....*....|...
gi 1806636768 564 TKLFEAFGDFDGK 576
Cdd:PLN02573 505 TGLVDAIHNGEGK 517
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
28-571 |
1.29e-46 |
|
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: 172.65 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:COG0028 6 ADALVEALEAEGVETVFGVPGGAILPLYDALR----RQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGVAksidsrSSNFSDRNLHHLVPQLhdsnfkgpnhkvyhDMVKDrVACSVAYLEDIETACDQ 187
Cdd:COG0028 82 VTGLADAYMDSVPVLAITGQV------PTSLIGRGAFQEVDQV--------------GLFRP-ITKWSYLVTDPEDLPEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 188 VDNVIRdIYKYSKPG--YIFVPADFADMsvTCDNLVNVPRISQQDCIVYPSENQLSDIINKITswiySSKTPAIL--GDV 263
Cdd:COG0028 141 LRRAFR-IATSGRPGpvVLDIPKDVQAA--EAEEEPAPPELRGYRPRPAPDPEAIEEAAELLA----AAKRPVILagGGA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 264 LtdRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTfT 343
Cdd:COG0028 214 R--RAGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLYLGML-GMHGTPAANEALAEADLVLAVGARFDDRVTGNWD-E 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 344 YKPNAKIIQFHP-------NY---IRLV-DTRQgneqmfkginfapILKELYKRIDvsKLSLQYDSNVTQYTNETMRLED 412
Cdd:COG0028 290 FAPDAKIIHIDIdpaeigkNYpvdLPIVgDAKA-------------VLAALLEALE--PRADDRAAWLARIAAWRAEYLA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 413 PTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQ-FSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHsna 491
Cdd:COG0028 355 AYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQmWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDR--- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 492 hinggnvkedykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIM----GPTRSYNDVMSWKWTKLF 567
Cdd:COG0028 432 -------------PVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQelfyGGRYSGTDLPNPDFAKLA 498
|
....
gi 1806636768 568 EAFG 571
Cdd:COG0028 499 EAFG 502
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
28-218 |
1.22e-30 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 117.72 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:pfam02776 2 AEALADVLKALGVDTVFGVPGGHILPLLDALA----KSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGvaksidsrSSNFSDRNLHHLVPQLHDSNFKGPnhkvyhdmvkdrVACSVAYLEDIETACDQ 187
Cdd:pfam02776 78 LTGLANAYVDSVPLLVISG--------QRPRSLVGRGALQQELDQLALFRP------------VTKWAVRVTSADEIPEV 137
|
170 180 190
....*....|....*....|....*....|..
gi 1806636768 188 VDNVIRD-IYKYSKPGYIFVPADFADMSVTCD 218
Cdd:pfam02776 138 LRRAFRAaLSGRPGPVYLEIPLDVLLEEVDED 169
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
244-383 |
3.92e-27 |
|
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: 106.88 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 244 INKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGqYNGKEGLKQVYEHFELCD 323
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 324 LVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRLVDTRQGNEQMFKGInfAPILKEL 383
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDA--KETLEAL 137
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
30-208 |
7.05e-25 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 100.88 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 30 YIFKRLLSIDTKSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRySNKIGCLITTYGVGELSALN 109
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALR----EGDKRIIDTVIHELGAAGAAAGYAR-AGGPPVVIVTSGTGLLNAIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 110 GIAGSFAENVKVLHIVGVAKSIDSrssnfsdrnlhhlVPQLHDSNFkgpnhkvYHDMVKDrVACSVAYLEDIETACDQVD 189
Cdd:cd06586 77 GLADAAAEHLPVVFLIGARGISAQ-------------AKQTFQSMF-------DLGMYRS-IPEANISSPSPAELPAGID 135
|
170
....*....|....*....
gi 1806636768 190 NVIRDIYKYSKPGYIFVPA 208
Cdd:cd06586 136 HAIRTAYASQGPVVVRLPR 154
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
29-147 |
6.72e-23 |
|
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: 95.29 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPsvesaGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARS-----GIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAV 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 1806636768 109 NGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLV 147
Cdd:cd07035 76 TGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALF 114
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
432-571 |
1.10e-20 |
|
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: 89.62 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 432 KFLNPGDVVVCETGSFQFSV-RDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFE 510
Cdd:cd00568 8 AALPEDAIVVNDAGNSAYWAyRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDR----------------PVVCIA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806636768 511 GDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGP----TRSYNDVMSWKWTKLFEAFG 571
Cdd:cd00568 72 GDGGFMMTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAfyggRVSGTDLSNPDFAALAEAYG 136
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
29-581 |
1.80e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 92.34 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSpsvesAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:PRK06725 19 GHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-----SGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVG-VAKSIDSRSSnFSDRNLHHLVPQLHDSNFKgpnhkvyhdmVKDrvacsvayledietaCDQ 187
Cdd:PRK06725 94 TGLADAYMDSIPLVVITGqVATPLIGKDG-FQEADVVGITVPVTKHNYQ----------VRD---------------VNQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 188 VDNVIRD---IYKYSKPG--YIFVPADFADMSVTC--DNLVNVPRISQQdciVYPSENQLSdiinKITSWIYSSKTPA-- 258
Cdd:PRK06725 148 LSRIVQEafyIAESGRPGpvLIDIPKDVQNEKVTSfyNEVVEIPGYKPE---PRPDSMKLR----EVAKAISKAKRPLly 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 259 ILGDVLtdRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGVDINEINNG 338
Cdd:PRK06725 221 IGGGVI--HSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGML-GMHGTYAANMAVTECDLLLALGVRFDDRVTG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 339 HYTFtYKPNAKII-------QFHPNYIrlVDTrqgneqmfkginfaPILKELYKRIDV---SKLSLQYDSNVTQYtnETM 408
Cdd:PRK06725 298 KLEL-FSPHSKKVhididpsEFHKNVA--VEY--------------PVVGDVKKALHMllhMSIHTQTDEWLQKV--KTW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 409 RLEDPT--NGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDF-AFPSQLKYISQGFFLSIGMALPAALGVGIAM 485
Cdd:PRK06725 359 KEEYPLsyKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFyKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 486 QDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNN--GYTIERAIMGPTRSYND--VMSW 561
Cdd:PRK06725 439 EEEL----------------VICIAGDASFQMNIQELQTIAENNIPVKVFIINNKflGMVRQWQEMFYENRLSEskIGSP 502
|
570 580
....*....|....*....|
gi 1806636768 562 KWTKLFEAFGDFDGKYTNST 581
Cdd:PRK06725 503 DFVKVAEAYGVKGLRATNST 522
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
28-601 |
1.25e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 89.81 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSvesagLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSD-----LIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKgpnhkvyhdmvkdrvacsvayledIETACDq 187
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQ------------------------IKKPEE- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 188 VDNVIR---DIYKYSKPG--YIFVPADFADMSVtcdNLVNVPRISQQDCIVY-PSENQLSDIINKITSWIYSSKTPAIL- 260
Cdd:PRK06276 134 IPEIFRaafEIAKTGRPGpvHIDLPKDVQEGEL---DLEKYPIPAKIDLPGYkPTTFGHPLQIKKAAELIAEAERPVILa 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 261 --GDVLTDR----YGVSNFLNKLICktgiwnfSTVMGKSVIDESNPTYMGQYnGKEGLK----QVYEhfelCDLVLHFGV 330
Cdd:PRK06276 211 ggGVIISGAseelIELSELVKIPVC-------TTLMGKGAFPEDHPLALGMV-GMHGTKaanySVTE----SDVLIAIGC 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 331 DINEINNGHYTfTYKPNAKIIQ--FHPNYIrlvdtrqgneqmfkGINFA---PI-----------LKELYKRIDVSKlsL 394
Cdd:PRK06276 279 RFSDRTTGDIS-SFAPNAKIIHidIDPAEI--------------GKNVRvdvPIvgdaknvlrdlLAELMKKEIKNK--S 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 395 QYDSNVTQYTNETMRLED----PTNGQSSIitqvhlqKTMPKFLNPGD-----VVVCETGSFQFSVRDFaFPSQL--KYI 463
Cdd:PRK06276 342 EWLERVKKLKKESIPRMDfddkPIKPQRVI-------KELMEVLREIDpskntIITTDVGQNQMWMAHF-FKTSAprSFI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 464 SQGFFLSIGMALPAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNG-- 541
Cdd:PRK06276 414 SSGGLGTMGFGFPAAIGAKVAKPDAN----------------VIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTlg 477
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1806636768 542 --YTIERAIMGPTRSYNDV-MSWKWTKLFEAFGdfdgkyTNSTLIQCPSKLALKLEELKNSNK 601
Cdd:PRK06276 478 mvYQWQNLYYGKRQSEVHLgETPDFVKLAESYG------VKADRVEKPDEIKEALKEAIKSGE 534
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
41-590 |
8.93e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 87.14 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 41 KSVFGVPGDFNLSLLEYLYSpsvesAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVK 120
Cdd:PRK06048 24 EVIFGYPGGAIIPVYDELYD-----SDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGIATAYMDSVP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 121 VLHIVG-VAKSIDSRSSnFSDRNLHHLVPQLHDSNFkgpnhkvyhdMVKDRvacsvayledietacDQVDNVIRD---IY 196
Cdd:PRK06048 99 IVALTGqVPRSMIGNDA-FQEADITGITMPITKHNY----------LVQDA---------------KDLPRIIKEafhIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 197 KYSKPGYIfvpadfadmsvtcdnLVNVPRISQQDCI--VYPSENQL----------SDIINKITSWIYSSKTPAIL--GD 262
Cdd:PRK06048 153 STGRPGPV---------------LIDLPKDVTTAEIdfDYPDKVELrgykptykgnPQQIKRAAELIMKAERPIIYagGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 263 VLTDRygVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGqYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTf 342
Cdd:PRK06048 218 VISSN--ASEELVELAETIPAPVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLA- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 343 TYKPNAKIIQFHpnyirlVDTrqgnEQMFKGINF-API-------LKELYKRIDvSKLSLQYDSNVTQYTNE---TMRLE 411
Cdd:PRK06048 294 SFAPNAKIIHID------IDP----AEISKNVKVdVPIvgdakqvLKSLIKYVQ-YCDRKEWLDKINQWKKEyplKYKER 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 412 DPTNGQSSIITQVHLqktmpkfLNPGDVVVCETGSFQ-FSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSn 490
Cdd:PRK06048 363 EDVIKPQYVIEQIYE-------LCPDAIIVTEVGQHQmWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKT- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 491 ahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWnNNGYtieraiMGPTRsyndvmswKWTKLFeaf 570
Cdd:PRK06048 435 ---------------VIDIAGDGSFQMNSQELATAVQNDIPVIVAIL-NNGY------LGMVR--------QWQELF--- 481
|
570 580
....*....|....*....|..
gi 1806636768 571 gdFDGKYTNSTLIQCPS--KLA 590
Cdd:PRK06048 482 --YDKRYSHTCIKGSVDfvKLA 501
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
43-579 |
2.81e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 85.26 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 43 VFGVPGDFNLSLLEylyspSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVL 122
Cdd:PRK08322 19 IFGIPGEENLDLLE-----ALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGMPMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 123 HIVGvAKSIDSrssnfsdrnlhhlvpqlhdsnfkgpNHKVYHDMVkDrvacSVAYLEDIETACDQV---DN---VIRDIY 196
Cdd:PRK08322 94 AITG-QKPIKR-------------------------SKQGSFQIV-D----VVAMMAPLTKWTRQIvspDNipeVVREAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 197 KYS---KPG--YIFVPADFADMSVTcdnLVNVPRISQQdcIVYPSENQlsdiINKITSWIYSSKTPAILGDVLTDRYGVS 271
Cdd:PRK08322 143 RLAeeeRPGavHLELPEDIAAEETD---GKPLPRSYSR--RPYASPKA----IERAAEAIQAAKNPLILIGAGANRKTAS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 272 NFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYngkeGLKQV-YEH--FELCDLVLHFGVDINEinnghYT-FTYKPN 347
Cdd:PRK08322 214 KALTEFVDKTGIPFFTTQMGKGVIPETHPLSLGTA----GLSQGdYVHcaIEHADLIINVGHDVIE-----KPpFFMNPN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 348 A--KIIQFH-------PNYIRLVDTrQGneqmfkgiNFAPILKELYKRI-DVSKLSLQYDSNVTQytNETMRLEDPTNGQ 417
Cdd:PRK08322 285 GdkKVIHINflpaevdPVYFPQVEV-VG--------DIANSLWQLKERLaDQPHWDFPRFLKIRE--AIEAHLEEGADDD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 418 S-SIITQ--VH-LQKTMPkflnPGDVVVCETGSFQFSvrdFA--FPSQLK---YISQGfFLSIGMALPAALGVGIAMQDH 488
Cdd:PRK08322 354 RfPMKPQriVAdLRKVMP----DDDIVILDNGAYKIW---FArnYRAYEPntcLLDNA-LATMGAGLPSAIAAKLVHPDR 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 489 snahinggnvkedykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGY-TIEraimgptrsyndvmsWKWTKLF 567
Cdd:PRK08322 426 ----------------KVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYgMIR---------------WKQENMG 474
|
570
....*....|..
gi 1806636768 568 eaFGDFDGKYTN 579
Cdd:PRK08322 475 --FEDFGLDFGN 484
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
29-540 |
1.12e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 83.33 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSpsveSAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:PRK07282 14 DLVLETLRDLGVDTIFGYPGGAVLPLYDAIYN----FEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVG-VAKSIDSRSSnFSDRNLHHLVPQLHDSNFKgpnhkvyhdmVKdrvacsvaylediETAcdQ 187
Cdd:PRK07282 90 TGIADAMSDSVPLLVFTGqVARAGIGKDA-FQEADIVGITMPITKYNYQ----------IR-------------ETA--D 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 188 VDNVIRDIYKYS---KPG--YIFVPADFADMSVTC--DNLVNVPriSQQDCIVyPSENQlsdiINKITSWIYSSKTPAIL 260
Cdd:PRK07282 144 IPRIITEAVHIAttgRPGpvVIDLPKDVSALETDFiyDPEVNLP--SYQPTLE-PNDMQ----IKKILKQLSKAKKPVIL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 261 GDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQyNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHY 340
Cdd:PRK07282 217 AGGGINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLFLGM-GGMHGSYAANIAMTEADFMINIGSRFDDRLTGNP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 341 TfTYKPNAKI--IQFHPNYI-RLVDTRqgneqmfkginfAPIL----KELYKRIDVSKLSLQYDSNVTQYTNETMRLedP 413
Cdd:PRK07282 296 K-TFAKNAKVahIDIDPAEIgKIIKTD------------IPVVgdakKALQMLLAEPTVHNNTEKWIEKVTKDKNRV--R 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 414 T-NGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFaFPSQ--LKYISQGFFLSIGMALPAALGVGIAMQDhsn 490
Cdd:PRK07282 361 SyDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQY-YPYQneRQLVTSGGLGTMGFGIPAAIGAKIANPD--- 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1806636768 491 ahinggnvKEdykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNN 540
Cdd:PRK07282 437 --------KE-----VILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNH 473
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
29-599 |
3.78e-15 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 78.72 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEylyspSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVD-----AIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVpqlhdsnfkgpnhkvyhdmvkDRVACSVAYLEDIETACDQV 188
Cdd:PRK06457 81 NGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLF---------------------DDVAVFNQILINPENAEYII 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 189 DNVIRDiyKYSKPG--YIFVPADFADMSVTCDNLVNVPRISQQdcivYPSE-NQLSDIINKitswiysSKTPAILgdVLT 265
Cdd:PRK06457 140 RRAIRE--AISKRGvaHINLPVDILRKSSEYKGSKNTEVGKVK----YSIDfSRAKELIKE-------SEKPVLL--IGG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 266 DRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGVDINEINnghytFTYK 345
Cdd:PRK06457 205 GTRGLGKEINRFAEKIGAPIIYTLNGKGILPDLDPKVMGGI-GLLGTKPSIEAMDKADLLIMLGTSFPYVN-----FLNK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 346 pNAKIIQfhpnyirlVDTRQGNEQMFKGINFA-PILKELYKRIDVS----KLSLQYDSNVTQYTNETMRLEdptNGQSSI 420
Cdd:PRK06457 279 -SAKVIQ--------VDIDNSNIGKRLDVDLSyPIPVAEFLNIDIEeksdKFYEELKGKKEDWLDSISKQE---NSLDKP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 421 ITQVHLQKTMPKFLNPGDVVVCETGSFQ-FSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMqdhsnahinggnvk 499
Cdd:PRK06457 347 MKPQRVAYIVSQKCKKDAVIVTDTGNVTmWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAV-------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 500 eDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGY---TIERAIMGPTRSYNDVMSWKWTKLFEAFGdfdgk 576
Cdd:PRK06457 413 -ENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLgmiKFEQEVMGYPEWGVDLYNPDFTKIAESIG----- 486
|
570 580
....*....|....*....|...
gi 1806636768 577 yTNSTLIQCPSKLALKLEELKNS 599
Cdd:PRK06457 487 -FKGFRLEEPKEAEEIIEEFLNT 508
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
28-540 |
7.40e-15 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 77.73 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSpsvESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:PRK08611 7 GEALVKLLQDWGIDHVYGIPGDSIDAVVDALRK---EQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLhhlvPQLHD--SNFkgpNHKVyhdMVKDRVAcsvayledietac 185
Cdd:PRK08611 84 LNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNL----EKMFEdvAVY---NHQI---MSAENLP------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 186 DQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDciVYPSENQlsdiINKITSWIYSSKTPAILGDVLT 265
Cdd:PRK08611 141 EIVNQAIRTAYEKKGVAVLTIPDDLPAQKIKDTTNKTVDTFRPTV--PSPKPKD----IKKAAKLINKAKKPVILAGLGA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 266 DRYGVSnfLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGVDineinnghYTFT-Y 344
Cdd:PRK08611 215 KHAKEE--LLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNL-GKIGTKPAYEAMQEADLLIMVGTN--------YPYVdY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 345 KPN-AKIIQfhpnyirlVDTRQgnEQMFK------GI--NFAPILKELYKRIDVSKlslqyDSNVTQYTNETMR-----L 410
Cdd:PRK08611 284 LPKkAKAIQ--------IDTDP--ANIGKrypvnvGLvgDAKKALHQLTENIKHVE-----DRRFLEACQENMAkwwkwM 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 411 EDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETG-SFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHS 489
Cdd:PRK08611 349 EEDENNASTPIKPERVMAAIQKIADDDAVLSVDVGtVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQ 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1806636768 490 NahinggnvkedykprlILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNN 540
Cdd:PRK08611 429 A----------------IAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQ 463
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
29-539 |
1.95e-14 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 76.49 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSpsveSAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:PRK06882 8 EMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHT----LGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFkgpnhkvyhdMVKDRvacsvaylEDIETACDQV 188
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSF----------IVKNA--------EDIPSTIKKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 189 DNvirdIYKYSKPG--YIFVPADfadmsvtcdnLVNvPriSQQDCIVYPSENQLSDI----------INKITSWIYSSKT 256
Cdd:PRK06882 146 FY----IASTGRPGpvVIDIPKD----------MVN-P--ANKFTYEYPEEVSLRSYnptvqghkgqIKKALKALLVAKK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 257 PAIL--GDVLTDRygVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGV--DI 332
Cdd:PRK06882 209 PVLFvgGGVITAE--CSEQLTQFAQKLNLPVTSSLMGLGAYPSTDKQFLGML-GMHGTYEANNAMHESDLILGIGVrfDD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 333 NEINNghyTFTYKPNAKIIQFH----------PNYIRLVDTRQGNEQMFKGI----NFA---PILKELYKRIDVSK---- 391
Cdd:PRK06882 286 RTTNN---LAKYCPNAKVIHIDidptsisknvPAYIPIVGSAKNVLEEFLSLleeeNLAksqTDLTAWWQQINEWKakkc 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 392 LSLQYDSNVTQYTNETMRLEDPTNGQSSIITQVHlQKTMpkflnpgdvvvcetgsfqFSVRDFAFPSQLKYISQGFFLSI 471
Cdd:PRK06882 363 LEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVG-QHQM------------------FAALHYPFDKPRRWINSGGAGTM 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1806636768 472 GMALPAALGVGIAMQDHsnahinggnvkedykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNN 539
Cdd:PRK06882 424 GFGLPAAIGVKFAHPEA----------------TVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
29-539 |
4.20e-14 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 75.24 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:PRK08979 8 SMIVRSLIDEGVKHIFGYPGGSVLDIYDALH----EKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVGVaksidsrssnfsdrnlhhlVPqlhdSNFKGPNhkvyhdmvkdrvacsvAYLEdietaCDQV 188
Cdd:PRK08979 84 TGIATAYMDSIPMVVLSGQ-------------------VP----SNLIGND----------------AFQE-----CDMI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 189 dNVIRDIYKYSkpgyiFVPADFADMSVTCDN-------------LVNVPRisqqDCI--------VYPSENQLSDI---- 243
Cdd:PRK08979 120 -GISRPVVKHS-----FLVKDAEDIPEIIKKafyiastgrpgpvVIDLPK----DCLnpailhpyEYPESIKMRSYnptt 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 244 ------INKITSWIYSSKTPAIL---GDVLTdryGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQ 314
Cdd:PRK08979 190 sghkgqIKRGLQALLAAKKPVLYvggGAIIS---GADKQILQLAEKLNLPVVSTLMGLGAFPGTHKNSLGML-GMHGRYE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 315 VYEHFELCDLVLHFGV--DINEINNGHytfTYKPNAKI--IQFHPNYI---------------RLVDT--RQGNEQmfKG 373
Cdd:PRK08979 266 ANMAMHNADLIFGIGVrfDDRTTNNLE---KYCPNATIlhIDIDPSSIsktvrvdipivgsadKVLDSmlALLDES--GE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 374 INFAPILKELYKRIDV--SKLSLQYDSNvtqytnetmrledptngqSSIITQVHLQKTMPKFLNPGDVVVCETGSFQ-FS 450
Cdd:PRK08979 341 TNDEAAIASWWNEIEVwrSRNCLAYDKS------------------SERIKPQQVIETLYKLTNGDAYVASDVGQHQmFA 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 451 VRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNI 530
Cdd:PRK08979 403 ALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDET----------------VVCVTGDGSIQMNIQELSTALQYDI 466
|
....*....
gi 1806636768 531 PLEVIIWNN 539
Cdd:PRK08979 467 PVKIINLNN 475
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
35-539 |
8.10e-14 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 74.35 E-value: 8.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 35 LLSIDTKSVFGVPGDFNLSLLEYLYSpsVESAGL-RWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAG 113
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDELYA--WEKKGLiKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIAT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 114 SFAENVKVLHIVG-VAKSI---DSrssnFSDRNLHHLVPQLhdsnfkgpnhkVYHDMVkdrvacsvayledIETACDQVD 189
Cdd:CHL00099 98 AQMDSVPLLVITGqVGRAFigtDA----FQEVDIFGITLPI-----------VKHSYV-------------VRDARDISR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 190 NVIRDIY--KYSKPG--YIFVPADfadmsVTCDNLVNVPRISQQDCIVY----PSENQLSDIINKITSWIYSSKTPAIL- 260
Cdd:CHL00099 150 IVAEAFYiaKHGRPGpvLIDIPKD-----VGLEKFDYYPPEPGNTIIKIlgcrPIYKPTIKRIEQAAKLILQSSQPLLYv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 261 --GDVLTDrygVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGlkQVYEHFEL--CDLVLHFGVDINEIN 336
Cdd:CHL00099 225 ggGAIISD---AHQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGML-GMHG--TAYANFAVseCDLLIALGARFDDRV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 337 NGHYTfTYKPNAKIIqfhpnYIRLVDTRQG-NEQMFKGI--NFAPILKELykrIDVSKLS-LQYDSNVTQYTNETMR--- 409
Cdd:CHL00099 299 TGKLD-EFACNAQVI-----HIDIDPAEIGkNRIPQVAIvgDVKKVLQEL---LELLKNSpNLLESEQTQAWRERINrwr 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 410 ----LEDPTNGQS----SIITQvhLQKTMPKFLNPGDVvvcetGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGV 481
Cdd:CHL00099 370 keypLLIPKPSTSlspqEVINE--ISQLAPDAYFTTDV-----GQHQMWAAQFLKCKPRKWLSSAGLGTMGYGLPAAIGA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1806636768 482 GIAmqdHSNAHInggnvkedykprlILFEGDGAAQMTIQELSTILKCNIPLEVIIWNN 539
Cdd:CHL00099 443 QIA---HPNELV-------------ICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
28-214 |
5.65e-13 |
|
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: 67.19 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALR----REGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGvakSIDSR---SSNFSDRNLhhlvpqlhdsnfkgpnHKVYHDmvkdrVACSVAYLEDIETA 184
Cdd:cd07039 79 LNGLYDAKRDRAPVLAIAG---QVPTDelgTDYFQEVDL----------------LALFKD-----VAVYNETVTSPEQL 134
|
170 180 190
....*....|....*....|....*....|
gi 1806636768 185 CDQVDNVIRDIYKYSKPGYIFVPADFADMS 214
Cdd:cd07039 135 PELLDRAIRTAIAKRGVAVLILPGDVQDAP 164
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
443-542 |
7.38e-13 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 66.45 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 443 ETGSFQFSV-RDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDhsnahinggnvkedykPRLILFEGDGAAQMTIQE 521
Cdd:pfam02775 1 DIGCHQMWAaQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPD----------------RPVVAIAGDGGFQMNLQE 64
|
90 100
....*....|....*....|.
gi 1806636768 522 LSTILKCNIPLEVIIWNNNGY 542
Cdd:pfam02775 65 LATAVRYNLPITVVVLNNGGY 85
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
41-540 |
6.31e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 68.59 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 41 KSVFGVPGDFNLSLLEYLYspsvESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVK 120
Cdd:PRK08527 19 KVVFGYPGGAILNIYDEIY----KQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTGLATAYMDSIP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 121 VLHIVG-VAKS---------ID----SRS---SNFSDRNLHHLvPQLHDSNF-------KGPnhkVYHDMVKDrVACSVA 176
Cdd:PRK08527 95 LVLISGqVPNSligtdafqeIDavgiSRPcvkHNYLVKSIEEL-PRILKEAFyiarsgrPGP---VHIDIPKD-VTATLG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 177 ---YLEDIetacdqvdnvirDIYKYsKPGYIFVPadfadmsvtcdnlvnvprisqqdcivypseNQlsdiINKITSWIYS 253
Cdd:PRK08527 170 efeYPKEI------------SLKTY-KPTYKGNS------------------------------RQ----IKKAAEAIKE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 254 SKTPAIL---GDVLTDrygVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGV 330
Cdd:PRK08527 203 AKKPLFYlggGAILSN---ASEEIRELVKKTGIPAVETLMARGVLRSDDPLLLGML-GMHGSYAANMAMSECDLLISLGA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 331 DINEINNGHyTFTYKPNAKIIQ--FHPNYI-RLVDTrqgneqmfkgiNFaPILKELyKRIDVSKLSLQYDSNVTQYTN-- 405
Cdd:PRK08527 279 RFDDRVTGK-LSEFAKHAKIIHvdIDPSSIsKIVNA-----------DY-PIVGDL-KNVLKEMLEELKEENPTTYKEwr 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 406 ETMRLEDPTNGQS------SIITQVHLQKTMPkfLNPGDVVVC-ETGSFQFSVRD---FAFPSQLkyISQGFFLSIGMAL 475
Cdd:PRK08527 345 EILKRYNELHPLSyedsdeVLKPQWVIERVGE--LLGDDAIIStDVGQHQMWVAQfypFNYPRQL--ATSGGLGTMGYGL 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806636768 476 PAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNN 540
Cdd:PRK08527 421 PAALGAKLAVPDKV----------------VINFTGDGSILMNIQELMTAVEYKIPVINIILNNN 469
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
436-571 |
2.86e-11 |
|
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: 62.61 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 436 PGDVVVCETGSFQfsvrDFAFPSQLKYISQGFFL-----SIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFE 510
Cdd:cd02002 15 PEDAIIVDEAVTN----GLPLRDQLPLTRPGSYFtlrggGLGWGLPAAVGAALANPDR----------------KVVAII 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806636768 511 GDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIM------GPTRSYNDVMSW-----KWTKLFEAFG 571
Cdd:cd02002 75 GDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLkrvgpeGPGENAPDGLDLldpgiDFAAIAKAFG 146
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
28-590 |
6.21e-10 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 62.13 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSP-SVESAGLRwvgtcNELNAAYAADGYSRYSNKIGCLITTYGVGELS 106
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQdKIQHVLVR-----HEQAAVHAADGYARATGKVGVALVTSGPGVTN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 107 ALNGIAGSFAENVKVLHIVGvaksidsrssnfsdrnlhhlvpqlhdsnfKGPNHKVYHDmvkdrvacsvAYLEdietaCD 186
Cdd:PRK06965 99 AVTGIATAYMDSIPMVVISG-----------------------------QVPTAAIGQD----------AFQE-----CD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 187 QVdNVIRDIYKYSkpgyiFVPADFADMSVTCDN-------------LVNVPR-ISQQDCIV-YPSENQL----------S 241
Cdd:PRK06965 135 TV-GITRPIVKHN-----FLVKDVRDLAETVKKafyiartgrpgpvVVDIPKdVSKTPCEYeYPKSVEMrsynpvtkghS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 242 DIINKITSWIYSSKTPAIL---GDVLTDrygVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEH 318
Cdd:PRK06965 209 GQIRKAVSLLLSAKRPYIYtggGVILAN---ASRELRQLADLLGYPVTNTLMGLGAYPASDKKFLGML-GMHGTYEANMA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 319 FELCDLVLHFGVDINE--INNGHYtFTYKPNAKI-IQFHPNYIrlvDTRQGNEQMFKGiNFAPILKELYKRIDVSKLSLQ 395
Cdd:PRK06965 285 MQHCDVLIAIGARFDDrvIGNPAH-FASRPRKIIhIDIDPSSI---SKRVKVDIPIVG-DVKEVLKELIEQLQTAEHGPD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 396 YDSNVTQY-TNETMRLED--PTNGQSSIITQVHLQKTMPKfLNPGDVVVC-ETGSFQ-FSVRDFAFPSQLKYISQGFFLS 470
Cdd:PRK06965 360 ADALAQWWkQIEGWRSRDclKYDRESEIIKPQYVVEKLWE-LTDGDAFVCsDVGQHQmWAAQFYRFNEPRRWINSGGLGT 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 471 IGMALPAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWnNNGYtieraiMG 550
Cdd:PRK06965 439 MGVGLPYAMGIKMAHPDDD----------------VVCITGEGSIQMCIQELSTCLQYDTPVKIISL-NNRY------LG 495
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1806636768 551 PTRSYNDVmswkwtklfeafgDFDGKYTNSTLIQCPS--KLA 590
Cdd:PRK06965 496 MVRQWQEI-------------EYSKRYSHSYMDALPDfvKLA 524
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
472-590 |
1.25e-09 |
|
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: 57.89 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 472 GMALPAALGVGIAMQDHsnahinggnvkedykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGytieraiMGp 551
Cdd:cd02015 53 GFGLPAAIGAKVARPDK----------------TVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGS-------LG- 108
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1806636768 552 trsyndvMSWKWTKLFeafgdFDGKYTNSTLIQCPS--KLA 590
Cdd:cd02015 109 -------MVRQWQELF-----YEGRYSHTTLDSNPDfvKLA 137
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
29-598 |
2.24e-09 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 60.25 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 29 EYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSpsveSAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSAL 108
Cdd:PRK07979 8 EMVVRSLIDQGVKQVFGYPGGAVLDIYDALHT----VGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 109 NGIAGSFAENVKVLHIVG-VAKSIDSRSSnfsdrnlhhlvpqLHDSNFKGPNHKVyhdmVKDRVAcsVAYLEDIETacdq 187
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGqVATSLIGYDA-------------FQECDMVGISRPV----VKHSFL--VKQTEDIPQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 188 vdnVIRDIYKYS---KPGYIFV--PADfadmsvTCDNLVNVPRISQQDCIVY---PSENQLSDIINKITSWIYSSKTPAI 259
Cdd:PRK07979 141 ---VLKKAFWLAasgRPGPVVVdlPKD------ILNPANKLPYVWPESVSMRsynPTTQGHKGQIKRALQTLVAAKKPVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 260 L--GDVLTDryGVSNFLNKLICKTGIWNFSTVMGKSVIdesnPTYMGQYNGKEGLKQVYEH---FELCDLVLHFGV--DI 332
Cdd:PRK07979 212 YvgGGAINA--ACHQQLKELVEKLNLPVVSSLMGLGAF----PATHRQSLGMLGMHGTYEAnmtMHNADVIFAVGVrfDD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 333 NEINNghyTFTYKPNAKI--IQFHPNYIR---------LVDTRQGNEQMFKGINFAP------ILKELYKRIDV--SKLS 393
Cdd:PRK07979 286 RTTNN---LAKYCPNATVlhIDIDPTSISktvtadipiVGDARQVLEQMLELLSQESahqpldEIRDWWQQIEQwrARQC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 394 LQYDSNvtqytnetmrlEDPTNGQSSIITQVHLQKtmpkflnpGDV-VVCETGSFQ-FSVRDFAFPSQLKYISQGFFLSI 471
Cdd:PRK07979 363 LKYDTH-----------SEKIKPQAVIETLWRLTK--------GDAyVTSDVGQHQmFAALYYPFDKPRRWINSGGLGTM 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 472 GMALPAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPleVIIWN-NNGYtieraiMG 550
Cdd:PRK07979 424 GFGLPAALGVKMALPEET----------------VVCVTGDGSIQMNIQELSTALQYELP--VLVLNlNNRY------LG 479
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806636768 551 PTRSYNDVM-------SW-----KWTKLFEAFGDFdgkytnSTLIQCP----SKLALKLEELKN 598
Cdd:PRK07979 480 MVKQWQDMIysgrhsqSYmqslpDFVRLAEAYGHV------GIQISHPdeleSKLSEALEQVRN 537
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
434-542 |
2.40e-09 |
|
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: 56.91 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 434 LNPGDVVVCETGSFQ--FSVRDFAF-PSQLkYISQGFfLSIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFE 510
Cdd:cd02010 12 MGDDDIVLLDVGAHKiwMARYYRTYaPNTC-LISNGL-ATMGVALPGAIGAKLVYPDR----------------KVVAVS 73
|
90 100 110
....*....|....*....|....*....|..
gi 1806636768 511 GDGAAQMTIQELSTILKCNIPLEVIIWNNNGY 542
Cdd:cd02010 74 GDGGFMMNSQELETAVRLKIPLVVLIWNDNGY 105
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
43-591 |
3.06e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 59.77 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 43 VFGVPGDFNLSLLEYLYSpsvesAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVL 122
Cdd:PRK07710 34 IFGYPGGAVLPLYDALYD-----CGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLADAMIDSLPLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 123 HIVG-VAKSIDSrSSNFSDRNLHHLVPQLHDSNFKgpnhkvyhdmvkdrvacsvayLEDIEtacdQVDNVIRD---IYKY 198
Cdd:PRK07710 109 VFTGqVATSVIG-SDAFQEADIMGITMPVTKHNYQ---------------------VRKAS----DLPRIIKEafhIATT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 199 SKPG--YIFVPADFA--DMSVTCDNLVNVPRISQQdciVYPseNQLSdiINKITSWIYSSKTPAILGDVLTDRYGVSNFL 274
Cdd:PRK07710 163 GRPGpvLIDIPKDMVveEGEFCYDVQMDLPGYQPN---YEP--NLLQ--IRKLVQAVSVAKKPVILAGAGVLHAKASKEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 275 NKLICKTGIWNFSTVMGKSVIDESNPTYMGQ------YNGKEGLkqvYEhfelCDLVLHFGVDINEINNGHYTFtYKPNA 348
Cdd:PRK07710 236 TSYAEQQEIPVVHTLLGLGGFPADHPLFLGMagmhgtYTANMAL---YE----CDLLINIGARFDDRVTGNLAY-FAKEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 349 KIIQFH----------PNYIRLV-DTRQGNEQMfkginfapiLKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQ 417
Cdd:PRK07710 308 TVAHIDidpaeigknvPTEIPIVaDAKQALQVL---------LQQEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 418 SsIITQVHlqktmpKFLNPGDVVVCETGSFQFSVRDF-AFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSnahingg 496
Cdd:PRK07710 379 K-AIEMLY------EITKGEAIVTTDVGQHQMWAAQYyPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDET------- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 497 nvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGytieraiMGPTRsyndvmswKWTKLFeafgdFDGK 576
Cdd:PRK07710 445 ---------VVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEA-------LGMVR--------QWQEEF-----YNQR 495
|
570
....*....|....*
gi 1806636768 577 YTNSTLIQCPSKLAL 591
Cdd:PRK07710 496 YSHSLLSCQPDFVKL 510
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
28-571 |
6.41e-09 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 58.85 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEylyspSVESAG-LRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGels 106
Cdd:PRK07064 6 GELIAAFLEQCGVKTAFGVISIHNMPILD-----AIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 107 ALNgIAGSFAE----NVKVLHIVGvakSIDSRssnFSDRNLH--HLVP-QLhdsnfkgpnhkvyhDMVKdrvACSVAYLE 179
Cdd:PRK07064 78 AGN-AAGALVEaltaGTPLLHITG---QIETP---YLDQDLGyiHEAPdQL--------------TMLR---AVSKAAFR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 180 --DIETACDQVDNVIRD-IYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDcivyPSENQLSDIINKITswiySSKT 256
Cdd:PRK07064 134 vrSAETALATIREAVRVaLTAPTGPVSVEIPIDIQAAEIELPDDLAPVHVAVPE----PDAAAVAELAERLA----AARR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 257 PAIL--GDVLTDRYGVsnflnKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHfelCDLVLHFGVDIne 334
Cdd:PRK07064 206 PLLWlgGGARHAGAEV-----KRLVDLGFGVVTSTQGRGVVPEDHPASLGAFNNSAAVEALYKT---CDLLLVVGSRL-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 335 inNGHYTFTYKpnakiIQFHPNYIRL-VDTRQGNE----QMFKGINFAPILKELYKRI-DVSKLSLQYDSNVTQYTNETM 408
Cdd:PRK07064 276 --RGNETLKYS-----LALPRPLIRVdADAAADGRgypnDLFVHGDAARVLARLADRLeGRLSVDPAFAADLRAAREAAV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 409 RLEDPTNGQSSIITQvHLQKTMPK-FLNPGDVVVCET--GSFQFSVRDfafPSQLKYISQGfflSIGMALPAALGVGIAM 485
Cdd:PRK07064 349 ADLRKGLGPYAKLVD-ALRAALPRdGNWVRDVTISNStwGNRLLPIFE---PRANVHALGG---GIGQGLAMAIGAALAG 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 486 QDhsnahinggnvkedyKPRLILFeGDGAAQMTIQELSTILKCNIPLEVIIWNNNGY----TIERAIMGPTRSYNDVMSW 561
Cdd:PRK07064 422 PG---------------RKTVGLV-GDGGLMLNLGELATAVQENANMVIVLMNDGGYgvirNIQDAQYGGRRYYVELHTP 485
|
570
....*....|
gi 1806636768 562 KWTKLFEAFG 571
Cdd:PRK07064 486 DFALLAASLG 495
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
41-539 |
1.03e-08 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 58.21 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 41 KSVFGVPGDFNLSLLEYLyspsVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVK 120
Cdd:PLN02470 29 DTVFAYPGGASMEIHQAL----TRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTGLADALLDSVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 121 VLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFkgpnhkvyhdMVKDrvacsvayLEDIEtacdqvdNVIRDIY---K 197
Cdd:PLN02470 105 LVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNY----------LVMD--------VEDIP-------RVIREAFflaS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 198 YSKPGYIfvpadfadmsvtcdnLVNVPRISQQDCIV------------------YPSENQLSDIINKITSwiysSKTPAI 259
Cdd:PLN02470 160 SGRPGPV---------------LVDIPKDIQQQLAVpnwnqpmklpgylsrlpkPPEKSQLEQIVRLISE----SKRPVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 260 L--GDVLTdrygVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMgQYNGKEGlkQVYEHFEL--CDLVLHFGVDINEI 335
Cdd:PLN02470 221 YvgGGCLN----SSEELREFVELTGIPVASTLMGLGAFPASDELSL-QMLGMHG--TVYANYAVdsADLLLAFGVRFDDR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 336 NNGHYTfTYKPNAKIIQFHPNYIRLVDTRQGN-------EQMFKGINfAPILKELYKRIDVS-----------KLSLQY- 396
Cdd:PLN02470 294 VTGKLE-AFASRASIVHIDIDPAEIGKNKQPHvsvcadvKLALQGLN-KLLEERKAKRPDFSawraeldeqkeKFPLSYp 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 397 ---DSNVTQYTNETmrLEDPTNGQSSIITQVHlQKTMpkflnpgdvvvcetgsfqFSVRDFAFPSQLKYISQGFFLSIGM 473
Cdd:PLN02470 372 tfgDAIPPQYAIQV--LDELTDGNAIISTGVG-QHQM------------------WAAQWYKYKEPRRWLTSGGLGAMGF 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806636768 474 ALPAALGVGIAMQDHSNAHInggnvkedykprlilfEGDGAAQMTIQELSTILKCNIPLEVIIWNN 539
Cdd:PLN02470 431 GLPAAIGAAAANPDAIVVDI----------------DGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
432-540 |
1.14e-08 |
|
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: 54.84 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 432 KFLNPGDVVVCETGSF-QFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFE 510
Cdd:cd02014 13 KRAPDDAIFTIDVGNVtVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDR----------------QVIALS 76
|
90 100 110
....*....|....*....|....*....|
gi 1806636768 511 GDGAAQMTIQELSTILKCNIPLEVIIWNNN 540
Cdd:cd02014 77 GDGGFAMLMGDLITAVKYNLPVIVVVFNNS 106
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
470-571 |
2.56e-08 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 56.78 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 470 SIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTI---ER 546
Cdd:PRK07586 386 AIGQGLPLATGAAVACPDR----------------KVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAIlrgEL 449
|
90 100 110
....*....|....*....|....*....|...
gi 1806636768 547 AIMG---PTRSYNDVMS-----WKWTKLFEAFG 571
Cdd:PRK07586 450 ARVGagnPGPRALDMLDlddpdLDWVALAEGMG 482
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
28-542 |
2.59e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 56.94 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSVEsagLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:PRK08266 7 GEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDR---IRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 108 LNGIAGSFAENVKVLHIVGvakSIdsrSSNFSDRN---LHHLVPQL--------------HDSNFKGPNHKVYHDMVKDR 170
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTG---QI---PSALIGKGrghLHEMPDQLatlrsftkwaerieHPSEAPALVAEAFQQMLSGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 171 vacsvayledietacdqvdnvirdiykySKPGYIFVPADFADMSVTCDNLVNVPRISQqdcivyPSENQlsDIINKITSW 250
Cdd:PRK08266 158 ----------------------------PRPVALEMPWDVFGQRAPVAAAPPLRPAPP------PAPDP--DAIAAAAAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 251 IYSSKTPAILgdVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQvyehfelCDLVLHFGv 330
Cdd:PRK08266 202 IAAAKNPMIF--VGGGAAGAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLGLNFAAAYELWPQ-------TDVVIGIG- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 331 diNEINNGHYTFTYKP-NAKIIQ----------FHPNYIRLVDTRQGneqmfkginfapiLKELYKRidVSKLSLQYDSN 399
Cdd:PRK08266 272 --SRLELPTFRWPWRPdGLKVIRididptemrrLKPDVAIVADAKAG-------------TAALLDA--LSKAGSKRPSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 400 vtqyTNETMRLEDPTNGQSSIIT-QVHLQKTMPKFLNPGDVVVCETGSFQFSVRdFAFP--SQLKYISQGFFLSIGMALP 476
Cdd:PRK08266 335 ----RAELRELKAAARQRIQAVQpQASYLRAIREALPDDGIFVDELSQVGFASW-FAFPvyAPRTFVTCGYQGTLGYGFP 409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806636768 477 AALGVGIAMQDHSNAHINGgnvkedykprlilfegDGAAQMTIQELSTILKCNIPLEVIIWNNNGY 542
Cdd:PRK08266 410 TALGAKVANPDRPVVSITG----------------DGGFMFGVQELATAVQHNIGVVTVVFNNNAY 459
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
28-595 |
2.87e-08 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 56.68 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLY-SPSVESAGLRwvgtcNELNAAYAADGYSRYSNKIGCLITTYGVGELS 106
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVR-----HEQAATHMADGYARATGKTGVVLVTSGPGATN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 107 ALNGIAGSFAENVKVLHIVGVAKSidsrssnfsdrnlhHLVPQ--LHDSNFKGpnhkVYHDMVKDRVacSVAYLEDIETa 184
Cdd:PRK06466 82 AITGIATAYMDSIPMVVLSGQVPS--------------TLIGEdaFQETDMVG----ISRPIVKHSF--MVKHASEIPE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 185 cdqvdnVIRD---IYKYSKPGYIFV--PADFADmsvtcdnlvnvPriSQQDCIVYPSENQL----------SDIINKITS 249
Cdd:PRK06466 141 ------IIKKafyIAQSGRPGPVVVdiPKDMTN-----------P--AEKFEYEYPKKVKLrsyspavrghSGQIRKAVE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 250 WIYSSKTPAIL--GDVLTDryGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPtymgQYNGKEGLKQVYE-----HFElc 322
Cdd:PRK06466 202 MLLAAKRPVIYsgGGVVLG--NASALLTELAHLLNLPVTNTLMGLGGFPGTDR----QFLGMLGMHGTYEanmamHHA-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 323 DLVLHFGVDINE-INNGHYTFTykPNAKIIQFHPNYIRLVDTRQGN-----------EQMFKginfapILKELYKRIDVS 390
Cdd:PRK06466 274 DVILAVGARFDDrVTNGPAKFC--PNAKIIHIDIDPASISKTIKADipivgpvesvlTEMLA------ILKEIGEKPDKE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 391 KLSLQYdSNVTQYtNETMRLEDPTNGQSSIITQVHLQKTMPKFLNpGDVVVC-ETGSFQ-FSVRDFAFPSQLKYISQGFF 468
Cdd:PRK06466 346 ALAAWW-KQIDEW-RGRHGLFPYDKGDGGIIKPQQVVETLYEVTN-GDAYVTsDVGQHQmFAAQYYKFNKPNRWINSGGL 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 469 LSIGMALPAALGVGIAMQDHSNAHINGgnvkedykprlilfegDGAAQMTIQELSTILKCNIPLEVIIWNNngytierAI 548
Cdd:PRK06466 423 GTMGFGLPAAMGVKLAFPDQDVACVTG----------------EGSIQMNIQELSTCLQYGLPVKIINLNN-------GA 479
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 549 MGPTRSYNDvMSWK-------------WTKLFEAFGDFDGKYTNstliqcPSKLALKLEE 595
Cdd:PRK06466 480 LGMVRQWQD-MQYEgrhshsymeslpdFVKLAEAYGHVGIRITD------LKDLKPKLEE 532
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
287-539 |
5.30e-08 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 55.83 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 287 STVMGKSVIDESNPTYMGQYnGKEGlkQVYEHFEL--CDLVLHFGVDINEINNGHYTfTYKPNAKIIQFH---------- 354
Cdd:PRK07418 257 TTLMGKGAFDEHHPLSVGML-GMHG--TAYANFAVteCDLLIAVGARFDDRVTGKLD-EFASRAKVIHIDidpaevgknr 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 355 -PNYIRLVDTRQGNEQM---FKGINFAPILKELYKRIDVSKlslqydsnvTQYTNETMRLEDPTNGQSSIitqVHLQKTM 430
Cdd:PRK07418 333 rPDVPIVGDVRKVLVKLlerSLEPTTPPRTQAWLERINRWK---------QDYPLVVPPYEGEIYPQEVL---LAVRDLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 431 PKFLNPGDVvvcetGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFE 510
Cdd:PRK07418 401 PDAYYTTDV-----GQHQMWAAQFLRNGPRRWISSAGLGTMGFGMPAAMGVKVALPDE----------------EVICIA 459
|
250 260
....*....|....*....|....*....
gi 1806636768 511 GDGAAQMTIQELSTILKCNIPLEVIIWNN 539
Cdd:PRK07418 460 GDASFLMNIQELGTLAQYGINVKTVIINN 488
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
244-601 |
8.55e-08 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 55.10 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 244 INKITSWIYSSKTPAIL--GDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFEL 321
Cdd:PRK09107 202 ITEAVELLANAKRPVIYsgGGVINSGPEASRLLRELVELTGFPITSTLMGLGAYPASGKNWLGML-GMHGTYEANMAMHD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 322 CDLVLHFGVDINEINNGHyTFTYKPNAKIIQFH--PNYIR----------------LVDTRQgneqMFKGINFAP---IL 380
Cdd:PRK09107 281 CDVMLCVGARFDDRITGR-LDAFSPNSKKIHIDidPSSINknvrvdvpiigdvghvLEDMLR----LWKARGKKPdkeAL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 381 KELYKRIDV--SKLSLQYDSNVT----QYTNEtmRLEDPTNGQSSIITQvhlqktmpkflnpgdvvvcETGSFQ-FSVRD 453
Cdd:PRK09107 356 ADWWGQIARwrARNSLAYTPSDDvimpQYAIQ--RLYELTKGRDTYITT-------------------EVGQHQmWAAQF 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 454 FAFPSQLKYISQGFFLSIGMALPAALGVGIAmqdHSNAHInggnvkedykprlILFEGDGAAQMTIQELSTILKCNIPLE 533
Cdd:PRK09107 415 FGFEEPNRWMTSGGLGTMGYGLPAALGVQIA---HPDALV-------------IDIAGDASIQMCIQEMSTAVQYNLPVK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 534 VIIWNNngytiERaiMGPTR-------------SYNDVMSwKWTKLFEAFGdfdgkytnSTLIQC--PSKLALKLEELKN 598
Cdd:PRK09107 479 IFILNN-----QY--MGMVRqwqqllhgnrlshSYTEAMP-DFVKLAEAYG--------AVGIRCekPGDLDDAIQEMID 542
|
...
gi 1806636768 599 SNK 601
Cdd:PRK09107 543 VDK 545
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
38-591 |
4.79e-07 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 52.96 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 38 IDTksVFGVPGDFNLSLLEYLYSPSVESAGLRwvgtcNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAE 117
Cdd:PRK08978 16 VDT--VFGYPGGAIMPVYDALYDGGVEHLLCR-----HEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGLADALLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 118 NVKVLHIVG-VAksidsrssnfsdrnlhhlvpqlhdSNFKGPNHKVYHDMVKDRVACSV-AYL-EDIetacDQVDNVIRD 194
Cdd:PRK08978 89 SVPVVAITGqVS------------------------SPLIGTDAFQEIDVLGLSLACTKhSFLvQSL----EELPEIMAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 195 ---IYKYSKPGYIFV--PAD--FADMSVTcDNLVNVPRISQqdcivyPSENQLSDIINKITSwiysSKTPAIlgdvltdr 267
Cdd:PRK08978 141 afeIASSGRPGPVLVdiPKDiqLAEGELE-PHLTTVENEPA------FPAAELEQARALLAQ----AKKPVL-------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 268 Y---GVS-----NFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYnGKEGLKQVYEHFELCDLVLHFGVDINEINNGH 339
Cdd:PRK08978 202 YvggGVGmagavPALREFLAATGMPAVATLKGLGAVEADHPYYLGML-GMHGTKAANLAVQECDLLIAVGARFDDRVTGK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 340 YTfTYKPNAKIIQF-----HPNYIRLVD-TRQGNeqmfkginFAPILKELYKRIDVSKLslqydsnvtQYTNETMRLEDP 413
Cdd:PRK08978 281 LN-TFAPHAKVIHLdidpaEINKLRQAHvALQGD--------LNALLPALQQPLNIDAW---------RQHCAQLRAEHA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 414 --TNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVR---DFAFPSQlkYISQGFFLSIGMALPAALGVGIAMQDH 488
Cdd:PRK08978 343 wrYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAqhmRFTRPEN--FITSSGLGTMGFGLPAAIGAQVARPDD 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 489 SnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGytieraiMGptrsyndvMSWKWTKLFe 568
Cdd:PRK08978 421 T----------------VICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQR-------LG--------MVRQWQQLF- 468
|
570 580
....*....|....*....|...
gi 1806636768 569 afgdFDGKYTNSTLIQCPSKLAL 591
Cdd:PRK08978 469 ----FDERYSETDLSDNPDFVML 487
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
470-546 |
7.06e-07 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 52.28 E-value: 7.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1806636768 470 SIGMALPAALGVGIAMQDhsnahinggnvkedyKPRLILFeGDGAAQMTIQELSTILKCNIPLEVIIWNNNGY-TIER 546
Cdd:PRK07524 408 TLGYGLPAAIGAALGAPE---------------RPVVCLV-GDGGLQFTLPELASAVEADLPLIVLLWNNDGYgEIRR 469
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
465-560 |
1.77e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 49.06 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 465 QGFFL--SIGMALPAALGVGIAMQdhsnahinggnvkedyKPRLILFEGDGAAQMTIQELSTILKCNIP-LEVIIWNNNG 541
Cdd:PRK06163 51 QNFYMlgSMGLAFPIALGVALAQP----------------KRRVIALEGDGSLLMQLGALGTIAALAPKnLTIIVMDNGV 114
|
90
....*....|....*....
gi 1806636768 542 YTIERAIMGPTRSYNDVMS 560
Cdd:PRK06163 115 YQITGGQPTLTSQTVDVVA 133
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
425-612 |
2.20e-06 |
|
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: 48.30 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 425 HLQKTMPKflnpGDVVVCETGSFQFSVRDFAFPSQ-LKYISQGFFLSIGMALPAALGVGIAMQDHsnahinggnvkedyk 503
Cdd:cd02004 7 ELQEALPD----DAIIVSDGGNTMDWARYILRPRKpRHRLDAGTFGTLGVGLGYAIAAALARPDK--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 504 pRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYN-DVMSW----KWTKLFEAFGdfdGKyt 578
Cdd:cd02004 68 -RVVLVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGlPVTTLlpdtRYDLVAEAFG---GK-- 141
|
170 180 190
....*....|....*....|....*....|....
gi 1806636768 579 nSTLIQCPSKLALKLEELKNSNKRSgieLLEVKL 612
Cdd:cd02004 142 -GELVTTPEELKPALKRALASGKPA---LINVII 171
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
426-547 |
4.81e-06 |
|
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: 47.50 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 426 LQKTMPKflnpgDVVVC-ETGSFQFSVRD-FAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDhsnahinggnvkedyK 503
Cdd:cd02013 13 LEKAMPE-----DAIVStDIGNICSVANSyLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPD---------------R 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1806636768 504 PrLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERA 547
Cdd:cd02013 73 P-VVAIAGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKK 115
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
66-539 |
6.95e-06 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 49.23 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 66 AGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDrnlhh 145
Cdd:PRK07525 42 AGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQE----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 146 lVPQLhdsnfkgpnhKVYHDMVKdrvacsvaYLE---DIETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDnlvn 222
Cdd:PRK07525 117 -AEQM----------PMFEDMTK--------YQEevrDPSRMAEVLNRVFDKAKRESGPAQINIPRDYFYGVIDVE---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 223 VPRISQQDcivYPSENQLSdiINKITSWIYSSKTPAIL-------GDVLTDRYGVSNFLNKLICKTGIWNFStvmgksvI 295
Cdd:PRK07525 174 IPQPVRLE---RGAGGEQS--LAEAAELLSEAKFPVILsgagvvlSDAIEECKALAERLDAPVACGYLHNDA-------F 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 296 DESNPTYMGQ--YNG-KEGLKQVYEhfelCDLVLHFGVDINEINN-GHYTFTYKP-NAKIIQ--FHPNYIRLV------- 361
Cdd:PRK07525 242 PGSHPLWVGPlgYNGsKAAMELIAK----ADVVLALGTRLNPFGTlPQYGIDYWPkDAKIIQvdINPDRIGLTkkvsvgi 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 362 --DTRQGNEQMFKGINFAP----ILKELYKRI---------DVSKLSLQYDSNVTQYtNETMRLEDPTngqssiitQVH- 425
Cdd:PRK07525 318 cgDAKAVARELLARLAERLagdaGREERKALIaaeksaweqELSSWDHEDDDPGTDW-NEEARARKPD--------YMHp 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 426 ------LQKTMPKflnpgDVVV-------CETGSFQFSvrdfaFPSQLKYISQGFFLSIGMALPAALGVGIAMQDhsnah 492
Cdd:PRK07525 389 rqalreIQKALPE-----DAIVstdignnCSIANSYLR-----FEKGRKYLAPGSFGNCGYAFPAIIGAKIACPD----- 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1806636768 493 inggnvkedyKPrLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNN 539
Cdd:PRK07525 454 ----------RP-VVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRN 489
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
41-126 |
1.41e-05 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 48.30 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 41 KSVFGVPGDFNLSLLEYLYSpSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVK 120
Cdd:PRK06456 18 KVIFGIPGLSNMQIYDAFVE-DLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGLITAYWDSSP 96
|
....*.
gi 1806636768 121 VLHIVG 126
Cdd:PRK06456 97 VIAITG 102
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
472-582 |
1.57e-04 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 44.59 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 472 GMALPAALGVGIAMQDHSNAHInggnvkedykprlilfEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERaimgp 551
Cdd:PRK07789 450 GYAVPAAMGAKVGRPDKEVWAI----------------DGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVR----- 508
|
90 100 110
....*....|....*....|....*....|.
gi 1806636768 552 trsyndvmswKWTKLFeafgdFDGKYTNSTL 582
Cdd:PRK07789 509 ----------QWQTLF-----YEERYSNTDL 524
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
28-126 |
3.64e-04 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 43.75 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 28 GEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLyspSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSA 107
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGAL---GRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHL 82
|
90
....*....|....*....
gi 1806636768 108 LNGIAGSFAENVKVLHIVG 126
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVG 101
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
457-540 |
7.94e-04 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 42.39 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 457 PSQlkYISQGFFLSIGMALPAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTILKCNIPLEVII 536
Cdd:PRK08155 409 PRQ--WLTSGGLGTMGFGLPAAIGAALANPERK----------------VLCFSGDGSLMMNIQEMATAAENQLDVKIIL 470
|
....
gi 1806636768 537 WNNN 540
Cdd:PRK08155 471 MNNE 474
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
43-127 |
9.28e-04 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 42.27 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 43 VFGVPGDFNLSLLEYLyspsvESAGLRWVGTCNELNAAYAADGYSRYSNKIG-CLITTyGVGELSALNGIAGSFAENVKV 121
Cdd:PRK07524 20 VFGIPGVHTVELYRGL-----AGSGIRHVTPRHEQGAGFMADGYARVSGKPGvCFIIT-GPGMTNIATAMGQAYADSIPM 93
|
....*.
gi 1806636768 122 LHIVGV 127
Cdd:PRK07524 94 LVISSV 99
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
436-544 |
1.11e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 41.78 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 436 PGDVVVCE-----TGSFQFSVrDFAFPSQLKYISQGfflSIGMALPAALGVGIAMQDHsnahinggnvkedykpRLILFE 510
Cdd:PRK12474 355 PDQAIYADealtsGLFFDMSY-DRARPHTHLPLTGG---SIGQGLPLAAGAAVAAPDR----------------KVVCPQ 414
|
90 100 110
....*....|....*....|....*....|....
gi 1806636768 511 GDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTI 544
Cdd:PRK12474 415 GDGGAAYTMQALWTMARENLDVTVVIFANRSYAI 448
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
434-542 |
2.54e-03 |
|
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: 39.60 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 434 LNPGDVVVCETGSFQ---FSVRDfafpsQLKYISQGFFLSIG-MALPAALGVGIAMQdhsnahinggnvkedyKP--RLI 507
Cdd:cd03371 12 APATAAVVSTTGMTSrelFELRD-----RPGGGHAQDFLTVGsMGHASQIALGIALA----------------RPdrKVV 70
|
90 100 110
....*....|....*....|....*....|....*.
gi 1806636768 508 LFEGDGAAQMTIQELSTILKCNIP-LEVIIWNNNGY 542
Cdd:cd03371 71 CIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAH 106
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
447-544 |
4.00e-03 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 40.24 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806636768 447 FQFSvrdfAFPSQLKYISqGfflSIGMALPAALGVGIAMQDHSnahinggnvkedykprLILFEGDGAAQMTIQELSTIL 526
Cdd:PRK08199 401 FRFR----RYRTQLAPTS-G---SMGYGLPAAIAAKLLFPERT----------------VVAFAGDGCFLMNGQELATAV 456
|
90
....*....|....*....
gi 1806636768 527 KCNIPLEVIIWNNNGY-TI 544
Cdd:PRK08199 457 QYGLPIIVIVVNNGMYgTI 475
|
|
| |
