|
Name |
Accession |
Description |
Interval |
E-value |
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-551 |
0e+00 |
|
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: 625.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELS 80
Cdd:COG3961 2 PMTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 81 ALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITdIATAPSEIDRLIRTTFITQ 160
Cdd:COG3961 82 AINGIAGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLGDGDFDHFLRMFEEVTVAQAVLT-PENAAAEIDRVLAAALREK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 161 RPSYLGLPANLVDLKVPGSllEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQF 240
Cdd:COG3961 161 RPVYIELPRDVADAPIEPP--EAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 241 PAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKNAT 320
Cdd:COG3961 239 PVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 321 FLGVQMKFALQNLLKVIPDVVKGYksvPVPTKTPANKGVPASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIF 400
Cdd:COG3961 319 YPGVSLADFLEALAELLKKRSAPL---PAPAPPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 401 PKDAYGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI 480
Cdd:COG3961 396 PEGATFIAQPLWGSIGYTLPAALGAALAA----PDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAI 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365599 481 HGPHAEYNEIQTWDHLALLPAFGAKKYENHKIATTGEWDALTTDSEFQKNSVIrLIELKLPVFDAPESLIK 551
Cdd:COG3961 472 HGPDGPYNDIANWDYAKLPEAFGGGNALGFRVTTEGELEEALAAAEANTDRLT-LIEVVLDKMDAPPLLKR 541
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
2-502 |
2.48e-103 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 322.81 E-value: 2.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 2 SEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSA 81
Cdd:PLN02573 14 SDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 82 LNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQR 161
Cdd:PLN02573 94 LNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAISTALKESK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 162 PSYLGLPANLVDLKVPgSLLEKPIDLSLKP---NDPEAEKEViDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLT 238
Cdd:PLN02573 174 PVYISVSCNLAAIPHP-TFSREPVPFFLTPrlsNKMSLEAAV-EAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADAS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 239 QFPAFVTPLGKGSIDEQHPRYGGVYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKN 318
Cdd:PLN02573 252 GYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 319 -ATFLGVQMKFALQNLLKVI---PDVVKGYKSVPVPTKTPAnKGVPAStPLKQEWLWNELSKFLQEGDVIISETGTSAFG 394
Cdd:PLN02573 332 gPAFGCVLMKDFLEALAKRVkknTTAYENYKRIFVPEGEPL-KSEPGE-PLRVNVLFKHIQKMLSGDTAVIAETGDSWFN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 395 INQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PLN02573 410 CQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAA----PDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGY 485
|
490 500
....*....|....*....|....*....
gi 398365599 475 TIEKLIH-GPhaeYNEIQTWDHLALLPAF 502
Cdd:PLN02573 486 TIEVEIHdGP---YNVIKNWNYTGLVDAI 511
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
364-549 |
8.30e-91 |
|
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: 276.72 E-value: 8.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 364 PLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFIG 443
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALA----APDRRVILLVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 444 DGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPHAEYNEIQTWDHLALLPAFGAK-KYENHKIATTGEWDALT 522
Cdd:cd02005 77 DGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGgGGLSFRVKTEGELDEAL 156
|
170 180
....*....|....*....|....*..
gi 398365599 523 TDSEFqKNSVIRLIELKLPVFDAPESL 549
Cdd:cd02005 157 KDALF-NRDKLSLIEVILPKDDAPEAL 182
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
9-169 |
8.25e-88 |
|
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: 268.21 E-value: 8.25e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 9 YLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSALNGIAGS 88
Cdd:cd07038 2 YLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 89 YAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGLP 168
Cdd:cd07038 82 YAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEIP 161
|
.
gi 398365599 169 A 169
Cdd:cd07038 162 R 162
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
3-505 |
1.17e-65 |
|
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: 223.11 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 3 EITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSA 81
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 82 LNGIAGSYAEhvgvlhvvgvpS-----ISAQAKQlllhHTLGNGDFTVFH--RMSANISETTSMITDIATAPSEIDRLIR 154
Cdd:COG0028 82 VTGLADAYMD-----------SvpvlaITGQVPT----SLIGRGAFQEVDqvGLFRPITKWSYLVTDPEDLPEVLRRAFR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 155 TtFITQR--PSYLGLPANLVDLKVPGSllEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQ 232
Cdd:COG0028 147 I-ATSGRpgPVVLDIPKDVQAAEAEEE--PAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 233 KLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSD 312
Cdd:COG0028 224 ALAERLGAPVVTTLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDID 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 313 YV---KVKNATfLGVQ--MKFALQNLLKVIPDVVKGYKS----VPVPTKTPANKGVPASTPLKQEWLWNELSKFLQEGDV 383
Cdd:COG0028 303 PAeigKNYPVD-LPIVgdAKAVLAALLEALEPRADDRAAwlarIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 384 IISETGTSAFGINQTIfpkDAYGISQVL----WGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIR 459
Cdd:COG0028 382 VVTDVGQHQMWAARYL---RFRRPRRFLtsggLGTMGYGLPAAIGAKLAR----PDRPVVAITGDGGFQMNLQELATAVR 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 398365599 460 WGLKPYLFVLNNDGYTIEK----LIHGPHAEYNEIQTWDHLALLPAFGAK 505
Cdd:COG0028 455 YGLPVKVVVLNNGGLGMVRqwqeLFYGGRYSGTDLPNPDFAKLAEAFGAK 504
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-169 |
1.61e-47 |
|
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: 162.90 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 8 KYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLSVLVTTFGVGELSALNGIAG 87
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 88 SYAEHVGVLHVVGVPSISAQAKQLllhhtlgnGDFTVFHRMSANISETTSMITDIATAPSEIDRLIRTTFITQRPSYLGL 167
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQT--------FQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRL 152
|
..
gi 398365599 168 PA 169
Cdd:cd06586 153 PR 154
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-177 |
3.36e-31 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 118.88 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 6 LGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNG 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 85 IAGSYAEhvgvlhvvGVP--SISAQAK-QLLLHHTLGNGDFTVfhRMSANISETTSMITDIATAPSEIDRLIRTTFI-TQ 160
Cdd:pfam02776 81 LANAYVD--------SVPllVISGQRPrSLVGRGALQQELDQL--ALFRPVTKWAVRVTSADEIPEVLRRAFRAALSgRP 150
|
170
....*....|....*..
gi 398365599 161 RPSYLGLPANLVDLKVP 177
Cdd:pfam02776 151 GPVYLEIPLDVLLEEVD 167
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
7-471 |
1.42e-30 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 126.02 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 7 GKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDgLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGI 85
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSD-LIHILTRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 86 AGSYAEHVgvlhvvgvPSIsAQAKQLLLHhTLGNGDFT------VFhrMSanISETTSMITDiataPSEIDRLIRTTF-- 157
Cdd:PRK06276 83 ATAYADSS--------PVI-ALTGQVPTK-LIGNDAFQeidalgIF--MP--ITKHNFQIKK----PEEIPEIFRAAFei 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 158 -ITQRPS--YLGLPANLVDLKVPGSLLEKPIDLSL---KPNDPEAEKEvIDTVLELIQNSKNPVILSDACASRHNVKKET 231
Cdd:PRK06276 145 aKTGRPGpvHIDLPKDVQEGELDLEKYPIPAKIDLpgyKPTTFGHPLQ-IKKAAELIAEAERPVILAGGGVIISGASEEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 232 QKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHS 311
Cdd:PRK06276 224 IELSELVKIPVCTTLMGKGAFPEDHPLALGM-VGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 312 DYVKV-KNatfLGVQM------KFALQNLLKVIP-----------DVVKGYKSVPVPTKTPANKgvpastPLKQEWLWNE 373
Cdd:PRK06276 303 DPAEIgKN---VRVDVpivgdaKNVLRDLLAELMkkeiknksewlERVKKLKKESIPRMDFDDK------PIKPQRVIKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 374 LSKFLQEGDVIISETGTSAFGINQ--------TIFPKDAygISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDG 445
Cdd:PRK06276 374 LMEVLREIDPSKNTIITTDVGQNQmwmahffkTSAPRSF--ISSGGLGTMGFGFPAAIGAKVAK----PDANVIAITGDG 447
|
490 500
....*....|....*....|....*.
gi 398365599 446 SLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06276 448 GFLMNSQELATIAEYDIPVVICIFDN 473
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-474 |
3.50e-28 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 118.72 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDgLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGEL 79
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGkVGVCVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 80 SALNGIAGSYAEHVGVLhvvgvpSISAQAKQLLLhhtlGNGDFtvfhrMSANISETTSMITD---IATAPSEIDRLIRTT 156
Cdd:PRK06048 84 NLVTGIATAYMDSVPIV------ALTGQVPRSMI----GNDAF-----QEADITGITMPITKhnyLVQDAKDLPRIIKEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 157 FI---TQRPSylglPAnLVDLkvPGSLLEKPIDL------SLKPNDP--EAEKEVIDTVLELIQNSKNPVILSDACASRH 225
Cdd:PRK06048 149 FHiasTGRPG----PV-LIDL--PKDVTTAEIDFdypdkvELRGYKPtyKGNPQQIKRAAELIMKAERPIIYAGGGVISS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 226 NVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGvYVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKN 305
Cdd:PRK06048 222 NASEELVELAETIPAPVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 306 VVEFHSDYVKVKNATFLGVQM----KFALQNLLKVIP--------DVVKGYKSvPVPTKTPANKGVpastpLKQEWLWNE 373
Cdd:PRK06048 301 IIHIDIDPAEISKNVKVDVPIvgdaKQVLKSLIKYVQycdrkewlDKINQWKK-EYPLKYKEREDV-----IKPQYVIEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 374 LSKFLQEGdVIISETGTSAFGINQtiFPKDAYGISQVLWGSIGfTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQE 453
Cdd:PRK06048 375 IYELCPDA-IIVTEVGQHQMWAAQ--YFKYKYPRTFITSGGLG-TMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQE 450
|
490 500
....*....|....*....|.
gi 398365599 454 ISTMIRWGLKPYLFVLNNdGY 474
Cdd:PRK06048 451 LATAVQNDIPVIVAILNN-GY 470
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
370-539 |
1.15e-27 |
|
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: 108.88 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 370 LWNELSKFLQEGDVIISETGTSAFGINQTIFPKDAYG-ISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQ 448
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRfLTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDGGFM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 449 LTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPH----AEYNEIQTWDHLALLPAFGAKkyeNHKIATTGEWDALTtd 524
Cdd:cd00568 78 MTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFyggrVSGTDLSNPDFAALAEAYGAK---GVRVEDPEDLEAAL-- 152
|
170
....*....|....*
gi 398365599 525 SEFQKNSVIRLIELK 539
Cdd:cd00568 153 AEALAAGGPALIEVK 167
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
201-316 |
2.08e-25 |
|
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: 101.49 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 201 IDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGvYVGTLSKQDVKQAVESAD 280
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 398365599 281 LILSVGALLSDFNTGSFSYSY-KTKNVVEFHSDYVKV 316
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFaPDAKIIHIDIDPAEI 116
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
1-471 |
2.59e-25 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 109.91 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITL-----GKYL-FERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTT 73
Cdd:PRK07282 1 MEKISLespksGSDLvLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGkLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 74 FGVGELSALNGIAGSYAEHV---GVLHVVGVPSISAQAKQLLlhHTLGngdftvfhrMSANISETTSMITDIAtapsEID 150
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVpllVFTGQVARAGIGKDAFQEA--DIVG---------ITMPITKYNYQIRETA----DIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 151 RLIRTTF---ITQRPS--YLGLPANLVDLKVpGSLLEKPIDL-----SLKPNDPEAEKevidtVLELIQNSKNPVILSDA 220
Cdd:PRK07282 146 RIITEAVhiaTTGRPGpvVIDLPKDVSALET-DFIYDPEVNLpsyqpTLEPNDMQIKK-----ILKQLSKAKKPVILAGG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 221 CASRHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYS 300
Cdd:PRK07282 220 GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLFLGM-GGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 301 YKTKNVVEFHSDYVK----VKNATFLGVQMKFALQNLL---KVIPDVVKGYKSV-----PVPTKTPANKGVPASTPLkqe 368
Cdd:PRK07282 299 AKNAKVAHIDIDPAEigkiIKTDIPVVGDAKKALQMLLaepTVHNNTEKWIEKVtkdknRVRSYDKKERVVQPQAVI--- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 369 wlwnELSKFLQEGD-VIISETGTSAFGINQTIFPKDAYG-ISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFIGDGS 446
Cdd:PRK07282 376 ----ERIGELTNGDaIVVTDVGQHQMWAAQYYPYQNERQlVTSGGLGTMGFGIPAAIGAKIA----NPDKEVILFVGDGG 447
|
490 500
....*....|....*....|....*
gi 398365599 447 LQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07282 448 FQMTNQELAILNIYKVPIKVVMLNN 472
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
14-507 |
3.71e-24 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 106.45 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 14 LKQVNVNTIFGLPGDFNLSLLDKIYEVDgLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAgsYAeh 92
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGkAGVCLSTLGPGATNLVTGVA--YA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 93 vgvlHVVGVP--SISAQAKQLLLHHtlgnGDFTVFH--RMSANISETTSMITDIATAPSeidrLIRTTF---ITQRP--S 163
Cdd:PRK08322 86 ----QLGGMPmvAITGQKPIKRSKQ----GSFQIVDvvAMMAPLTKWTRQIVSPDNIPE----VVREAFrlaEEERPgaV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 164 YLGLPANLVDLKVPGslleKPIDLSLkPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAF 243
Cdd:PRK08322 154 HLELPEDIAAEETDG----KPLPRSY-SRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 244 VTPLGKGSIDEQHPRYGGVyVGtLSKQD-VKQAVESADLILSVGALLSDFnTGSFSYSYKTKNVVEFHSDYVKVKNATFl 322
Cdd:PRK08322 229 TTQMGKGVIPETHPLSLGT-AG-LSQGDyVHCAIEHADLIINVGHDVIEK-PPFFMNPNGDKKVIHINFLPAEVDPVYF- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 323 gVQMKF------ALQNLLKVIPDVVKGYKSVPVPTKTP-----ANKGVPASTPLKQEWLWNELSKFLQEGDVIISETGts 391
Cdd:PRK08322 305 -PQVEVvgdianSLWQLKERLADQPHWDFPRFLKIREAieahlEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNG-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 392 afginqtifpkdAYGIsqvlWG--------------SIGFTT-GATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEIST 456
Cdd:PRK08322 382 ------------AYKI----WFarnyrayepntcllDNALATmGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELET 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 398365599 457 MIRWGLKPYLFVLNNDGY-TIE---KLIHGPHAeYNEIQTWDHLALLPAFGAKKY 507
Cdd:PRK08322 446 AVRLGLPLVVLILNDNAYgMIRwkqENMGFEDF-GLDFGNPDFVKYAESYGAKGY 499
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
2-471 |
5.85e-24 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 105.95 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 2 SEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELS 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 81 ALNGIAGSYAEHVGVLHvvgvpsISAQAKQlllhhTLGNGDftVFHRMSA-NISETTSMITDIATAPSEIDRLIRTTFIT 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVL------ISGQVPN-----SLIGTD--AFQEIDAvGISRPCVKHNYLVKSIEELPRILKEAFYI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 160 QR-----PSYLGLPAnlvDLKVPGSLLEKPIDLSLKPNDP--EAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQ 232
Cdd:PRK08527 148 ARsgrpgPVHIDIPK---DVTATLGEFEYPKEISLKTYKPtyKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 233 KLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVefHSD 312
Cdd:PRK08527 225 ELVKKTGIPAVETLMARGVLRSDDPLLLGM-LGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKII--HVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 313 -----YVKVKNATFLGV-QMKFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVPAS-----TPLKQEWLWNELSKFLQEG 381
Cdd:PRK08527 302 idpssISKIVNADYPIVgDLKNVLKEMLEELKEENPTTYKEWREILKRYNELHPLSyedsdEVLKPQWVIERVGELLGDD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 382 DVIISETGTSAFGINQTI-FPKDAYGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRW 460
Cdd:PRK08527 382 AIISTDVGQHQMWVAQFYpFNYPRQLATSGGLGTMGYGLPAALGAKLAV----PDKVVINFTGDGSILMNIQELMTAVEY 457
|
490
....*....|.
gi 398365599 461 GLKPYLFVLNN 471
Cdd:PRK08527 458 KIPVINIILNN 468
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-471 |
1.82e-21 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 98.15 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFnlslLDKIyeVDGLRWAGNA-------NELNAAYAADGYARIKG-LSVLVT 72
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDS----IDAV--VDALRKEQDKikfiqvrHEEVAALAAAAYAKLTGkIGVCLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 73 TFGVGELSALNGIAGSYAEhvgvlhvvgvpsisaQAKQLLLhhtLGNGDFTVFHRMSANISETTSMITDIA--------- 143
Cdd:PRK08611 75 IGGPGAIHLLNGLYDAKMD---------------HVPVLAL---AGQVTSDLLGTDFFQEVNLEKMFEDVAvynhqimsa 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 144 -TAPSEIDRLIRTTFITQRPSYLGLPANLVDLKVPGSlLEKPIDLSlKPNDPEAEKEVIDTVLELIQNSKNPVILSDACA 222
Cdd:PRK08611 137 eNLPEIVNQAIRTAYEKKGVAVLTIPDDLPAQKIKDT-TNKTVDTF-RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 223 srHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRyggvYVGTLSKQDVK---QAVESADLILSVGAllsdfntgsfSY 299
Cdd:PRK08611 215 --KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPY----SLGNLGKIGTKpayEAMQEADLLIMVGT----------NY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 300 SY------KTKnVVEFHSDYVKVK-----NATFLGvQMKFALQNLLKVIPDVvkgyKSVPVPTKTPANKGV--------- 359
Cdd:PRK08611 279 PYvdylpkKAK-AIQIDTDPANIGkrypvNVGLVG-DAKKALHQLTENIKHV----EDRRFLEACQENMAKwwkwmeede 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 360 -PASTPLKQEWLWNELSKFLqEGDVIIS-ETGTS----AFGINQTifPKDAYGISQVLWgsigfTTGATLGAAFAAEEID 433
Cdd:PRK08611 353 nNASTPIKPERVMAAIQKIA-DDDAVLSvDVGTVtvwsARYLNLG--TNQKFIISSWLG-----TMGCGLPGAIAAKIAF 424
|
490 500 510
....*....|....*....|....*....|....*...
gi 398365599 434 PNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK08611 425 PDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNN 462
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
9-169 |
1.07e-19 |
|
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: 86.05 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 9 YLFERLKQVNVNTIFGLPGDFNLSLLDKIYEvDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAG 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 88 SYAEhvgvlhvvgvpS-----ISAQAKQlllhHTLGNGDFTVF--HRMSANISETTSMITDIATAPSEIDRLIRT-TFIT 159
Cdd:cd07035 81 AYLD-----------SipllvITGQRPT----AGEGRGAFQEIdqVALFRPITKWAYRVTSPEEIPEALRRAFRIaLSGR 145
|
170
....*....|
gi 398365599 160 QRPSYLGLPA 169
Cdd:cd07035 146 PGPVALDLPK 155
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
4-458 |
4.41e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 90.67 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 4 ITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYE---VDGLRWAGNANELNAAYAADGYARIKGL-SVLVTTFGVGEL 79
Cdd:PRK06456 2 PTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlaNGELRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 80 SALNGIAGSYAEHV---GVLHVVGVPSISAQAKQllLHHTLGngdftVFhrmsANISETTSMITDIatapSEIDRLIRTT 156
Cdd:PRK06456 82 NLVTGLITAYWDSSpviAITGQVPRSVMGKMAFQ--EADAMG-----VF----ENVTKYVIGIKRI----DEIPQWIKNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 157 FI---TQRPS--YLGLPANLVDLKVPG-SLLEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKE 230
Cdd:PRK06456 147 FYiatTGRPGpvVIDIPRDIFYEKMEEiKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 231 TQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKT-KNVVEF 309
Cdd:PRK06456 227 VLELAELLHIPIVSTFPGKTAIPHDHPLYFGP-MGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 310 HSDYVKVKNATFLGVQM----KFALQNLLKVIPDVVKGYKsvpvptktpankgvpastplKQEWL--WNELSKFLQEGDV 383
Cdd:PRK06456 306 NIDPTDGEKAIKVDVGIygnaKIILRELIKAITELGQKRD--------------------RSAWLkrVKEYKEYYSQFYY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 384 IISETGTSAFGINQTI---FPKDAY---GISQ------VLW--------------GSIGFTTGATLGAAFAAeeidPNKR 437
Cdd:PRK06456 366 TEENGKLKPWKIMKTIrqaLPRDAIvttGVGQhqmwaeVFWevleprtfltssgmGTMGFGLPAAMGAKLAR----PDKV 441
|
490 500
....*....|....*....|.
gi 398365599 438 VILFIGDGSLQLTVQEISTMI 458
Cdd:PRK06456 442 VVDLDGDGSFLMTGTNLATAV 462
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-474 |
2.06e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 85.45 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEV-DGLRWAGNANELNAAYAADGYARIKGLS-VLVTTFGVGE 78
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAgDRIRVIHTRHEQAAGYMAFGYARSTGRPgVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 79 LSALNGIAGSYAehvgvlhvvgvpsisAQAKQLLL-----HHTLGNGdFTVFHRMSANISETTSMI--TDIATAPSEIDR 151
Cdd:PRK08266 81 LNAGAALLTAYG---------------CNSPVLCLtgqipSALIGKG-RGHLHEMPDQLATLRSFTkwAERIEHPSEAPA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 152 LIRTTFIT-----QRPSYLGLPANLVDLKVPGSLLEKPIDLSLKPNDPEAekevIDTVLELIQNSKNPVILSDACASrhN 226
Cdd:PRK08266 145 LVAEAFQQmlsgrPRPVALEMPWDVFGQRAPVAAAPPLRPAPPPAPDPDA----IAAAAALIAAAKNPMIFVGGGAA--G 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 227 VKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYggvyvgtLSKQDVKQAVESADLILSVGallSDFNTGSFSYSYKTKNV 306
Cdd:PRK08266 219 AGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG-------LNFAAAYELWPQTDVVIGIG---SRLELPTFRWPWRPDGL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 307 VEFHSDYVKVKNATF---LGVQ--MKFALQNLLkvipDVVKGYKSvpvptKTPANKGvpASTPLKQEWLwnELSKFLQEG 381
Cdd:PRK08266 289 KVIRIDIDPTEMRRLkpdVAIVadAKAGTAALL----DALSKAGS-----KRPSRRA--ELRELKAAAR--QRIQAVQPQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 382 ----DVIISETGTSAFGINQtifpkdaygISQV-LWGSIGF---------TTG--ATLGAAFA----AEEIDPNKRVILF 441
Cdd:PRK08266 356 asylRAIREALPDDGIFVDE---------LSQVgFASWFAFpvyaprtfvTCGyqGTLGYGFPtalgAKVANPDRPVVSI 426
|
490 500 510
....*....|....*....|....*....|...
gi 398365599 442 IGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PRK08266 427 TGDGGFMFGVQELATAVQHNIGVVTVVFNNNAY 459
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-507 |
2.50e-17 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 85.04 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 2 SEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGels 80
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGgLGVALTSTGTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 81 ALNgIAGSYAEhvgvlhvvgvpsiSAQAKQLLLHHTlGNGDFTVFHRMSANISETT---SM----------ITDIATAPS 147
Cdd:PRK07064 78 AGN-AAGALVE-------------ALTAGTPLLHIT-GQIETPYLDQDLGYIHEAPdqlTMlravskaafrVRSAETALA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 148 EIDRLIRTTfitqrpsyLGLPANLVDLKVP----GSLLEKPIDLS-LKPNDPEAEKEVIDTVLELIQNSKNPVILSDACA 222
Cdd:PRK07064 143 TIREAVRVA--------LTAPTGPVSVEIPidiqAAEIELPDDLApVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 223 sRHNVKkETQKLIDLTqFPAFVTPLGKGSIDEQHPRYGGVYVGTLSkqdVKQAVESADLILSVGALLSDFNTGSFSYSYK 302
Cdd:PRK07064 215 -RHAGA-EVKRLVDLG-FGVVTSTQGRGVVPEDHPASLGAFNNSAA---VEALYKTCDLLLVVGSRLRGNETLKYSLALP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 303 TkNVVEFHSDYVKV----KNATFLGVQMKFALQNLLKVIPDVVKG---YKSVPVPTKTPANKGVpastpLKQEWLWNELS 375
Cdd:PRK07064 289 R-PLIRVDADAAADgrgyPNDLFVHGDAARVLARLADRLEGRLSVdpaFAADLRAAREAAVADL-----RKGLGPYAKLV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 376 KFLQEG---------DVIISET--GTSAFGI---NQTIFPkdaygisqvLWGSIGFTTGATLGAAFAaeeiDPNKRVILF 441
Cdd:PRK07064 363 DALRAAlprdgnwvrDVTISNStwGNRLLPIfepRANVHA---------LGGGIGQGLAMAIGAALA----GPGRKTVGL 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 442 IGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY----TIEKLIHGPHAEYNEIQTWDHLALLPAFGAKKY 507
Cdd:PRK07064 430 VGDGGLMLNLGELATAVQENANMVIVLMNDGGYgvirNIQDAQYGGRRYYVELHTPDFALLAASLGLPHW 499
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-471 |
3.67e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 84.63 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 3 EITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEvDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSA 81
Cdd:PRK06725 14 EVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 82 LNGIAGSYAEHVGVLHvvgvpsISAQ-AKQLLLHHTLGNGDFTvfhRMSANISETTSMITDIAtapsEIDRLIRTTFI-- 158
Cdd:PRK06725 93 VTGLADAYMDSIPLVV------ITGQvATPLIGKDGFQEADVV---GITVPVTKHNYQVRDVN----QLSRIVQEAFYia 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 159 -TQRPS--YLGLPANLVDLKVPgSLLEKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLI 235
Cdd:PRK06725 160 eSGRPGpvLIDIPKDVQNEKVT-SFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 236 DLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFS-YSYKTKNV------VE 308
Cdd:PRK06725 239 RENRIPVVSTLMGLGAYPPGDPLFLGM-LGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLElFSPHSKKVhididpSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 309 FHsdyvkvKNATF---LGVQMKFALQNLL-KVIP-------DVVKGYKSvPVPTKTPANKGVpastpLKQEWLWNELSKf 377
Cdd:PRK06725 318 FH------KNVAVeypVVGDVKKALHMLLhMSIHtqtdewlQKVKTWKE-EYPLSYKQKESE-----LKPQHVINLVSE- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 378 LQEGDVIIsetgTSAFGINQ---TIFPKDAYGISQVLWGSIGfTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQEI 454
Cdd:PRK06725 385 LTNGEAIV----TTEVGQHQmwaAHFYKAKNPRTFLTSGGLG-TMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQEL 459
|
490
....*....|....*..
gi 398365599 455 STMIRWGLKPYLFVLNN 471
Cdd:PRK06725 460 QTIAENNIPVKVFIINN 476
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
10-471 |
1.19e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 83.27 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 10 LFERLKQVNVNTIFGLPGDFNLSLLDKIYEvDGLRWAGNANELNAAYAADGYARIKGL-SVLVTTFGVGELSALNGIAGS 88
Cdd:PRK07710 22 LIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKpGVVIATSGPGATNVVTGLADA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 89 YAEHVGVLHVVGVPSISaqakqlllhhTLGNGDFtvfhrMSANISETTSMITD---IATAPSEIDRLIRTTF---ITQRP 162
Cdd:PRK07710 101 MIDSLPLVVFTGQVATS----------VIGSDAF-----QEADIMGITMPVTKhnyQVRKASDLPRIIKEAFhiaTTGRP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 163 S--YLGLPAnlvDLKVPGSLLEKPIDLSLKPNDPEAEKEV--IDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLT 238
Cdd:PRK07710 166 GpvLIDIPK---DMVVEEGEFCYDVQMDLPGYQPNYEPNLlqIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 239 QFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKV-K 317
Cdd:PRK07710 243 EIPVVHTLLGLGGFPADHPLFLGM-AGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIgK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 318 NA-TFLGV--QMKFALQNLLKvipdvvkgyksvpvptktpaNKGVPASTP--LKQ--EW-----LWNE----------LS 375
Cdd:PRK07710 322 NVpTEIPIvaDAKQALQVLLQ--------------------QEGKKENHHewLSLlkNWkekypLSYKrnsesikpqkAI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 376 KFLQE---GDVIIsetgTSAFGINQtIFPKDAYGISQ----VLWGSIGfTTGATLGAAFAAEEIDPNKRVILFIGDGSLQ 448
Cdd:PRK07710 382 EMLYEitkGEAIV----TTDVGQHQ-MWAAQYYPFKTpdkwVTSGGLG-TMGFGLPAAIGAQLAKPDETVVAIVGDGGFQ 455
|
490 500
....*....|....*....|...
gi 398365599 449 LTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07710 456 MTLQELSVIKELSLPVKVVILNN 478
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
2-503 |
4.29e-16 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 81.35 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 2 SEITLGKYLFERLKQVNVNTIFG--LPGDFNLSLldkiyEVDGLRWAGNANELNAAYAADGYARIKGlsvlvttfGVGEL 79
Cdd:PRK06112 12 LNGTVAHAIARALKRHGVEQIFGqsLPSALFLAA-----EAIGIRQIAYRTENAGGAMADGYARVSG--------KVAVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 80 SALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTlgngDFTVFHRMS--ANISETTSMITDIaTAPSEIDRLIRTTF 157
Cdd:PRK06112 79 TAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQT----DRNAFQELDhiALFQSCTKWVRRV-TVAERIDDYVDQAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 158 I---TQR--PSYLGLPANLVDLKVPGSLLEKPIDLSLKPND-PEAEKEVIDTVLELIQNSKNPVI-------LSDACAsr 224
Cdd:PRK06112 154 TaatSGRpgPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDrTVPAPQRLAEAASLLAQAQRPVVvagggvhISGASA-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 225 hnvkkETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGV---YVGTLSK-QDVKQAVESADLILSVGALLSDFNTGSFSYS 300
Cdd:PRK06112 232 -----ALAALQSLAGLPVATTNMGKGAVDETHPLSLGVvgsLMGPRSPgRHLRDLVREADVVLLVGTRTNQNGTDSWSLY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 301 YKTKNVVEFHSDYVKV-KN--ATFLGVQMKFALQNLLKVIpdvvkgyKSVPVPTKTPANKGVPA---------------- 361
Cdd:PRK06112 307 PEQAQYIHIDVDGEEVgRNyeALRLVGDARLTLAALTDAL-------RGRDLAARAGRRAALEPaiaagreahredsapv 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 362 ----STPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFPKDA-------YGISQVLWGsIGFTTGATLGAafaae 430
Cdd:PRK06112 380 alsdASPIRPERIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAgmrfltpRGLAGLGWG-VPMAIGAKVAR----- 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365599 431 eidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNND--GYTI--EKLIHGPHAEYNEIQTWDHLALLPAFG 503
Cdd:PRK06112 454 ---PGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGFQKhaETVKFGTHTDACHFAAVDHAAIARACG 527
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
10-471 |
5.11e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 81.25 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 10 LFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGN---ANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGI 85
Cdd:PRK07418 25 LMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKHilvRHEQGAAHAADGYARATGkVGVCFGTSGPGATNLVTGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 86 AGSYAEH---VGVLHVVGVPSISAQAKQlllhhtlgngdftvfhrmSANISETTSMITD---IATAPSEIDRLIRTTFI- 158
Cdd:PRK07418 105 ATAQMDSvpmVVITGQVPRPAIGTDAFQ------------------ETDIFGITLPIVKhsyVVRDPSDMARIVAEAFHi 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 159 --TQRPSylglPAnLVDLK-------------VPGSLLEKPIDLSLKPNDPEaekevIDTVLELIQNSKNPVILSDACAS 223
Cdd:PRK07418 167 asSGRPG----PV-LIDIPkdvgqeefdyvpvEPGSVKPPGYRPTVKGNPRQ-----INAALKLIEEAERPLLYVGGGAI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 224 RHNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPryggVYVGTLSKQDVKQ---AVESADLILSVGALLSDFNTG---SF 297
Cdd:PRK07418 237 SAGAHAELKELAERFQIPVTTTLMGKGAFDEHHP----LSVGMLGMHGTAYanfAVTECDLLIAVGARFDDRVTGkldEF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 298 SYSYKtknVVEFHSDYVKV-KNAT----FLGvqmkfalqNLLKVIPDVVKGYKSVPVPTKTpankgvpastplkQEWLwN 372
Cdd:PRK07418 313 ASRAK---VIHIDIDPAEVgKNRRpdvpIVG--------DVRKVLVKLLERSLEPTTPPRT-------------QAWL-E 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 373 ELSKFLQEGDVIISETGTSafginqtIFPK-----------DAYGISQV----LW------------------GSIGFTT 419
Cdd:PRK07418 368 RINRWKQDYPLVVPPYEGE-------IYPQevllavrdlapDAYYTTDVgqhqMWaaqflrngprrwissaglGTMGFGM 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 398365599 420 GATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07418 441 PAAMGVKVAL----PDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN 488
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-471 |
7.08e-16 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 80.73 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGL--SVLVTTfGVGE 78
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKvgCVLVTS-GPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 79 LSALNGIAGSYAEHVGVLHvvgvpsISAQAKQLLlhhtLGNGDFTVFHRMSanISETTSMITDIATAPSEIDRLIRTTFI 158
Cdd:PRK06882 80 TNAITGIATAYTDSVPLVI------LSGQVPSNL----IGTDAFQECDMLG--ISRPVVKHSFIVKNAEDIPSTIKKAFY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 159 ---TQRPS--YLGLPANLVDlkvPGSLL--EKPIDLSLKPNDP--EAEKEVIDTVLELIQNSKNPVILSDACASRHNVKK 229
Cdd:PRK06882 148 iasTGRPGpvVIDIPKDMVN---PANKFtyEYPEEVSLRSYNPtvQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 230 ETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEF 309
Cdd:PRK06882 225 QLTQFAQKLNLPVTSSLMGLGAYPSTDKQFLGM-LGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 310 HSDYVKV-KNAT---------------FLGVqmkFALQNLLKVIPDVVKGYKSVPVPTKTPANKGVPASTPLKQEWLWNE 373
Cdd:PRK06882 304 DIDPTSIsKNVPayipivgsaknvleeFLSL---LEEENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 374 LSKFLQEGDVIISETGT-SAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFIGDGSLQLTVQ 452
Cdd:PRK06882 381 IYRLTNGDAYVASDVGQhQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFA----HPEATVVCVTGDGSIQMNIQ 456
|
490
....*....|....*....
gi 398365599 453 EISTMIRWGLKPYLFVLNN 471
Cdd:PRK06882 457 ELSTAKQYDIPVVIVSLNN 475
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
18-471 |
5.99e-14 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 74.47 E-value: 5.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 18 NVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAGSYAEHVGVL 96
Cdd:PRK08979 18 GVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYMDSIPMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 97 HvvgvpsISAQAKQLLlhhtLGNGDFTVFHR--MSANISETTSMITDiataPSEIDRLIRTTFI---TQRPS--YLGLPA 169
Cdd:PRK08979 98 V------LSGQVPSNL----IGNDAFQECDMigISRPVVKHSFLVKD----AEDIPEIIKKAFYiasTGRPGpvVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 170 NLVDlkvPGSLL--EKPIDLSLKPNDP--EAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVT 245
Cdd:PRK08979 164 DCLN---PAILHpyEYPESIKMRSYNPttSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 246 PLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDfntgsfsysyKTKNVVEFHsdyvkVKNATFLGVQ 325
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGM-LGMHGRYEANMAMHNADLIFGIGVRFDD----------RTTNNLEKY-----CPNATILHID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 326 MKfalqnllkviPDVVKGYKSVPVPTKTPANKGVPASTPLKQE------------WlWNELSKFlQEGDVIISETGTSAF 393
Cdd:PRK08979 305 ID----------PSSISKTVRVDIPIVGSADKVLDSMLALLDEsgetndeaaiasW-WNEIEVW-RSRNCLAYDKSSERI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 394 GINQTI------FPKDAYGISQV-----------------LW------GSIGFTTGATLGAAFAAeeidPNKRVILFIGD 444
Cdd:PRK08979 373 KPQQVIetlyklTNGDAYVASDVgqhqmfaalyypfdkprRWinsgglGTMGFGLPAAMGVKFAM----PDETVVCVTGD 448
|
490 500
....*....|....*....|....*..
gi 398365599 445 GSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK08979 449 GSIQMNIQELSTALQYDIPVKIINLNN 475
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
12-478 |
6.70e-14 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 74.26 E-value: 6.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 12 ERLKQVNVNTIFGLPGDFNLSLLDkIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAGSYA 90
Cdd:PRK07525 14 ETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 91 EHVGVLHvvgvpsISAQAKQLllhhTLGNGDF------TVFHRMSA---------NISETTSMITDIA---TAPSEIDrl 152
Cdd:PRK07525 93 AHTPVVL------VTPQAGTK----TIGQGGFqeaeqmPMFEDMTKyqeevrdpsRMAEVLNRVFDKAkreSGPAQIN-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 153 IRTTFITQrpsylglpanLVDLKVPgslleKPIDLSLKPNDPEAekevIDTVLELIQNSKNPVILSDACASRHNVKKETQ 232
Cdd:PRK07525 161 IPRDYFYG----------VIDVEIP-----QPVRLERGAGGEQS----LAEAAELLSEAKFPVILSGAGVVLSDAIEECK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 233 KLIDLTQFPAFVTPLGKGSIDEQHPryggVYVGTLSKQDVKQAVES---ADLILSVGALLSDFNT-GSFSYSY------- 301
Cdd:PRK07525 222 ALAERLDAPVACGYLHNDAFPGSHP----LWVGPLGYNGSKAAMELiakADVVLALGTRLNPFGTlPQYGIDYwpkdaki 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 302 -----------KTKNV-VEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKS-----------VPVPTKTPANKG 358
Cdd:PRK07525 298 iqvdinpdrigLTKKVsVGICGDAKAVARELLARLAERLAGDAGREERKALIAAEKSaweqelsswdhEDDDPGTDWNEE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 359 VPASTPlkqEWL-----WNELSKFLQEGDVIISETG-TSAFGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAAeei 432
Cdd:PRK07525 378 ARARKP---DYMhprqaLREIQKALPEDAIVSTDIGnNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIAC--- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 398365599 433 dPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEK 478
Cdd:PRK07525 452 -PDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEK 496
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
387-505 |
2.15e-13 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 67.61 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 387 ETGTSAFGINQTIFPKDAYG-ISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPY 465
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRyLTSGGLGTMGYGLPAAIGAKLA----RPDRPVVAIAGDGGFQMNLQELATAVRYNLPIT 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 398365599 466 LFVLNNDGYTIEKLIHGP-------HAEYNEIQTWDHLALLPAFGAK 505
Cdd:pfam02775 77 VVVLNNGGYGMTRGQQTPfgggrysGPSGKILPPVDFAKLAEAYGAK 123
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
5-471 |
3.23e-13 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 72.17 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 5 TLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDgLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSK-VKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 84 GIAGSYAEHVGVLhvvgvpSISAQAKQLLLHHtlgngDFtvFH-----RMSANISETTSMITDIATAPSEIDRLIRTTFI 158
Cdd:PRK06457 82 GLYDAKMDHAPVI------ALTGQVESDMIGH-----DY--FQevnltKLFDDVAVFNQILINPENAEYIIRRAIREAIS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 159 TQRPSYLGLPanlVDlkvpgsLLEKPIDLSLKPNDPEAEKEV---IDTVLELIQNSKNPVILSDACASRHNvkKETQKLI 235
Cdd:PRK06457 149 KRGVAHINLP---VD------ILRKSSEYKGSKNTEVGKVKYsidFSRAKELIKESEKPVLLIGGGTRGLG--KEINRFA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 236 DLTQFPAFVTPLGKGSIDEQHPR-YGGvyVGTLSKQDVKQAVESADLILSVGAllsdfntgSFSYSyktkNVVEFHSDYV 314
Cdd:PRK06457 218 EKIGAPIIYTLNGKGILPDLDPKvMGG--IGLLGTKPSIEAMDKADLLIMLGT--------SFPYV----NFLNKSAKVI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 315 KVK-NATFLGVQMKFAL------QNLLKVIP--------DVVKGYKSVPVptKTPANKGVPASTPLKQEWLWNELSKFLQ 379
Cdd:PRK06457 284 QVDiDNSNIGKRLDVDLsypipvAEFLNIDIeeksdkfyEELKGKKEDWL--DSISKQENSLDKPMKPQRVAYIVSQKCK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 380 EGDVIISETGTSAFGINQTIFPKDAYGISQVLW-GSIGFTTGATLGAAFAAeeiDPNKRVILFIGDGSLQLTVQEISTMI 458
Cdd:PRK06457 362 KDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWlGSMGIGVPGSVGASFAV---ENKRQVISFVGDGGFTMTMMELITAK 438
|
490
....*....|...
gi 398365599 459 RWGLKPYLFVLNN 471
Cdd:PRK06457 439 KYDLPVKIIIYNN 451
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
5-175 |
5.87e-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: 66.81 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 5 TLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 84 GIAGSYAEhvgvlhvvGVP--SISAQakqllLHHTLGNGDF---TVFHRMSANISETTSMITDIATAPSEIDRLIRTTFI 158
Cdd:cd07039 81 GLYDAKRD--------RAPvlAIAGQ-----VPTDELGTDYfqeVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIA 147
|
170
....*....|....*..
gi 398365599 159 TQRPSYLGLPANLVDLK 175
Cdd:cd07039 148 KRGVAVLILPGDVQDAP 164
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
19-471 |
1.75e-12 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 69.88 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 19 VNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAGSYAEHVGVLH 97
Cdd:PRK07979 19 VKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIPLVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 98 vvgvpsISAQ-AKQLLLHHTLGNGDFTVFHRMSANISETTSMITDIATapseidrLIRTTF---ITQRPS--YLGLPANL 171
Cdd:PRK07979 99 ------LSGQvATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQ-------VLKKAFwlaASGRPGpvVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 172 VD--LKVPGSLlekPIDLSLKPNDP--EAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDLTQFPAFVTPL 247
Cdd:PRK07979 166 LNpaNKLPYVW---PESVSMRSYNPttQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 248 GKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTKNVVEFHSDYVKVKNATFLGVQM- 326
Cdd:PRK07979 243 GLGAFPATHRQSLGM-LGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIv 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 327 ---KFALQNLLKVIP---------DVVKGYKSVPVPTKTPANKGVPASTPLKQEWLWNELSKfLQEGDVIIsetgTSAFG 394
Cdd:PRK07979 322 gdaRQVLEQMLELLSqesahqpldEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWR-LTKGDAYV----TSDVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 395 INQTI------FPKDAYGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFV 468
Cdd:PRK07979 397 QHQMFaalyypFDKPRRWINSGGLGTMGFGLPAALGVKMAL----PEETVVCVTGDGSIQMNIQELSTALQYELPVLVLN 472
|
...
gi 398365599 469 LNN 471
Cdd:PRK07979 473 LNN 475
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
10-471 |
9.59e-12 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 67.45 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 10 LFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAGS 88
Cdd:PLN02470 19 LVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGkVGVCIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 89 YAEHVGVLhvvgvpSISAQAKQLLlhhtLGNGDFtvfhrMSANISETTSMITD---IATAPSEIDRLIRTTFI---TQRP 162
Cdd:PLN02470 99 LLDSVPLV------AITGQVPRRM----IGTDAF-----QETPIVEVTRSITKhnyLVMDVEDIPRVIREAFFlasSGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 163 SylglPAnLVD--------LKVPGslLEKPIDL----SLKPNDPeaEKEVIDTVLELIQNSKNPVILS-DACAsrhNVKK 229
Cdd:PLN02470 164 G----PV-LVDipkdiqqqLAVPN--WNQPMKLpgylSRLPKPP--EKSQLEQIVRLISESKRPVVYVgGGCL---NSSE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 230 ETQKLIDLTQFPAFVTPLGKGSIDEQHPRY-------GGVYvgtlskqdVKQAVESADLILSVGALLSDFNTGSFSYSYK 302
Cdd:PLN02470 232 ELREFVELTGIPVASTLMGLGAFPASDELSlqmlgmhGTVY--------ANYAVDSADLLLAFGVRFDDRVTGKLEAFAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 303 TKNVVEFHSDYVKV-KNAT-FLGV--QMKFALQNLLKVI-------PDVVKGYKSV-------PVPTKTPANKGVPastp 364
Cdd:PLN02470 304 RASIVHIDIDPAEIgKNKQpHVSVcaDVKLALQGLNKLLeerkakrPDFSAWRAELdeqkekfPLSYPTFGDAIPP---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 365 lkqEWLWNELSKfLQEGDVIISeTGTsafGINQT------IFPKDAYGISQVLWGSIGFTTGATLGAAFAaeeiDPNKRV 438
Cdd:PLN02470 380 ---QYAIQVLDE-LTDGNAIIS-TGV---GQHQMwaaqwyKYKEPRRWLTSGGLGAMGFGLPAAIGAAAA----NPDAIV 447
|
490 500 510
....*....|....*....|....*....|...
gi 398365599 439 ILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PLN02470 448 VDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
368-478 |
9.76e-12 |
|
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: 63.77 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 368 EWLWNELSKFLQEGDVIISETGTSAFGINQ---TIFPKDAYGISQvlwGSIGFTTGATLGAAFAaeeiDPNKRVILFIGD 444
Cdd:cd02002 4 EYLAAALAAALPEDAIIVDEAVTNGLPLRDqlpLTRPGSYFTLRG---GGLGWGLPAAVGAALA----NPDRKVVAIIGD 76
|
90 100 110
....*....|....*....|....*....|....*
gi 398365599 445 GSLQLTVQEISTMIRWGLkPYLFV-LNNDGYTIEK 478
Cdd:cd02002 77 GSFMYTIQALWTAARYGL-PVTVViLNNRGYGALR 110
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
10-471 |
1.58e-11 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 67.03 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 10 LFERLKQVNVNTIFGLPGDFNLSLLDKIY--EVDGL------RwagnaNELNAAYAADGYARIKG-LSVLVTTFGVGELS 80
Cdd:CHL00099 16 LIDSLVRHGVKHIFGYPGGAILPIYDELYawEKKGLikhilvR-----HEQGAAHAADGYARSTGkVGVCFATSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 81 ALNGIAGSYAEHVGVLHvvgvpsISAQAKQLLLhhtlGNGDFT-----------VFHrmSANISETTSMITDIATApsei 149
Cdd:CHL00099 91 LVTGIATAQMDSVPLLV------ITGQVGRAFI----GTDAFQevdifgitlpiVKH--SYVVRDARDISRIVAEA---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 150 drlirtTFITQ--RPSylglPAnLVDlkVPGSL-LEKPIDLSLKPND-----------PEAEKEVIDTVLELIQNSKNP- 214
Cdd:CHL00099 155 ------FYIAKhgRPG----PV-LID--IPKDVgLEKFDYYPPEPGNtiikilgcrpiYKPTIKRIEQAAKLILQSSQPl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 215 ------VILSDAcasrhnvKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGAL 288
Cdd:CHL00099 222 lyvgggAIISDA-------HQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGM-LGMHGTAYANFAVSECDLLIALGAR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 289 LSDFNTGSFSYSYKTKNVVEFHSDYVKV-KNATflgVQmkfalqnlLKVIPDVVKGYKSVPVPTKTPANKGVPASTplkQ 367
Cdd:CHL00099 294 FDDRVTGKLDEFACNAQVIHIDIDPAEIgKNRI---PQ--------VAIVGDVKKVLQELLELLKNSPNLLESEQT---Q 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 368 EWL-----WNEL--------SKFLQEGDVI--ISETGTSAF-----GINQT-----IFPKDAYGISQVLWGSIGFTTGAT 422
Cdd:CHL00099 360 AWRerinrWRKEypllipkpSTSLSPQEVIneISQLAPDAYfttdvGQHQMwaaqfLKCKPRKWLSSAGLGTMGYGLPAA 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 398365599 423 LGAAFAaeeiDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:CHL00099 440 IGAQIA----HPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-471 |
2.02e-11 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 66.69 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLS--VLVTTfGVGE 78
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTgvVLVTS-GPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 79 LSALNGIAGSYAEHVGVLHvvgvpsISAQAKQlllhHTLGNGDF--TVFHRMSANISETTSMITDiataPSEIDRLIRTT 156
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVV------LSGQVPS----TLIGEDAFqeTDMVGISRPIVKHSFMVKH----ASEIPEIIKKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 157 FitqrpsYL---GLPANLV-----DLKVPGSLLEK--PIDLSLKPNDPEAEKEV--IDTVLELIQNSKNPVILSDACASR 224
Cdd:PRK06466 146 F------YIaqsGRPGPVVvdipkDMTNPAEKFEYeyPKKVKLRSYSPAVRGHSgqIRKAVEMLLAAKRPVIYSGGGVVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 225 HNVKKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFSYSYKTK 304
Cdd:PRK06466 220 GNASALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGM-LGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 305 NVVEFHSDYVKVKNATFLGVQMKFALQNLLKVIPDVVKGYKSVPvptktpaNKGVPAStplkqeWlWNELSKFLQEGDVI 384
Cdd:PRK06466 299 KIIHIDIDPASISKTIKADIPIVGPVESVLTEMLAILKEIGEKP-------DKEALAA------W-WKQIDEWRGRHGLF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 385 ISETGTSAFGINQTIFPK-------DAYGISQV-----------------LW---GSIGfTTGATLGAAFAAEEIDPNKR 437
Cdd:PRK06466 365 PYDKGDGGIIKPQQVVETlyevtngDAYVTSDVgqhqmfaaqyykfnkpnRWinsGGLG-TMGFGLPAAMGVKLAFPDQD 443
|
490 500 510
....*....|....*....|....*....|....
gi 398365599 438 VILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06466 444 VACVTGEGSIQMNIQELSTCLQYGLPVKIINLNN 477
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
11-474 |
2.03e-11 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 66.52 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 11 FERLKQVNVNTIFGLPGDFNLSLL----DKIYEVDGLRwagnanELNAAYAADGYARIKGLSVLV---TTFGVGelSALN 83
Cdd:PRK07092 19 IDLLRRFGITTVFGNPGSTELPFLrdfpDDFRYVLGLQ------EAVVVGMADGYAQATGNAAFVnlhSAAGVG--NAMG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 84 GIAGSYAehvgvlhvVGVP-SISA--QAKQLL-LHHTLGNGDFTVFHRMSANISETTSMITDIataPSEIDRLIRTTFIT 159
Cdd:PRK07092 91 NLFTAFK--------NHTPlVITAgqQARSILpFEPFLAAVQAAELPKPYVKWSIEPARAEDV---PAAIARAYHIAMQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 160 QR-PSYLGLPANlvDLKVP-GSLLEKPIDLSLKPnDPEAekevIDTVLELIQNSKNPVILSDACASRHNVKKETQKLIDL 237
Cdd:PRK07092 160 PRgPVFVSIPYD--DWDQPaEPLPARTVSSAVRP-DPAA----LARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 238 TQFPAFVTPL-GKGSIDEQHPRYGGVYvgTLSKQDVKQAVESADLILSVGALLsdfntgsFSYSyktknvVEFHSDYVKv 316
Cdd:PRK07092 233 HRAPVWVAPMsGRCSFPEDHPLFAGFL--PASREKISALLDGHDLVLVIGAPV-------FTYH------VEGPGPHLP- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 317 KNATFLGV------------------QMKFALQNLLKVIPDvvkGYKSVPVPTKTPAnKGVPASTPLKQEWLWNELSKFL 378
Cdd:PRK07092 297 EGAELVQLtddpgeaawapmgdaivgDIRLALRDLLALLPP---SARPAPPARPMPP-PAPAPGEPLSVAFVLQTLAALR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 379 QEGDVIISETgTSAFGINQTIFP---KDAY--GISqvlwGSIGFTTGATLGAAFAaeeiDPNKRVILFIGDGSLQLTVQE 453
Cdd:PRK07092 373 PADAIVVEEA-PSTRPAMQEHLPmrrQGSFytMAS----GGLGYGLPAAVGVALA----QPGRRVIGLIGDGSAMYSIQA 443
|
490 500
....*....|....*....|..
gi 398365599 454 ISTMIRWGLkPYLFV-LNNDGY 474
Cdd:PRK07092 444 LWSAAQLKL-PVTFViLNNGRY 464
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
14-471 |
7.50e-11 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 64.52 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 14 LKQVNVNTIFGLPGDFNLSLLDKIYEvDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAGSYAEH 92
Cdd:PRK08978 11 LRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGkVGVCIATSGPGATNLITGLADALLDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 93 VgvlhvvgvP--SISAQAKQLLLhhtlGNGDFT---VFHrMSANISETTSMITDIATAPSEIDRLIRttfITQ--RPSyl 165
Cdd:PRK08978 90 V--------PvvAITGQVSSPLI----GTDAFQeidVLG-LSLACTKHSFLVQSLEELPEIMAEAFE---IASsgRPG-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 166 glPAnLVDLkvPGSLLEKPIDLSLKPNDPEAEKEVIDTVLE----LIQNSKNPVI-------LSDACAS-RHnvkketqk 233
Cdd:PRK08978 152 --PV-LVDI--PKDIQLAEGELEPHLTTVENEPAFPAAELEqaraLLAQAKKPVLyvgggvgMAGAVPAlRE-------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 234 LIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTG---SFSYSYKtknVVEFH 310
Cdd:PRK08978 219 FLAATGMPAVATLKGLGAVEADHPYYLGM-LGMHGTKAANLAVQECDLLIAVGARFDDRVTGklnTFAPHAK---VIHLD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 311 SDYV---KVKNA--TFLG--VQMKFALQNLLKVIP--DVVKGYKsvpvpTKTPA---NKGVPASTPlkqeWLWNELSKFL 378
Cdd:PRK08978 295 IDPAeinKLRQAhvALQGdlNALLPALQQPLNIDAwrQHCAQLR-----AEHAWrydHPGEAIYAP----ALLKQLSDRK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 379 QEGDVIISETGTSAFGINQTIF---PKDAygISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFIGDGSLQLTVQEIS 455
Cdd:PRK08978 366 PADTVVTTDVGQHQMWVAQHMRftrPENF--ITSSGLGTMGFGLPAAIGAQVA----RPDDTVICVSGDGSFMMNVQELG 439
|
490
....*....|....*.
gi 398365599 456 TMIRWGLKPYLFVLNN 471
Cdd:PRK08978 440 TIKRKQLPVKIVLLDN 455
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-471 |
1.12e-10 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 64.05 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 2 SEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELS 80
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVALVTSGPGVTN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 81 ALNGIAGSYAEHVGVLHvvgvpsISAQAKQlllhHTLGNGDF----TVfhRMSANISETTSMITDiataPSEIDRLIRTT 156
Cdd:PRK06965 99 AVTGIATAYMDSIPMVV------ISGQVPT----AAIGQDAFqecdTV--GITRPIVKHNFLVKD----VRDLAETVKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 157 FITQRPsylGLPANLV-----DLKVPGSLLEKPIDLSLKPNDP--EAEKEVIDTVLELIQNSKNP-------VILSDACA 222
Cdd:PRK06965 163 FYIART---GRPGPVVvdipkDVSKTPCEYEYPKSVEMRSYNPvtKGHSGQIRKAVSLLLSAKRPyiytgggVILANASR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 223 srhnvkkETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTGSFS-YSY 301
Cdd:PRK06965 240 -------ELRQLADLLGYPVTNTLMGLGAYPASDKKFLGM-LGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAhFAS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 302 KTKNVVEFH------SDYVKVkNATFLGvQMKFALQNLLKVIPDvvkgyksvpvPTKTPANKGVPASTPLKQEWLWNELS 375
Cdd:PRK06965 312 RPRKIIHIDidpssiSKRVKV-DIPIVG-DVKEVLKELIEQLQT----------AEHGPDADALAQWWKQIEGWRSRDCL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 376 KFLQEGDVIISETgtsafgINQTIF---PKDAYGISQV----LW----------------GSIGfTTGATLGAAFAAEEI 432
Cdd:PRK06965 380 KYDRESEIIKPQY------VVEKLWeltDGDAFVCSDVgqhqMWaaqfyrfneprrwinsGGLG-TMGVGLPYAMGIKMA 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 398365599 433 DPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06965 453 HPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNN 491
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-539 |
1.66e-10 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 63.46 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 4 ITLGKYLFERLKQVNVNTIFGLPGDFNLSLldkiY---EVDGLRWAGNANELNAAYAADGYARIKGLS--VLVTTfGVGE 78
Cdd:PRK07524 2 TTCGEALVRLLEAYGVETVFGIPGVHTVEL----YrglAGSGIRHVTPRHEQGAGFMADGYARVSGKPgvCFIIT-GPGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 79 LSALNGIAGSYAEhvgvlhvvgvpSI------SAQAKQLLLHhtlGNGdftVFHR------MSANISETTSMITDIATAP 146
Cdd:PRK07524 77 TNIATAMGQAYAD-----------SIpmlvisSVNRRASLGK---GRG---KLHElpdqraMVAGVAAFSHTLMSAEDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 147 SEIDRLIrTTFITQRPSylglPanlVDLKVPGSLLEKPIDLSLK-----PNDPEAEKEVIDTVLELIQNSKNPVILSDAC 221
Cdd:PRK07524 140 EVLARAF-AVFDSARPR----P---VHIEIPLDVLAAPADHLLPapptrPARPGPAPAALAQAAERLAAARRPLILAGGG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 222 ASRHNvkKETQKLIDLTQFPAFVTPLGKGSIDEQHPRYGGvyvGTLSKQDVKQAVESADLILSVGALLSD-----FNTGS 296
Cdd:PRK07524 212 ALAAA--AALRALAERLDAPVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLAVGTELGEtdydvYFDGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 297 FSYSyktKNVVEFHSDYVK-VKN-ATFLGVQ--MKFALQNLLKVIPdvvkgyksvpvPTKTPANKGVPASTPLKQEwLWN 372
Cdd:PRK07524 287 FPLP---GELIRIDIDPDQlARNyPPALALVgdARAALEALLARLP-----------GQAAAADWGAARVAALRQA-LRA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 373 ELS-------KFLQ------EGDVIISETGTSAFGINQTiFPKDAYGI---SQVLWGSIGFTTGATLGAAFAAeeidPNK 436
Cdd:PRK07524 352 EWDpltaaqvALLDtilaalPDAIFVGDSTQPVYAGNLY-FDADAPRRwfnASTGYGTLGYGLPAAIGAALGA----PER 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 437 RVILFIGDGSLQLTVQEISTMIRWGLkPYLFVL-NNDGY-TIEK--LIHGPHAEYNEIQTWDHLALLPAFGAkkyENHKI 512
Cdd:PRK07524 427 PVVCLVGDGGLQFTLPELASAVEADL-PLIVLLwNNDGYgEIRRymVARDIEPVGVDPYTPDFIALARAFGC---AAERV 502
|
570 580
....*....|....*....|....*..
gi 398365599 513 ATTGEWDALTTDSeFQKNSVIrLIELK 539
Cdd:PRK07524 503 ADLEQLQAALRAA-FARPGPT-LIEVD 527
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
373-507 |
1.88e-10 |
|
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: 59.85 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 373 ELSKFLQEGDVIISEtGTSAFGINQTIFPKDAYGisQVL----WGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQ 448
Cdd:cd02004 7 ELQEALPDDAIIVSD-GGNTMDWARYILRPRKPR--HRLdagtFGTLGVGLGYAIAAALAR----PDKRVVLVEGDGAFG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365599 449 LTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPHAEYNEiqtwDHLALLP---------AFGAKKY 507
Cdd:cd02004 80 FSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGL----PVTTLLPdtrydlvaeAFGGKGE 143
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-505 |
2.54e-09 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 59.72 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 3 EITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGLS--VLVTTfGVGELS 80
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPgvVLVTS-GPGATN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 81 ALNGIAGSYAEHVGVLhvvgvpSISAQAKQlllhHTLGNGDF----TVfhRMSANISETTSMITDIatapSEIDRLIRTT 156
Cdd:PRK09107 89 AVTPLQDALMDSIPLV------CITGQVPT----HLIGSDAFqecdTV--GITRPCTKHNWLVKDV----NDLARVIHEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 157 F---ITQRPSylglPAnLVDlkVPGSLL----------EKPIDLSLKP---NDPEAekevIDTVLELIQNSKNPVILSDA 220
Cdd:PRK09107 153 FhvaTSGRPG----PV-VVD--IPKDVQfatgtytppqKAPVHVSYQPkvkGDAEA----ITEAVELLANAKRPVIYSGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 221 --CASRHNVKKETQKLIDLTQFPAFVTPLGKGSideqHPRYGGVYVGTLSKQ---DVKQAVESADLILSVGALLSDFNTG 295
Cdd:PRK09107 222 gvINSGPEASRLLRELVELTGFPITSTLMGLGA----YPASGKNWLGMLGMHgtyEANMAMHDCDVMLCVGARFDDRITG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 296 SF-SYSYKTKNVvefHSDY--------VKVkNATFLGvqmkfalqNLLKVIPDVVKGYKSVPvptKTPANKGVPASTPLK 366
Cdd:PRK09107 298 RLdAFSPNSKKI---HIDIdpssinknVRV-DVPIIG--------DVGHVLEDMLRLWKARG---KKPDKEALADWWGQI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 367 QEWLWNELSKFLQEGDVIISEtgtsaFGInQTIFP----KDAYGISQV----LWGS--IGF-------------TTGATL 423
Cdd:PRK09107 363 ARWRARNSLAYTPSDDVIMPQ-----YAI-QRLYEltkgRDTYITTEVgqhqMWAAqfFGFeepnrwmtsgglgTMGYGL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 424 GAAFAAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI----EKLIHG---PHAeYNEIQTwDHL 496
Cdd:PRK09107 437 PAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGMvrqwQQLLHGnrlSHS-YTEAMP-DFV 514
|
....*....
gi 398365599 497 ALLPAFGAK 505
Cdd:PRK09107 515 KLAEAYGAV 523
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
413-471 |
2.82e-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: 56.74 E-value: 2.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365599 413 GSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:cd02015 50 GTMGFGLPAAIGAKVAR----PDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNN 104
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
14-286 |
9.87e-09 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 57.94 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 14 LKQVNVNTIFGLPG---D--FNlSLLDKIYEVDGLRwagnaNELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAG 87
Cdd:PRK08617 15 LINQGVKYVFGIPGakiDrvFD-ALEDSGPELIVTR-----HEQNAAFMAAAIGRLTGkPGVVLVTSGPGVSNLATGLVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 88 SYAEHVgvlhvvgvP--SISAQAK---QL-LLHHTLGN-GDFTVFHRMSA------NISETTSMITDIATAPseidrlir 154
Cdd:PRK08617 89 ATAEGD--------PvvAIGGQVKradRLkRTHQSMDNvALFRPITKYSAevqdpdNLSEVLANAFRAAESG-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 155 ttfitqRP--SYLGLPANLVDLKVPGSLLEKPIDLSLKPNDPEAekevIDTVLELIQNSKNPVILSDACASRHNVKKETQ 232
Cdd:PRK08617 153 ------RPgaAFVSLPQDVVDAPVTSKAIAPLSKPKLGPASPED----INYLAELIKNAKLPVLLLGMRASSPEVTAAIR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398365599 233 KLIDLTQFPAFVTPLGKGSIDEQH-PRYGGvYVGTLSKQDVKQAVESADLILSVG 286
Cdd:PRK08617 223 RLLERTNLPVVETFQAAGVISRELeDHFFG-RVGLFRNQPGDELLKKADLVITIG 276
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
329-476 |
8.17e-08 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 54.85 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 329 ALQNLLKVIpdvvkGYKSVPVPTKTPANKGVPaSTPLKQEWLWNELSKFLQEGDVIISETGTSAFGInqtiFPKDA---- 404
Cdd:PRK07586 307 ALEALADAL-----GAKPAAPPLAAPARPPLP-TGALTPEAIAQVIAALLPENAIVVDESITSGRGF----FPATAgaap 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365599 405 YGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI 476
Cdd:PRK07586 377 HDWLTLTGGAIGQGLPLATGAAVAC----PDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAI 444
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
14-472 |
1.10e-07 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 54.71 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 14 LKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGL-SVLVTTFGVGELSALNGIAGSYAEH 92
Cdd:PRK08155 23 LERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKpAVCMACSGPGATNLVTAIADARLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 93 VGVLhvvgvpSISAQAKQLLLhhtlGNGDFTVF--HRMSANISETTSMITDIATAPSEIDRLIRttfITQ--RPSylglP 168
Cdd:PRK08155 103 IPLV------CITGQVPASMI----GTDAFQEVdtYGISIPITKHNYLVRDIEELPQVISDAFR---IAQsgRPG----P 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 169 AnLVDlkVPGSLLEKPIDLSLKPND------PEAEKEVIDTVLELIQNSKNPV-------ILSDACAsrhnvkkETQKLI 235
Cdd:PRK08155 166 V-WID--IPKDVQTAVIELEALPAPaekdaaPAFDEESIRDAAAMINAAKRPVlylgggvINSGAPA-------RARELA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 236 DLTQFPAFVTPLGKGSIDEQHPRYGGVyVGTLSKQDVKQAVESADLILSVGALLSDFNTG---SFSYSYKTKNVVEFHSD 312
Cdd:PRK08155 236 EKAQLPTTMTLMALGMLPKAHPLSLGM-LGMHGARSTNYILQEADLLIVLGARFDDRAIGkteQFCPNAKIIHVDIDRAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 313 YVKVKNAtFLGVQ--MKFALQNLLKVIP--------DVVKGYKSvPVPTKTPAnkgvpASTPLKQEWLWNELSKFLQEGD 382
Cdd:PRK08155 315 LGKIKQP-HVAIQadVDDVLAQLLPLVEaqpraewhQLVADLQR-EFPCPIPK-----ADDPLSHYGLINAVAACVDDNA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 383 VIISETGTSAFGINQtifpkdAYGIS---QVL----WGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEIS 455
Cdd:PRK08155 388 IITTDVGQHQMWTAQ------AYPLNrprQWLtsggLGTMGFGLPAAIGAALAN----PERKVLCFSGDGSLMMNIQEMA 457
|
490
....*....|....*..
gi 398365599 456 TMIRWGLKPYLFVLNND 472
Cdd:PRK08155 458 TAAENQLDVKIILMNNE 474
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
7-478 |
1.87e-07 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 53.96 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 7 GKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEvDGLRWAGNANELNAAYAADGYA---RIKGLSVLvtTFGVGELSALN 83
Cdd:PRK05858 8 GRLAARRLKAHGVDTMFTLSGGHLFPLYDGARE-EGIRLIDVRHEQTAAFAAEAWAkltRVPGVAVL--TAGPGVTNGMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 84 GIAGSYAEHVGVLHvvgvpsISAQAKQLllhhTLGNG-----DFTVFHRMSANISETtsmITDIATAPSEIDRLIRTTFI 158
Cdd:PRK05858 85 AMAAAQFNQSPLVV------LGGRAPAL----RWGMGslqeiDHVPFVAPVTKFAAT---AQSAENAGRLVDQALQAAVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 159 TQR-PSYLGLPANLV-----DLKVPGSLLEKPIDLSlkpNDPEAekevIDTVLELIQNSKNPVIL--SDACASRhnVKKE 230
Cdd:PRK05858 152 PHRgPVFVDFPMDHAfsmadDDGRPGALTELPAGPT---PDPDA----LARAAGLLAEAQRPVIMagTDVWWGH--AEAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 231 TQKLIDLTQFPAFVTPLGKGSIDEQHPryggvyvgTLSKQDVKQAVESADLILSVGALLsDFNTGSFSYSYKTKNVvefH 310
Cdd:PRK05858 223 LLRLAEELGIPVLMNGMGRGVVPADHP--------LAFSRARGKALGEADVVLVVGVPM-DFRLGFGVFGGTAQLV---H 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 311 SDYVKVKNATFLGVQMkfALQNLLKVIPDVVKGYKSVPV-------------PTKTPANKGVPAS--TPLKQEWLWNELS 375
Cdd:PRK05858 291 VDDAPPQRAHHRPVAA--GLYGDLSAILSALAGAGGDRTdhqgwieelrtaeTAARARDAAELADdrDPIHPMRVYGELA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 376 KFLQEGDVIISETGTSAFGINQTIFPKDAYGisqvlW---GSIGfTTGATLGAAFAAEEIDPNKRVILFIGDGSLQLTVQ 452
Cdd:PRK05858 369 PLLDRDAIVIGDGGDFVSYAGRYIDPYRPGC-----WldpGPFG-CLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLM 442
|
490 500
....*....|....*....|....*..
gi 398365599 453 EISTMIRWGLkPYLFVLNNDG-YTIEK 478
Cdd:PRK05858 443 DVDTLVRHNL-PVVSVIGNNGiWGLEK 468
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
372-508 |
2.08e-07 |
|
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: 51.14 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 372 NELSKFLQEGDVIISETGTSAFGINQTIFpkdAYGISQVLWgSIGFTT-GATLGAAFAAEEIDPNKRVILFIGDGSLQLT 450
Cdd:cd02010 6 HDLRAVMGDDDIVLLDVGAHKIWMARYYR---TYAPNTCLI-SNGLATmGVALPGAIGAKLVYPDRKVVAVSGDGGFMMN 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365599 451 VQEISTMIRWGLKPYLFVLNNDGYTI----EKLIHGPHAeYNEIQTWDHLALLPAFGAKKYE 508
Cdd:cd02010 82 SQELETAVRLKIPLVVLIWNDNGYGLikwkQEKEYGRDS-GVDFGNPDFVKYAESFGAKGYR 142
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
364-471 |
4.48e-07 |
|
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: 50.22 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 364 PLKQEWLWNELSKFLQEGDVIISETGTSA-FGINQTIFPKDAYGISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFI 442
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTvWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLA----YPDRQVIALS 76
|
90 100
....*....|....*....|....*....
gi 398365599 443 GDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:cd02014 77 GDGGFAMLMGDLITAVKYNLPVIVVVFNN 105
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-476 |
9.30e-07 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 51.80 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEITLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKGL-SVLVTTFGVGEL 79
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRpGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 80 SALNGIAgsyaehvgvlhvvgvpsisaQAKQ----LLL------HHTLGNGDFTV--FHRMSANISETTSMITDIATAPS 147
Cdd:PRK08199 85 NASIGVH--------------------TAFQdstpMILfvgqvaRDFREREAFQEidYRRMFGPMAKWVAEIDDAARIPE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 148 EIDRLIRTTfITQRPSylglPanlVDLKVPGSLL----EKPIDLSLKPNDPEAEKEVIDTVLELIQNSKNPVIL------ 217
Cdd:PRK08199 145 LVSRAFHVA-TSGRPG----P---VVLALPEDVLsetaEVPDAPPYRRVAAAPGAADLARLAELLARAERPLVIlggsgw 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 218 -SDACAsrhnvkketqkliDLTQFP-AFVTPLG-----KGSIDEQHPRYGGvYVGTLSKQDVKQAVESADLILSVGALLS 290
Cdd:PRK08199 217 tEAAVA-------------DLRAFAeRWGLPVAcafrrQDLFDNRHPNYAG-DLGLGINPALAARIREADLVLAVGTRLG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 291 DFNTGSFS---YSYKTKNVVEFHSDYV---KVKNATfLGVQ--MKFALQNLLKVIPDVV-----------KGYKSVPVPT 351
Cdd:PRK08199 283 EVTTQGYTlldIPVPRQTLVHVHPDAEelgRVYRPD-LAIVadPAAFAAALAALEPPASpawaewtaaahADYLAWSAPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 352 KTPankgvpasTPLKQEWLWNELSKFLQEgDVIISeTGTSAF-GINQTIFPKDAYGisqvlwGSIGFTTGAT---LGAAF 427
Cdd:PRK08199 362 PGP--------GAVQLGEVMAWLRERLPA-DAIIT-NGAGNYaTWLHRFFRFRRYR------TQLAPTSGSMgygLPAAI 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 398365599 428 AAEEIDPNKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY-TI 476
Cdd:PRK08199 426 AAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTI 475
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
14-297 |
1.11e-06 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 51.52 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 14 LKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALNGIAGSYAEh 92
Cdd:PRK07789 41 LEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGrVGVCMATSGPGATNLVTPIADANMD- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 93 vgvlhvvGVP--SISAQAKQLLlhhtLGNGDFtvfhrMSANISETTSMITD---IATAPSEIDRLIRTTF---ITQRPSy 164
Cdd:PRK07789 120 -------SVPvvAITGQVGRGL----IGTDAF-----QEADIVGITMPITKhnfLVTDADDIPRVIAEAFhiaSTGRPG- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 165 lglpANLVDlkVPGSLLEKPIDLSLKP--------NDPEAEKEVIDTVLELIQNSKNPVILSDACASRHNVKKETQKLID 236
Cdd:PRK07789 183 ----PVLVD--IPKDALQAQTTFSWPPrmdlpgyrPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAE 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365599 237 LTQFPAFVTPLGKGSIDEQHPRYGGV--YVGTLSkqdVKQAVESADLILSVGALLSDFNTG---SF 297
Cdd:PRK07789 257 LTGIPVVTTLMARGAFPDSHPQHLGMpgMHGTVA---AVAALQRSDLLIALGARFDDRVTGkldSF 319
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
360-474 |
2.01e-06 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 50.38 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 360 PASTPLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTiFPKDAYGISQVlwGSIGFTTGATLGAAFAaeeiDPNKRVI 439
Cdd:PRK08327 380 KDRGPITPAYLSYCLGEVADEYDAIVTEYPFVPRQARLN-KPGSYFGDGSA--GGLGWALGAALGAKLA----TPDRLVI 452
|
90 100 110
....*....|....*....|....*....|....*..
gi 398365599 440 LFIGDGSLQLTVQEISTMI--RWGLKPYLFVLNNDGY 474
Cdd:PRK08327 453 ATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
364-478 |
4.59e-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: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 364 PLKQEWLWNELSKFLQEgDVIIS-ETGTSAFGINQTI-FPKDAYGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILF 441
Cdd:cd02013 3 PMHPRQVLRELEKAMPE-DAIVStDIGNICSVANSYLrFEKPRSFIAPLSFGNCGYALPAIIGAKAAA----PDRPVVAI 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 398365599 442 IGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEK 478
Cdd:cd02013 78 AGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
5-85 |
6.64e-05 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 45.75 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 5 TLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDGLRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGELSALN 83
Cdd:PRK09124 4 TVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNLHLIN 83
|
..
gi 398365599 84 GI 85
Cdd:PRK09124 84 GL 85
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-84 |
3.79e-04 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 43.36 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 1 MSEiTLGKYLFERLKQVNVNTIFGLPGDFNLSLLDKIYEVDG-LRWAGNANELNAAYAADGYARIKG-LSVLVTTFGVGE 78
Cdd:PRK08273 1 MSQ-TVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGA 79
|
....*.
gi 398365599 79 LSALNG 84
Cdd:PRK08273 80 IHLLNG 85
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
374-474 |
5.22e-04 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 41.52 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 374 LSKFLQEGDVIISETGTSAFGIN---QTIFPKDA---YGISqvlwgSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSL 447
Cdd:cd02003 8 LNEAIGDDDVVINAAGSLPGDLHklwRARTPGGYhleYGYS-----CMGYEIAAGLGAKLAK----PDREVYVLVGDGSY 78
|
90 100
....*....|....*....|....*..
gi 398365599 448 QLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:cd02003 79 LMLHSEIVTAVQEGLKIIIVLFDNHGF 105
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
364-474 |
5.93e-04 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 41.50 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 364 PLKQEWLWNELSKFLQEGDVIISETGTSAFGINQTIFP-KDAYGISQVLWGSIGFTTGATLGAAFAaeeiDPNKRVILFI 442
Cdd:cd02006 7 PIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVyKPRHWINCGQAGPLGWTVPAALGVAAA----DPDRQVVALS 82
|
90 100 110
....*....|....*....|....*....|..
gi 398365599 443 GDGSLQLTVQEISTMIRWGLkPYLFVLNNDGY 474
Cdd:cd02006 83 GDYDFQFMIEELAVGAQHRI-PYIHVLVNNAY 113
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
384-476 |
1.82e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 41.01 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365599 384 IISETGTSAFGINQTIFPKDA-YGISQVLWGSIGFTTGATLGAAFAAeeidPNKRVILFIGDGSLQLTVQEISTMIRWGL 462
Cdd:PRK12474 359 IYADEALTSGLFFDMSYDRARpHTHLPLTGGSIGQGLPLAAGAAVAA----PDRKVVCPQGDGGAAYTMQALWTMARENL 434
|
90
....*....|....
gi 398365599 463 KPYLFVLNNDGYTI 476
Cdd:PRK12474 435 DVTVVIFANRSYAI 448
|
|
| |
