|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
61-635 |
0e+00 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 1076.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 61 GSPLVIVPPPTTAPSTLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRGVGA 140
Cdd:PLN02573 2 SSAPKPATPVSSSDATLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 141 CAVTFTVGSLSLINAIAGAYSEDLPVICIVGGPNSNDYGSKKILHHTIGLPDFSQELRCFQNVTCYQAIIDSLEDAQWQI 220
Cdd:PLN02573 82 CVVTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVINNLEDAHELI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 221 DKAICKCLEESKPVYISICCNLVAIPHPSFSAQPlIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKA 300
Cdd:PLN02573 162 DTAISTALKESKPVYISVSCNLAAIPHPTFSREP-VPFFLTPRLSNKMSLEAAVEAAAEFLNKAVKPVLVGGPKLRVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 301 EAAFLELADSCGYAVAVTPSAKGMFPENHPHFIGTYWGTVSTAFCGETVEIADASIFVGANLDELETVGYSLAYKKNKAI 380
Cdd:PLN02573 241 CKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 381 IVKPDSVVFPNGESYGAVQMKDFLWALGKRLKPNSRAYENYRRIYIAESSPPESEAGEELRVNVLFKHIQKMLSSNMTVI 460
Cdd:PLN02573 321 IVQPDRVTIGNGPAFGCVLMKDFLEALAKRVKKNTTAYENYKRIFVPEGEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 461 AETGDSWFHSQKLKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLI 540
Cdd:PLN02573 401 AETGDSWFNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 541 NNGGYTIEVEIHDGPYNIINNWDYTAFVDAVNNHQSNCWTTKVHTEEELVNAIEIAMKDRNDCLCFIEVIAHRDDTSKEL 620
Cdd:PLN02573 481 NNGGYTIEVEIHDGPYNVIKNWNYTGLVDAIHNGEGKCWTAKVRTEEELIEAIATATGEKKDCLCFIEVIVHKDDTSKEL 560
|
570
....*....|....*
gi 1784872638 621 LEFGSRIAAMGSHPP 635
Cdd:PLN02573 561 LEWGSRVSAANSRPP 575
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
76-626 |
0e+00 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 612.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRGVGACAVTFTVGSLSLINA 155
Cdd:COG3961 6 TVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAING 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 156 IAGAYSEDLPVICIVGGPNSNDYGSKKILHHTIGLPDFSQELRCFQNVTCYQAIIDSlEDAQWQIDKAICKCLEESKPVY 235
Cdd:COG3961 86 IAGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLGDGDFDHFLRMFEEVTVAQAVLTP-ENAAAEIDRVLAAALREKRPVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 236 ISICCNLVAIPhpsfSAQPLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAV 315
Cdd:COG3961 165 IELPRDVADAP----IEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 316 AVTPSAKGMFPENHPHFIGTYWGTVSTAFCGETVEIADASIFVGANLDELETVGYSLAYKKNKAIIVKPDSVVFpNGESY 395
Cdd:COG3961 241 ATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRV-GGHIY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 396 GAVQMKDFLWALGKRLKPNSRayenYRRIYIAESSPPESEAGEELRVNVLFKHIQKMLSSNMTVIAETGDSWFHSQKLKL 475
Cdd:COG3961 320 PGVSLADFLEALAELLKKRSA----PLPAPAPPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 476 PKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLINNGGYTIEVEIH--D 553
Cdd:COG3961 396 PEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHgpD 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784872638 554 GPYNIINNWDYTAFVDAVNNHQSNCWttKVHTEEELVNAIEIAMKDRnDCLCFIEVIAHRDDTSKELLEFGSR 626
Cdd:COG3961 476 GPYNDIANWDYAKLPEAFGGGNALGF--RVTTEGELEEALAAAEANT-DRLTLIEVVLDKMDAPPLLKRLGKA 545
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
80-240 |
4.14e-87 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 268.59 E-value: 4.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 80 YLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRGVGACAVTFTVGSLSLINAIAGA 159
Cdd:cd07038 2 YLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 160 YSEDLPVICIVGGPNSNDYGSKKILHHTIGLPDFSQELRCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEESKPVYISIC 239
Cdd:cd07038 82 YAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTDPENAAEEIDRVLRTALRESRPVYIEIP 161
|
.
gi 1784872638 240 C 240
Cdd:cd07038 162 R 162
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
440-621 |
5.71e-78 |
|
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: 245.52 E-value: 5.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 440 LRVNVLFKHIQKMLSSNMTVIAETGDSWFHSQKLKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQ 519
Cdd:cd02005 2 LTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 520 MAPQDVSTMLKLGQKNIIFLINNGGYTIEVEIHDG--PYNIINNWDYTAFVDAVNNhQSNCWTTKVHTEEELVNAIEIAm 597
Cdd:cd02005 82 MTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPeaSYNDIANWNYTKLPEVFGG-GGGGLSFRVKTEGELDEALKDA- 159
|
170 180
....*....|....*....|....
gi 1784872638 598 KDRNDCLCFIEVIAHRDDTSKELL 621
Cdd:cd02005 160 LFNRDKLSLIEVILPKDDAPEALK 183
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
76-615 |
1.66e-69 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 235.44 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLIN 154
Cdd:COG0028 4 TGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 155 AIAGAYSEDLPVICIVGGPNSNDYGSkkilhhtiglpDFSQEL---RCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEES 231
Cdd:COG0028 84 GLADAYMDSVPVLAITGQVPTSLIGR-----------GAFQEVdqvGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 232 K-PVYISICCNLVAIPhpsFSAQPLiPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADS 310
Cdd:COG0028 153 PgPVVLDIPKDVQAAE---AEEEPA-PPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 311 CGYAVAVTPSAKGMFPENHPHFIGTyWGTVSTAFCGETVEIADASIFVGANLDELETVGYSLAYKKNKAIIVKPDSVVFp 390
Cdd:COG0028 229 LGAPVVTTLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEI- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 391 nGESYGA---VQ--MKDFLWALGKRLKPNSRA-------YENYRRIYIAEssppESEAGEELRVNVLFKHIQKMLSSNMT 458
Cdd:COG0028 307 -GKNYPVdlpIVgdAKAVLAALLEALEPRADDraawlarIAAWRAEYLAA----YAADDGPIKPQRVIAALREALPDDAI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 459 VIAETGDS--WFHsQKLKLPK------SCGyevqllYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLK 530
Cdd:COG0028 382 VVTDVGQHqmWAA-RYLRFRRprrfltSGG------LGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 531 LGQKNIIFLINNGGYTIEVEIHDGPYN------IINNWDYTAFVDAVnnhqsNCWTTKVHTEEELVNAIEIAMkdRNDCL 604
Cdd:COG0028 455 YGLPVKVVVLNNGGLGMVRQWQELFYGgrysgtDLPNPDFAKLAEAF-----GAKGERVETPEELEAALEEAL--ASDGP 527
|
570
....*....|.
gi 1784872638 605 CFIEVIAHRDD 615
Cdd:COG0028 528 ALIDVRVDPEE 538
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
77-238 |
2.73e-37 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 136.60 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 77 LGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYAR-SRGVGACAVTFTVGSLSLINA 155
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARaTGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 156 IAGAYSEDLPVICIVGGPNSNDYGskkilHHTIGLPDFSQELrcFQNVTCYQAIIDSLEDAQWQIDKAICKCLEESK-PV 234
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVG-----RGALQQELDQLAL--FRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPgPV 153
|
....
gi 1784872638 235 YISI 238
Cdd:pfam02776 154 YLEI 157
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
80-238 |
2.91e-30 |
|
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: 116.29 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 80 YLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRGVGACAVTFTVGSLSLINAIAGA 159
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1784872638 160 YSEDLPVICIVGGPNSNDygskkilhHTIGLPDFSQELRCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEESKPVYISI 238
Cdd:cd06586 82 AAEHLPVVFLIGARGISA--------QAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRL 152
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
79-238 |
2.24e-28 |
|
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: 111.08 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 79 HYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEkGLNLVGCCNELNAGYAADGYAR-SRGVGACAVTFTVGSLSLINAIA 157
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARS-GIRYILVRHEQGAVGMADGYARaTGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 158 GAYSEDLPVICIVGGPNSNDYGskkilhhTIGLPDFSQeLRCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEESK-PVYI 236
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEG-------RGAFQEIDQ-VALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPgPVAL 151
|
..
gi 1784872638 237 SI 238
Cdd:cd07035 152 DL 153
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
274-381 |
8.91e-25 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 99.95 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 274 VEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVAVTPSAKGMFPENHPHFIGtYWGTVSTAFCGETVEIAD 353
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100
....*....|....*....|....*...
gi 1784872638 354 ASIFVGANLDELETVGYSLAYKKNKAII 381
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPDAKII 107
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
76-542 |
9.18e-22 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 99.69 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSnlvlFDYFV-----AEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGS 149
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDS----IDAVVdalrkEQDKIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 150 LSLINAIAGAYSEDLPVICIVGGPNSNDYGSkkilhhtiglpDFSQEL---RCFQNVTCYQAIIDSLEDAQWQIDKAICK 226
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGT-----------DFFQEVnleKMFEDVAVYNHQIMSAENLPEIVNQAIRT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 227 CLEEsKPVYISICCN------LVAIPHPSFSAQPLIPLSLSPKQsnqmglemaVEKAADLLNTAIKPVMIGGKKLRPAKA 300
Cdd:PRK08611 150 AYEK-KGVAVLTIPDdlpaqkIKDTTNKTVDTFRPTVPSPKPKD---------IKKAAKLINKAKKPVILAGLGAKHAKE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 301 EaaFLELADSCGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGAN---LDELEtvgyslayKKN 377
Cdd:PRK08611 220 E--LLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNL-GKIGTKPAYEAMQEADLLIMVGTNypyVDYLP--------KKA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 378 KAIIV--KPDSVvfpnGESY----GAV-QMKDFLWALGKRLKPNS-RAY-----ENYRRiYIAESSPPESEAGEELRVNV 444
Cdd:PRK08611 289 KAIQIdtDPANI----GKRYpvnvGLVgDAKKALHQLTENIKHVEdRRFleacqENMAK-WWKWMEEDENNASTPIKPER 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 445 LFKHIQKMLSSNMTVIAETGDS--WfHSQKLKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAP 522
Cdd:PRK08611 364 VMAAIQKIADDDAVLSVDVGTVtvW-SARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVM 442
|
490 500
....*....|....*....|
gi 1784872638 523 QDVSTMLKLGQKNIIFLINN 542
Cdd:PRK08611 443 QDFVTAVKYKLPIVVVVLNN 462
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
76-615 |
1.47e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 95.46 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKG-LNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLI 153
Cdd:PRK08266 5 TGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGrPGVCSVVPGPGVLNAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 154 NAIAGAYSEDLPVICIVGgpnsndygskKILHHTIG--------LPDFSQELRCFqnvTCYQAIIDSLEDAQWQIDKAIC 225
Cdd:PRK08266 85 AALLTAYGCNSPVLCLTG----------QIPSALIGkgrghlheMPDQLATLRSF---TKWAERIEHPSEAPALVAEAFQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 226 KCLE-ESKPVyisiccnLVAIPHPSFSAQ-PLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPV-MIGGKklrPAKAEA 302
Cdd:PRK08266 152 QMLSgRPRPV-------ALEMPWDVFGQRaPVAAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMiFVGGG---AAGAGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 303 AFLELADSCGYAVAVTPSAKGMFPENHP---HFIGTY--WGTvstafcgetveiADASIFVGANLdELETVGYSLAYKKN 377
Cdd:PRK08266 222 EIRELAEMLQAPVVAFRSGRGIVSDRHPlglNFAAAYelWPQ------------TDVVIGIGSRL-ELPTFRWPWRPDGL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 378 KAIIVKPDsvvfpngesygAVQMKDFLWALG--KRLKPNSRAYENYRRIYIAESSPPESEAGE-ELRVNVLFKHIQKMLS 454
Cdd:PRK08266 289 KVIRIDID-----------PTEMRRLKPDVAivADAKAGTAALLDALSKAGSKRPSRRAELRElKAAARQRIQAVQPQAS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 455 SNMTVIAETGD--------------SWF----HSQKLKLpkSCGYEvqllyASIGWSLGATLGYAQAAPHKRLLLCIGDG 516
Cdd:PRK08266 358 YLRAIREALPDdgifvdelsqvgfaSWFafpvYAPRTFV--TCGYQ-----GTLGYGFPTALGAKVANPDRPVVSITGDG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 517 SFQMAPQDVSTMLKLGQKNIIFLINNGGY----TIEVEIHDGPY--NIINNWDYTAFVDAVNNHqsncwTTKVHTEEELV 590
Cdd:PRK08266 431 GFMFGVQELATAVQHNIGVVTVVFNNNAYgnvrRDQKRRFGGRVvaSDLVNPDFVKLAESFGVA-----AFRVDSPEELR 505
|
570 580
....*....|....*....|....*
gi 1784872638 591 NAIEIAMKDRNDCLcfIEVIAHRDD 615
Cdd:PRK08266 506 AALEAALAHGGPVL--IEVPVPRGS 528
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
67-610 |
2.61e-20 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 95.21 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 67 VPPPTTAPS-----TLGHYLASRLVEIGVSDIF--SVPgdSNLVLfdyfVAEK-GLNLVGCCNELNAGYAADGYAR-SRG 137
Cdd:PRK06112 1 LSKPLSAPGftlngTVAHAIARALKRHGVEQIFgqSLP--SALFL----AAEAiGIRQIAYRTENAGGAMADGYARvSGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 138 VGACAVTFTVGSLSLINAIAGAYSEDLPVICIVGGPNSN--DYGSKKILHHtIGLpdfsqelrcFQNVTCYQAIIDSLED 215
Cdd:PRK06112 75 VAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDqtDRNAFQELDH-IAL---------FQSCTKWVRRVTVAER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 216 AQWQIDKAI-CKCLEESKPVYISICCNLVAIPHPsfsaqpliplSLSPKQSNQMG---LEMAV------EKAADLLNTAI 285
Cdd:PRK06112 145 IDDYVDQAFtAATSGRPGPVVLLLPADLLTAAAA----------APAAPRSNSLGhfpLDRTVpapqrlAEAASLLAQAQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 286 KPVMIGGKKLRPAKAEAAFLELADSCGYAVAVTPSAKGMFPENHP---HFIGTYWGTVSTA-FCGETVEIADASIFVGAN 361
Cdd:PRK06112 215 RPVVVAGGGVHISGASAALAALQSLAGLPVATTNMGKGAVDETHPlslGVVGSLMGPRSPGrHLRDLVREADVVLLVGTR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 362 LDELETVGYSLaYKKNKAII---VKPDSVvfpnGESYGAVQM----KDFLWALGKRLKP-------NSRA-----YENYR 422
Cdd:PRK06112 295 TNQNGTDSWSL-YPEQAQYIhidVDGEEV----GRNYEALRLvgdaRLTLAALTDALRGrdlaaraGRRAalepaIAAGR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 423 RIYIAESSPPESEAGEELRVNVLFKHIQKMLSSNMTVIAETGDS--WFhSQKLKLPKScgyEVQLL----YASIGWSLGA 496
Cdd:PRK06112 370 EAHREDSAPVALSDASPIRPERIMAELQAVLTGDTIVVADASYSsiWV-ANFLTARRA---GMRFLtprgLAGLGWGVPM 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 497 TLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLINNG--GYTIEVE-IHDGPYNIINNW---DYTAFVDA 570
Cdd:PRK06112 446 AIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGFQKHAEtVKFGTHTDACHFaavDHAAIARA 525
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1784872638 571 VnnhqsNCWTTKVHTEEELVNAIEIAMKDRNDCLcfIEVI 610
Cdd:PRK06112 526 C-----GCDGVRVEDPAELAQALAAAMAAPGPTL--IEVI 558
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
85-613 |
3.60e-20 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 94.68 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFvAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK07525 16 LQAHGITHAFGIIGSAFMDASDLF-PPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYWAH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVggPNSndyGSKkilhhTIGLPDFsQE---LRCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEESKPVYISICC 240
Cdd:PRK07525 95 TPVVLVT--PQA---GTK-----TIGQGGF-QEaeqMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRESGPAQINIPR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 241 NL------VAIPHPS-FSAQPliplslspkqsnqmGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGY 313
Cdd:PRK07525 164 DYfygvidVEIPQPVrLERGA--------------GGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 314 AVAVTPSAKGMFPENHPHFIGT--YWGtvSTAfCGETVEIADASIFVGANLDELETV-GYSLAY-KKNKAII---VKPDS 386
Cdd:PRK07525 230 PVACGYLHNDAFPGSHPLWVGPlgYNG--SKA-AMELIAKADVVLALGTRLNPFGTLpQYGIDYwPKDAKIIqvdINPDR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 387 VVFPNGESYGAV-QMKDFLWALGKRLKPNSRAYENY--RRIYIA---------------ESSPPESEAGEELRVNV---- 444
Cdd:PRK07525 307 IGLTKKVSVGICgDAKAVARELLARLAERLAGDAGReeRKALIAaeksaweqelsswdhEDDDPGTDWNEEARARKpdym 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 445 ----LFKHIQK------MLSSNMTVIAETGDSWFhsqKLKLPKScgYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIG 514
Cdd:PRK07525 387 hprqALREIQKalpedaIVSTDIGNNCSIANSYL---RFEKGRK--YLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 515 DGSFQMAPQDVSTmlkLGQKNI-----IFliNNGGYTIE----VEIHDGPY---NIINNWDYTAFVDAVNNHqsncwTTK 582
Cdd:PRK07525 462 DGAWGISMNEVMT---AVRHNWpvtavVF--RNYQWGAEkknqVDFYNNRFvgtELDNNVSYAGIAEAMGAE-----GVV 531
|
570 580 590
....*....|....*....|....*....|..
gi 1784872638 583 VHTEEELVNAIEIAMKDRNDCL-CFIEVIAHR 613
Cdd:PRK07525 532 VDTQEELGPALKRAIDAQNEGKtTVIEIMCNQ 563
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
89-636 |
2.87e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 91.82 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 89 GVSDIFSVPGDSNLVLFDYF---VAEKGLNLVGCCNELNAGYAADGYARSRGV-GACAVTFTVGSLSLINAIAGAYSEDL 164
Cdd:PRK06456 16 GVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGTTNLVTGLITAYWDSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 165 PVICIVGGPNSNDYGSKKILH-HTIGLpdfsqelrcFQNVTCYQAIIDSLEDAQWQIDKAIckcleeskpvYISICCN-- 241
Cdd:PRK06456 96 PVIAITGQVPRSVMGKMAFQEaDAMGV---------FENVTKYVIGIKRIDEIPQWIKNAF----------YIATTGRpg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 242 --LVAIPHPSFSAQ------PLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGY 313
Cdd:PRK06456 157 pvVIDIPRDIFYEKmeeikwPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 314 AVAVTPSAKGMFPENHPHFIGT--YWGTVSTAFCGetVEiADASIFVGANLDELETVGYSLAYKKNKAII---------- 381
Cdd:PRK06456 237 PIVSTFPGKTAIPHDHPLYFGPmgYYGRAEASMAA--LE-SDAMLVVGARFSDRTFTSYDEMVETRKKFImvnidptdge 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 382 --VKPDSVVFPNGESYGAVQMKDFLwALGKRLKPNS--RAYENYRRIYiaeSSPPESEAGEELRVNVLFKHIQKMLSSNM 457
Cdd:PRK06456 314 kaIKVDVGIYGNAKIILRELIKAIT-ELGQKRDRSAwlKRVKEYKEYY---SQFYYTEENGKLKPWKIMKTIRQALPRDA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 458 TVIAETGDS-------WFHSQKLKLPKSCGyevqllYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLK 530
Cdd:PRK06456 390 IVTTGVGQHqmwaevfWEVLEPRTFLTSSG------MGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 531 LGQKNIIFLINNGGYTIEVEIHDGPYN-IINNWDYTAFVDAVNNHQS-NCWTTKVHTEEELVNAIEIAMKDrnDCLCFIE 608
Cdd:PRK06456 464 EHIPVISVIFDNRTLGLVRQVQDLFFGkRIVGVDYGPSPDFVKLAEAfGALGFNVTTYEDIEKSLKSAIKE--DIPAVIR 541
|
570 580
....*....|....*....|....*...
gi 1784872638 609 VIAHRDDTSKELLEFGSRIAAMGSHPPK 636
Cdd:PRK06456 542 VPVDKEELALPTLPPGGRLKQVILRDPR 569
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
68-547 |
6.93e-19 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 90.32 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 68 PPPTTAPSTLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFT 146
Cdd:PRK08199 1 MTSTPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGrPGICFVTRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 147 VGSlslINAIAG---AYSEDLPVICIVGgpnsndygskkilhhTIGLPDFSQElrCFQNVTcYQAIIDSLedAQW--QID 221
Cdd:PRK08199 81 PGA---TNASIGvhtAFQDSTPMILFVG---------------QVARDFRERE--AFQEID-YRRMFGPM--AKWvaEID 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 222 KAickcleESKPVYIS---------------------ICCNLVAIPhpsfSAQPLIPLSLSPKQSnqmglemAVEKAADL 280
Cdd:PRK08199 138 DA------ARIPELVSrafhvatsgrpgpvvlalpedVLSETAEVP----DAPPYRRVAAAPGAA-------DLARLAEL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 281 LNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGA 360
Cdd:PRK08199 201 LARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDL-GLGINPALAARIREADLVLAVGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 361 NLDELETVGYSL---AYKKNKAIIVKPDSVVFpnGESYGAVQ-----MKDFLWALgKRLKPNSR-----AYENYRRIYIA 427
Cdd:PRK08199 280 RLGEVTTQGYTLldiPVPRQTLVHVHPDAEEL--GRVYRPDLaivadPAAFAAAL-AALEPPASpawaeWTAAAHADYLA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 428 ESSPPESEAGeeLRVNVLFKHIQKMLSSN--MTVIAETGDSW---------FHSQklkLPKSCGyevqllyaSIGWSLGA 496
Cdd:PRK08199 357 WSAPLPGPGA--VQLGEVMAWLRERLPADaiITNGAGNYATWlhrffrfrrYRTQ---LAPTSG--------SMGYGLPA 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1784872638 497 TLGYAQAAPHkRLLLCI-GDGSFQMAPQDVSTMLKLGQKNIIFLINNGGY-TI 547
Cdd:PRK08199 424 AIAAKLLFPE-RTVVAFaGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTI 475
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
69-620 |
9.19e-18 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 86.79 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 69 PPTTAPSTLGHYLASRLVEIGVSDIFSVPGDSnlvLFDYfVAEKGLNLVGCCNELNAGYAADGYARS---RGVGACAVTF 145
Cdd:PRK06154 14 PAEAKTMKVAEAVAEILKEEGVELLFGFPVNE---LFDA-AAAAGIRPVIARTERVAVHMADGYARAtsgERVGVFAVQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 146 TVGSLSLINAIAGAYSEDLPVICIVGGPNSndyGSKKILhhtiglPDFSQeLRCFQNVTCYQAIIDSLEDAQWQIDKAIC 225
Cdd:PRK06154 90 GPGAENAFGGVAQAYGDSVPVLFLPTGYPR---GSTDVA------PNFES-LRNYRHITKWCEQVTLPDEVPELMRRAFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 226 KCLEES-KPVYISICCNLVAIPHPSfsaqplIPLSLSPKQSNQMGLE-MAVEKAADLLNTAIKPVMIGGKKLRPAKAEAA 303
Cdd:PRK06154 160 RLRNGRpGPVVLELPVDVLAEELDE------LPLDHRPSRRSRPGADpVEVVEAAALLLAAERPVIYAGQGVLYAQATPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 304 FLELADSCGYAVAVTPSAKGMFPENHPHFIGT----YWGTVsTAFCGEtveiADASIFVGANLDEletVGYSLAYKKNKA 379
Cdd:PRK06154 234 LKELAELLEIPVMTTLNGKSAFPEDHPLALGSggraRPATV-AHFLRE----ADVLFGIGCSLTR---SYYGLPMPEGKT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 380 IIvkpDSVVFPN--GESYGAVQ---------MKDFLWALGKRLKPNSR-------AYENYRRIYIAESSPPESEAGEELR 441
Cdd:PRK06154 306 II---HSTLDDAdlNKDYPIDHglvgdaalvLKQMIEELRRRVGPDRGraqqvaaEIEAVRAAWLAKWMPKLTSDSTPIN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 442 VNVLFKHIQKMLSSNMTVIaeTGDSWFHSQKLklpkSCGYEVQLLYASIGW--------SLGATLGYAQAAPHKrllLCI 513
Cdd:PRK06154 383 PYRVVWELQHAVDIKTVII--THDAGSPRDQL----SPFYVASRPGSYLGWgkttqlgyGLGLAMGAKLARPDA---LVI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 514 ---GDGSFQMAPQDVSTMLKLGQKNIIFLINN---GGYTIEVEIHDGPYNIIN-NWDYTAFVDAVnnhqsNCWTTKVHTE 586
Cdd:PRK06154 454 nlwGDAAFGMTGMDFETAVRERIPILTILLNNfsmGGYDKVMPVSTTKYRATDiSGDYAAIARAL-----GGYGERVEDP 528
|
570 580 590
....*....|....*....|....*....|....*
gi 1784872638 587 EELVNAIEIAM-KDRNDCLCFIEVIahrddTSKEL 620
Cdd:PRK06154 529 EMLVPALLRALrKVKEGTPALLEVI-----TSEET 558
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
89-545 |
3.38e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 85.26 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 89 GVSDIFSVPGDSNLVLFDYfVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSEDLPVI 167
Cdd:PRK08322 15 GVEYIFGIPGEENLDLLEA-LRDSSIKLILTRHEQGAAFMAATYGRLTGkAGVCLSTLGPGATNLVTGVAYAQLGGMPMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 168 CIVG--GPNSndygSKKILHHTIGLpdfsqeLRCFQNVTCYQAIIDSLEDAQWQIDKAIcKCLEESKP--VYISICCNLV 243
Cdd:PRK08322 94 AITGqkPIKR----SKQGSFQIVDV------VAMMAPLTKWTRQIVSPDNIPEVVREAF-RLAEEERPgaVHLELPEDIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 244 AIPHPsfsAQPLiPLSLSPKQsnqMGLEMAVEKAADLLNTAIKPV-MIGGKKLRpAKAEAAFLELADSCGYAVAVTPSAK 322
Cdd:PRK08322 163 AEETD---GKPL-PRSYSRRP---YASPKAIERAAEAIQAAKNPLiLIGAGANR-KTASKALTEFVDKTGIPFFTTQMGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 323 GMFPENHPHFIGTywgtvsTAF-------CGetVEIADASIfvganldeleTVGYSLAYKK--------NKAII------ 381
Cdd:PRK08322 235 GVIPETHPLSLGT------AGLsqgdyvhCA--IEHADLII----------NVGHDVIEKPpffmnpngDKKVIhinflp 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 382 VKPDSVVFPNGESYGavQMKDFLWALGKRLKPNSR----AYENYRRIYIAESSPPESEAGEELRVNVLFKHIQKMLSSNM 457
Cdd:PRK08322 297 AEVDPVYFPQVEVVG--DIANSLWQLKERLADQPHwdfpRFLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 458 TVIAETG--DSWF----HSQKlklPKSCgyevqLL---YASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTM 528
Cdd:PRK08322 375 IVILDNGayKIWFarnyRAYE---PNTC-----LLdnaLATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETA 446
|
490
....*....|....*...
gi 1784872638 529 LKLGQkNIIFLI-NNGGY 545
Cdd:PRK08322 447 VRLGL-PLVVLIlNDNAY 463
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
85-542 |
2.10e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 82.88 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVgCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK06276 11 LEAEGVKIIFGYPGGALLPFYDALYDSDLIHIL-TRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGIATAYADS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGgpnsndygskKILHHTIGLPDFsQE---LRCFQNVT--CYQaiidsLEDAQwQIDKAICKCLEESK-----P 233
Cdd:PRK06276 90 SPVIALTG----------QVPTKLIGNDAF-QEidaLGIFMPITkhNFQ-----IKKPE-EIPEIFRAAFEIAKtgrpgP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 234 VYISICCNLVAIPHPSFSAQPLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGY 313
Cdd:PRK06276 153 VHIDLPKDVQEGELDLEKYPIPAKIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 314 AVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLDElETVGYSLAYKKNKAII---VKPDSVvfp 390
Cdd:PRK06276 233 PVCTTLMGKGAFPEDHPLALGMV-GMHGTKAANYSVTESDVLIAIGCRFSD-RTTGDISSFAPNAKIIhidIDPAEI--- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 391 nGESYGA---------VQMKDFLWALGKR-LKPNSRAYENYRriYIAESSPPESEAGEE-LRVNVLFKHIQKMLS----- 454
Cdd:PRK06276 308 -GKNVRVdvpivgdakNVLRDLLAELMKKeIKNKSEWLERVK--KLKKESIPRMDFDDKpIKPQRVIKELMEVLReidps 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 455 SNMTVIAETGDS--WF-HSQKLKLPKSCGYEVQLlyASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKL 531
Cdd:PRK06276 385 KNTIITTDVGQNqmWMaHFFKTSAPRSFISSGGL--GTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEY 462
|
490
....*....|.
gi 1784872638 532 GQKNIIFLINN 542
Cdd:PRK06276 463 DIPVVICIFDN 473
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
76-545 |
4.19e-16 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 81.56 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYfVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLIN 154
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGVHTVELYRG-LAGSGIRHVTPRHEQGAGFMADGYARVSGkPGVCFIITGPGMTNIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 155 AIAGAYSEDLPVICIVGGPNSNDYGSKK-ILHHtigLPDfsqELRCFQNVTCYQAIIDSLEDAQWQIDKAICKCL-EESK 232
Cdd:PRK07524 82 AMGQAYADSIPMLVISSVNRRASLGKGRgKLHE---LPD---QRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDsARPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 233 PVYISICCNLVAIPHPSFSAQPLIPLSLSPKQSNqmglemAVEKAADLLNTAIKPVMI-GGKKLRpakAEAAFLELADSC 311
Cdd:PRK07524 156 PVHIEIPLDVLAAPADHLLPAPPTRPARPGPAPA------ALAQAAERLAAARRPLILaGGGALA---AAAALRALAERL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 312 GYAVAVTPSAKGMFPENHPHFIGtywGTVSTAFCGETVEIADASIFVGANLDELETVGYSLA-YKKNKAII---VKPDSV 387
Cdd:PRK07524 227 DAPVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLAVGTELGETDYDVYFDGgFPLPGELIridIDPDQL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 388 V-----------------------FPNGES---YGAVQMKDFLWALGKRLKPNSRAyenYRRIY--IAESSPPESEAGEE 439
Cdd:PRK07524 304 ArnyppalalvgdaraaleallarLPGQAAaadWGAARVAALRQALRAEWDPLTAA---QVALLdtILAALPDAIFVGDS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 440 lrvnvlfkhIQKMLSSNMTVIAETGDSWFHSqklklpkSCGyevqllYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQ 519
Cdd:PRK07524 381 ---------TQPVYAGNLYFDADAPRRWFNA-------STG------YGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQ 438
|
490 500
....*....|....*....|....*.
gi 1784872638 520 MAPQDVSTMLKLGQKNIIFLINNGGY 545
Cdd:PRK07524 439 FTLPELASAVEADLPLIVLLWNNDGY 464
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
445-611 |
6.45e-15 |
|
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: 72.67 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 445 LFKHIQKMLSSNMTVIAETGDS--WFHSQkLKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAP 522
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSayWAYRY-LPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 523 QDVSTMLKLGQKNIIFLINNGGYTIEVEIHDGPYNI------INNWDYTAFVDAVnnhqsNCWTTKVHTEEELVNAIEIA 596
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGrvsgtdLSNPDFAALAEAY-----GAKGVRVEDPEDLEAALAEA 155
|
170
....*....|....*
gi 1784872638 597 MKDrnDCLCFIEVIA 611
Cdd:cd00568 156 LAA--GGPALIEVKT 168
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
76-557 |
6.92e-15 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 77.72 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRGVGACAVTFT-------VG 148
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTgtgagnaAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 149 slSLINAI-AGAysedlPVICIVGGPNSNDYGSKK-ILHHTiglPDfsqELRCFQNVTCYQAIIDSLEDAQWQIDKAICK 226
Cdd:PRK07064 84 --ALVEALtAGT-----PLLHITGQIETPYLDQDLgYIHEA---PD---QLTMLRAVSKAAFRVRSAETALATIREAVRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 227 CLEE-SKPVYISICCNLVA--IPHPSfSAQPLIPLSLSPKQSnqmglemAVEKAADLLNTAIKPVM-IGGKKLRPAKAEA 302
Cdd:PRK07064 151 ALTApTGPVSVEIPIDIQAaeIELPD-DLAPVHVAVPEPDAA-------AVAELAERLAAARRPLLwLGGGARHAGAEVK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 303 AFLELadscGYAVAVTPSAKGMFPENHPHFIGTYWGTVSTAfcgETVEIADASIFVGANLDELETVGYSLAYKKNkaiIV 382
Cdd:PRK07064 223 RLVDL----GFGVVTSTQGRGVVPEDHPASLGAFNNSAAVE---ALYKTCDLLLVVGSRLRGNETLKYSLALPRP---LI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 383 KPD-----------SVVFPNGESygavqmKDFLWALGKRLKPNSRAYENyrriYIAESSPPESEAGEELR-----VNVLF 446
Cdd:PRK07064 293 RVDadaaadgrgypNDLFVHGDA------ARVLARLADRLEGRLSVDPA----FAADLRAAREAAVADLRkglgpYAKLV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 447 KHIQKMLSSNMTV---IAETGDSWFHSQ-KLKLPKScgyEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAP 522
Cdd:PRK07064 363 DALRAALPRDGNWvrdVTISNSTWGNRLlPIFEPRA---NVHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNL 439
|
490 500 510
....*....|....*....|....*....|....*
gi 1784872638 523 QDVSTMLKLGQKNIIFLINNGGYTIEVEIHDGPYN 557
Cdd:PRK07064 440 GELATAVQENANMVIVLMNDGGYGVIRNIQDAQYG 474
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
62-364 |
2.64e-14 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 76.17 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 62 SPLVIVPPPTTAPS--TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-V 138
Cdd:PRK07789 16 PAAPAARPRIVAPErmTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGrV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 139 GACAVTFTVGSLSLINAIAGAYSEDLPVICIVGGPNSNDYGSKkilhhtiglpdfsqelrCFQN---------VTCYQAI 209
Cdd:PRK07789 96 GVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTD-----------------AFQEadivgitmpITKHNFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 210 IDSLEDaqwqIDKAICKCLEESK-----PVyisiccnLVAIPHP------SFSAQPLIPLS-----LSP--KQsnqmgle 271
Cdd:PRK07789 159 VTDADD----IPRVIAEAFHIAStgrpgPV-------LVDIPKDalqaqtTFSWPPRMDLPgyrpvTKPhgKQ------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 272 maVEKAADLLNTAIKPVM-IGGKKLRpAKAEAAFLELADSCGYAVAVTPSAKGMFPENHPHFIGT--YWGTVS--TAfcg 346
Cdd:PRK07789 221 --IREAAKLIAAARRPVLyVGGGVIR-AEASAELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgMHGTVAavAA--- 294
|
330
....*....|....*...
gi 1784872638 347 etVEIADASIFVGANLDE 364
Cdd:PRK07789 295 --LQRSDLLIALGARFDD 310
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
76-238 |
2.65e-14 |
|
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: 71.04 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLIN 154
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 155 AIAGAYSEDLPVICIVGGPNSNDYGSkkilhhtiglpDFSQE---LRCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEES 231
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGT-----------DYFQEvdlLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR 149
|
....*..
gi 1784872638 232 KPVYISI 238
Cdd:cd07039 150 GVAVLIL 156
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
85-543 |
6.91e-14 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 74.74 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFD--YFVAEKGL-NLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAY 160
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDelYAWEKKGLiKHILVRHEQGAAHAADGYARSTGkVGVCFATSGPGATNLVTGIATAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 161 SEDLPVICIVGgpnsndygskKILHHTIGLPDFsQELRCFqNVTCyqAIIDS---LEDAqwqidKAICKCLEESkpvyIS 237
Cdd:CHL00099 100 MDSVPLLVITG----------QVGRAFIGTDAF-QEVDIF-GITL--PIVKHsyvVRDA-----RDISRIVAEA----FY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 238 ICCN------LVAIP----------HPSFSAQPLIPLS----LSPKQSNQmglemaVEKAADLLNTAIKPVM-IGGKKLr 296
Cdd:CHL00099 157 IAKHgrpgpvLIDIPkdvglekfdyYPPEPGNTIIKILgcrpIYKPTIKR------IEQAAKLILQSSQPLLyVGGGAI- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 297 PAKAEAAFLELADSCGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLDELETvGYSLAYKK 376
Cdd:CHL00099 230 ISDAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCLGML-GMHGTAYANFAVSECDLLIALGARFDDRVT-GKLDEFAC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 377 NKAII---VKPDSV---VFPNGESYGAVqmKDFLWALGKRLKPNSRAYEN------YRRIYIAESSPPeseageelrvnV 444
Cdd:CHL00099 308 NAQVIhidIDPAEIgknRIPQVAIVGDV--KKVLQELLELLKNSPNLLESeqtqawRERINRWRKEYP-----------L 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 445 LFKHIQKMLSSNmTVIAETG----DSWF------H----SQKLK-LPK----SCGyevqllYASIGWSLGATLGyAQAAP 505
Cdd:CHL00099 375 LIPKPSTSLSPQ-EVINEISqlapDAYFttdvgqHqmwaAQFLKcKPRkwlsSAG------LGTMGYGLPAAIG-AQIAH 446
|
490 500 510
....*....|....*....|....*....|....*....
gi 1784872638 506 HKRLLLCI-GDGSFQMAPQDVSTMLKLGQKNIIFLINNG 543
Cdd:CHL00099 447 PNELVICIsGDASFQMNLQELGTIAQYNLPIKIIIINNK 485
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
78-542 |
9.94e-14 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 74.36 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 78 GHYLASRLVE-IGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRGVGA-CAVTFTVGSLSLINA 155
Cdd:PRK08155 15 GAELIVRLLErQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAvCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 156 IAGAYSEDLPVICIVGG-PNS----------NDYG-SKKILHHTIGLPDFSQELrcfqnvtcyQAIIDSLEDAQwqidka 223
Cdd:PRK08155 95 IADARLDSIPLVCITGQvPASmigtdafqevDTYGiSIPITKHNYLVRDIEELP---------QVISDAFRIAQ------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 224 ickcLEESKPVYISI-------CCNLVAIPHPsfsAQPLIPLSLSPKqsnqmglemAVEKAADLLNTAIKPVM-IGGKKL 295
Cdd:PRK08155 160 ----SGRPGPVWIDIpkdvqtaVIELEALPAP---AEKDAAPAFDEE---------SIRDAAAMINAAKRPVLyLGGGVI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 296 RPAKAEAAfLELADSCGYAVAVTPSAKGMFPENHPHFIGT--YWGTVSTAFcgeTVEIADASIFVGANLDElETVGYSLA 373
Cdd:PRK08155 224 NSGAPARA-RELAEKAQLPTTMTLMALGMLPKAHPLSLGMlgMHGARSTNY---ILQEADLLIVLGARFDD-RAIGKTEQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 374 YKKNKAII---VKP---DSVVFPNGESYGAVqmKDFLWALGKRLKPNSRA-----YENYRRIY---IAESSPPESEAGee 439
Cdd:PRK08155 299 FCPNAKIIhvdIDRaelGKIKQPHVAIQADV--DDVLAQLLPLVEAQPRAewhqlVADLQREFpcpIPKADDPLSHYG-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 440 lrvnvLFKHIQKMLSSNMTVIAETGDS--WF-HSQKLKLPKscgyevQLL----YASIGWSLGATLGYAQAAPHKRLLLC 512
Cdd:PRK08155 375 -----LINAVAACVDDNAIITTDVGQHqmWTaQAYPLNRPR------QWLtsggLGTMGFGLPAAIGAALANPERKVLCF 443
|
490 500 510
....*....|....*....|....*....|
gi 1784872638 513 IGDGSFQMAPQDVSTMLKLGQKNIIFLINN 542
Cdd:PRK08155 444 SGDGSLMMNIQEMATAAENQLDVKIILMNN 473
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
62-543 |
2.19e-13 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 73.16 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 62 SPLVIVPPPTTAPS--TLGHYLASRLVEIGVSDIFSVPGDSNLVLFD--YFVAEKG-LNLVGCCNELNAGYAADGYARSR 136
Cdd:PRK07418 4 SPPKIGDSTTVTPQraTGAYALMDSLKRHGVKHIFGYPGGAILPIYDelYKAEAEGwLKHILVRHEQGAAHAADGYARAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 137 G-VGACAVTFTVGSLSLINAIAGAYSEDLPVICIVGgpnsndygskKILHHTIGLPDFsQELRCFqnvtcyqAIIDSLED 215
Cdd:PRK07418 84 GkVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITG----------QVPRPAIGTDAF-QETDIF-------GITLPIVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 216 AQWQIDKA--ICKCLEES---------KPVyisiccnLVAIP----HPSFSAQPLIPLSLSPK--QSNQMGLEMAVEKAA 278
Cdd:PRK07418 146 HSYVVRDPsdMARIVAEAfhiassgrpGPV-------LIDIPkdvgQEEFDYVPVEPGSVKPPgyRPTVKGNPRQINAAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 279 DLLNTAIKPVM-IGGKKLrPAKAEAAFLELADSCGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIF 357
Cdd:PRK07418 219 KLIEEAERPLLyVGGGAI-SAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGML-GMHGTAYANFAVTECDLLIA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 358 VGANLDE-----LET----------------VGyslaykKNKAiivkPDSVVFpngesyGAVQ--MKDFL-WALGKRLKP 413
Cdd:PRK07418 297 VGARFDDrvtgkLDEfasrakvihididpaeVG------KNRR----PDVPIV------GDVRkvLVKLLeRSLEPTTPP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 414 NSRAY----ENYRRIYIAESSPPESE-AGEELRVNVlfkhiqKMLSSNMTVIAETGDS--WfHSQKLK-LPK----SCGy 481
Cdd:PRK07418 361 RTQAWleriNRWKQDYPLVVPPYEGEiYPQEVLLAV------RDLAPDAYYTTDVGQHqmW-AAQFLRnGPRrwisSAG- 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1784872638 482 evqllYASIGWSLGATLGyAQAAPHKRLLLCI-GDGSFQMAPQDVSTMLKLGQKNIIFLINNG 543
Cdd:PRK07418 433 -----LGTMGFGMPAAMG-VKVALPDEEVICIaGDASFLMNIQELGTLAQYGINVKTVIINNG 489
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
85-543 |
2.36e-13 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 72.89 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYfVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK06048 18 LEKEGVEVIFGYPGGAIIPVYDE-LYDSDLRHILVRHEQAAAHAADGYARATGkVGVCVATSGPGATNLVTGIATAYMDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGGPNSNDYGSkkilhhtiglpDFSQElrcfQNVTCYQAIIDS----LEDAqwqidKAICKCLEES-------- 231
Cdd:PRK06048 97 VPIVALTGQVPRSMIGN-----------DAFQE----ADITGITMPITKhnylVQDA-----KDLPRIIKEAfhiastgr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 232 -KPVYISICCNlVAIPHPSFSAQPLIPL-SLSPKQSnqmGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELAD 309
Cdd:PRK06048 157 pGPVLIDLPKD-VTTAEIDFDYPDKVELrGYKPTYK---GNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 310 SCGYAVAVTPSAKGMFPENHPHFIGtYWGTVSTAFCGETVEIADASIFVGANLDElETVGYSLAYKKNKAII-------- 381
Cdd:PRK06048 233 TIPAPVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDD-RVTGKLASFAPNAKIIhididpae 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 382 ----VKPDSVVFPNGesygavqmKDFLWALGKRLKPNSRAyENYRRIYIAESSPPESEAGEELRVNVLFKhIQKM--LSS 455
Cdd:PRK06048 311 isknVKVDVPIVGDA--------KQVLKSLIKYVQYCDRK-EWLDKINQWKKEYPLKYKEREDVIKPQYV-IEQIyeLCP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 456 NMTVIAETGDS--WfHSQKLKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQ 533
Cdd:PRK06048 381 DAIIVTEVGQHqmW-AAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDI 459
|
490
....*....|
gi 1784872638 534 KNIIFLINNG 543
Cdd:PRK06048 460 PVIVAILNNG 469
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
85-543 |
6.48e-13 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 71.70 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK06466 14 LRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGkTGVVLVTSGPGATNAITGIATAYMDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGGPNSNDYG------------SKKILHHTIGLPDFSQelrcfqnvtcyqaIIDSLEDAQWqidkaickcLEES 231
Cdd:PRK06466 94 IPMVVLSGQVPSTLIGedafqetdmvgiSRPIVKHSFMVKHASE-------------IPEIIKKAFY---------IAQS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 232 ---KPVYISICCNLVAiPHPSFSAQPLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELA 308
Cdd:PRK06466 152 grpGPVVVDIPKDMTN-PAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 309 DSCGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLDELETVGYSlAYKKNKAII---VKPD 385
Cdd:PRK06466 231 HLLNLPVTNTLMGLGGFPGTDRQFLGML-GMHGTYEANMAMHHADVILAVGARFDDRVTNGPA-KFCPNAKIIhidIDPA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 386 SV---VFPNGESYGAVQ-----MKDFLWALGKRLKPNSRA--------YENYRRIYiaessPPESEAGEELRVNVLFKHI 449
Cdd:PRK06466 309 SIsktIKADIPIVGPVEsvlteMLAILKEIGEKPDKEALAawwkqideWRGRHGLF-----PYDKGDGGIIKPQQVVETL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 450 QKMLSSNMTVIAETGD-SWFHSQKLKLPK------SCGyevqllYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAP 522
Cdd:PRK06466 384 YEVTNGDAYVTSDVGQhQMFAAQYYKFNKpnrwinSGG------LGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNI 457
|
490 500
....*....|....*....|.
gi 1784872638 523 QDVSTMLKLGQKNIIFLINNG 543
Cdd:PRK06466 458 QELSTCLQYGLPVKIINLNNG 478
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
89-542 |
1.10e-12 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 70.71 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 89 GVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSEDLPVI 167
Cdd:PRK06882 18 GVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGIATAYTDSVPLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 168 CIVGGPNSNDYGSKKILH-HTIGLPdfsqelrcfQNVTCYQAIIDSLEDAQWQIDKAI-CKCLEESKPVYISICCNLVAi 245
Cdd:PRK06882 98 ILSGQVPSNLIGTDAFQEcDMLGIS---------RPVVKHSFIVKNAEDIPSTIKKAFyIASTGRPGPVVIDIPKDMVN- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 246 PHPSFSAQPLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVAVTPSAKGMF 325
Cdd:PRK06882 168 PANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMGLGAY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 326 PENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLDELETVGYSlAYKKNKAII---VKPDSV---VFPNGESYGAVQ 399
Cdd:PRK06882 248 PSTDKQFLGML-GMHGTYEANNAMHESDLILGIGVRFDDRTTNNLA-KYCPNAKVIhidIDPTSIsknVPAYIPIVGSAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 400 --MKDFLWALGKR--LKPNSRAYENYRRI--YIAESSPPESEAGEELRVNVLFKHIQKMLSSNMTVIAETGD-SWFHSQK 472
Cdd:PRK06882 326 nvLEEFLSLLEEEnlAKSQTDLTAWWQQIneWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQhQMFAALH 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 473 LKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLINN 542
Cdd:PRK06882 406 YPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
76-545 |
1.39e-12 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 70.41 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 76 TLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFVA--EKGLNL---VGCCNELNAGYAADGYARSRG-VGACAVTFTVGS 149
Cdd:PRK08327 8 TAAELFLELLKELGVDYIFINSGTDYPPIIEAKARarAAGRPLpefVICPHEIVAISMAHGYALVTGkPQAVMVHVDVGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 150 LSLINAIAGAYSEDLPVICIVG-GPNSND--YGSKKILHHtiglpdFSQELR----CFQNVTCYQAIIDSLEDAQWQIDK 222
Cdd:PRK08327 88 ANALGGVHNAARSRIPVLVFAGrSPYTEEgeLGSRNTRIH------WTQEMRdqggLVREYVKWDYEIRRGDQIGEVVAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 223 AI-CKCLEESKPVYISICCNLVAIPHPSFSAQPLIPLSLSPKQsnqmGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAE 301
Cdd:PRK08327 162 AIqIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPA----PDPEDIARAAEMLAAAERPVIITWRAGRTAEGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 302 AAFLELADSCGYAVaVTPSAKGM-FPENHPHFIGtywgtvstAFCGETVEIADASIFVGANLDELETVgysLAYKKNKAI 380
Cdd:PRK08327 238 ASLRRLAEELAIPV-VEYAGEVVnYPSDHPLHLG--------PDPRADLAEADLVLVVDSDVPWIPKK---IRPDADARV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 381 I-VKPDSVV-------FPnGESYGAVQMKDFLWALGKRLKP---NSRAYENYRRIYIAESSPPESEA----------GEE 439
Cdd:PRK08327 306 IqIDVDPLKsriplwgFP-CDLCIQADTSTALDQLEERLKSlasAERRRARRRRAAVRELRIRQEAAkraeierlkdRGP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 440 LRVNVLFKHIQKMLSSNMTVIAETGdswFHSQKLKLPKSCGYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQ 519
Cdd:PRK08327 385 ITPAYLSYCLGEVADEYDAIVTEYP---FVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFI 461
|
490 500
....*....|....*....|....*...
gi 1784872638 520 MAPQDVSTMLKLGQKNIIFLI--NNGGY 545
Cdd:PRK08327 462 FGVPEAAHWVAERYGLPVLVVvfNNGGW 489
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
85-334 |
1.02e-11 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 67.92 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK08979 14 LIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYMDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGGPNSNDYGSkkilhhtiglpDFSQE---LRCFQNVTCYQAIIDSLEDAQWQIDKAI-CKCLEESKPVYISI- 238
Cdd:PRK08979 94 IPMVVLSGQVPSNLIGN-----------DAFQEcdmIGISRPVVKHSFLVKDAEDIPEIIKKAFyIASTGRPGPVVIDLp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 239 --CCNlVAIPHPSFSAQPLIPLSLSPKQSNQMGlemAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVA 316
Cdd:PRK08979 163 kdCLN-PAILHPYEYPESIKMRSYNPTTSGHKG---QIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVV 238
|
250
....*....|....*...
gi 1784872638 317 VTPSAKGMFPENHPHFIG 334
Cdd:PRK08979 239 STLMGLGAFPGTHKNSLG 256
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
487-609 |
9.85e-11 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 60.29 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 487 YASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLINNGGYTI----EVEIHDGPY-----N 557
Cdd:pfam02775 27 LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGYGMtrgqQTPFGGGRYsgpsgK 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1784872638 558 IINNWDYTAFVDAVnnhqsNCWTTKVHTEEELVNAIEIAMKdrNDCLCFIEV 609
Cdd:pfam02775 107 ILPPVDFAKLAEAY-----GAKGARVESPEELEEALKEALE--HDGPALIDV 151
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
81-364 |
1.11e-10 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 64.44 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 81 LASRLVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGA 159
Cdd:PRK06965 27 LMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVALVTSGPGVTNAVTGIATA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 160 YSEDLPVICIVGgpnsndygskKILHHTIGLPDFsQELRCF---QNVTCYQAIIDSLEDAQWQIDKA--ICKClEESKPV 234
Cdd:PRK06965 107 YMDSIPMVVISG----------QVPTAAIGQDAF-QECDTVgitRPIVKHNFLVKDVRDLAETVKKAfyIART-GRPGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 235 yisiccnLVAIPHP-SFSAQPL-IPLSLSPKQSN--QMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADS 310
Cdd:PRK06965 175 -------VVDIPKDvSKTPCEYeYPKSVEMRSYNpvTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADL 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1784872638 311 CGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLDE 364
Cdd:PRK06965 248 LGYPVTNTLMGLGAYPASDKKFLGML-GMHGTYEANMAMQHCDVLIAIGARFDD 300
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
89-363 |
6.83e-10 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 61.82 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 89 GVSDIFSVPGDSNLVLFDYFVaEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSEDLPVI 167
Cdd:PRK08978 15 GVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGkVGVCIATSGPGATNLITGLADALLDSVPVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 168 CIVGGPNSndygskkilhHTIGLPDFsQE-------LRCfqnvTCYQAIIDSLEDAQWQIDKAIckCLEESK---PVyis 237
Cdd:PRK08978 94 AITGQVSS----------PLIGTDAF-QEidvlglsLAC----TKHSFLVQSLEELPEIMAEAF--EIASSGrpgPV--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 238 iccnLVAIPHPSFSAQPLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVAV 317
Cdd:PRK08978 154 ----LVDIPKDIQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1784872638 318 TPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLD 363
Cdd:PRK08978 230 TLKGLGAVEADHPYYLGML-GMHGTKAANLAVQECDLLIAVGARFD 274
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
85-542 |
8.69e-10 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 61.79 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK07979 14 LIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGgpnsndygskKILHHTIGLPDFsQELRCF---QNVTCYQAIIDSLEDAQWQIDKAI-CKCLEESKPVYISIC 239
Cdd:PRK07979 94 IPLVVLSG----------QVATSLIGYDAF-QECDMVgisRPVVKHSFLVKQTEDIPQVLKKAFwLAASGRPGPVVVDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 240 CNLVaipHPSFSAQPLIPLSLSPKQSNQM--GLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVAV 317
Cdd:PRK07979 163 KDIL---NPANKLPYVWPESVSMRSYNPTtqGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 318 TPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGANLDELETvgYSLA-YKKNKAII---VKPDSV------ 387
Cdd:PRK07979 240 SLMGLGAFPATHRQSLGML-GMHGTYEANMTMHNADVIFAVGVRFDDRTT--NNLAkYCPNATVLhidIDPTSIsktvta 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 388 -VFPNGESYGAV-QMKDFLWALGKRLKPNS-----RAYENYRriyiAESSPPESEAGEELRVNVLFKHIQKMLSSNMTVI 460
Cdd:PRK07979 317 dIPIVGDARQVLeQMLELLSQESAHQPLDEirdwwQQIEQWR----ARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 461 AETGD---------------SWFHSQKLklpkscgyevqllyASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDV 525
Cdd:PRK07979 393 SDVGQhqmfaalyypfdkprRWINSGGL--------------GTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQEL 458
|
490
....*....|....*..
gi 1784872638 526 STMLKLGQKNIIFLINN 542
Cdd:PRK07979 459 STALQYELPVLVLNLNN 475
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
480-545 |
2.65e-09 |
|
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: 57.32 E-value: 2.65e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1784872638 480 GYEVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLINNGGY 545
Cdd:cd02003 40 GYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGF 105
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
440-547 |
3.30e-09 |
|
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: 56.45 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 440 LRVNVLFKHIQKMLSSNMTVIAE---TGDSWFHSQKLKLPKScgYeVQLLYASIGWSLGATLGYAQAAPHKRLLLCIGDG 516
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEavtNGLPLRDQLPLTRPGS--Y-FTLRGGGLGWGLPAAVGAALANPDRKVVAIIGDG 77
|
90 100 110
....*....|....*....|....*....|...
gi 1784872638 517 SFQMAPQDVSTM--LKLGQKNIIFliNNGGYTI 547
Cdd:cd02002 78 SFMYTIQALWTAarYGLPVTVVIL--NNRGYGA 108
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
85-613 |
4.84e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 59.34 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK08527 13 LKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTNAVTGLATAYMDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGG-PNSndygskkilhhTIGLPDFsQELRCF---QNVTCYQAIIDSLEDaqwqidkaICKCLEES-------- 231
Cdd:PRK08527 93 IPLVLISGQvPNS-----------LIGTDAF-QEIDAVgisRPCVKHNYLVKSIEE--------LPRILKEAfyiarsgr 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 232 -KPVYISICCNL-VAIPHPSFSAQplipLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVM-IGGKKLRPAKAEAAfLELA 308
Cdd:PRK08527 153 pGPVHIDIPKDVtATLGEFEYPKE----ISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFyLGGGAILSNASEEI-RELV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 309 DSCGYAVAVTPSAKGMFPENHPHFI------GTYWGTVSTAFCgetveiaDASIFVGANLDELETvGYSLAYKKNKAII- 381
Cdd:PRK08527 228 KKTGIPAVETLMARGVLRSDDPLLLgmlgmhGSYAANMAMSEC-------DLLISLGARFDDRVT-GKLSEFAKHAKIIh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 382 --VKPDSVVFPNGESYGAV-QMKDFLWALGKRLKP-NSRAYENYRRI---YiAESSPPESEAGEE-LRVNVLFKHIQKML 453
Cdd:PRK08527 300 vdIDPSSISKIVNADYPIVgDLKNVLKEMLEELKEeNPTTYKEWREIlkrY-NELHPLSYEDSDEvLKPQWVIERVGELL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 454 SSNMTVIAETGDSWFHSQKLkLPKScgYEVQLLYA----SIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTML 529
Cdd:PRK08527 379 GDDAIISTDVGQHQMWVAQF-YPFN--YPRQLATSgglgTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 530 KLGQKNIIFLINNgGYTIEVE-----IHDGPYniiNNWDYTAFVDAVNNHQS-NCWTTKVHTEEELVNAIEIAMKdrNDC 603
Cdd:PRK08527 456 EYKIPVINIILNN-NFLGMVRqwqtfFYEERY---SETDLSTQPDFVKLAESfGGIGFRVTTKEEFDKALKEALE--SDK 529
|
570
....*....|
gi 1784872638 604 LCFIEVIAHR 613
Cdd:PRK08527 530 VALIDVKIDR 539
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
85-360 |
1.16e-08 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 57.92 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKgLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK06457 12 LEDNGIQRIYGIPGDSIDPLVDAIRKSK-VKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLLNGLYDAKMDH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 164 LPVICIVGGPNSNdygskkILHHtiglpDFSQEL---RCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEESKPVYISICC 240
Cdd:PRK06457 91 APVIALTGQVESD------MIGH-----DYFQEVnltKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHINLPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 241 NLV------------AIPHPSFSAQPliplslspkqsnqmglemavEKAADLLNTAIKPVMIGGKKLRPAKAEaaFLELA 308
Cdd:PRK06457 160 DILrksseykgskntEVGKVKYSIDF--------------------SRAKELIKESEKPVLLIGGGTRGLGKE--INRFA 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1784872638 309 DSCGYAVAVTPSAKGMFPENHPHFIGTYwGTVSTAFCGETVEIADASIFVGA 360
Cdd:PRK06457 218 EKIGAPIIYTLNGKGILPDLDPKVMGGI-GLLGTKPSIEAMDKADLLIMLGT 268
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
445-610 |
1.53e-07 |
|
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: 51.76 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 445 LFKHIQKMLSSNMTVIAETGD------SWFHSQKLKLPKSCGYevqllYASIGWSLGATLGYAQAAPHKRLLLCIGDGSF 518
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNtmdwarYILRPRKPRHRLDAGT-----FGTLGVGLGYAIAAALARPDKRVVLVEGDGAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 519 QMAPQDVSTMLKLGQKNIIFLINNGGYTIEVEIHDGPYNIINNW-------DYTAFVDAVNNHqsncwTTKVHTEEELVN 591
Cdd:cd02004 79 GFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVttllpdtRYDLVAEAFGGK-----GELVTTPEELKP 153
|
170
....*....|....*....
gi 1784872638 592 AIEIAMKDRNDCLcfIEVI 610
Cdd:cd02004 154 ALKRALASGKPAL--INVI 170
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
85-171 |
2.63e-07 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 53.56 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEIGVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGAYSED 163
Cdd:PRK09107 21 LKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGATNAVTPLQDALMDS 100
|
....*...
gi 1784872638 164 LPVICIVG 171
Cdd:PRK09107 101 IPLVCITG 108
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
75-335 |
9.26e-07 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 51.83 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 75 STLGHYLASRLVEIGVSDIFSVPGDSNLVLFDYFV-AEKGLNLVGCCNELNAGYAADGYAR-SRGVGACAVTFTVGSLSL 152
Cdd:PRK08273 3 QTVADFILERLREWGVRRVFGYPGDGINGLLGALGrADDKPEFVQARHEEMAAFMAVAHAKfTGEVGVCLATSGPGAIHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 153 INAIAGAYSEDLPVICIVGGPNSNDYGSkkilhhtiglpDFSQEL---RCFQNVTC-YQAIIDSLEDAQWQIDKAICKCL 228
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVGQQARAALGG-----------HYQQEVdlqSLFKDVAGaFVQMVTVPEQLRHLVDRAVRTAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 229 EESKPvyisiCCnlVAIPHP----SFSAQP----LIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKA 300
Cdd:PRK08273 152 AERTV-----TA--VILPNDvqelEYEPPPhahgTVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATD 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1784872638 301 EaaFLELADSCGYAVAVTPSAKGMFPENHPHFIGT 335
Cdd:PRK08273 225 E--VIAVAERLGAGVAKALLGKAALPDDLPWVTGS 257
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
491-543 |
4.68e-06 |
|
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: 47.49 E-value: 4.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1784872638 491 GWSLGATLGyAQAAPHKRLLLCI-GDGSFQMAPQDVSTMLKLGQKNIIFLINNG 543
Cdd:cd02015 53 GFGLPAAIG-AKVARPDKTVICIdGDGSFQMNIQELATAAQYNLPVKIVILNNG 105
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
85-542 |
9.00e-06 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 48.58 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 85 LVEI----GVSDIFSVPGDSNLVLFDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLINAIAGA 159
Cdd:PLN02470 19 LVEAlereGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGkVGVCIATSGPGATNLVTGLADA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 160 YSEDLPVICIVGgpnsndygskKILHHTIGLPDFsQE---LRCFQNVTCYQAIIDSLEDAQWQIDKAIckCLEES---KP 233
Cdd:PLN02470 99 LLDSVPLVAITG----------QVPRRMIGTDAF-QEtpiVEVTRSITKHNYLVMDVEDIPRVIREAF--FLASSgrpGP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 234 VYISICCNL---VAIPHPSfsaQPL-IPLSLS--PKQSNQMGLEMAVekaaDLLNTAIKPVM-IGGKKLRPAKAEAAFLE 306
Cdd:PLN02470 166 VLVDIPKDIqqqLAVPNWN---QPMkLPGYLSrlPKPPEKSQLEQIV----RLISESKRPVVyVGGGCLNSSEELREFVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 307 LAdscGYAVAVTPSAKGMFP---ENHPHFIGTYwGTVSTAFcgeTVEIADASIFVGANLDELETvGYSLAYKKNKAII-V 382
Cdd:PLN02470 239 LT---GIPVASTLMGLGAFPasdELSLQMLGMH-GTVYANY---AVDSADLLLAFGVRFDDRVT-GKLEAFASRASIVhI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 383 KPDSV-VFPNGESYGAV--QMKDFLWALGKRLKPNSRAYENYR--RIYIAESSP--PES--EAGEELRVNVLFKHIQKML 453
Cdd:PLN02470 311 DIDPAeIGKNKQPHVSVcaDVKLALQGLNKLLEERKAKRPDFSawRAELDEQKEkfPLSypTFGDAIPPQYAIQVLDELT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 454 SSNmtVIAETG--------DSWFhsqKLKLPK----SCGyevqllYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMA 521
Cdd:PLN02470 391 DGN--AIISTGvgqhqmwaAQWY---KYKEPRrwltSGG------LGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMN 459
|
490 500
....*....|....*....|...
gi 1784872638 522 PQDVSTML--KLGQKniIFLINN 542
Cdd:PLN02470 460 IQELATIHveNLPVK--IMVLNN 480
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
273-378 |
4.26e-05 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 46.52 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 273 AVEKAADLLNTAIKPVMIGGKKLRPAKAEAAFLELADSCGYAVAVTPSAKGMFPENHPHfigtywgtvSTAFCGETV-EI 351
Cdd:PRK09259 202 AVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQ---------SAAAARSLAlAN 272
|
90 100
....*....|....*....|....*..
gi 1784872638 352 ADASIFVGANLDELetvgysLAYKKNK 378
Cdd:PRK09259 273 ADVVLLVGARLNWL------LSHGKGK 293
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
81-309 |
3.10e-04 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 43.82 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 81 LASRLVEI----GVSDIFSVPGDS-NLVLfDYFVAEKGLNLVGCCNELNAGYAADGYARSRG-VGACAVTFTVGSLSLIN 154
Cdd:PRK06546 5 VAEQLVEQlvaaGVKRIYGIVGDSlNPIV-DAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGkLAVCAGSCGPGNLHLIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 155 AIAGAYSEDLPVICIVGGPNSNDYGSKkilhhtiglpdFSQEL---RCFQNVTCYQAIIDSLEDAQWQIDKAICKCLEES 231
Cdd:PRK06546 84 GLYDAHRSGAPVLAIASHIPSAQIGSG-----------FFQEThpdRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1784872638 232 KPVYISICCNLVAIPhpsfSAQPLIPLSLSPKQSNQMGLEMAVEKAADLLNTAIKPVMIGGKKLRPAKAEAafLELAD 309
Cdd:PRK06546 153 GVSVVTLPGDIADEP----APEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAEV--LALAE 224
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
488-545 |
1.53e-03 |
|
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: 39.96 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1784872638 488 ASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLINNGGY 545
Cdd:cd02010 48 ATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGY 105
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
489-547 |
2.01e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 39.81 E-value: 2.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 489 SIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTMLKLGQKNIIFLI-NNGGYTI 547
Cdd:PRK06163 58 SMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVmDNGVYQI 117
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
484-547 |
5.10e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 39.83 E-value: 5.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1784872638 484 QLLYASIGWSLGATLGYAQAAPHKRLLLCIGDGSFQMAPQDVSTML--KLGQKNIIFliNNGGYTI 547
Cdd:PRK07586 381 TLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQAreNLDVTTVIF--ANRAYAI 444
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
440-610 |
6.95e-03 |
|
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: 37.90 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 440 LRVNVLFKHIQKMLSSNMTVIAETGDS--WFhSQKLKLPKSCGYEVQLLYASIGWSLGATLGyAQAA-PHKRLLLCIGDG 516
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVtvWA-ARHLRMNGKQRFILSGLLATMGNGLPGAIA-AKLAyPDRQVIALSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784872638 517 SFQMAPQDVST--MLKLGQKNIIFliNNG--GYtIEVEIHDGPYNII----NNWDYTAFVDAVNNHqsncwTTKVHTEEE 588
Cdd:cd02014 80 GFAMLMGDLITavKYNLPVIVVVF--NNSdlGF-IKWEQEVMGQPEFgvdlPNPDFAKIAEAMGIK-----GIRVEDPDE 151
|
170 180
....*....|....*....|..
gi 1784872638 589 LVNAIEIAMKdrNDCLCFIEVI 610
Cdd:cd02014 152 LEAALDEALA--ADGPVVIDVV 171
|
|
| |
