|
Name |
Accession |
Description |
Interval |
E-value |
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-556 |
0e+00 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 226470 [Multi-domain] Cd Length: 557 Bit Score: 933.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELS 80
Cdd:COG3961 1 SSPITVGDYLFDRLAQLGIKSIFGVPGDYNLSLLDKIYSVPGLRWVGNANELNAAYAADGYARLNGISALVTTFGVGELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 81 ALNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQ 160
Cdd:COG3961 81 ALNGIAGSYAEHVPVVHIVGVPTTSAQASGLLLHHTLGDGDFKVFHRMSKEITCAQAMLTDINTAPREIDRVIRTALKQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 161 RPVYLGLPANLVDLNVPAKLlqTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:COG3961 161 RPVYIGLPADVADLPIEAPL--TPLDLQLKTSDPEALSEVIDTIAELINKAKKPVILADALVSRFGLEKELKKLINATGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 241 PAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNAT 320
Cdd:COG3961 239 PVATLPMGKGVIDESHPNYLGVYNGKLSEPEVREAVESADLILTIGVLLTDFNTGGFTYQYKPANIIEIHPDSVKIKDAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 321 FPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTF 400
Cdd:COG3961 319 FTNLSMKDALQELAKKIDKRNLSAPPVAYPARTPPTPYPPANEPLTQEWLWNTVQNFLKPGDVIIAETGTSFFGALDIRL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 401 PNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI 480
Cdd:COG3961 399 PKGATFISQPLWGSIGYTLPAALGAALAA----PDRRVILFIGDGSLQLTVQEISTMIRWGLKPIIFVLNNDGYTIERAI 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A 481 HGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVKQAKLT 556
Cdd:COG3961 475 HGPTAPYNDIQSWDYTALPEAFGAKNGEAKFRATTGEELALALDVAFANNDRIRLIEVMLPVLDAPELLIDQAKAT 550
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
2-502 |
1.75e-105 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 328.20 E-value: 1.75e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSA 81
Cdd:PLN02573 14 SDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 82 LNGIAGSYAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQR 161
Cdd:PLN02573 94 LNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELIDTAISTALKESK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 162 PVYLGLPANLVDLNVPAkLLQTPIDMSLKP---NDAESEKEViDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLT 238
Cdd:PLN02573 174 PVYISVSCNLAAIPHPT-FSREPVPFFLTPrlsNKMSLEAAV-EAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADAS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 239 QFPAFVTPMGKGSISEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRN 318
Cdd:PLN02573 252 GYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 319 -ATFPGVQMK-FV--LQKLLTNIADAAKGYKPVAVPARTPANAAvpASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFG 394
Cdd:PLN02573 332 gPAFGCVLMKdFLeaLAKRVKKNTTAYENYKRIFVPEGEPLKSE--PGEPLRVNVLFKHIQKMLSGDTAVIAETGDSWFN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 395 INQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PLN02573 410 CQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAA----PDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGY 485
|
490 500
....*....|....*....|....*....
1PYD_A 475 TIEKLIH-GPkaqYNEIQGWDHLSLLPTF 502
Cdd:PLN02573 486 TIEVEIHdGP---YNVIKNWNYTGLVDAI 511
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
364-550 |
2.51e-94 |
|
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: 285.58 E-value: 2.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 364 PLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIG 443
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALA----APDRRVILLVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 444 DGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAK-DYETHRVATTGEWDKLT 522
Cdd:cd02005 77 DGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGgGGLSFRVKTEGELDEAL 156
|
170 180
....*....|....*....|....*...
1PYD_A 523 QDKSFNdNSKIRMIEIMLPVFDAPQNLV 550
Cdd:cd02005 157 KDALFN-RDKLSLIEVILPKDDAPEALK 183
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
9-169 |
6.79e-91 |
|
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: 275.91 E-value: 6.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 9 YLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGS 88
Cdd:cd07038 2 YLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 89 YAEHVGVLHVVGVPSISSQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLP 168
Cdd:cd07038 82 YAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEIP 161
|
.
1PYD_A 169 A 169
Cdd:cd07038 162 R 162
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
10-474 |
7.79e-59 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 223107 [Multi-domain] Cd Length: 550 Bit Score: 204.80 E-value: 7.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGS 88
Cdd:COG0028 8 LVEALEANGVDTVFGIPGGSILPLYDALYD-SGIRHILVRHEQGAAFAADGYARATGkPGVCLVTSGPGATNLLTGLADA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 89 YAEHVgvlhvvgvP--SISSQAKQLLLhhtlGNGDF--TVFHRMSANISETTAMITDIATAPAEIDRCIRTTyVTQR--P 162
Cdd:COG0028 87 YMDSV--------PllAITGQVPTSLI----GTDAFqeVDQVGLFRPITKYNFEVRSPEDIPEVVARAFRIA-LSGRpgP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 163 VYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKevIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPA 242
Cdd:COG0028 154 VVVDLPKDVLAAEAEEPGPEPAILPPYRPAPPPPEA--IRKAAELLAEAKRPVILAGGGVRRAGASEELRELAEKLGAPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 243 FVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKtKNIVEFHSDHMKIRNATFP 322
Cdd:COG0028 232 VTTLMGKGAVPEDHPLSLGM-LGMHGTKAANEALEEADLLLAVGARFDDRVTGYSGFAPP-AAIIHIDIDPAEIGKNYPV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 323 GVQ----MKFVLQKLLTNIADA-AKGYKPVA--VPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTS---A 392
Cdd:COG0028 310 DVPivgdAKATLEALLEELKPErAAWLEELLeaRAAYRDLALEELADDGIKPQYVIKVLRELLPDDAIVVTDVGQHqmwA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 393 FGINQTTFPNNTYgISqVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNND 472
Cdd:COG0028 390 ARYFDFYRPRRFL-TS-GGLGTMGFGLPAAIGAKLAA----PDRKVVAIAGDGGFMMNGQELETAVRYGLPVKIVVLNNG 463
|
..
1PYD_A 473 GY 474
Cdd:COG0028 464 GY 465
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-169 |
1.05e-51 |
|
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: 173.68 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 8 KYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAG 87
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 88 SYAEHVGVLHVVGVPSISSQAKQLllhhtlgnGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGL 167
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQT--------FQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRL 152
|
..
1PYD_A 168 PA 169
Cdd:cd06586 153 PR 154
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-178 |
1.75e-31 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 426975 [Multi-domain] Cd Length: 169 Bit Score: 119.65 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 6 LGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNG 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGTILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 85 IAGSYAEhvgvlhvvGVP--SISSQAK-QLLLHHTLGNGDFTVfhRMSANISETTAMITDIATAPAEIDRCIRT-TYVTQ 160
Cdd:pfam02776 81 LANAYVD--------SVPliVISGQRPrSLVGRGALQQELDQL--ALFRPVTKWAVRVTSPDEIPEVLRRAFRAaMSGRP 150
|
170
....*....|....*...
1PYD_A 161 RPVYLGLPANLVDLNVPA 178
Cdd:pfam02776 151 GPVYLEIPLDVLLEEVDE 168
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
201-333 |
2.29e-28 |
|
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: 109.96 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 201 IDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGvYVGTLSKPEVKEAVESAD 280
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
1PYD_A 281 LILSVGALLSDFNTGSFSYSY-KTKNIVEFHSDHMKIRNATFPGVQM----KFVLQKL 333
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFaPDAKIIHIDIDPAEIGKNYPVDVPIvgdaKETLEAL 137
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
7-471 |
2.24e-26 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 113.31 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 7 GKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEgMRWAGNANELNAAYAADGYARIKGMS--CIITTfGVGELSALNG 84
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSD-LIHILTRHEQAAAHAADGYARASGKVgvCVATS-GPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 85 IAGSYAEHVGVLhvvgvpSISSQAKQlllhHTLGNGDFT------VFhrMSanISETTAMITDiataPAEIDRCIRTTY- 157
Cdd:PRK06276 82 IATAYADSSPVI------ALTGQVPT----KLIGNDAFQeidalgIF--MP--ITKHNFQIKK----PEEIPEIFRAAFe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 158 --VTQRP--VYLGLPANLVDLNVPAKLLQTPIDMSL---KPNDAESEKEvIDTILALVKDAKNPVILADACCSRHDVKAE 230
Cdd:PRK06276 144 iaKTGRPgpVHIDLPKDVQEGELDLEKYPIPAKIDLpgyKPTTFGHPLQ-IKKAAELIAEAERPVILAGGGVIISGASEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 231 TKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFH 310
Cdd:PRK06276 223 LIELSELVKIPVCTTLMGKGAFPEDHPLALGM-VGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHID 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 311 SDHMKI-RN--ATFPGV-QMKFVLQKLLTNI-ADAAKGYKPVAVPARTPANAAVPAST----PLKQEWMWNQLGNFLQEG 381
Cdd:PRK06276 302 IDPAEIgKNvrVDVPIVgDAKNVLRDLLAELmKKEIKNKSEWLERVKKLKKESIPRMDfddkPIKPQRVIKELMEVLREI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 382 DVVIAETGTSAFGINQ--------TTFPNNTygISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQE 453
Cdd:PRK06276 382 DPSKNTIITTDVGQNQmwmahffkTSAPRSF--ISSGGLGTMGFGFPAAIGAKVAK----PDANVIAITGDGGFLMNSQE 455
|
490
....*....|....*...
1PYD_A 454 ISTMIRWGLKPYLFVLNN 471
Cdd:PRK06276 456 LATIAEYDIPVVICIFDN 473
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
371-539 |
2.66e-26 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 105.03 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 371 WNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYG-ISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQL 449
Cdd:cd00568 3 LAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRfLTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDGGFMM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 450 TVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGP----KAQYNEIQGWDHLSLLPTFGAKdyeTHRVATTGEWDKLTQDk 525
Cdd:cd00568 79 TGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAfyggRVSGTDLSNPDFAALAEAYGAK---GVRVEDPEDLEAALAE- 154
|
170
....*....|....
1PYD_A 526 sFNDNSKIRMIEIM 539
Cdd:cd00568 155 -ALAAGGPALIEVK 167
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
1-471 |
3.17e-25 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 109.53 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITL-----GKYL-FERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITT 73
Cdd:PRK07282 1 MEKISLespksGSDLvLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGkLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 74 FGVGELSALNGIAGSYAEHV---GVLHVVGVPSISSQAKQLLlhHTLGngdftvfhrMSANISETTAMITDIatapAEID 150
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVpllVFTGQVARAGIGKDAFQEA--DIVG---------ITMPITKYNYQIRET----ADIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 151 RCIRTTY---VTQR--PVYLGLPANLVDLNVpAKLLQTPIDM-----SLKPNDAESEKevidtILALVKDAKNPVILADA 220
Cdd:PRK07282 146 RIITEAVhiaTTGRpgPVVIDLPKDVSALET-DFIYDPEVNLpsyqpTLEPNDMQIKK-----ILKQLSKAKKPVILAGG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 221 CCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTG---SF 297
Cdd:PRK07282 220 GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLFLGM-GGMHGSYAANIAMTEADFMINIGSRFDDRLTGnpkTF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 298 SysyktKNIVEFHSD-----HMKIRNATFPGV-QMKFVLQKLL------TNIADAAKgyKPVAVPARTPANAavPASTPL 365
Cdd:PRK07282 299 A-----KNAKVAHIDidpaeIGKIIKTDIPVVgDAKKALQMLLaeptvhNNTEKWIE--KVTKDKNRVRSYD--KKERVV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 366 KQEWMWNQLGNFLQEGDVVIAETGTSAFGINQ-TTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGD 444
Cdd:PRK07282 370 QPQAVIERIGELTNGDAIVVTDVGQHQMWAAQyYPYQNERQLVTSGGLGTMGFGIPAAIGAKIA----NPDKEVILFVGD 445
|
490 500
....*....|....*....|....*..
1PYD_A 445 GSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07282 446 GGFQMTNQELAILNIYKVPIKVVMLNN 472
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-474 |
3.96e-24 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 106.01 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKGMSCI-ITTFGVGEL 79
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVcVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 SALNGIAGSYAEHVGVLhvvgvpSISSQAKQLLLhhtlGNGDFtvfhrMSANISETTAMITD---IATAPAEIDRCIRTT 156
Cdd:PRK06048 84 NLVTGIATAYMDSVPIV------ALTGQVPRSMI----GNDAF-----QEADITGITMPITKhnyLVQDAKDLPRIIKEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 157 Y---VTQR--PVYLGLPANL----VDLNVPAKLLQTPIDMSLKPNDAESEKEVidtilALVKDAKNPVILADACCSRHDV 227
Cdd:PRK06048 149 FhiaSTGRpgPVLIDLPKDVttaeIDFDYPDKVELRGYKPTYKGNPQQIKRAA-----ELIMKAERPIIYAGGGVISSNA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 228 KAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGvYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIV 307
Cdd:PRK06048 224 SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKII 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 308 EFHSDHMKIR---NATFPGV-QMKFVLQKLLTNIA--DAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEG 381
Cdd:PRK06048 303 HIDIDPAEISknvKVDVPIVgDAKQVLKSLIKYVQycDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCPDA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 382 dVVIAETGTSAFGINQttFPNNTYGISQVLWGSIGfTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWG 461
Cdd:PRK06048 383 -IIVTEVGQHQMWAAQ--YFKYKYPRTFITSGGLG-TMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQND 458
|
490
....*....|...
1PYD_A 462 LKPYLFVLNNdGY 474
Cdd:PRK06048 459 IPVIVAILNN-GY 470
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
2-471 |
5.30e-23 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 102.87 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELS 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 81 ALNGIAGSYAEHVGVLHvvgvpsISSQAKQlllhhTLGNGDftVFHRMSA-NISETTAMITDIATAPAEIDRCIRTTYVT 159
Cdd:PRK08527 81 AVTGLATAYMDSIPLVL------ISGQVPN-----SLIGTD--AFQEIDAvGISRPCVKHNYLVKSIEELPRILKEAFYI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 160 QR-----PVYLGLP----ANLVDLNVPAKllqtpIDM-SLKPNDAESEKEvIDTILALVKDAKNPVILADACCSRHDVKA 229
Cdd:PRK08527 148 ARsgrpgPVHIDIPkdvtATLGEFEYPKE-----ISLkTYKPTYKGNSRQ-IKKAAEAIKEAKKPLFYLGGGAILSNASE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 230 ETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEF 309
Cdd:PRK08527 222 EIRELVKKTGIPAVETLMARGVLRSDDPLLLGM-LGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 310 HSDHM---KIRNATFPGV-QMKFVLQKLLTNIAD-AAKGYKP-VAVPARTpaNAAVPAS-----TPLKQEWMWNQLGNFL 378
Cdd:PRK08527 301 DIDPSsisKIVNADYPIVgDLKNVLKEMLEELKEeNPTTYKEwREILKRY--NELHPLSyedsdEVLKPQWVIERVGELL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 379 QEGDVVIAETGTSAFGINQT---TFP---NNTYGIsqvlwGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQ 452
Cdd:PRK08527 379 GDDAIISTDVGQHQMWVAQFypfNYPrqlATSGGL-----GTMGYGLPAALGAKLAV----PDKVVINFTGDGSILMNIQ 449
|
490
....*....|....*....
1PYD_A 453 EISTMIRWGLKPYLFVLNN 471
Cdd:PRK08527 450 ELMTAVEYKIPVINIILNN 468
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
14-474 |
1.29e-22 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 101.44 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKGMS--CIiTTFGVGELSALNGIAgsYAe 91
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRD-SSIKLILTRHEQGAAFMAATYGRLTGKAgvCL-STLGPGATNLVTGVA--YA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 92 hvgvlHVVGVP--SISSQAKQLLLHHtlgnGDFTVFH--RMSANISETTAMITDIATAPAEIDRCIRTTyVTQRP--VYL 165
Cdd:PRK08322 86 -----QLGGMPmvAITGQKPIKRSKQ----GSFQIVDvvAMMAPLTKWTRQIVSPDNIPEVVREAFRLA-EEERPgaVHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 166 GLPANLVDLNVPAKLLqtPIDMSLKPNdaeSEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVT 245
Cdd:PRK08322 156 ELPEDIAAEETDGKPL--PRSYSRRPY---ASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 246 PMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFnTGSFSYSYKTKNIVEFHSDHMKIRNATFPgvQ 325
Cdd:PRK08322 231 QMGKGVIPETHPLSLGT-AGLSQGDYVHCAIEHADLIINVGHDVIEK-PPFFMNPNGDKKVIHINFLPAEVDPVYFP--Q 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 326 MKFV------LQKLLTNIADAAKGYKPVAVPARTP-----ANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGtsAFG 394
Cdd:PRK08322 307 VEVVgdiansLWQLKERLADQPHWDFPRFLKIREAieahlEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNG--AYK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 395 I----NQTTFPNNTYGISQvlwgsiGFTT-GATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVL 469
Cdd:PRK08322 385 IwfarNYRAYEPNTCLLDN------ALATmGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLIL 458
|
....*
1PYD_A 470 NNDGY 474
Cdd:PRK08322 459 NDNAY 463
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
9-169 |
3.00e-22 |
|
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: 93.37 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 9 YLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAG 87
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 88 SYAEhvgvlhvvgvpS-----ISSQAKQlllhHTLGNGDFTVF--HRMSANISETTAMITDIATAPAEIDRCIRTTYVT- 159
Cdd:cd07035 81 AYLD-----------SipllvITGQRPT----AGEGRGAFQEIdqVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGr 145
|
170
....*....|
1PYD_A 160 QRPVYLGLPA 169
Cdd:cd07035 146 PGPVALDLPK 155
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-513 |
1.25e-20 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 95.44 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGels 80
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGgLGVALTSTGTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 81 ALNgIAGSYAEHVGvlhvvgvpsissqAKQLLLHHT-------LGNgDFTVFHR------MSANISETTAMITDIATAPA 147
Cdd:PRK07064 78 AGN-AAGALVEALT-------------AGTPLLHITgqietpyLDQ-DLGYIHEapdqltMLRAVSKAAFRVRSAETALA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 148 EIDRCIRTTyvtqrpvyLGLPANLVDLNVPAKLLQTPIDMS-----LKPNDAESEKEVIDTILALVKDAKNPVILADAcC 222
Cdd:PRK07064 143 TIREAVRVA--------LTAPTGPVSVEIPIDIQAAEIELPddlapVHVAVPEPDAAAVAELAERLAAARRPLLWLGG-G 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 223 SRHDVKaETKKLIDLTqFPAFVTPMGKGSISEQHPRYGGVYVGTlskPEVKEAVESADLILSVGALLSDFNTGSFSysyk 302
Cdd:PRK07064 214 ARHAGA-EVKRLVDLG-FGVVTSTQGRGVVPEDHPASLGAFNNS---AAVEALYKTCDLLLVVGSRLRGNETLKYS---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 303 tkniVEFHSDHMKI-----------RNATFPGVQMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPAstplkqewMW 371
Cdd:PRK07064 285 ----LALPRPLIRVdadaaadgrgyPNDLFVHGDAARVLARLADRLEGRLSVDPAFAADLRAAREAAVAD--------LR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 372 NQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQV-----------LWGSIGFTTGATLGAAFAaeeiDPKKRVIL 440
Cdd:PRK07064 353 KGLGPYAKLVDALRAALPRDGNWVRDVTISNSTWGNRLLpifepranvhaLGGGIGQGLAMAIGAALA----GPGRKTVG 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PYD_A 441 FIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY----TIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVA 513
Cdd:PRK07064 429 LVGDGGLMLNLGELATAVQENANMVIVLMNDGGYgvirNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSAD 505
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
2-471 |
1.68e-18 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 88.66 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 2 SEITLGKYLFERLKQVNVNTVFG--LPGDFNLSLldkiyEVEGMRWAGNANELNAAYAADGYARIKGMSCIITtfgvgel 79
Cdd:PRK06112 12 LNGTVAHAIARALKRHGVEQIFGqsLPSALFLAA-----EAIGIRQIAYRTENAGGAMADGYARVSGKVAVVT------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 sALNGIAGS-----YAEHVGVLHvvgvPSIS-----------SQAKQLLLHHTLGNGDFTVFHRMSanISETTAMITDIA 143
Cdd:PRK06112 80 -AQNGPAATllvapLAEALKASV----PIVAlvqdvnrdqtdRNAFQELDHIALFQSCTKWVRRVT--VAERIDDYVDQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 144 TAPAEIDRcirttyvtQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPND-AESEKEVIDTILALVKDAKNPVILADACC 222
Cdd:PRK06112 153 FTAATSGR--------PGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDrTVPAPQRLAEAASLLAQAQRPVVVAGGGV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 223 SRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPE-----VKEAVESADLILSVGALLSDFNTGSF 297
Cdd:PRK06112 225 HISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGV-VGSLMGPRspgrhLRDLVREADVVLLVGTRTNQNGTDSW 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 298 SYSYKTKNIVEFHSDHMKI-RNATfpgvQMKFVLQKLLTnIADAAKGYKPVAVPARTPANAAVPA--------------- 361
Cdd:PRK06112 304 SLYPEQAQYIHIDVDGEEVgRNYE----ALRLVGDARLT-LAALTDALRGRDLAARAGRRAALEPaiaagreahredsap 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 362 -----STPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGI-NQTTFPN------NTYGISQVLWGsIGFTTGATLGAafaa 429
Cdd:PRK06112 379 valsdASPIRPERIMAELQAVLTGDTIVVADASYSSIWVaNFLTARRagmrflTPRGLAGLGWG-VPMAIGAKVAR---- 453
|
490 500 510 520
....*....|....*....|....*....|....*....|..
1PYD_A 430 eeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06112 454 ----PGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNN 491
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-474 |
8.46e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 86.60 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEG-MRWAGNANELNAAYAADGYARIKGMSCIITTF-GVGE 78
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVpGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 79 LSALNGIAGSYAehvgvlhvvgvpsisSQAKQLLL-----HHTLGNGdFTVFHRMSANiSETTAMIT---DIATAPAEID 150
Cdd:PRK08266 81 LNAGAALLTAYG---------------CNSPVLCLtgqipSALIGKG-RGHLHEMPDQ-LATLRSFTkwaERIEHPSEAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 151 RCIRTTYVT-----QRPVYLGLPANLVDLNVP-AKLLQTPIDMSLKPNDaesekEVIDTILALVKDAKNPVILADAccSR 224
Cdd:PRK08266 144 ALVAEAFQQmlsgrPRPVALEMPWDVFGQRAPvAAAPPLRPAPPPAPDP-----DAIAAAAALIAAAKNPMIFVGG--GA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 225 HDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYggvyvgtLSKPEVKEAVESADLILSVGallSDFNTGSFSYSYKTK 304
Cdd:PRK08266 217 AGAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG-------LNFAAAYELWPQTDVVIGIG---SRLELPTFRWPWRPD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 305 N--IVEFHSDHMKIRNATfPGVQMKFVLQKLLTNIADAAKGYKPVAvPARTPANAAVPASTPLKQEWMWNQLGnFLQegd 382
Cdd:PRK08266 287 GlkVIRIDIDPTEMRRLK-PDVAIVADAKAGTAALLDALSKAGSKR-PSRRAELRELKAAARQRIQAVQPQAS-YLR--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 383 VVIAETGTSAFGINQttfpnntygISQV-LWGSIGF---------TTG--ATLGAAFA----AEEIDPKKRVILFIGDGS 446
Cdd:PRK08266 361 AIREALPDDGIFVDE---------LSQVgFASWFAFpvyaprtfvTCGyqGTLGYGFPtalgAKVANPDRPVVSITGDGG 431
|
490 500
....*....|....*....|....*...
1PYD_A 447 LQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:PRK08266 432 FMFGVQELATAVQHNIGVVTVVFNNNAY 459
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-471 |
9.59e-18 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 86.59 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKI-YEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGE 78
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 79 LSALNGIAGSYAEhvgvlhvvgvpsissQAKQLLLhhtLGNGDFTVFHRMSANISETTAMITDIA----------TAPAE 148
Cdd:PRK08611 81 IHLLNGLYDAKMD---------------HVPVLAL---AGQVTSDLLGTDFFQEVNLEKMFEDVAvynhqimsaeNLPEI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 149 IDRCIRTTYVTQRPVYLGLPANLVDLNVPAKlLQTPIDmSLKPNDAESEKEVIDTILALVKDAKNPVILADAccSRHDVK 228
Cdd:PRK08611 143 VNQAIRTAYEKKGVAVLTIPDDLPAQKIKDT-TNKTVD-TFRPTVPSPKPKDIKKAAKLINKAKKPVILAGL--GAKHAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 229 AETKKLIDLTQFPAFVTPMGKGSISEQHPRY-GGV-YVGTlsKPEVkEAVESADLILSVGAllsdfntgsfSYSY----- 301
Cdd:PRK08611 219 EELLAFAEKAKIPIIHTLPAKGIIPDDHPYSlGNLgKIGT--KPAY-EAMQEADLLIMVGT----------NYPYvdylp 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 302 -KTKNIvEFHSDHMKI--RNATFPGVQ--MKFVLQKLLTNIAdaakgykpvAVPAR-----TPANAAV----------PA 361
Cdd:PRK08611 286 kKAKAI-QIDTDPANIgkRYPVNVGLVgdAKKALHQLTENIK---------HVEDRrfleaCQENMAKwwkwmeedenNA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 362 STPLKQEWMWNQLGNFLQEGDVVIAETGTS----AFGINQTtfPNNTYGISQVLWgsigfTTGATLGAAFAAEEIDPKKR 437
Cdd:PRK08611 356 STPIKPERVMAAIQKIADDDAVLSVDVGTVtvwsARYLNLG--TNQKFIISSWLG-----TMGCGLPGAIAAKIAFPDRQ 428
|
490 500 510
....*....|....*....|....*....|....
1PYD_A 438 VILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK08611 429 AIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNN 462
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-471 |
8.26e-17 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 83.42 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGEL 79
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 SALNGIAGSYAEHVGVLHvvgvpsISSQAKQLLlhhtLGNGDFTVFHRMSanISETTAMITDIATAPAEIDRCIRTTYV- 158
Cdd:PRK06882 81 NAITGIATAYTDSVPLVI------LSGQVPSNL----IGTDAFQECDMLG--ISRPVVKHSFIVKNAEDIPSTIKKAFYi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 159 --TQR--PVYLGLPANLVDlnvPAKLL--QTPIDMSLK---PNdAESEKEVIDTILALVKDAKNPVILADACCsrhdVKA 229
Cdd:PRK06882 149 asTGRpgPVVIDIPKDMVN---PANKFtyEYPEEVSLRsynPT-VQGHKGQIKKALKALLVAKKPVLFVGGGV----ITA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 230 E-TKKLIDLTQ---FPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKN 305
Cdd:PRK06882 221 EcSEQLTQFAQklnLPVTSSLMGLGAYPSTDKQFLGM-LGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 306 IVEFHSDHMKIRN---ATFPGV-QMKFVLQKLLTNIADA--AKGykpvavpartpaNAAVPASTPLKQEWMWNQLGNF-- 377
Cdd:PRK06882 300 VIHIDIDPTSISKnvpAYIPIVgSAKNVLEEFLSLLEEEnlAKS------------QTDLTAWWQQINEWKAKKCLEFdr 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 378 ----------------LQEGDVVIA-ETGT-SAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVI 439
Cdd:PRK06882 368 tsdvikpqqvveaiyrLTNGDAYVAsDVGQhQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFA----HPEATVV 443
|
490 500 510
....*....|....*....|....*....|..
1PYD_A 440 LFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06882 444 CVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-471 |
5.01e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 81.17 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 3 EITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSA 81
Cdd:PRK06725 14 EVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 82 LNGIAGSYAEHVGVLHvvgvpsISSQ-AKQLLLHHTLGNGDFTvfhRMSANISETTAMITDIAtapaEIDRCIRTTYVTQ 160
Cdd:PRK06725 93 VTGLADAYMDSIPLVV------ITGQvATPLIGKDGFQEADVV---GITVPVTKHNYQVRDVN----QLSRIVQEAFYIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 161 R-----PVYLGLPANLVDLNVPA-----------KLLQTPIDMSLKpndaesekEVIDTIlalvKDAKNPVILADACCSR 224
Cdd:PRK06725 160 EsgrpgPVLIDIPKDVQNEKVTSfynevveipgyKPEPRPDSMKLR--------EVAKAI----SKAKRPLLYIGGGVIH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 225 HDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGS---FSYSY 301
Cdd:PRK06725 228 SGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLFLGM-LGMHGTYAANMAVTECDLLLALGVRFDDRVTGKlelFSPHS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 302 KTKNI----VEFHS----------DHMKIRNATFP---GVQMKFVLQKLLTNIADAAKGYKPvavpartpanaavpASTP 364
Cdd:PRK06725 307 KKVHIdidpSEFHKnvaveypvvgDVKKALHMLLHmsiHTQTDEWLQKVKTWKEEYPLSYKQ--------------KESE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 365 LKQEWMWNQLGNFLQEGDVVIAETGT-SAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEidpkKRVILFIG 443
Cdd:PRK06725 373 LKPQHVINLVSELTNGEAIVTTEVGQhQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEE----ELVICIAG 448
|
490 500
....*....|....*....|....*...
1PYD_A 444 DGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06725 449 DASFQMNIQELQTIAENNIPVKVFIINN 476
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-474 |
7.15e-16 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 80.40 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 4 ITLGKYLFERLKQVNVNTVFGLPGdfnlslldkIYEVE--------GMRWAGNANELNAAYAADGYARIKGMS--CIITT 73
Cdd:PRK07524 2 TTCGEALVRLLEAYGVETVFGIPG---------VHTVElyrglagsGIRHVTPRHEQGAGFMADGYARVSGKPgvCFIIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 74 fGVGELSALNGIAGSYAEhvgvlhvvGVPS--ISS-QAKQLLLHhtlGNGdftVFHR------MSANISETTAMITDIAT 144
Cdd:PRK07524 73 -GPGMTNIATAMGQAYAD--------SIPMlvISSvNRRASLGK---GRG---KLHElpdqraMVAGVAAFSHTLMSAED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 145 APAEIDR------CIRTtyvtqRPVYLGLPANLVDLNVPAKLLQTPidmsLKPNDAESEKEVIDTILALVKDAKNPVILA 218
Cdd:PRK07524 138 LPEVLARafavfdSARP-----RPVHIEIPLDVLAAPADHLLPAPP----TRPARPGPAPAALAQAAERLAAARRPLILA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 219 DACCSrhDVKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGvyvGTLSKPEVKEAVESADLILSVGALLSD-----FN 293
Cdd:PRK07524 209 GGGAL--AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLAVGTELGEtdydvYF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 294 TGSFSYSyktKNIVEFHSDHMKI-RNATfPGVQM----KFVLQKLLTNIADAAKgykpvavPARTPANAAVPASTPLKQE 368
Cdd:PRK07524 284 DGGFPLP---GELIRIDIDPDQLaRNYP-PALALvgdaRAALEALLARLPGQAA-------AADWGAARVAALRQALRAE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 369 WMWNQLG--NFLQegdvVIAETGTSAFGINQTTFP----NNTYGISQVL-W-------GSIGFTTGATLGAAFAAeeidP 434
Cdd:PRK07524 353 WDPLTAAqvALLD----TILAALPDAIFVGDSTQPvyagNLYFDADAPRrWfnastgyGTLGYGLPAAIGAALGA----P 424
|
490 500 510 520
....*....|....*....|....*....|....*....|.
1PYD_A 435 KKRVILFIGDGSLQLTVQEISTMIRWGLkPYLFVL-NNDGY 474
Cdd:PRK07524 425 ERPVVCLVGDGGLQFTLPELASAVEADL-PLIVLLwNNDGY 464
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-476 |
2.43e-15 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 78.76 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCI-ITTFGVGEL 79
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGIcFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 SALNGIagsyaehvgvlhvvgvpsisSQAKQ----LLL------HHTLGNGDFTV--FHRMSANISETTAMITDIATAPA 147
Cdd:PRK08199 85 NASIGV--------------------HTAFQdstpMILfvgqvaRDFREREAFQEidYRRMFGPMAKWVAEIDDAARIPE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 148 EIDRCIRTTyVTQR--PVYLGLPAN-LVDLNVPAKLLQTPIDMSlKPNDAEsekevIDTILALVKDAKNPVILADAccSR 224
Cdd:PRK08199 145 LVSRAFHVA-TSGRpgPVVLALPEDvLSETAEVPDAPPYRRVAA-APGAAD-----LARLAELLARAERPLVILGG--SG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 225 HDVKAEtkklIDLTQFP-AFVTPMG-----KGSISEQHPRYGGvYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFS 298
Cdd:PRK08199 216 WTEAAV----ADLRAFAeRWGLPVAcafrrQDLFDNRHPNYAG-DLGLGINPALAARIREADLVLAVGTRLGEVTTQGYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 299 ---YSYKTKNIVEFHSDHMKIrNATFPGVQMkfvLQKLLTNIADAAKGYKPVAVPARTPANAAVPA-----STPLKQEWM 370
Cdd:PRK08199 291 lldIPVPRQTLVHVHPDAEEL-GRVYRPDLA---IVADPAAFAAALAALEPPASPAWAEWTAAAHAdylawSAPLPGPGA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 371 wNQLG---NFLQE---GDVVIAeTGTSAF-GINQTTFPNNTYGisqvlwGSIGFTTGAT---LGAAFAAEEIDPKKRVIL 440
Cdd:PRK08199 367 -VQLGevmAWLRErlpADAIIT-NGAGNYaTWLHRFFRFRRYR------TQLAPTSGSMgygLPAAIAAKLLFPERTVVA 438
|
490 500 510
....*....|....*....|....*....|....*..
1PYD_A 441 FIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY-TI 476
Cdd:PRK08199 439 FAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTI 475
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
4-458 |
3.62e-15 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 78.34 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 4 ITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYE-VEG--MRWAGNANELNAAYAADGYARIKGMSCIIT-TFGVGEL 79
Cdd:PRK06456 2 PTGARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdLANgeLRHVLMRHEQAAAHAADGYARASGVPGVCTaTSGPGTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 SALNGIAGSYAEHV---GVLHVVGVPSISSQAKQllLHHTLGngdftVFhrmsANISETTAMITDIATAPAEIDRCIrtt 156
Cdd:PRK06456 82 NLVTGLITAYWDSSpviAITGQVPRSVMGKMAFQ--EADAMG-----VF----ENVTKYVIGIKRIDEIPQWIKNAF--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 157 YV--TQR--PVYLGLPANLVDLNVP-AKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAET 231
Cdd:PRK06456 148 YIatTGRpgPVVIDIPRDIFYEKMEeIKWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 232 KKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKT-KNIVEFH 310
Cdd:PRK06456 228 LELAELLHIPIVSTFPGKTAIPHDHPLYFGP-MGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 311 SDHMKIRNATFPGVQM----KFVLQKLLTNIADAAKGYKPVAVPART--------------------------------P 354
Cdd:PRK06456 307 IDPTDGEKAIKVDVGIygnaKIILRELIKAITELGQKRDRSAWLKRVkeykeyysqfyyteengklkpwkimktirqalP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 355 ANAAVpaSTPLKQEWMWNQLGNFLQEGDVVIAETGTsafginqttfpnntygisqvlwGSIGFTTGATLGAAFAAeeidP 434
Cdd:PRK06456 387 RDAIV--TTGVGQHQMWAEVFWEVLEPRTFLTSSGM----------------------GTMGFGLPAAMGAKLAR----P 438
|
490 500
....*....|....*....|....
1PYD_A 435 KKRVILFIGDGSLQLTVQEISTMI 458
Cdd:PRK06456 439 DKVVVDLDGDGSFLMTGTNLATAV 462
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
12-478 |
2.58e-14 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 75.80 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 12 ERLKQVNVNTVFGLPGDFNLSLLDkIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGSYA 90
Cdd:PRK07525 14 ETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 91 EHVGVLHvvgvpsISSQAKQLllhhTLGNGDF------TVFHRMSANISEttamITDIATAPAEIDRCIRTTYVTQRPVY 164
Cdd:PRK07525 93 AHTPVVL------VTPQAGTK----TIGQGGFqeaeqmPMFEDMTKYQEE----VRDPSRMAEVLNRVFDKAKRESGPAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 165 LGLPANL----VDLNVPAkllqtPIDMSLKPNDAESekevIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:PRK07525 159 INIPRDYfygvIDVEIPQ-----PVRLERGAGGEQS----LAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 241 PAFVTPMGKGSISEQHPryggVYVGTLSKPEVKEAVES---ADLILSVGALLSDFNT---GSFSYSYKTKNI--VEFHSD 312
Cdd:PRK07525 230 PVACGYLHNDAFPGSHP----LWVGPLGYNGSKAAMELiakADVVLALGTRLNPFGTlpqYGIDYWPKDAKIiqVDINPD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 313 HMKIRNATFPGVQ--MKFVLQKLLTNIADAAKG------------------YKPVA------VPARTPANAAVPASTPlk 366
Cdd:PRK07525 306 RIGLTKKVSVGICgdAKAVARELLARLAERLAGdagreerkaliaaeksawEQELSswdhedDDPGTDWNEEARARKP-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 367 qEWM-----WNQLGNFLQEGDVVIAETG-TSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVIL 440
Cdd:PRK07525 384 -DYMhprqaLREIQKALPEDAIVSTDIGnNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIAC----PDRPVVG 458
|
490 500 510
....*....|....*....|....*....|....*...
1PYD_A 441 FIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEK 478
Cdd:PRK07525 459 FAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEK 496
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
201-510 |
7.21e-14 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 226471 [Multi-domain] Cd Length: 617 Bit Score: 74.35 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 201 IDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSISEQHP-RYGGVYV-GTLSkpeVKEAVES 278
Cdd:COG3962 219 LADAAALIKSAKKPLIVAGGGVLYSGAREALRAFAETHGIPVVETQAGKSALAWDHPlNLGGVGVtGTLA---ANRAAEE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 279 ADLILSVGALLSDFNTGSfsysyktknivefhsdhmkirNATFPGVQMKFvlqkLLTNIA--DAAK-GYKPVAVPARTPA 355
Cdd:COG3962 296 ADLVIGIGTRLQDFTTGS---------------------KALFKNPGVKF----LNLNVQpfDAYKhDALPLVADARAGL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 356 NAAVPASTPLKQEWMW-----NQLGNFLQEGDVVIAETG--------TSAFG-INQTTFPNNTY--------GISQVLWG 413
Cdd:COG3962 351 EALSEALGGYRTAAGWtdereRLKAAWDAEADAPTAKNHflntlptqTQVIGaVQRTISDDSVVvcaagslpGDLHKLWR 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 414 S--------------IGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY-TIEK 478
Cdd:COG3962 431 AgvpgtyhleygfscMGYEIAGGLGAKAA----EPDREVYVMVGDGSYMMLNSELATSVMLGKKIIVVLLDNRGYgCINR 506
|
330 340 350 360
....*....|....*....|....*....|....*....|...
1PYD_A 479 L--IHGPKAQYNEIQGWDHLSLLP---------TFGAKDYETH 510
Cdd:COG3962 507 LqmATGGASFNNLLRDTDHEEEILqvdfaahaeSYGAKAYKVG 549
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
10-471 |
1.44e-13 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 73.26 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKGM-SCIITTFGVGELSALNGIAGS 88
Cdd:PRK07710 22 LIEALEKEGVEVIFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKpGVVIATSGPGATNVVTGLADA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 89 YAEH---VGVLHVVGVPSISSQAKQlllhhtlgngdftvfhrmSANISETTAMITD---IATAPAEIDRCIRTTY---VT 159
Cdd:PRK07710 101 MIDSlplVVFTGQVATSVIGSDAFQ------------------EADIMGITMPVTKhnyQVRKASDLPRIIKEAFhiaTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 160 QR--PVYLGLPANLVdlnVPAKLLQTPIDMSL---KPNdAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKL 234
Cdd:PRK07710 163 GRpgPVLIDIPKDMV---VEEGEFCYDVQMDLpgyQPN-YEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 235 IDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHM 314
Cdd:PRK07710 239 AEQQEIPVVHTLLGLGGFPADHPLFLGM-AGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 315 KI-RN--ATFPGV-QMKFVLQKLLT---NIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAE 387
Cdd:PRK07710 318 EIgKNvpTEIPIVaDAKQALQVLLQqegKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 388 TGTSAFGINQ-TTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYL 466
Cdd:PRK07710 398 VGQHQMWAAQyYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLA----KPDETVVAIVGDGGFQMTLQELSVIKELSLPVKV 473
|
....*
1PYD_A 467 FVLNN 471
Cdd:PRK07710 474 VILNN 478
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
11-474 |
2.07e-13 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 72.68 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 11 FERLKQVNVNTVFGLPGDFNLSLL----DKIYEVEGMRwagnanELNAAYAADGYARIKGMSCII---TTFGVGelSALN 83
Cdd:PRK07092 19 IDLLRRFGITTVFGNPGSTELPFLrdfpDDFRYVLGLQ------EAVVVGMADGYAQATGNAAFVnlhSAAGVG--NAMG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 84 GIAGSYAehvgvlhvVGVPSI---SSQAKQLL-LHHTLGNGDFTVFHRMSANISETTAMITDIataPAEIDRCIRTTYVT 159
Cdd:PRK07092 91 NLFTAFK--------NHTPLVitaGQQARSILpFEPFLAAVQAAELPKPYVKWSIEPARAEDV---PAAIARAYHIAMQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 160 QR-PVYLGLPANlvDLNVPAKLLqTPIDMSlkpNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLT 238
Cdd:PRK07092 160 PRgPVFVSIPYD--DWDQPAEPL-PARTVS---SAVRPDPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 239 QFPAFVTPM-GKGSISEQHPRYGGVYvgTLSKPEVKEAVESADLILSVGALLsdfntgsFSYSyktkniVEFHSDHMKIR 317
Cdd:PRK07092 234 RAPVWVAPMsGRCSFPEDHPLFAGFL--PASREKISALLDGHDLVLVIGAPV-------FTYH------VEGPGPHLPEG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 318 NATF-----PGV------------QMKFVLQKLLTNIADAAKgykpVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQE 380
Cdd:PRK07092 299 AELVqltddPGEaawapmgdaivgDIRLALRDLLALLPPSAR----PAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 381 GDVVIAETgTSAFGINQTTFP---NNTY--GISqvlwGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEIS 455
Cdd:PRK07092 375 DAIVVEEA-PSTRPAMQEHLPmrrQGSFytMAS----GGLGYGLPAAVGVALA----QPGRRVIGLIGDGSAMYSIQALW 445
|
490 500
....*....|....*....|
1PYD_A 456 TMIRWGLkPYLFV-LNNDGY 474
Cdd:PRK07092 446 SAAQLKL-PVTFViLNNGRY 464
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
19-471 |
2.33e-13 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 72.58 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 19 VNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGSYAEHVGVLH 97
Cdd:PRK07979 19 VKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIPLVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 98 vvgvpsISSQ-AKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIataPAEIDRCIRTTyVTQRP--VYLGLPANLVDl 174
Cdd:PRK07979 99 ------LSGQvATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDI---PQVLKKAFWLA-ASGRPgpVVVDLPKDILN- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 175 nvPAKLLQT--PIDMSLKPND--AESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKG 250
Cdd:PRK07979 168 --PANKLPYvwPESVSMRSYNptTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 251 SISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIR---NATFPGV-QM 326
Cdd:PRK07979 246 AFPATHRQSLGM-LGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISktvTADIPIVgDA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 327 KFVLQKLLTNIADAAKGYKPVAVP----------ARTPANAAVPASTPLKQ---EWMWNqlgnfLQEGDVVIaetgTSAF 393
Cdd:PRK07979 325 RQVLEQMLELLSQESAHQPLDEIRdwwqqieqwrARQCLKYDTHSEKIKPQaviETLWR-----LTKGDAYV----TSDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 394 GINQT------TFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLF 467
Cdd:PRK07979 396 GQHQMfaalyyPFDKPRRWINSGGLGTMGFGLPAALGVKMAL----PEETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471
|
....
1PYD_A 468 VLNN 471
Cdd:PRK07979 472 NLNN 475
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
10-471 |
5.25e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 68.54 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGN---ANELNAAYAADGYARIKGM--SCIITTfGVGELSALNG 84
Cdd:PRK07418 25 LMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKHilvRHEQGAAHAADGYARATGKvgVCFGTS-GPGATNLVTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 85 IAGSYAEH---VGVLHVVGVPSISSQAKQlllhhtlgngdftvfhrmSANISETTAMITD---IATAPAEIDRCIRTTY- 157
Cdd:PRK07418 104 IATAQMDSvpmVVITGQVPRPAIGTDAFQ------------------ETDIFGITLPIVKhsyVVRDPSDMARIVAEAFh 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 158 --VTQR--PVYLGLPANlVDLN----VPAKllqtPIDMSL-------KPNDAEsekevIDTILALVKDAKNP-------V 215
Cdd:PRK07418 166 iaSSGRpgPVLIDIPKD-VGQEefdyVPVE----PGSVKPpgyrptvKGNPRQ-----INAALKLIEEAERPllyvgggA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 216 ILADAccsrHDvkaETKKLIDLTQFPAFVTPMGKGSISEQHPryggVYVGTL---SKPEVKEAVESADLILSVGALLSDF 292
Cdd:PRK07418 236 ISAGA----HA---ELKELAERFQIPVTTTLMGKGAFDEHHP----LSVGMLgmhGTAYANFAVTECDLLIAVGARFDDR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 293 NTGSF-SYSYKTKNIvefhsdHMKI--------RNATFPGV-QMKFVLQKLLtniadaaKGYKPVAVPARTpanaavpas 362
Cdd:PRK07418 305 VTGKLdEFASRAKVI------HIDIdpaevgknRRPDVPIVgDVRKVLVKLL-------ERSLEPTTPPRT--------- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 363 tplkQEWM-----WNQLGNFL---QEGDV----VIAETG--------TSAFGINQ---TTFPNNtyG----ISQVLWGSI 415
Cdd:PRK07418 363 ----QAWLerinrWKQDYPLVvppYEGEIypqeVLLAVRdlapdayyTTDVGQHQmwaAQFLRN--GprrwISSAGLGTM 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A 416 GFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK07418 437 GFGMPAAMGVKVAL----PDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN 488
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
387-474 |
7.21e-12 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 426974 [Multi-domain] Cd Length: 151 Bit Score: 63.37 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 387 ETGTSAFGINQ--TTFPNNTYgISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKP 464
Cdd:pfam02775 1 DIGCHQMWAAQyyRFRPPRRY-LTSGGLGTMGYGLPAAIGAKLA----RPDRPVVAIAGDGGFQMNLQELATAVRYNLPI 75
|
90
....*....|
1PYD_A 465 YLFVLNNDGY 474
Cdd:pfam02775 76 TVVVLNNGGY 85
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
10-471 |
8.02e-12 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 67.84 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 10 LFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCI-ITTFGVGELSALNGIAGS 88
Cdd:PLN02470 19 LVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVcIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 89 YAEHVGVLhvvgvpSISSQAKQLLLhhtlGNGDF--TVFHRMSANISETTAMITDIAtapaEIDRCIRTTYVTQR----- 161
Cdd:PLN02470 99 LLDSVPLV------AITGQVPRRMI----GTDAFqeTPIVEVTRSITKHNYLVMDVE----DIPRVIREAFFLASsgrpg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 162 PVYLGLPANLV------DLNVPAKLlqtPIDMSLKPndAESEKEVIDTILALVKDAKNPVILADACCSrhDVKAETKKLI 235
Cdd:PLN02470 165 PVLVDIPKDIQqqlavpNWNQPMKL---PGYLSRLP--KPPEKSQLEQIVRLISESKRPVVYVGGGCL--NSSEELREFV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 236 DLTQFPAFVTPMGKGSISEQHPRY-------GGVYVGTlskpevkeAVESADLILSVGALLSDFNTGSFSYSYKTKNIVE 308
Cdd:PLN02470 238 ELTGIPVASTLMGLGAFPASDELSlqmlgmhGTVYANY--------AVDSADLLLAFGVRFDDRVTGKLEAFASRASIVH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 309 FHSDHMKIRNATFPGVQM----KFVLQKLLTNI-ADAAKGYKPVAVPARTPAN-AAVPASTPLKQEWMWNQ----LGNFL 378
Cdd:PLN02470 310 IDIDPAEIGKNKQPHVSVcadvKLALQGLNKLLeERKAKRPDFSAWRAELDEQkEKFPLSYPTFGDAIPPQyaiqVLDEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 379 QEGDVVIAeTGTsafGINQT------TFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQ 452
Cdd:PLN02470 390 TDGNAIIS-TGV---GQHQMwaaqwyKYKEPRRWLTSGGLGAMGFGLPAAIGAAAA----NPDAIVVDIDGDGSFIMNIQ 461
|
490
....*....|....*....
1PYD_A 453 EISTMIRWGLKPYLFVLNN 471
Cdd:PLN02470 462 ELATIHVENLPVKIMVLNN 480
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
14-471 |
8.50e-12 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 67.60 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPGDFNLSLLDKIY--EVEGM--RwagnaNELNAAYAADGYARIKGMS--CIITTfGVGELSALNGIAG 87
Cdd:PRK08978 11 LRAQGVDTVFGYPGGAIMPVYDALYdgGVEHLlcR-----HEQGAAMAAIGYARATGKVgvCIATS-GPGATNLITGLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 88 SYAEhvgvlhvvGVP--SISSQAKQLLlhhtLGNGDFT---VFHrMSANISETTAMITDIATAPAEIDRCIRttyVTQR- 161
Cdd:PRK08978 85 ALLD--------SVPvvAITGQVSSPL----IGTDAFQeidVLG-LSLACTKHSFLVQSLEELPEIMAEAFE---IASSg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 162 ---PVylglpanLVDLNVPAKLLQTPIDMSLKPNDAESE--KEVIDTILALVKDAKNPVI-------LADAccsrhdVKA 229
Cdd:PRK08978 149 rpgPV-------LVDIPKDIQLAEGELEPHLTTVENEPAfpAAELEQARALLAQAKKPVLyvgggvgMAGA------VPA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 230 eTKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSF-SYSYKTKNIve 308
Cdd:PRK08978 216 -LREFLAATGMPAVATLKGLGAVEADHPYYLGM-LGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLnTFAPHAKVI-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 309 fhsdHM--------KIR----------NATFPGVQMKFVLQKLLTNIADAAKGYK--------PVAVPA-------RTPA 355
Cdd:PRK08978 292 ----HLdidpaeinKLRqahvalqgdlNALLPALQQPLNIDAWRQHCAQLRAEHAwrydhpgeAIYAPAllkqlsdRKPA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 356 NAAVpaSTPLKQEWMW-------NQLGNFLqegdvviaetgTSAfGInqttfpnntygisqvlwGSIGFTTGATLGAAFA 428
Cdd:PRK08978 368 DTVV--TTDVGQHQMWvaqhmrfTRPENFI-----------TSS-GL-----------------GTMGFGLPAAIGAQVA 416
|
490 500 510 520
....*....|....*....|....*....|....*....|...
1PYD_A 429 aeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK08978 417 ----RPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDN 455
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
5-171 |
1.26e-11 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 62.95 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 5 TLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALN 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 84 GIAGSYAEhvgvlhvvGVP--SISSQakqllLHHTLGNGDF---TVFHRMSANISETTAMITDIATAPAEIDRCIRTTYV 158
Cdd:cd07039 81 GLYDAKRD--------RAPvlAIAGQ-----VPTDELGTDYfqeVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIA 147
|
170
....*....|...
1PYD_A 159 TQRPVYLGLPANL 171
Cdd:cd07039 148 KRGVAVLILPGDV 160
|
|
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
14-474 |
1.43e-11 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226469 [Multi-domain] Cd Length: 592 Bit Score: 66.83 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPGdfnlSLLDKIYEveGMRWAGNANEL------NAAYAADGYARIK--GMSCIITTFGVGELSALNGI 85
Cdd:COG3960 14 LEKEGITTAFGVPG----AAINPFYS--ALRKHGGIRHIlarhveGASHMAEGYTRATagNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 86 AGSYAEHVGVLhvvgvpSISSQAKQLLLHHTlgngDFtvfhrMSANISETTAMITDIATA---PAEIDRCIRTTYVTQRP 162
Cdd:COG3960 88 YSASADSIPIL------CITGQAPRARLHKE----DF-----QAVDIEAIAKPVSKWAVTvrePALVPRVLQQAFHLMRS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 163 vylGLPAN-LVDLNVPAKLLQTPIDMS----LKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDL 237
Cdd:COG3960 153 ---GRPGPvLIDLPFDVQVAEIEFDPDmyepLPVYKPAATRVQAEKALAMLIQAERPLIVAGGGVINADAAALLQEFAEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 238 TQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEA-VESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKI 316
Cdd:COG3960 230 TGVPVIPTLMGWGCIPDDHPLMAGM-VGLQTSHRYGNAtLLASDMVFGIGNRWANRHTGSVEVYTEGRKFIHVDIEPTQI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 317 RNATFPGVQMKFVLQKLLTNIADAAKGYKPVA-VPARTPANAAVPA------------STPLKQEWMWNQLGNFLQEGDV 383
Cdd:COG3960 309 GRVFCPDLGIVSDAKAALTLLLDVAQEWKKAGkLPCRKAWVADCQQrkrtllrkthfdNVPVKPQRVYEEMNKAFGRDVC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 384 VIAETGTSAFGINQTTF---PNNTYGISQVlwGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRW 460
Cdd:COG3960 389 YVTTIGLSQIAAAQFLHvfkPRHWINCGQA--GPLGWTIPAALGVCAA----DPKRNVVAISGDYDFQFLIEELAVGAQF 462
|
490
....*....|....
1PYD_A 461 GLkPYLFVLNNDGY 474
Cdd:COG3960 463 KI-PYIHVLVNNAY 475
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
18-471 |
4.92e-11 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 65.23 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 18 NVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALNGIAGSYAEHVGVL 96
Cdd:PRK08979 18 GVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYMDSIPMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 97 HvvgvpsISSQAKQLLlhhtLGNGDFTVFHR--MSANISETTAMITDIATAPAEIDRCIrttYV--TQR--PVYLGLPAN 170
Cdd:PRK08979 98 V------LSGQVPSNL----IGNDAFQECDMigISRPVVKHSFLVKDAEDIPEIIKKAF---YIasTGRpgPVVIDLPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 171 LVDlnvPAKLL--QTPIDMSLK---PNDAESEKEVIDTILALVKdAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVT 245
Cdd:PRK08979 165 CLN---PAILHpyEYPESIKMRsynPTTSGHKGQIKRGLQALLA-AKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 246 PMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRN---ATFP 322
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGM-LGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKtvrVDIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 323 GV-QMKFVLQKLLTNIADAAKGYKPVAVPA--------RTPANAAVPASTP-LKQEWMWNQLGNfLQEGDVVIAetgtSA 392
Cdd:PRK08979 320 IVgSADKVLDSMLALLDESGETNDEAAIASwwneievwRSRNCLAYDKSSErIKPQQVIETLYK-LTNGDAYVA----SD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 393 FGINQT------TFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYL 466
Cdd:PRK08979 395 VGQHQMfaalyyPFDKPRRWINSGGLGTMGFGLPAAMGVKFAM----PDETVVCVTGDGSIQMNIQELSTALQYDIPVKI 470
|
....*
1PYD_A 467 FVLNN 471
Cdd:PRK08979 471 INLNN 475
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
9-473 |
6.12e-11 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 65.01 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 9 YLFERLKQVNVNTVFGLPGdFNLSLLDKIYEVEGMRWAGNANELNAAYAA--DGYARIKGMSCIiTTFGVGELSALNGIA 86
Cdd:PRK09259 15 LVIDALKLNGIDTIYGVVG-IPITDLARLAQAEGIRYIGFRHEQSAGNAAaaAGFLTQKPGVCL-TVSAPGFLNGLTALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 87 GSyaehvgvlHVVGVPSI----SSQAKQLLLHHtlgnGDFTVFHRMSANISETTAM-----ITDIATAPAeidRCIRTTy 157
Cdd:PRK09259 93 NA--------TTNCFPMImisgSSEREIVDLQQ----GDYEELDQLNAAKPFCKAAfrvnrAEDIGIGVA---RAIRTA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 158 VTQRP--VYLGLPANLV----DLNVPAKLLQTPIDMSLK--PNDaesekEVIDTILALVKDAKNPVIL--ADACCSRHDv 227
Cdd:PRK09259 157 VSGRPggVYLDLPAKVLaqtmDADEALTSLVKVVDPAPAqlPAP-----EAVDRALDLLKKAKRPLIIlgKGAAYAQAD- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 228 kAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVYVGTlskpevkeAVESADLILSVGA----LLSDFNTGSFSYSYKT 303
Cdd:PRK09259 231 -EQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSL--------ALANADVVLLVGArlnwLLSHGKGKTWGADKKF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 304 KNI----VEFHSDhMKIrNATFPGvQMKFVLQKLLTNIadAAKGYKPVA-----VPARTPANAAVPAST------PLKqe 368
Cdd:PRK09259 302 IQIdiepQEIDSN-RPI-AAPVVG-DIGSVMQALLAGL--KQNTFKAPAewldaLAERKEKNAAKMAEKlstdtqPMN-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 369 wMWNQLG---NFLQEG-DV-VIAEtgtsafGINQTTFPNNTYGISQV-------LWGSIGFTTGATLGAAfaaeeIDPKK 436
Cdd:PRK09259 375 -FYNALGairDVLKENpDIyLVNE------GANTLDLARNIIDMYKPrhrldcgTWGVMGIGMGYAIAAA-----VETGK 442
|
490 500 510
....*....|....*....|....*....|....*..
1PYD_A 437 RVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDG 473
Cdd:PRK09259 443 PVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG 479
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
334-476 |
1.67e-10 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 63.32 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 334 LTNIADA--AKGYKPVAVPARTPAnaavPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTT-------FPNNT 404
Cdd:PRK07586 308 LEALADAlgAKPAAPPLAAPARPP----LPTGALTPEAIAQVIAALLPENAIVVDESITSGRGFFPATagaaphdWLTLT 383
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PYD_A 405 yGisqvlwGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI 476
Cdd:PRK07586 384 -G------GAIGQGLPLATGAAVAC----PDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAI 444
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-471 |
1.74e-10 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 63.67 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 2 SEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELS 80
Cdd:PRK06965 19 ADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVALVTSGPGVTN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 81 ALNGIAGSYAEHVGVLHvvgvpsISSQAKQlllhHTLGNGDF----TVfhRMSANISETTAMITDiataPAEIDRCIRTT 156
Cdd:PRK06965 99 AVTGIATAYMDSIPMVV------ISGQVPT----AAIGQDAFqecdTV--GITRPIVKHNFLVKD----VRDLAETVKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 157 YVTQRPvylGLPANLVdlnvpaklLQTPIDMSLKPNDAESEKEV---------------IDTILALVKDAKNP------- 214
Cdd:PRK06965 163 FYIART---GRPGPVV--------VDIPKDVSKTPCEYEYPKSVemrsynpvtkghsgqIRKAVSLLLSAKRPyiytggg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 215 VILADACcsrhdvkAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNT 294
Cdd:PRK06965 232 VILANAS-------RELRQLADLLGYPVTNTLMGLGAYPASDKKFLGM-LGMHGTYEANMAMQHCDVLIAIGARFDDRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 295 GSFS-YSYKTKNIVEFHSDHMKIR---NATFPGV-QMKFVLQKLLTNIADAAKGYKPVAVPARTPANAAVPASTPLKQ-- 367
Cdd:PRK06965 304 GNPAhFASRPRKIIHIDIDPSSISkrvKVDIPIVgDVKEVLKELIEQLQTAEHGPDADALAQWWKQIEGWRSRDCLKYdr 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 368 -----------EWMWNqlgnfLQEGDVVIaetgTSAFGINQtTFPNNTYGISQV-LW---GSIGfTTGATLGAAFAAEEI 432
Cdd:PRK06965 384 eseiikpqyvvEKLWE-----LTDGDAFV----CSDVGQHQ-MWAAQFYRFNEPrRWinsGGLG-TMGVGLPYAMGIKMA 452
|
490 500 510
....*....|....*....|....*....|....*....
1PYD_A 433 DPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06965 453 HPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNN 491
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
373-478 |
5.59e-10 |
|
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: 58.38 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 373 QLGNFLQEGDVVIAETGTSAFGINQ---TTFPNNTYGISQvlwGSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQL 449
Cdd:cd02002 9 ALAAALPEDAIIVDEAVTNGLPLRDqlpLTRPGSYFTLRG---GGLGWGLPAAVGAALA----NPDRKVVAIIGDGSFMY 81
|
90 100 110
....*....|....*....|....*....|
1PYD_A 450 TVQEISTMIRWGLkPYLFV-LNNDGYTIEK 478
Cdd:cd02002 82 TIQALWTAARYGL-PVTVViLNNRGYGALR 110
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
14-456 |
7.39e-10 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 61.54 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMS--CIITTfGVGELSALNGIAGSYAE 91
Cdd:PRK07789 41 LEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVgvCMATS-GPGATNLVTPIADANMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 92 hvgvlhvvGVP--SISSQAKQLLlhhtLGNGDFtvfhrMSANISETTAMITD---IATAPAEIDRCIRTTY---VTQRPv 163
Cdd:PRK07789 120 --------SVPvvAITGQVGRGL----IGTDAF-----QEADIVGITMPITKhnfLVTDADDIPRVIAEAFhiaSTGRP- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 164 ylGlpANLVDlnVPAKLLQT------PIDMSL---KPNDAESEKeVIDTILALVKDAKNPVILADACCSRHDVKAETKKL 234
Cdd:PRK07789 182 --G--PVLVD--IPKDALQAqttfswPPRMDLpgyRPVTKPHGK-QIREAAKLIAAARRPVLYVGGGVIRAEASAELREL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 235 IDLTQFPAFVTPMGKGSISEQHPRYGGV--YVGTLskPEVKeAVESADLILSVGALLSDFNTG---SFSYSYKtknIVef 309
Cdd:PRK07789 255 AELTGIPVVTTLMARGAFPDSHPQHLGMpgMHGTV--AAVA-ALQRSDLLIALGARFDDRVTGkldSFAPDAK---VI-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 310 HSD-----HMKIRNATFPGV-QMKFVLQKLLTNI-ADAAKGYKPV---------AVPARTPANAAVPASTPLKQEWMWNQ 373
Cdd:PRK07789 327 HADidpaeIGKNRHADVPIVgDVKEVIAELIAALrAEHAAGGKPDltawwayldGWRETYPLGYDEPSDGSLAPQYVIER 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 374 LGnflqegdvviAETGTSAF---GINQ-----TTF-----PN---NTYGIsqvlwGSIGFTTGATLGAAFAAeeidPKKR 437
Cdd:PRK07789 407 LG----------EIAGPDAIyvaGVGQhqmwaAQFidyekPRtwlNSGGL-----GTMGYAVPAAMGAKVGR----PDKE 467
|
490
....*....|....*....
1PYD_A 438 VILFIGDGSLQLTVQEIST 456
Cdd:PRK07789 468 VWAIDGDGCFQMTNQELAT 486
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
413-471 |
3.78e-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: 56.35 E-value: 3.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
1PYD_A 413 GSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:cd02015 50 GTMGFGLPAAIGAKVAR----PDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNN 104
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
376-507 |
6.12e-09 |
|
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: 55.23 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 376 NFLQEGDVVIAEtGTSAFGINQTTFPNN---TYGISQVlWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQ 452
Cdd:cd02004 10 EALPDDAIIVSD-GGNTMDWARYILRPRkprHRLDAGT-FGTLGVGLGYAIAAALAR----PDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
1PYD_A 453 EISTMIRWGLKPYLFVLNNDGYTIEKliHGPKAQYNEIQgwDHLSLLPT---------FGAKDY 507
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGL--DGQQLSYGLGL--PVTTLLPDtrydlvaeaFGGKGE 143
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
5-471 |
6.54e-09 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 58.30 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 5 TLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEvEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSALN 83
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRK-SKVKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 84 GIAGSYAEHVGVLhvvgvpSISSQAKQLLLHHtlgngDFtvFH-----RMSANISETTAMITDIATAPAEIDRCIRTTyV 158
Cdd:PRK06457 82 GLYDAKMDHAPVI------ALTGQVESDMIGH-----DY--FQevnltKLFDDVAVFNQILINPENAEYIIRRAIREA-I 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 159 TQRPV-YLGLPANLVDLNVPAKLLQ-TPIDMSLKPNDAESEKEVIDtilalvkDAKNPVILADAccSRHDVKAETKKLID 236
Cdd:PRK06457 148 SKRGVaHINLPVDILRKSSEYKGSKnTEVGKVKYSIDFSRAKELIK-------ESEKPVLLIGG--GTRGLGKEINRFAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 237 LTQFPAFVTPMGKGSISEQHPR-YGGV-YVGTlsKPEVkEAVESADLILSVGAllsdfntgSFSYS----YKTKNI-VEF 309
Cdd:PRK06457 219 KIGAPIIYTLNGKGILPDLDPKvMGGIgLLGT--KPSI-EAMDKADLLIMLGT--------SFPYVnflnKSAKVIqVDI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 310 HSDHMKIR----------NATFPGVQMKFVLQKLLTNIADAAKGYKpvavpaRTPANAAVPASTPLKQEWMWNQLGNFLQ 379
Cdd:PRK06457 288 DNSNIGKRldvdlsypipVAEFLNIDIEEKSDKFYEELKGKKEDWL------DSISKQENSLDKPMKPQRVAYIVSQKCK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 380 EGDVVIAETGTSAFGINQ--TTFPNNTYGISQVLwGSIGFTTGATLGAAFAAeeiDPKKRVILFIGDGSLQLTVQEISTM 457
Cdd:PRK06457 362 KDAVIVTDTGNVTMWTARhfRASGEQTFIFSAWL-GSMGIGVPGSVGASFAV---ENKRQVISFVGDGGFTMTMMELITA 437
|
490
....*....|....
1PYD_A 458 IRWGLKPYLFVLNN 471
Cdd:PRK06457 438 KKYDLPVKIIIYNN 451
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-471 |
1.08e-08 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 57.83 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMS-CIITTFGVGEL 79
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTgVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 SALNGIAGSYAEHVGVLHvvgvpsISSQAKQlllhHTLGNGDF--TVFHRMSANISETTAMITDiataPAEIDRCIRTT- 156
Cdd:PRK06466 81 NAITGIATAYMDSIPMVV------LSGQVPS----TLIGEDAFqeTDMVGISRPIVKHSFMVKH----ASEIPEIIKKAf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 157 YVTQR----PVYLGLPANLVDLNV------PAKLLQTPIDMSLKPNDAESEKEViDTILAlvkdAKNPVILADACCSRHD 226
Cdd:PRK06466 147 YIAQSgrpgPVVVDIPKDMTNPAEkfeyeyPKKVKLRSYSPAVRGHSGQIRKAV-EMLLA----AKRPVIYSGGGVVLGN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 227 VKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNI 306
Cdd:PRK06466 222 ASALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGM-LGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 307 VEFHSDHMKIRN---ATFPGV-QMKFVLQKLLTNIADAAKgykpvavparTPANAAVPAstplkqeWmWNQLGNFLQEGD 382
Cdd:PRK06466 301 IHIDIDPASISKtikADIPIVgPVESVLTEMLAILKEIGE----------KPDKEALAA-------W-WKQIDEWRGRHG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 383 VVIAETGTSAFGINQTTFP-------NNTYGISQV-----------------LW---GSIGfTTGATLGAAFAAEEIDPK 435
Cdd:PRK06466 363 LFPYDKGDGGIIKPQQVVEtlyevtnGDAYVTSDVgqhqmfaaqyykfnkpnRWinsGGLG-TMGFGLPAAMGVKLAFPD 441
|
490 500 510
....*....|....*....|....*....|....*.
1PYD_A 436 KRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK06466 442 QDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNN 477
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
10-471 |
1.11e-08 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 57.79 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 10 LFERLKQVNVNTVFGLPGDFNLSLLDKIY--EVEGM------RwagnaNELNAAYAADGYARIKGMS--CIITTfGVGEL 79
Cdd:CHL00099 16 LIDSLVRHGVKHIFGYPGGAILPIYDELYawEKKGLikhilvR-----HEQGAAHAADGYARSTGKVgvCFATS-GPGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 80 SALNGIAGSYAEHVGVLHvvgvpsISSQAKQLLLhhtlGNGDFT-----------VFHrmSANISETTAMITDIATApae 148
Cdd:CHL00099 90 NLVTGIATAQMDSVPLLV------ITGQVGRAFI----GTDAFQevdifgitlpiVKH--SYVVRDARDISRIVAEA--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 149 idrcirtTYVTQR----PVYLGLPANL----------VDLNVPAKLLQTPIDMSLKPNDaesekevIDTILALVKDAKNP 214
Cdd:CHL00099 155 -------FYIAKHgrpgPVLIDIPKDVglekfdyyppEPGNTIIKILGCRPIYKPTIKR-------IEQAAKLILQSSQP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 215 -------VILADAccsrhdvKAETKKLIDLTQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGA 287
Cdd:CHL00099 221 llyvgggAIISDA-------HQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGM-LGMHGTAYANFAVSECDLLIALGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 288 LLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGV----QMKFVLQKLLTNIADAAKGYKPVAVPA-RTPANA---AV 359
Cdd:CHL00099 293 RFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVaivgDVKKVLQELLELLKNSPNLLESEQTQAwRERINRwrkEY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 360 PASTPLKQEWMWNQlgnflqegdVVIAETGTSAfginQTTFPNNTYGISQvLW------------------GSIGFTTGA 421
Cdd:CHL00099 373 PLLIPKPSTSLSPQ---------EVINEISQLA----PDAYFTTDVGQHQ-MWaaqflkckprkwlssaglGTMGYGLPA 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
1PYD_A 422 TLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:CHL00099 439 AIGAQIA----HPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
14-472 |
5.64e-07 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 52.40 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMS--CIITTfGVGELSALNGIAGSYAE 91
Cdd:PRK08155 23 LERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPavCMACS-GPGATNLVTAIADARLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 92 HV-GVLHVVGVPS--ISSQAKQLLlhHTLGngdftvfhrMSANISETTAMITDIATAPAEIDRCIRttyVTQR----PVY 164
Cdd:PRK08155 102 SIpLVCITGQVPAsmIGTDAFQEV--DTYG---------ISIPITKHNYLVRDIEELPQVISDAFR---IAQSgrpgPVW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 165 LGLPAN----LVDLnvpAKLLQTPIDMSLKPNDAESekevIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF 240
Cdd:PRK08155 168 IDIPKDvqtaVIEL---EALPAPAEKDAAPAFDEES----IRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 241 PAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEAVESADLILSVGALLSDFNTG---SFSYSYKTKNIVEFHSDHMKIR 317
Cdd:PRK08155 241 PTTMTLMALGMLPKAHPLSLGM-LGMHGARSTNYILQEADLLIVLGARFDDRAIGkteQFCPNAKIIHVDIDRAELGKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 318 NATFpGVQ--MKFVLQKLLTNIADAAKG--YKPVA-----VPARTPAnaavpASTPLKQEWMWNQLGNFLQEGDVVIAET 388
Cdd:PRK08155 320 QPHV-AIQadVDDVLAQLLPLVEAQPRAewHQLVAdlqreFPCPIPK-----ADDPLSHYGLINAVAACVDDNAIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 389 GTSAFGINQTtFPNNtyGISQVL----WGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKP 464
Cdd:PRK08155 394 GQHQMWTAQA-YPLN--RPRQWLtsggLGTMGFGLPAAIGAALAN----PERKVLCFSGDGSLMMNIQEMATAAENQLDV 466
|
....*...
1PYD_A 465 YLFVLNND 472
Cdd:PRK08155 467 KIILMNNE 474
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
14-474 |
6.76e-07 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 51.90 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIK----GMsCIITTFGVGElsalNGIAGSY 89
Cdd:PRK11269 14 LEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATagniGV-CIGTSGPAGT----DMITGLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 90 AehvgvLHVVGVP--SISSQAKQLLLHHTlgngDFtvfhrMSANISETTAMITDIATA---PAEIDRCIRTTYVTQR--- 161
Cdd:PRK11269 89 S-----ASADSIPilCITGQAPRARLHKE----DF-----QAVDIESIAKPVTKWAVTvrePALVPRVFQQAFHLMRsgr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 162 --PVYLGLPanlvdLNVPAKLLQTPIDM--SLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDL 237
Cdd:PRK11269 155 pgPVLIDLP-----FDVQVAEIEFDPDTyePLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 238 TQFPAFVTPMGKGSISEQHPRYGGVyVGTLSKPEVKEA--VESaDLILSVGALLSDFNTGSFSYSYKTKNIVE------- 308
Cdd:PRK11269 230 TGVPVIPTLMGWGAIPDDHPLMAGM-VGLQTSHRYGNAtlLAS-DFVLGIGNRWANRHTGSVEVYTKGRKFVHvdieptq 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 309 ----FHSDHMKIRNAtfpgvqmKFVLQKLLtniaDAAKGYKPV-AVPARTPANAAVPA------------STPLKQEWMW 371
Cdd:PRK11269 308 igrvFGPDLGIVSDA-------KAALELLV----EVAREWKAAgRLPDRSAWVADCQErkrtllrkthfdNVPIKPQRVY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 372 NQLgnflqegdvviaetgTSAFGiNQTTFPnNTYGISQVL------------W------GSIGFTTGATLGAAFAaeeiD 433
Cdd:PRK11269 377 EEM---------------NKAFG-RDTCYV-STIGLSQIAaaqflhvykprhWincgqaGPLGWTIPAALGVRAA----D 435
|
490 500 510 520
....*....|....*....|....*....|....*....|.
1PYD_A 434 PKKRVILFIGDGSLQLTVQEISTMIRWGLkPYLFVLNNDGY 474
Cdd:PRK11269 436 PDRNVVALSGDYDFQFLIEELAVGAQFNL-PYIHVLVNNAY 475
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-471 |
9.25e-07 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 51.63 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 3 EITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGELSA 81
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGATNA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 82 LNGIAGSYAEHVGVLhvvgvpSISSQAKQlllhHTLGNGDF----TVfhRMSANISETTAMITDIATAPAEIDRCIRTTy 157
Cdd:PRK09107 90 VTPLQDALMDSIPLV------CITGQVPT----HLIGSDAFqecdTV--GITRPCTKHNWLVKDVNDLARVIHEAFHVA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 158 VTQRP--VYLGLPANLV----DLNVPAKLLQTPIDMSLKPNDAESekevIDTILALVKDAKNPVILADACCSRHDVKAET 231
Cdd:PRK09107 157 TSGRPgpVVVDIPKDVQfatgTYTPPQKAPVHVSYQPKVKGDAEA----ITEAVELLANAKRPVIYSGGGVINSGPEASR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 232 --KKLIDLTQFPAFVTPMGKGSiseqHPRYGGVYVGTLSKP---EVKEAVESADLILSVGALLSDFNTG---SFSYSYKT 303
Cdd:PRK09107 233 llRELVELTGFPITSTLMGLGA----YPASGKNWLGMLGMHgtyEANMAMHDCDVMLCVGARFDDRITGrldAFSPNSKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 304 KNIVEFHSDHMKIRNATFPgvqmkfVLQKLLTNIADAAKGYKpvaVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDV 383
Cdd:PRK09107 309 IHIDIDPSSINKNVRVDVP------IIGDVGHVLEDMLRLWK---ARGKKPDKEALADWWGQIARWRARNSLAYTPSDDV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 384 VIAEtgtsaFGINQ---TTFPNNTYGISQV----LWGS--IGF-------------TTGATLGAAFAAEEIDPKKRVILF 441
Cdd:PRK09107 380 IMPQ-----YAIQRlyeLTKGRDTYITTEVgqhqMWAAqfFGFeepnrwmtsgglgTMGYGLPAALGVQIAHPDALVIDI 454
|
490 500 510
....*....|....*....|....*....|
1PYD_A 442 IGDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:PRK09107 455 AGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
14-286 |
9.71e-07 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 51.39 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 14 LKQVNVNTVFGLPG---D--FNlSLLDKIYEVEGMRwagnaNELNAAYAADGYARIKGMS-CIITTFGVGELSALNGIAG 87
Cdd:PRK08617 15 LINQGVKYVFGIPGakiDrvFD-ALEDSGPELIVTR-----HEQNAAFMAAAIGRLTGKPgVVLVTSGPGVSNLATGLVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 88 SYAEHVgvlhvvgvP--SISSQAK---QL-LLHHTLGNGDftvfhrMSANISETTAMITDIATAPAEIDRCIRTTyVTQR 161
Cdd:PRK08617 89 ATAEGD--------PvvAIGGQVKradRLkRTHQSMDNVA------LFRPITKYSAEVQDPDNLSEVLANAFRAA-ESGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 162 P--VYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAEsekeVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQ 239
Cdd:PRK08617 154 PgaAFVSLPQDVVDAPVTSKAIAPLSKPKLGPASPE----DINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTN 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
1PYD_A 240 FPAFVTPMGKGSISEQH-PRYGGvYVGTLSKPEVKEAVESADLILSVG 286
Cdd:PRK08617 230 LPVVETFQAAGVISRELeDHFFG-RVGLFRNQPGDELLKKADLVITIG 276
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
351-474 |
1.41e-06 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 51.15 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 351 ARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFpnNTYgISQVLWGSIGFTTGATLGAAFAae 430
Cdd:PRK08327 371 AKRAEIERLKDRGPITPAYLSYCLGEVADEYDAIVTEYPFVPRQARLNKP--GSY-FGDGSAGGLGWALGAALGAKLA-- 445
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
1PYD_A 431 eiDPKKRVILFIGDGSLQLTVQEISTMI--RWGLKPYLFVLNNDGY 474
Cdd:PRK08327 446 --TPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
364-471 |
5.86e-06 |
|
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: 46.75 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 364 PLKQEWMWNQLGNFLQEGDVVIAETGTSA-FGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAaeeiDPKKRVILFI 442
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTvWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLA----YPDRQVIALS 76
|
90 100
....*....|....*....|....*....
1PYD_A 443 GDGSLQLTVQEISTMIRWGLKPYLFVLNN 471
Cdd:cd02014 77 GDGGFAMLMGDLITAVKYNLPVIVVVFNN 105
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
334-476 |
4.70e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 46.02 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 334 LTNIADAAKGykPVAVPARTPANAAVPASTPLKQEwMWNQL-GNFLQEGDVVIAETGTS--AFGINQTTFPNNTYgiSQV 410
Cdd:PRK12474 312 LQDLADAVDA--PAEPAARTPLALPALPKGALNSL-GVAQLiAHRTPDQAIYADEALTSglFFDMSYDRARPHTH--LPL 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PYD_A 411 LWGSIGFTTGATLGAAFAAeeidPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI 476
Cdd:PRK12474 387 TGGSIGQGLPLAAGAAVAA----PDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAI 448
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
418-508 |
5.21e-05 |
|
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: 44.20 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 418 TTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTI----EKLIHGPKAqYNEIQGW 493
Cdd:cd02010 49 TMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGYGLikwkQEKEYGRDS-GVDFGNP 127
|
90
....*....|....*
1PYD_A 494 DHLSLLPTFGAKDYE 508
Cdd:cd02010 128 DFVKYAESFGAKGYR 142
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
364-478 |
3.32e-04 |
|
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: 42.11 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 364 PLKQEWMWNQLGNFLQEGDVVIAETG-TSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAeeidPKKRVILFI 442
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGnICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAA----PDRPVVAIA 78
|
90 100 110
....*....|....*....|....*....|....*.
1PYD_A 443 GDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEK 478
Cdd:cd02013 79 GDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
5-85 |
8.76e-04 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 41.90 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 5 TLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGM------SCiittfGVGE 78
Cdd:PRK09124 4 TVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGElavcagSC-----GPGN 78
|
....*..
1PYD_A 79 LSALNGI 85
Cdd:PRK09124 79 LHLINGL 85
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
405-474 |
1.14e-03 |
|
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: 40.37 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 405 YGISqvlwgSIGFTTGATLGAAFAAEEIDpkkrVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGY 474
Cdd:cd02003 45 YGYS-----CMGYEIAAGLGAKLAKPDRE----VYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGF 105
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-84 |
2.66e-03 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 40.66 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PYD_A 1 MSEiTLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEG-MRWAGNANELNAAYAADGYARIKG-MSCIITTFGVGE 78
Cdd:PRK08273 1 MSQ-TVADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGA 79
|
....*.
1PYD_A 79 LSALNG 84
Cdd:PRK08273 80 IHLLNG 85
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
413-474 |
3.90e-03 |
|
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: 38.80 E-value: 3.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
1PYD_A 413 GSIGFTTGATLGAAFAaeeiDPKKRVILFIGDGSLQLTVQEISTMIRWGLkPYLFVLNNDGY 474
Cdd:cd02006 57 GPLGWTVPAALGVAAA----DPDRQVVALSGDYDFQFMIEELAVGAQHRI-PYIHVLVNNAY 113
|
|
|