|
Name |
Accession |
Description |
Interval |
E-value |
| indolpyr_decarb |
TIGR03393 |
indolepyruvate decarboxylase, Erwinia family; A family of closely related, thiamine ... |
5-543 |
0e+00 |
|
indolepyruvate decarboxylase, Erwinia family; A family of closely related, thiamine pyrophosphate-dependent enzymes includes indolepyruvate decarboxylase (EC 4.1.1.74), phenylpyruvate decarboxylase (EC 4.1.1.43), pyruvate decarboxylase (EC 4.1.1.1), branched-chain alpha-ketoacid decarboxylase, etc.. Members of this group of homologs may overlap in specificity. Within the larger family, this model represents a clade of bacterial indolepyruvate decarboxylases, part of a pathway for biosynthesis of the plant hormone indole-3-acetic acid. Typically, these species interact with plants, as pathogens or as beneficial, root-associated bacteria. [Central intermediary metabolism, Other]
Pssm-ID: 274559 [Multi-domain] Cd Length: 539 Bit Score: 944.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 5 YCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMN 84
Cdd:TIGR03393 1 YTVGDYLLDRLTDIGIDHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNAAYAADGYARCKGAAALLTTFGVGELSAIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 85 GIAGSFAEHVPVLHIVGAPGMASQQRGELLHHTLGDGEFRHFYHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPGY 164
Cdd:TIGR03393 81 GIAGSYAEHLPVIHIVGAPGTAAQQRGELLHHTLGDGDFRHFYRMAAEVTVAQAVLTEQNATAEIDRVITTALRERRPGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 165 LMVPADVAKKAATPPVNAL-TLQPADADNAClKAFRDAARVRLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHATM 243
Cdd:TIGR03393 161 LMLPVDVAAKAVTPPVNPLvTHKPAHADSAL-RAFRDAAENKLAMAKRVSLLADFLALRHGLKHALQKWVKEVPMPHATL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 244 LMGKGIFDERQAGFYGTYSGSASAAPVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHASRVGDVWFTGIP 323
Cdd:TIGR03393 240 LMGKGILDEQQAGFYGTYSGSASTGAVKEAIEGADAVICVGVRFTDTITAGFTHQLTPEQTIDVQPHAARVGNVWFTGIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 324 MIQAIETLAELCKEHV----HDSPAPFVNndiawPTEGGS-LTQESFWSTLQTFIRPGDIILADQGTSAFGAIDLRLPAE 398
Cdd:TIGR03393 320 MNDAIETLVELCEHAGlmwsSSGAIPFPQ-----PDESRSaLSQENFWQTLQTFLRPGDIILADQGTSAFGAADLRLPAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 399 VNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVERAIHGPEQRY 478
Cdd:TIGR03393 395 VNFIVQPLWGSIGYTLPAAFGAQTACPNRRVILLIGDGSAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGAEQRY 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2216604589 479 NDIALWNWTQIPQALSLDPQAECYRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAIT 543
Cdd:TIGR03393 475 NDIALWNWTHLPQALSLDPQSECWRVSEAEQLADVLEKVAAHERLSLIEVVLPKADIPPLLGALT 539
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-545 |
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: 867.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 1 MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGEL 80
Cdd:COG3961 1 MPMTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 81 SAMNGIAGSFAEHVPVLHIVGAPGMASQQRGELLHHTLGDGEFRHFYHMSEPITAAQAILTEQNACYEIDRVLTTMLRER 160
Cdd:COG3961 81 SAINGIAGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLGDGDFDHFLRMFEEVTVAQAVLTPENAAAEIDRVLAAALREK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 161 RPGYLMVPADVAKKAATPPVNALTLQPADADNACLKAFRDAARVRLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAH 240
Cdd:COG3961 161 RPVYIELPRDVADAPIEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 241 ATMLMGKGIFDERQAGFYGTYSGSASAAPVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHASRVGDVWFT 320
Cdd:COG3961 241 ATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGHIYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 321 GIPMIQAIETLAELCKEHVHDSPAPFVNNDIAWPTEGGSLTQESFWSTLQTFIRPGDIILADQGTSAFGAIDLRLPAEVN 400
Cdd:COG3961 321 GVSLADFLEALAELLKKRSAPLPAPAPPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRLPEGAT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 401 FIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVERAIHGPEQRYND 480
Cdd:COG3961 401 FIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYND 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2216604589 481 IALWNWTQIPQALSLDpQAECYRVSEAEQLADVLEKV-AHHERLSLIEVMLPKADIPPLLGAITRA 545
Cdd:COG3961 481 IANWDYAKLPEAFGGG-NALGFRVTTEGELEEALAAAeANTDRLTLIEVVLDKMDAPPLLKRLGKA 545
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
9-169 |
3.00e-102 |
|
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: 304.80 E-value: 3.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 9 DYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMNGIAG 88
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 89 SFAEHVPVLHIVGAPGMASQQRGELLHHTLGDGEFRHFYHMSEPITAAQAILT-EQNACYEIDRVLTTMLRERRPGYLMV 167
Cdd:cd07038 81 AYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGDFDVFLKMFEEITCAAARLTdPENAAEEIDRVLRTALRESRPVYIEI 160
|
..
gi 2216604589 168 PA 169
Cdd:cd07038 161 PR 162
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
6-534 |
1.32e-91 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 291.99 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 6 CVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMNG 85
Cdd:PLN02573 17 TLGRHLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSVLNA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVGAPGmaSQQRG--ELLHHTLGDGEFRHFYHMSEPITAAQAILTE-QNACYEIDRVLTTMLRERRP 162
Cdd:PLN02573 97 IAGAYSENLPVICIVGGPN--SNDYGtnRILHHTIGLPDFSQELRCFQTVTCYQAVINNlEDAHELIDTAISTALKESKP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 163 GYLMV----PADVAKKAATPPVnALTLQPADADNACLKAFRDAARVRLAMAQRTALLADFLVLRHGLKPALQKWVKEVPM 238
Cdd:PLN02573 175 VYISVscnlAAIPHPTFSREPV-PFFLTPRLSNKMSLEAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 239 AHATMLMGKGIFDERQAGFYGTYSGSASAAPVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHASRVGD-V 317
Cdd:PLN02573 254 PVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQPDRVTIGNgP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 318 WFTGIPMIQAIETLAELCKehvHDSPApFVN-NDIAWPtEGGSLTQE--------SFWSTLQTFIRPGDIILADQGTSAF 388
Cdd:PLN02573 334 AFGCVLMKDFLEALAKRVK---KNTTA-YENyKRIFVP-EGEPLKSEpgeplrvnVLFKHIQKMLSGDTAVIAETGDSWF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 389 GAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVE 468
Cdd:PLN02573 409 NCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIE 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2216604589 469 RAIH-GPeqrYNDIALWNWTQIPQALSlDPQAECY--RVSEAEQLADVLEKVAHHERLSL--IEVMLPKAD 534
Cdd:PLN02573 489 VEIHdGP---YNVIKNWNYTGLVDAIH-NGEGKCWtaKVRTEEELIEAIATATGEKKDCLcfIEVIVHKDD 555
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
359-539 |
1.58e-91 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 278.26 E-value: 1.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 359 SLTQESFWSTLQTFIRPGDIILADQGTSAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAA 438
Cdd:cd02005 1 PLTQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 439 QLTIQEMGSMLRDKQRPVILVLNNEGYTVERAIHGPEQRYNDIALWNWTQIPQALSLDPQAECYRVSEAEQLADVLEKV- 517
Cdd:cd02005 81 QMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIANWNYTKLPEVFGGGGGGLSFRVKTEGELDEALKDAl 160
|
170 180
....*....|....*....|..
gi 2216604589 518 AHHERLSLIEVMLPKADIPPLL 539
Cdd:cd02005 161 FNRDKLSLIEVILPKDDAPEAL 182
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
7-537 |
4.85e-63 |
|
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: 215.79 E-value: 4.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNG 85
Cdd:COG0028 5 GADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVGAPgmASQQRGELLHHTLgdgefrHFYHMSEPITAAQAILTE-QNACYEIDRVLTTMLRERR-PG 163
Cdd:COG0028 85 LADAYMDSVPVLAITGQV--PTSLIGRGAFQEV------DQVGLFRPITKWSYLVTDpEDLPEVLRRAFRIATSGRPgPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 164 YLMVPADVAKKAATPPVNALTLQPADADNAC-LKAFRDAARvRLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHAT 242
Cdd:COG0028 157 VLDIPKDVQAAEAEEEPAPPELRGYRPRPAPdPEAIEEAAE-LLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 243 MLMGKGIFDERQAGFYGTySGSASAAPVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHASRVGDVWFTGI 322
Cdd:COG0028 236 TLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 323 PMI----QAIETLAELCKEHVHDSPAPF-------VNNDIAWPTEGGSLTQESFWSTLQTFIRPGDIILADQGTSA-FGA 390
Cdd:COG0028 315 PIVgdakAVLAALLEALEPRADDRAAWLariaawrAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQmWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 391 IDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVER- 469
Cdd:COG0028 395 RYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRq 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2216604589 470 ---AIHGPEQRYNDIALWNWTQIPQALSldpqAECYRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPP 537
Cdd:COG0028 475 wqeLFYGGRYSGTDLPNPDFAKLAEAFG----AKGERVETPEELEAALEEALASDGPALIDVRVDPEENPP 541
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
7-179 |
1.99e-32 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 122.34 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNG 85
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVGAPGMASQQRGELlhHTLGDGE--FRHFYHMSEPITAAQAILteqnacYEIDRVLTTMLRERR-P 162
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGAL--QQELDQLalFRPVTKWAVRVTSADEIP------EVLRRAFRAALSGRPgP 152
|
170
....*....|....*..
gi 2216604589 163 GYLMVPADVAKKAATPP 179
Cdd:pfam02776 153 VYLEIPLDVLLEEVDED 169
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
9-169 |
1.69e-28 |
|
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: 110.90 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 9 DYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGELSAMNGIAG 88
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 89 SFAEHVPVLHIVGAPGMASqqrgellhHTLGDGEFRHFYHMSEPITAAQAILTE-QNACYEIDRVLTTMLRERRPGYLMV 167
Cdd:cd06586 81 AAAEHLPVVFLIGARGISA--------QAKQTFQSMFDLGMYRSIPEANISSPSpAELPAGIDHAIRTAYASQGPVVVRL 152
|
..
gi 2216604589 168 PA 169
Cdd:cd06586 153 PR 154
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
365-529 |
6.72e-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: 103.87 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 365 FWSTLQTFIRPGDIILADQGTSAFGAID-LRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQ 443
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRyLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 444 EMGSMLRDKQRPVILVLNNEGYTVERAIHGPEQ----RYNDIALWNWTQIPQALSldpqAECYRVSEAEQLADVLEKVAH 519
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYggrvSGTDLSNPDFAALAEAYG----AKGVRVEDPEDLEAALAEALA 157
|
170
....*....|
gi 2216604589 520 HERLSLIEVM 529
Cdd:cd00568 158 AGGPALIEVK 167
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
9-169 |
8.38e-23 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 94.91 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 9 DYLLDRLTDCGADHLFGVPGDYNLQFLDHvIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGIA 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDA-LARSGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 88 GSFAEHVPVLHIVGapgmasqQRGELLHHTLGDGEFRHfYHMSEPIT-AAQAILTEQNACYEIDRVLTTMLRERR-PGYL 165
Cdd:cd07035 80 NAYLDSIPLLVITG-------QRPTAGEGRGAFQEIDQ-VALFRPITkWAYRVTSPEEIPEALRRAFRIALSGRPgPVAL 151
|
....
gi 2216604589 166 MVPA 169
Cdd:cd07035 152 DLPK 155
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
8-543 |
9.43e-23 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 102.14 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSpDICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNGI 86
Cdd:PRK06276 4 AEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGKVGVcVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVgapgmasqqrGELLHHTLGDGEFRHF--YHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPG- 163
Cdd:PRK06276 83 ATAYADSSPVIALT----------GQVPTKLIGNDAFQEIdaLGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 164 -YLMVPADVA-------KKAATPPVNALTLQPADADNAclKAFRDAARVrLAMAQRTALLADFLVLRHGLKPALQKWVKE 235
Cdd:PRK06276 153 vHIDLPKDVQegeldleKYPIPAKIDLPGYKPTTFGHP--LQIKKAAEL-IAEAERPVILAGGGVIISGASEELIELSEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 236 VPMAHATMLMGKGIFDERQ------AGFYGTysgsasaAPVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQP 309
Cdd:PRK06276 230 VKIPVCTTLMGKGAFPEDHplalgmVGMHGT-------KAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 310 HASRVGDVWFTGIPMI-QAIETLAELCKEHVHDSPapfvNNDIAWPTEGGSLTQES---------------FWSTLQTFI 373
Cdd:PRK06276 303 DPAEIGKNVRVDVPIVgDAKNVLRDLLAELMKKEI----KNKSEWLERVKKLKKESiprmdfddkpikpqrVIKELMEVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 374 RPGD-----IILADQGTSAFGA---IDLRLPAEvnFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEM 445
Cdd:PRK06276 379 REIDpskntIITTDVGQNQMWMahfFKTSAPRS--FISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQEL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 446 GSmLRDKQRPV-ILVLNNEG----YTVERAIHGpeQRYNDIALWNwtqIPQALSLdpqAECY-----RVSEAEQLADVLE 515
Cdd:PRK06276 457 AT-IAEYDIPVvICIFDNRTlgmvYQWQNLYYG--KRQSEVHLGE---TPDFVKL---AESYgvkadRVEKPDEIKEALK 527
|
570 580 590
....*....|....*....|....*....|.
gi 2216604589 516 KVAHHERLSLIEVMLPKADIPPLL---GAIT 543
Cdd:PRK06276 528 EAIKSGEPYLLDIIIDPAEALPMVppgGNLT 558
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
1-528 |
7.36e-22 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 98.89 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 1 MRTpycVADYLLDRLTDCGADHLFGVPGDYNLQfLDHVIDSPDICWVGCANELNASYAADGYARCKGF--AALLTTfGVG 78
Cdd:PRK07524 1 MTT---CGEALVRLLEAYGVETVFGIPGVHTVE-LYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKpgVCFIIT-GPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 79 ELSAMNGIAGSFAEHVPVLHIVGAPGMASQQRGELLHHTLGDGEfrhfyHMSEPITAAQAILTEQNACYE-IDRVLTTML 157
Cdd:PRK07524 76 MTNIATAMGQAYADSIPMLVISSVNRRASLGKGRGKLHELPDQR-----AMVAGVAAFSHTLMSAEDLPEvLARAFAVFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 158 RER-RPGYLMVPADVAKKAATPPVNALTLQPAdADNACLKAFRDAARvRLAMAQRTALLADFLVLRHGlkPALQKWVKEV 236
Cdd:PRK07524 151 SARpRPVHIEIPLDVLAAPADHLLPAPPTRPA-RPGPAPAALAQAAE-RLAAARRPLILAGGGALAAA--AALRALAERL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 237 PMAHATMLMGKGIFderQAGFYGTYSGSASAAPVKEAIEGADTVLCIGTRFTDT-----LTAGFTH-------QLTAAQT 304
Cdd:PRK07524 227 DAPVALTINAKGLL---PAGHPLLLGASQSLPAVRALIAEADVVLAVGTELGETdydvyFDGGFPLpgeliriDIDPDQL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 305 IEVQ-PHASRVGDvwftgipmiqAIETLAELCkEHVHDSPAPF---------VNNDIAWPTEGGSLTQESFWSTLQTFIr 374
Cdd:PRK07524 304 ARNYpPALALVGD----------ARAALEALL-ARLPGQAAAAdwgaarvaaLRQALRAEWDPLTAAQVALLDTILAAL- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 PGDIILADQGTSAFG---AIDLRLPAEvnfivqplW-------GSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQE 444
Cdd:PRK07524 372 PDAIFVGDSTQPVYAgnlYFDADAPRR--------WfnastgyGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 445 MGSMlRDKQRPVILVL-NNEGY------TVERAIhgpEQRYNDIALWNWTQIPQALSLDpqAEcyRVSEAEQLADVLEKV 517
Cdd:PRK07524 444 LASA-VEADLPLIVLLwNNDGYgeirryMVARDI---EPVGVDPYTPDFIALARAFGCA--AE--RVADLEQLQAALRAA 515
|
570
....*....|.
gi 2216604589 518 AHHERLSLIEV 528
Cdd:PRK07524 516 FARPGPTLIEV 526
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
1-462 |
1.37e-20 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 95.27 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 1 MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGE 79
Cdd:PRK07282 6 LESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGkLGVAVVTSGPGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 80 LSAMNGIAGSFAEHVPVLHIVGAPGMASqqrgellhhtLGDGEFRH--FYHMSEPITAAQAILTEQNacyEIDRVLTTML 157
Cdd:PRK07282 86 TNAITGIADAMSDSVPLLVFTGQVARAG----------IGKDAFQEadIVGITMPITKYNYQIRETA---DIPRIITEAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 158 ---RERRPGYLMV--PADVAKKAAT----PPVNALTLQPA-DADNACLKAFRDaarvRLAMAQRTALLADFLVLRHGLKP 227
Cdd:PRK07282 153 hiaTTGRPGPVVIdlPKDVSALETDfiydPEVNLPSYQPTlEPNDMQIKKILK----QLSKAKKPVILAGGGINYAEAAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 228 ALQKWVKEVPMAHATMLMGKG---IFDERQAGFYGTYsGSASAapvKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQT 304
Cdd:PRK07282 229 ELNAFAERYQIPVVTTLLGQGtiaTSHPLFLGMGGMH-GSYAA---NIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 305 IEVQPHASRVGDVWFTGIPMI-QAIETLAELCKEhvhdspaPFVNNDIAWPTEggSLTQES----FWSTLQTFIRP---- 375
Cdd:PRK07282 305 AHIDIDPAEIGKIIKTDIPVVgDAKKALQMLLAE-------PTVHNNTEKWIE--KVTKDKnrvrSYDKKERVVQPqavi 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 376 --------GD-IILADQGTSAFGAIDLR-LPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEM 445
Cdd:PRK07282 376 erigeltnGDaIVVTDVGQHQMWAAQYYpYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQEL 455
|
490
....*....|....*..
gi 2216604589 446 gSMLRDKQRPVILVLNN 462
Cdd:PRK07282 456 -AILNIYKVPIKVVMLN 471
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
400-528 |
1.25e-19 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 85.71 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 400 NFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVERaiHGPEQRYN 479
Cdd:pfam02775 20 RYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGYGMTR--GQQTPFGG 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2216604589 480 dialWNWTQIPQALSLDPQ----AECY-----RVSEAEQLADVLEKVAHHERLSLIEV 528
Cdd:pfam02775 98 ----GRYSGPSGKILPPVDfaklAEAYgakgaRVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
7-541 |
2.99e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 90.99 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSpDICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNG 85
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDS-DLRHILVRHEQAAAHAADGYARATGKVGVcVATSGPGATNLVTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVgapgmasqqrGELLHHTLGDGEFRH--FYHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPG 163
Cdd:PRK06048 89 IATAYMDSVPIVALT----------GQVPRSMIGNDAFQEadITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 164 YLMV--PADVAKKAAT----PPVNALTLQPADADNacLKAFRDAARVrLAMAQRTALLADFLVLRHGLKPALQKWVKEVP 237
Cdd:PRK06048 159 PVLIdlPKDVTTAEIDfdypDKVELRGYKPTYKGN--PQQIKRAAEL-IMKAERPIIYAGGGVISSNASEELVELAETIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 238 MAHATMLMGKGIFDERQ------AGFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHA 311
Cdd:PRK06048 236 APVTTTLMGIGAIPTEHplslgmLGMHGTKYANY-------AIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 312 SRVGDVWFTGIPMI-QAIETLAELCKEHVHDSPAPFVNNDIAWPTEgGSLTQESFWSTL--QTFIR------PGDIILAD 382
Cdd:PRK06048 309 AEISKNVKVDVPIVgDAKQVLKSLIKYVQYCDRKEWLDKINQWKKE-YPLKYKEREDVIkpQYVIEqiyelcPDAIIVTE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 383 QGTSAFGAID-LRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLN 461
Cdd:PRK06048 388 VGQHQMWAAQyFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 462 NEGYTVERAIHGP--EQRYNDialwnwTQIPQALSLDPQAECY-----RVSEAEQLADVLEKVAHHERLSLIEVMLPK-A 533
Cdd:PRK06048 468 NGYLGMVRQWQELfyDKRYSH------TCIKGSVDFVKLAEAYgalglRVEKPSEVRPAIEEAVASDRPVVIDFIVECeE 541
|
....*...
gi 2216604589 534 DIPPLLGA 541
Cdd:PRK06048 542 NVSPMVPA 549
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
8-462 |
1.31e-18 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 89.03 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAA-LLTTFGVGELSAMNGI 86
Cdd:PRK06466 7 AEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGvVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIvgapgmasqqRGELLHHTLGDGEFRH--FYHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPGY 164
Cdd:PRK06466 87 ATAYMDSIPMVVL----------SGQVPSTLIGEDAFQEtdMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 165 LMVpaDVAKKAATP----------PVNALTLQPADADNAclKAFRDAARVRLAmAQRTALLADFLVLRHGLKPALQKWVK 234
Cdd:PRK06466 157 VVV--DIPKDMTNPaekfeyeypkKVKLRSYSPAVRGHS--GQIRKAVEMLLA-AKRPVIYSGGGVVLGNASALLTELAH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 235 EVPMAHATMLMGKGIF--DERQ----AGFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQ 308
Cdd:PRK06466 232 LLNLPVTNTLMGLGGFpgTDRQflgmLGMHGTYEANM-------AMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 309 PHASRVGDVWFTGIPMIQAIET----LAELCKEHVHDSPAPFVNndiAW-----------------PTEGGSLTQESFWS 367
Cdd:PRK06466 305 IDPASISKTIKADIPIVGPVESvlteMLAILKEIGEKPDKEALA---AWwkqidewrgrhglfpydKGDGGIIKPQQVVE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 368 TLQTFIRPGDIILADQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMG 446
Cdd:PRK06466 382 TLYEVTNGDAYVTSDVGQhQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELS 461
|
490
....*....|....*..
gi 2216604589 447 SMLRdKQRPV-ILVLNN 462
Cdd:PRK06466 462 TCLQ-YGLPVkIINLNN 477
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
3-530 |
5.67e-18 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 86.93 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 3 TPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDspDICWVGCANELNASYAADGYARCKGFAALL---TTFGVGe 79
Cdd:PRK07092 10 AMTTVRDATIDLLRRFGITTVFGNPGSTELPFLRDFPD--DFRYVLGLQEAVVVGMADGYAQATGNAAFVnlhSAAGVG- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 80 lSAMNGIAGSFAEHVPVLHIVGA---------PGMASQQRGELLhhtlgdgefRHFYHMS-EPITA-------AQAILTe 142
Cdd:PRK07092 87 -NAMGNLFTAFKNHTPLVITAGQqarsilpfePFLAAVQAAELP---------KPYVKWSiEPARAedvpaaiARAYHI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 143 qnacyeidrvltTMLRERRPGYLMVPADVAKKAAtPPVNALTLQPADA-DNACLKAFRDAarvrLAMAQRTALL------ 215
Cdd:PRK07092 156 ------------AMQPPRGPVFVSIPYDDWDQPA-EPLPARTVSSAVRpDPAALARLGDA----LDAARRPALVvgpavd 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 216 ---ADFLVLRHGLKPALQKWVkeVPMAhatmlmGKGIFDERQAGFYGTYSgsASAAPVKEAIEGADTVLCIGTrftdtlt 292
Cdd:PRK07092 219 ragAWDDAVRLAERHRAPVWV--APMS------GRCSFPEDHPLFAGFLP--ASREKISALLDGHDLVLVIGA------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 293 AGFT-HQLTAA----------QTIEVQPHASR-------VGDvwftgipMIQAIETLAELCKEHVHDSPAPFVNNDiAWP 354
Cdd:PRK07092 282 PVFTyHVEGPGphlpegaelvQLTDDPGEAAWapmgdaiVGD-------IRLALRDLLALLPPSARPAPPARPMPP-PAP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 355 TEGGSLTQESFWSTLQTfIRPGDIILADQGTSAFGAIDLRLPaevnFIVQ-----PLWGSIGYTLAAAFGAQTACPNRRV 429
Cdd:PRK07092 354 APGEPLSVAFVLQTLAA-LRPADAIVVEEAPSTRPAMQEHLP----MRRQgsfytMASGGLGYGLPAAVGVALAQPGRRV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 430 IVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVERAIHGPEQRYN----DIALWNWTQIPQALSLDPQaecyRVS 505
Cdd:PRK07092 429 IGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPVFGVRDvpglDLPGLDFVALARGYGCEAV----RVS 504
|
570 580
....*....|....*....|....*
gi 2216604589 506 EAEQLADVLEKVAHHERLSLIEVML 530
Cdd:PRK07092 505 DAAELADALARALAADGPVLVEVEV 529
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
8-543 |
6.77e-18 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 86.98 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYnlqfLDHVIDS-----PDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELS 81
Cdd:PRK08611 7 GEALVKLLQDWGIDHVYGIPGDS----IDAVVDAlrkeqDKIKFIQVRHEEVAALAAAAYAKLTGkIGVCLSIGGPGAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 82 AMNGIAGSFAEHVPVLHIVGApgMASQQrgellhhtLGDGEFR--HFYHMSEPITA-AQAILTEQNACYEIDRVLTTMLR 158
Cdd:PRK08611 83 LLNGLYDAKMDHVPVLALAGQ--VTSDL--------LGTDFFQevNLEKMFEDVAVyNHQIMSAENLPEIVNQAIRTAYE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 159 ERRPGYLMVPADV----AKKAATPPVNALTLQPADADNACLKafrDAARVrLAMAQRTALLADfLVLRHGlKPALQKWVK 234
Cdd:PRK08611 153 KKGVAVLTIPDDLpaqkIKDTTNKTVDTFRPTVPSPKPKDIK---KAAKL-INKAKKPVILAG-LGAKHA-KEELLAFAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 235 E--VPMAHAtmLMGKGIFDERQAGFYGTYsGSASAAPVKEAIEGADTVLCIGTRF--TDTLTAGfthqltaAQTIEVQPH 310
Cdd:PRK08611 227 KakIPIIHT--LPAKGIIPDDHPYSLGNL-GKIGTKPAYEAMQEADLLIMVGTNYpyVDYLPKK-------AKAIQIDTD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 311 ASRVG-----DVWFTGipmiQAIETLAELCKEHVHDSPAPFVNNDIA-------WPTEGGSLTQ-----ESFWSTLQTfI 373
Cdd:PRK08611 297 PANIGkrypvNVGLVG----DAKKALHQLTENIKHVEDRRFLEACQEnmakwwkWMEEDENNAStpikpERVMAAIQK-I 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 374 RPGDIIL-ADQGTS-AFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRD 451
Cdd:PRK08611 372 ADDDAVLsVDVGTVtVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 452 KQRPVILVLNNEGYTV---ERAIHGPEQRYNDIALWNWTQIPQAlsldpqaeC----YRVSEAEQLADVLEKVAHHERLS 524
Cdd:PRK08611 452 KLPIVVVVLNNQQLAFikyEQQAAGELEYAIDLSDMDYAKFAEA--------CggkgYRVEKAEELDPAFEEALAQDKPV 523
|
570
....*....|....*....
gi 2216604589 525 LIEVMLpKADIPPLLGAIT 543
Cdd:PRK08611 524 IIDVYV-DPNAAPLPGKIV 541
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
7-174 |
1.34e-17 |
|
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: 80.29 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNG 85
Cdd:cd07039 2 VADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGkLGVCLGSSGPGAIHLLNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVG-----APGMASQQrgELLHHTLgdgeFRHFYHMSEPI-TAAQAIlteqnacYEIDRVLTTMLRE 159
Cdd:cd07039 82 LYDAKRDRAPVLAIAGqvptdELGTDYFQ--EVDLLAL----FKDVAVYNETVtSPEQLP-------ELLDRAIRTAIAK 148
|
170
....*....|....*
gi 2216604589 160 RRPGYLMVPADVAKK 174
Cdd:cd07039 149 RGVAVLILPGDVQDA 163
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
19-530 |
2.58e-17 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 85.05 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 19 GADHLFGVPGDYNLQFLDhVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGIAGSFAEHVPVL 97
Cdd:PRK07525 20 GITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYWAHTPVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 98 HIvgAPGMASQqrgellhhTLGDGEFRHFYHMS--EPITAAQAILTEQNACYEI-DRVLTTMLRERRPGYLMVPADVAkk 174
Cdd:PRK07525 99 LV--TPQAGTK--------TIGQGGFQEAEQMPmfEDMTKYQEEVRDPSRMAEVlNRVFDKAKRESGPAQINIPRDYF-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 175 aaTPPVNALTLQPADADNAC--LKAFRDAARVrLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHATMLMGKGIFDE 252
Cdd:PRK07525 167 --YGVIDVEIPQPVRLERGAggEQSLAEAAEL-LSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAFPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 253 RQAGFYGT--YSGSASAApvkEAIEGADTVLCIGTR---FTDTLTAGFTHQLTAAQTIEVQPHASRVG-----DVWFTGI 322
Cdd:PRK07525 244 SHPLWVGPlgYNGSKAAM---ELIAKADVVLALGTRlnpFGTLPQYGIDYWPKDAKIIQVDINPDRIGltkkvSVGICGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 323 PMIQAIETLAELC------------KEHVHDSPApfvnndiAWPTEGGSLTQES-----------------------FWS 367
Cdd:PRK07525 321 AKAVARELLARLAerlagdagreerKALIAAEKS-------AWEQELSSWDHEDddpgtdwneeararkpdymhprqALR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 368 TLQTFIRPGDIILADQG-TSAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMG 446
Cdd:PRK07525 394 EIQKALPEDAIVSTDIGnNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 447 SMLRdKQRPVI-LVLNNEGYtveraihGPEQR-----YND----IALWN---WTQIPQALSldpqAECYRVSEAEQLADV 513
Cdd:PRK07525 474 TAVR-HNWPVTaVVFRNYQW-------GAEKKnqvdfYNNrfvgTELDNnvsYAGIAEAMG----AEGVVVDTQEELGPA 541
|
570 580
....*....|....*....|
gi 2216604589 514 LEK---VAHHERLSLIEVML 530
Cdd:PRK07525 542 LKRaidAQNEGKTTVIEIMC 561
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
8-528 |
5.14e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 84.33 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVG---CANELNASYAADGYARCKG-----FAalltTFGVGE 79
Cdd:PRK07418 22 AYALMDSLKRHGVKHIFGYPGGAILPIYDELYKAEAEGWLKhilVRHEQGAAHAADGYARATGkvgvcFG----TSGPGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 80 LSAMNGIAGSFAEHVPVLHIVG-----APGMASQQRGELLHHTLGdgEFRHFYHMSEPI----TAAQAILTEQNAcyeid 150
Cdd:PRK07418 98 TNLVTGIATAQMDSVPMVVITGqvprpAIGTDAFQETDIFGITLP--IVKHSYVVRDPSdmarIVAEAFHIASSG----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 151 rvlttmlrerRPGYLM--VPADVAKK----------AATPPVNALTLQPADAD-NACLKAFRDAarvrlamaQRTALLAD 217
Cdd:PRK07418 171 ----------RPGPVLidIPKDVGQEefdyvpvepgSVKPPGYRPTVKGNPRQiNAALKLIEEA--------ERPLLYVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 218 FLVLRHGLKPALQKWVKEVPMAHATMLMGKGIFDERQA---GFYGTYsGSASAapvKEAIEGADTVLCIGTRFTDTLTAG 294
Cdd:PRK07418 233 GGAISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPlsvGMLGMH-GTAYA---NFAVTECDLLIAVGARFDDRVTGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 295 FTHQLTAAQTI-------EV----QPHASRVGDVWftgipmiQAIETLAELCKEHVHDspapfvNNDIAWpteggsLTQE 363
Cdd:PRK07418 309 LDEFASRAKVIhididpaEVgknrRPDVPIVGDVR-------KVLVKLLERSLEPTTP------PRTQAW------LERI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 364 SFWSTL--------QTFIRPGDIILA--DQGTSAFGAID-----------LRlPAEVNFIVQPLWGSIGYTLAAAFGAQT 422
Cdd:PRK07418 370 NRWKQDyplvvppyEGEIYPQEVLLAvrDLAPDAYYTTDvgqhqmwaaqfLR-NGPRRWISSAGLGTMGFGMPAAMGVKV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 423 ACPNRRVIVLTGDGAAQLTIQEMGSmLRDKQRPVILVLNNEGY-----TVERAIHGpeQRYNDIALWNwtQIPQALSLdp 497
Cdd:PRK07418 449 ALPDEEVICIAGDASFLMNIQELGT-LAQYGINVKTVIINNGWqgmvrQWQESFYG--ERYSASNMEP--GMPDFVKL-- 521
|
570 580 590
....*....|....*....|....*....|....*.
gi 2216604589 498 qAECY-----RVSEAEQLADVLEKVAHHERLSLIEV 528
Cdd:PRK07418 522 -AEAFgvkgmVISERDQLKDAIAEALAHDGPVLIDV 556
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
11-537 |
7.46e-17 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 83.77 E-value: 7.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 11 LLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-----FAalltTFGVGELSAMNG 85
Cdd:PRK08199 14 LVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGrpgicFV----TRGPGATNASIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVGApgMASQQRG-----ELlhhtlgdgEFRHFY-HMSEPITaaqailteqnacyEIDRVlttmlrE 159
Cdd:PRK08199 90 VHTAFQDSTPMILFVGQ--VARDFREreafqEI--------DYRRMFgPMAKWVA-------------EIDDA------A 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 160 R---------------RPG--YLMVPADVAKKAAT----PPVNALTLQPADADNACLKAFRDAARVRLAMA-------QR 211
Cdd:PRK08199 141 RipelvsrafhvatsgRPGpvVLALPEDVLSETAEvpdaPPYRRVAAAPGAADLARLAELLARAERPLVILggsgwteAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 212 TALLADFlVLRHGLkpalqkwvkevPMAhaTMLMGKGIFDERQAGFYGTYSGSASAApVKEAIEGADTVLCIGTRFTDTL 291
Cdd:PRK08199 221 VADLRAF-AERWGL-----------PVA--CAFRRQDLFDNRHPNYAGDLGLGINPA-LAARIREADLVLAVGTRLGEVT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 292 TAGFT---HQLTAAQTIEVQPHASRVGDVWFTGIPmIQA--IETLAELCKEHVHDSPAPFvnndiAWpTEGGSLTQESfW 366
Cdd:PRK08199 286 TQGYTlldIPVPRQTLVHVHPDAEELGRVYRPDLA-IVAdpAAFAAALAALEPPASPAWA-----EW-TAAAHADYLA-W 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 367 STLQTfiRPGDIILAdqgtSAFGAIDLRLPAEV-------NFIV---------------QPLWGSIGYTLAAAFGAQTAC 424
Cdd:PRK08199 358 SAPLP--GPGAVQLG----EVMAWLRERLPADAiitngagNYATwlhrffrfrryrtqlAPTSGSMGYGLPAAIAAKLLF 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 425 PNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGY-TV----ERA----IHGPEQRYNDIAlwnwtqipqALsl 495
Cdd:PRK08199 432 PERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYgTIrmhqEREypgrVSGTDLTNPDFA---------AL-- 500
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2216604589 496 dpqAECY-----RVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPP 537
Cdd:PRK08199 501 ---ARAYgghgeTVERTEDFAPAFERALASGKPALIEIRIDPEAITP 544
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
3-528 |
7.47e-17 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 83.50 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 3 TPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGels 81
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGgLGVALTSTGTG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 82 AMNgIAGSFAEHV----PVLHIVGapgmasQQRGELLHHTLGdgefrhFYH-------MSEPIT-AAQAILTEQNACYEI 149
Cdd:PRK07064 78 AGN-AAGALVEALtagtPLLHITG------QIETPYLDQDLG------YIHeapdqltMLRAVSkAAFRVRSAETALATI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 150 DR-VLTTMLRERRPGYLMVPADVAKKAATPPVNALTLQPA--DADNACLkafrDAARVRLAMAQRTALLADFLVLrhGLK 226
Cdd:PRK07064 145 REaVRVALTAPTGPVSVEIPIDIQAAEIELPDDLAPVHVAvpEPDAAAV----AELAERLAAARRPLLWLGGGAR--HAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 227 PALQKWVKE-VPMAHATMlmGKGIFDERQAGFYGTYSGSAsaaPVKEAIEGADTVLCIGTRFTDTLTAGFTHQLtAAQTI 305
Cdd:PRK07064 219 AEVKRLVDLgFGVVTSTQ--GRGVVPEDHPASLGAFNNSA---AVEALYKTCDLLLVVGSRLRGNETLKYSLAL-PRPLI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 306 EVQPHASRVG-----DVWFTGiPMIQAIETLAELCKEHVHDSPAPFVNNDIAWPTEGGSLTQE-----SFWSTLQTFIrP 375
Cdd:PRK07064 293 RVDADAAADGrgypnDLFVHG-DAARVLARLADRLEGRLSVDPAFAADLRAAREAAVADLRKGlgpyaKLVDALRAAL-P 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 376 GDIILADQGT---SAFGAIDLRLpAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDK 452
Cdd:PRK07064 371 RDGNWVRDVTisnSTWGNRLLPI-FEPRANVHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 453 QRPVILVLNNEGYTVERAI----HGPEQRYNDIALWNWTQIPQALSLdpqaECYRVSEAEQLADVLEKVAHHERLSLIEV 528
Cdd:PRK07064 450 ANMVIVLMNDGGYGVIRNIqdaqYGGRRYYVELHTPDFALLAASLGL----PHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
11-462 |
1.08e-16 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 83.21 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 11 LLDRLTDCGADHLFGVPGDYNL------------QFLDHVIdspdicwvgCANELNASYAADGYARCKG-----FAallt 73
Cdd:CHL00099 16 LIDSLVRHGVKHIFGYPGGAILpiydelyawekkGLIKHIL---------VRHEQGAAHAADGYARSTGkvgvcFA---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 74 TFGVGELSAMNGIAGSFAEHVPVLHIVGAPGMAsqqrgellhhTLGDGEFRH--FYHMSEPITAAQAILTEQNACYEIDR 151
Cdd:CHL00099 83 TSGPGATNLVTGIATAQMDSVPLLVITGQVGRA----------FIGTDAFQEvdIFGITLPIVKHSYVVRDARDISRIVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 152 VLTTMLRERRPGYLM--VPADVA--KKAATPPVNALTLQPadadnacLKAFRDAARV---RLAMAQRtalladflVLRHG 224
Cdd:CHL00099 153 EAFYIAKHGRPGPVLidIPKDVGleKFDYYPPEPGNTIIK-------ILGCRPIYKPtikRIEQAAK--------LILQS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 225 LKPAL-----------QKWVKE------VPMAhaTMLMGKGIFDERQA---GFYGTYsGSASAapvKEAIEGADTVLCIG 284
Cdd:CHL00099 218 SQPLLyvgggaiisdaHQEITElaelykIPVT--TTLMGKGIFDEDHPlclGMLGMH-GTAYA---NFAVSECDLLIALG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 285 TRFTDTLTAGFTHQLTAAQTIEV-----------QPHASRVGDVwftgipmiqaIETLAELCKEHVHDSPAPFVNNDIAW 353
Cdd:CHL00099 292 ARFDDRVTGKLDEFACNAQVIHIdidpaeigknrIPQVAIVGDV----------KKVLQELLELLKNSPNLLESEQTQAW 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 354 ---------------PTEGGSLTQESFWSTLQTfIRPGDIILADQGTSAFGAidlrlpaeVNFI-VQPL-W------GSI 410
Cdd:CHL00099 362 rerinrwrkeyplliPKPSTSLSPQEVINEISQ-LAPDAYFTTDVGQHQMWA--------AQFLkCKPRkWlssaglGTM 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2216604589 411 GYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNN 462
Cdd:CHL00099 433 GYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN 484
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
8-462 |
1.56e-16 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 82.65 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGI 86
Cdd:PRK06882 7 AEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVgapgmasqqrGELLHHTLGDGEFRH--FYHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPGY 164
Cdd:PRK06882 87 ATAYTDSVPLVILS----------GQVPSNLIGTDAFQEcdMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 165 LMV-----------------PADVAKKAATPPVNALTLQPADAdnacLKAfrdaarvrLAMAQRTALLADFLVLRHGLKP 227
Cdd:PRK06882 157 VVIdipkdmvnpankftyeyPEEVSLRSYNPTVQGHKGQIKKA----LKA--------LLVAKKPVLFVGGGVITAECSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 228 ALQKWVKEVPMAHATMLMGKGIF--DERQ----AGFYGTYSGSasaapvkEAIEGADTVLCIGTRFTDTLTAGFTHQLTA 301
Cdd:PRK06882 225 QLTQFAQKLNLPVTSSLMGLGAYpsTDKQflgmLGMHGTYEAN-------NAMHESDLILGIGVRFDDRTTNNLAKYCPN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 302 AQTIEVQPHASRVGDVWFTGIPMIQAI-----ETLAELCKEHVHDSPAPFVnndiAWpteggsLTQESFWSTLQ--TFIR 374
Cdd:PRK06882 298 AKVIHIDIDPTSISKNVPAYIPIVGSAknvleEFLSLLEEENLAKSQTDLT----AW------WQQINEWKAKKclEFDR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 PGDIILADQGTSA--------------------FGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTG 434
Cdd:PRK06882 368 TSDVIKPQQVVEAiyrltngdayvasdvgqhqmFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTG 447
|
490 500
....*....|....*....|....*...
gi 2216604589 435 DGAAQLTIQEMGSMLRDKQRPVILVLNN 462
Cdd:PRK06882 448 DGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
11-536 |
2.33e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 81.98 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 11 LLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPD-ICWVGCANELNASYAADGYARCKGFAALLTTF-GVGELSAMNGIAG 88
Cdd:PRK08266 10 IVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVpGPGVLNAGAALLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 89 SFAEHVPVLHIVG---APGMAsQQRGELlhHTLGD--GEFRHFyhmsepITAAQAILTEQNACYEIDRVLTTMLRER-RP 162
Cdd:PRK08266 90 AYGCNSPVLCLTGqipSALIG-KGRGHL--HEMPDqlATLRSF------TKWAERIEHPSEAPALVAEAFQQMLSGRpRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 163 GYLMVPADV----AKKAATPPVNALTLQPADADN-ACLKAFRDAARVRLAMAQRTALLADFLVLRhgLKPALQKWVkevp 237
Cdd:PRK08266 161 VALEMPWDVfgqrAPVAAAPPLRPAPPPAPDPDAiAAAAALIAAAKNPMIFVGGGAAGAGEEIRE--LAEMLQAPV---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 238 MAHATmlmGKGIFDERQagfygtYSGSASAApVKEAIEGADTVLCIGTRFTD-TLTAGFthqLTAAQT---IEVQP--HA 311
Cdd:PRK08266 235 VAFRS---GRGIVSDRH------PLGLNFAA-AYELWPQTDVVIGIGSRLELpTFRWPW---RPDGLKvirIDIDPteMR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 312 SRVGDVwftGIPMIQAIETLAELCKEHVHDSPAPFVNNDIAwptEGGSLTQESFWStLQ---TFIR------PGDIILAD 382
Cdd:PRK08266 302 RLKPDV---AIVADAKAGTAALLDALSKAGSKRPSRRAELR---ELKAAARQRIQA-VQpqaSYLRairealPDDGIFVD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 383 QGTSAFGAIDLRLP--AEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVL 460
Cdd:PRK08266 375 ELSQVGFASWFAFPvyAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVF 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2216604589 461 NNEGYTVERAIHgpEQRYNDIALWNWTQIP--QALSLDPQAECYRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIP 536
Cdd:PRK08266 455 NNNAYGNVRRDQ--KRRFGGRVVASDLVNPdfVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVPRGSEA 530
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
8-462 |
5.16e-16 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 81.08 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPdICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNGI 86
Cdd:PRK08978 4 AQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKVGVcIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHI---VGAPGMASQQRGELlhHTLGdgefrhfyhMSEPITAAQAILTEQNacyEIDRVLT---TMLRER 160
Cdd:PRK08978 83 ADALLDSVPVVAItgqVSSPLIGTDAFQEI--DVLG---------LSLACTKHSFLVQSLE---ELPEIMAeafEIASSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 161 RPGYLMV--PADV--AKKAATPPVNALTLQPADADNAClkafrDAARVRLAMAQRTALLADFLVLRHGLKPALQKWVKEV 236
Cdd:PRK08978 149 RPGPVLVdiPKDIqlAEGELEPHLTTVENEPAFPAAEL-----EQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAAT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 237 PMAHATMLMGKGIFDERQAGFYGTYS--GSASAapvKEAIEGADTVLCIGTRFTDTLT---AGFTHQltaAQTIEV---- 307
Cdd:PRK08978 224 GMPAVATLKGLGAVEADHPYYLGMLGmhGTKAA---NLAVQECDLLIAVGARFDDRVTgklNTFAPH---AKVIHLdidp 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 308 -------QPHASRVGDvwftgipMIQAIETLAElckehvhdspapfvNNDI-AWPTEGGSLTQESFWStlqtFIRPGDII 379
Cdd:PRK08978 298 aeinklrQAHVALQGD-------LNALLPALQQ--------------PLNIdAWRQHCAQLRAEHAWR----YDHPGEAI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 380 LAdqgTSAFGAIDLRLPAEV-----------------------NFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDG 436
Cdd:PRK08978 353 YA---PALLKQLSDRKPADTvvttdvgqhqmwvaqhmrftrpeNFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDG 429
|
490 500
....*....|....*....|....*..
gi 2216604589 437 AAQLTIQEMGSMLRdKQRPV-ILVLNN 462
Cdd:PRK08978 430 SFMMNVQELGTIKR-KQLPVkIVLLDN 455
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
161-538 |
2.18e-15 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 79.03 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 161 RPG--YLMVPADVAKKAATPPV----NALTLQPADADNACLKAFRDAARvRLAMAQRTALLADFLVLRHGLKPALQKWVK 234
Cdd:PRK06112 160 RPGpvVLLLPADLLTAAAAAPAaprsNSLGHFPLDRTVPAPQRLAEAAS-LLAQAQRPVVVAGGGVHISGASAALAALQS 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 235 EVPMAHATMLMGKGIFDERQ---AGFYGTYSGSASAAP-VKEAIEGADTVLCIGTRF----TDTLT-----AGFTHQLTA 301
Cdd:PRK06112 239 LAGLPVATTNMGKGAVDETHplsLGVVGSLMGPRSPGRhLRDLVREADVVLLVGTRTnqngTDSWSlypeqAQYIHIDVD 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 302 AQTIEVQPHASR-VGDVWFTGIPMIQAI----------------ETLAELCKEHVHDSpAPFVNNDiAWPteggsLTQES 364
Cdd:PRK06112 319 GEEVGRNYEALRlVGDARLTLAALTDALrgrdlaaragrraalePAIAAGREAHREDS-APVALSD-ASP-----IRPER 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 365 FWSTLQTFIRPGDIILADQGTSAFGAID-LRLPAEVNFIVQP--LWGsIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLT 441
Cdd:PRK06112 392 IMAELQAVLTGDTIVVADASYSSIWVANfLTARRAGMRFLTPrgLAG-LGWGVPMAIGAKVARPGAPVICLVGDGGFAHV 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 442 IQEMGSMLRDKQRPVILVLNNE--GYT--VERAIHGPEQRYNDIALWNWTQIPQALSLDpqaeCYRVSEAEQLADVLEKV 517
Cdd:PRK06112 471 WAELETARRMGVPVTIVVLNNGilGFQkhAETVKFGTHTDACHFAAVDHAAIARACGCD----GVRVEDPAELAQALAAA 546
|
410 420
....*....|....*....|.
gi 2216604589 518 AHHERLSLIEVMLPKADIPPL 538
Cdd:PRK06112 547 MAAPGPTLIEVITDPSAFPPI 567
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
408-541 |
2.38e-15 |
|
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: 74.46 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 408 GSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGsMLRDKQRPV-ILVLNNEGY----TVERAIHgpEQRYndia 482
Cdd:cd02015 50 GTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQELA-TAAQYNLPVkIVILNNGSLgmvrQWQELFY--EGRY---- 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2216604589 483 lwnwtqIPQALSLDPQ----AECY-----RVSEAEQLADVLEKVAHHERLSLIEVMLPK-ADIPPLLGA 541
Cdd:cd02015 123 ------SHTTLDSNPDfvklAEAYgikglRVEKPEELEAALKEALASDGPVLLDVLVDPeENVLPMVPP 185
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
369-537 |
3.34e-15 |
|
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: 73.72 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 369 LQTFIRPGDIILADQGTSA-FGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGS 447
Cdd:cd02014 11 LNKRAPDDAIFTIDVGNVTvWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMGDLIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 448 MLRDKQRPVILVLNNEGY---TVERAIHGPEQRYNDIALWNWTQIPQALSLDPqaecYRVSEAEQLADVLEKVAHHERLS 524
Cdd:cd02014 91 AVKYNLPVIVVVFNNSDLgfiKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKG----IRVEDPDELEAALDEALAADGPV 166
|
170
....*....|...
gi 2216604589 525 LIEVMLpKADIPP 537
Cdd:cd02014 167 VIDVVT-DPNEPP 178
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
7-532 |
7.26e-15 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 77.54 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPgdynlqfLDHVIDSP---DICWVGCANELNASYAADGYARC---KGFAALLTTFGVGEL 80
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGFP-------VNELFDAAaaaGIRPVIARTERVAVHMADGYARAtsgERVGVFAVQYGPGAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 81 SAMNGIAGSFAEHVPVLHIvgaPGMASQQRGELLHHTLGDGEFRHFYHMSEPITAAQAIlteqnacYEIDRVLTTMLRER 160
Cdd:PRK06154 95 NAFGGVAQAYGDSVPVLFL---PTGYPRGSTDVAPNFESLRNYRHITKWCEQVTLPDEV-------PELMRRAFTRLRNG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 161 RPG--YLMVPADVAKK--AATP----PVNALTLQPADADnaclkaFRDAARVRLAmAQRTALLADFLVLRHGLKPALQKW 232
Cdd:PRK06154 165 RPGpvVLELPVDVLAEelDELPldhrPSRRSRPGADPVE------VVEAAALLLA-AERPVIYAGQGVLYAQATPELKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 233 VKEVPMAHATMLMGKGIFDERQAGFYGTySGSASAAPVKEAIEGADTVLCIGTRFTDTLtagFTHQLTAAQTI------- 305
Cdd:PRK06154 238 AELLEIPVMTTLNGKSAFPEDHPLALGS-GGRARPATVAHFLREADVLFGIGCSLTRSY---YGLPMPEGKTIihstldd 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 306 -----EVQPHASRVGDVWFTGIPMIQAI------------ETLAELckEHVHDspapfvnndiAWPTEGGS-LTQES--- 364
Cdd:PRK06154 314 adlnkDYPIDHGLVGDAALVLKQMIEELrrrvgpdrgraqQVAAEI--EAVRA----------AWLAKWMPkLTSDStpi 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 365 -----FWSTLQTFIRPGDIILADQGTSAfgaiDLRLPAEVnfIVQPL----WG---SIGYTLAAAFGAQTACPNRRVIVL 432
Cdd:PRK06154 382 npyrvVWELQHAVDIKTVIITHDAGSPR----DQLSPFYV--ASRPGsylgWGkttQLGYGLGLAMGAKLARPDALVINL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 433 TGDGAAQLTIQEMGSMLRDKQRPVILVLNN---EGYTVERAIHGPEQRYNDIAlWNWTQIPQALSldpqaeCY--RVSEA 507
Cdd:PRK06154 456 WGDAAFGMTGMDFETAVRERIPILTILLNNfsmGGYDKVMPVSTTKYRATDIS-GDYAAIARALG------GYgeRVEDP 528
|
570 580
....*....|....*....|....*...
gi 2216604589 508 EQLADVLEK---VAHHERLSLIEVMLPK 532
Cdd:PRK06154 529 EMLVPALLRalrKVKEGTPALLEVITSE 556
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
8-462 |
9.20e-15 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 77.20 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGI 86
Cdd:PRK07979 7 AEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIvgapgmasqqRGELLHHTLGDGEFRH--FYHMSEPITAaQAILTEQNAcyEIDRVLTT---MLRERR 161
Cdd:PRK07979 87 ATAYMDSIPLVVL----------SGQVATSLIGYDAFQEcdMVGISRPVVK-HSFLVKQTE--DIPQVLKKafwLAASGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 162 PGYLMV--PADVAKKAATPPV---NALTLQPADADNACLKAFRDAARVRLAMAQRTALLADFLVLRHGLKPALQKWVKEV 236
Cdd:PRK07979 154 PGPVVVdlPKDILNPANKLPYvwpESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 237 PMAHATMLMGKGIF--DERQA----GFYGTYSGSasaapvkEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPH 310
Cdd:PRK07979 234 NLPVVSSLMGLGAFpaTHRQSlgmlGMHGTYEAN-------MTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 311 ASRVGDVWFTGIPMI--------QAIETLAELCKEHVHDSPAPFVNNDIAW--------PTEGGSLTQESFWSTLQTFIR 374
Cdd:PRK07979 307 PTSISKTVTADIPIVgdarqvleQMLELLSQESAHQPLDEIRDWWQQIEQWrarqclkyDTHSEKIKPQAVIETLWRLTK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 PGDIILADQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQ 453
Cdd:PRK07979 387 GDAYVTSDVGQhQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYEL 466
|
....*....
gi 2216604589 454 RPVILVLNN 462
Cdd:PRK07979 467 PVLVLNLNN 475
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
19-465 |
1.01e-14 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 76.79 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 19 GADHLFGVPGDYNLQFLDHVIDSPdICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNGIAGSFAEHVPVL 97
Cdd:PRK08322 15 GVEYIFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGKAGVcLSTLGPGATNLVTGVAYAQLGGMPMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 98 HIVGAPGMASQQRGellhhtlgdgefRHFY----HMSEPIT--AAQaILTEQNacyeidrvLTTMLRE-------RRPG- 163
Cdd:PRK08322 94 AITGQKPIKRSKQG------------SFQIvdvvAMMAPLTkwTRQ-IVSPDN--------IPEVVREafrlaeeERPGa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 164 -YLMVPADVAKKAATPPVnaLTLQPADADNACLKAFRDAARVrLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHAT 242
Cdd:PRK08322 153 vHLELPEDIAAEETDGKP--LPRSYSRRPYASPKAIERAAEA-IQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 243 MLMGKGIFDERQAGFYGTySGSASAAPVKEAIEGADTVLCIGtrftdtltagftHQLtaaqtIEVQP------------- 309
Cdd:PRK08322 230 TQMGKGVIPETHPLSLGT-AGLSQGDYVHCAIEHADLIINVG------------HDV-----IEKPPffmnpngdkkvih 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 310 ---HASRVGDVWFTGIPMI----QAIETLAELCKEHVHDSPAPFVN--NDIAWPTEGGSlTQESFWSTLQTFIR------ 374
Cdd:PRK08322 292 infLPAEVDPVYFPQVEVVgdiaNSLWQLKERLADQPHWDFPRFLKirEAIEAHLEEGA-DDDRFPMKPQRIVAdlrkvm 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 -PGDIILADQGtsafgaidlrlpaevnfiVQPLW-------------------GSIGYTLAAAFGAQTACPNRRVIVLTG 434
Cdd:PRK08322 371 pDDDIVILDNG------------------AYKIWfarnyrayepntclldnalATMGAGLPSAIAAKLVHPDRKVLAVCG 432
|
490 500 510
....*....|....*....|....*....|.
gi 2216604589 435 DGAAQLTIQEMGSMLRDKQRPVILVLNNEGY 465
Cdd:PRK08322 433 DGGFMMNSQELETAVRLGLPLVVLILNDNAY 463
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
8-530 |
1.93e-14 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 76.04 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQF---LDHVidsPDICWVGCANELNASYAADGYARCKGF-AALLTTFGVGelsAM 83
Cdd:PRK07586 4 AESLVRTLVDGGVDVCFANPGTSEMHFvaaLDRV---PGMRCVLGLFEGVATGAADGYARMAGKpAATLLHLGPG---LA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 84 NGIAG---SFAEHVPVLHIVG----------APgMASqqRGELLHHTLGdgefrHFYHMSEPIT-----AAQAIlteQNA 145
Cdd:PRK07586 78 NGLANlhnARRARTPIVNIVGdhatyhrkydAP-LTS--DIEALARPVS-----GWVRRSESAAdvaadAAAAV---AAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 146 CYEIDRVLTtmlrerrpgyLMVPADVAKKAATPPVNALTL-QPADADNAclkAFRDAARVrLAMAQRTALLADFLVLR-H 223
Cdd:PRK07586 147 RGAPGQVAT----------LILPADVAWSEGGPPAPPPPApAPAAVDPA---AVEAAAAA-LRSGEPTVLLLGGRALReR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 224 GLKPALQ-------KWVKEvpMAHATMLMGKGIFD-ERQAGFygtysgsasAAPVKEAIEGADTVLCIGTRftdTLTAGF 295
Cdd:PRK07586 213 GLAAAARiaaatgaRLLAE--TFPARMERGAGRPAvERLPYF---------AEQALAQLAGVRHLVLVGAK---APVAFF 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 296 THQ----LTAAQTIEVQPHASRVGDVwftgipmIQAIETLAE-LCKEhvhdSPAPFVNNDIAWPTEGGSLTQESFWSTLQ 370
Cdd:PRK07586 279 AYPgkpsRLVPEGCEVHTLAGPGEDA-------AAALEALADaLGAK----PAAPPLAAPARPPLPTGALTPEAIAQVIA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 371 TFIRPGDIILADQGTSAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLR 450
Cdd:PRK07586 348 ALLPENAIVVDESITSGRGFFPATAGAAPHDWLTLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQAR 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 451 DKQRPVILVLNNEGYTV--------------ERA-----IHGPEqryndialWNWTQIPQALSldpqAECYRVSEAEQLA 511
Cdd:PRK07586 428 ENLDVTTVIFANRAYAIlrgelarvgagnpgPRAldmldLDDPD--------LDWVALAEGMG----VPARRVTTAEEFA 495
|
570 580
....*....|....*....|
gi 2216604589 512 DVLEKvAHHER-LSLIEVML 530
Cdd:PRK07586 496 DALAA-ALAEPgPHLIEAVV 514
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
8-462 |
2.68e-14 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 75.63 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGI 86
Cdd:PRK08979 7 ASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIvgapgmasqqRGELLHHTLGDGEFRH--FYHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPGY 164
Cdd:PRK08979 87 ATAYMDSIPMVVL----------SGQVPSNLIGNDAFQEcdMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 165 LMVpaDVAKKAATPPVNALTLQPADADNACLKAFRDAARVRLAMAQRTALLADFLVLRHG-------LKPALQKWVKEVP 237
Cdd:PRK08979 157 VVI--DLPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGggaiisgADKQILQLAEKLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 238 MAHATMLMGKGIFDERQA------GFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHA 311
Cdd:PRK08979 235 LPVVSTLMGLGAFPGTHKnslgmlGMHGRYEANM-------AMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 312 SRVGDVWFTGIPMI----QAIETLAELCKEHVHDSPAPFVN------------NDIAWPTEGGSLTQESFWSTLQTFIRP 375
Cdd:PRK08979 308 SSISKTVRVDIPIVgsadKVLDSMLALLDESGETNDEAAIAswwneievwrsrNCLAYDKSSERIKPQQVIETLYKLTNG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 376 GDIILADQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRdKQR 454
Cdd:PRK08979 388 DAYVASDVGQhQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQ-YDI 466
|
....*....
gi 2216604589 455 PV-ILVLNN 462
Cdd:PRK08979 467 PVkIINLNN 475
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
375-530 |
3.23e-14 |
|
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: 70.70 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 PGDIILADQGTSAFGAIDLRLP-AEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQ 453
Cdd:cd02002 15 PEDAIIVDEAVTNGLPLRDQLPlTRPGSYFTLRGGGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 454 RPVILVLNNEGYTVER-------AIHGPEQRYNDIALW----NWTQIpqALSLDPQAEcyRVSEAEQLADVLEKVAHHER 522
Cdd:cd02002 95 PVTVVILNNRGYGALRsflkrvgPEGPGENAPDGLDLLdpgiDFAAI--AKAFGVEAE--RVETPEELDEALREALAEGG 170
|
....*...
gi 2216604589 523 LSLIEVML 530
Cdd:cd02002 171 PALIEVVV 178
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
199-334 |
1.56e-13 |
|
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: 67.59 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 199 RDAARvRLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHATMLMGKGIFDERQAGFYGtYSGSASAAPVKEAIEGAD 278
Cdd:pfam00205 2 EKAAE-LLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2216604589 279 TVLCIGTRFTDTLTAGFTHQLT-AAQTIEVQPHASRVGDVWFTGIPMI-QAIETLAEL 334
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFApDAKIIHIDIDPAEIGKNYPVDVPIVgDAKETLEAL 137
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
8-463 |
2.91e-13 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 72.46 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNGI 86
Cdd:PLN02470 16 ADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVcIATSGPGATNLVTGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVgapgmasqqrGELLHHTLGDGEFRHfyhmsEPITAAQAILTEQNacY------EIDRVLTT---ML 157
Cdd:PLN02470 96 ADALLDSVPLVAIT----------GQVPRRMIGTDAFQE-----TPIVEVTRSITKHN--YlvmdveDIPRVIREaffLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 158 RERRPGYLMV--PADVAKKAATP----PVNA---LTLQPADADNACLKAFrdaarVRL-AMAQRTALLADFLVLRHGlkP 227
Cdd:PLN02470 159 SSGRPGPVLVdiPKDIQQQLAVPnwnqPMKLpgyLSRLPKPPEKSQLEQI-----VRLiSESKRPVVYVGGGCLNSS--E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 228 ALQKWVKEVPMAHATMLMGKGIF---DERQAGFYGTYsGSASAapvKEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQT 304
Cdd:PLN02470 232 ELREFVELTGIPVASTLMGLGAFpasDELSLQMLGMH-GTVYA---NYAVDSADLLLAFGVRFDDRVTGKLEAFASRASI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 305 IEV-----------QPHASRVGDVwftgIPMIQAIETLAELCKEHVHDSPA-------PFVNNDIAWPTEGGSLTQESFW 366
Cdd:PLN02470 308 VHIdidpaeigknkQPHVSVCADV----KLALQGLNKLLEERKAKRPDFSAwraeldeQKEKFPLSYPTFGDAIPPQYAI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 367 STLQTFIRPGDIILADQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEM 445
Cdd:PLN02470 384 QVLDELTDGNAIISTGVGQhQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQEL 463
|
490
....*....|....*....
gi 2216604589 446 GSmLRDKQRPV-ILVLNNE 463
Cdd:PLN02470 464 AT-IHVENLPVkIMVLNNQ 481
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
8-530 |
1.31e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 70.29 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGF-AALLTTFGVGELSAMNGI 86
Cdd:PRK12474 8 ADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKpAVTLLHLGPGLANGLANL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVGAPGMASQQRGELLHHTLgDGEFRHFYHMSEPITAAQAILTEQNACYEIDRVLTtmlrerrPGY-- 164
Cdd:PRK12474 88 HNARRAASPIVNIVGDHAVEHLQYDAPLTSDI-DGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAP-------GGIat 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 165 LMVPADVAKKA---ATPPVNALTLQPADADN--ACLKAFRDAARVRLAM------------AQRTALLADFLVLRHGLKP 227
Cdd:PRK12474 160 LIMPADVAWNEaayAAQPLRGIGPAPVAAETveRIAALLRNGKKSALLLrgsalrgapleaAGRIQAKTGVRLYCDTFAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 228 ALQKWVKEVPMAHATMlmgkgiFDERQAGFygtysgsasaapvkeaIEGADTVLCIGTR-----FTDTLTAGFTHQLTAA 302
Cdd:PRK12474 240 RIERGAGRVPIERIPY------FHEQITAF----------------LKDVEQLVLVGAKppvsfFAYPGKPSWGAPPGCE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 303 QTIEVQPHASrvgdvwftgipMIQAIETLAELCkehvhDSPA-PFVNNDIAWPT-EGGSLTQESFWSTLQTFIrPGDIIL 380
Cdd:PRK12474 298 IVYLAQPDED-----------LAQALQDLADAV-----DAPAePAARTPLALPAlPKGALNSLGVAQLIAHRT-PDQAIY 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 381 ADQGTSAFGAIDLRLP-AEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILV 459
Cdd:PRK12474 361 ADEALTSGLFFDMSYDrARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 460 LNNEGYTV-----ERA--------------IHGPEQryndialwNWTQIPQALSLdpqaECYRVSEAEQLADVLEKVAHH 520
Cdd:PRK12474 441 FANRSYAIlngelQRVgaqgagrnalsmldLHNPEL--------NWMKIAEGLGV----EASRATTAEEFSAQYAAAMAQ 508
|
570
....*....|
gi 2216604589 521 ERLSLIEVML 530
Cdd:PRK12474 509 RGPRLIEAMI 518
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
7-538 |
1.33e-12 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 70.32 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYN---LQFLDHVIDSPDicWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSA 82
Cdd:PRK08273 5 VADFILERLREWGVRRVFGYPGDGInglLGALGRADDKPE--FVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGAIHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 83 MNGIAGSFAEHVPVLHIVG-----APGMASQQrgEL-LHHTLGD--GEFRHfyhmsepitaaQAILTEQnACYEIDRVLT 154
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVGqqaraALGGHYQQ--EVdLQSLFKDvaGAFVQ-----------MVTVPEQ-LRHLVDRAVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 155 TMLRERRPGYLMVPADVAKKAATPPVNAL------------TLQPADADnaclkaFRDAARVrLAMAQRTALLADflvlr 222
Cdd:PRK08273 149 TALAERTVTAVILPNDVQELEYEPPPHAHgtvhsgvgytrpRVVPYDED------LRRAAEV-LNAGRKVAILVG----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 223 HGLKPALQKwVKEVpmAH------ATMLMGKGIFDER------QAGFYGTysgsasaAPVKEAIEGADTVLCIGTRF--T 288
Cdd:PRK08273 217 AGALGATDE-VIAV--AErlgagvAKALLGKAALPDDlpwvtgSIGLLGT-------KPSYELMRECDTLLMVGSSFpyS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 289 DTLTAgfTHQLTAAQtIEVQPH---------ASRVGDVWFT---GIPMIQ-------------AIETLAELCKEHVHDSP 343
Cdd:PRK08273 287 EFLPK--EGQARGVQ-IDIDGRmlglrypmeVNLVGDAAETlraLLPLLErkkdrswreriekWVARWWETLEARAMVPA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 344 APfVNndiawPteggsltQESFWStLQTFIRPGDIILADQGTSAFG-AIDLRLPAEVNfivqplwGSIGYTLAA------ 416
Cdd:PRK08273 364 DP-VN-----P-------QRVFWE-LSPRLPDNAILTADSGSCANWyARDLRMRRGMM-------ASLSGTLATmgpavp 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 417 -AFGAQTACPNRRVIVLTGDGAAQLT-IQEM---GSMLRDKQRP--VILVLNNegytveraihgpeqryNDIALWNWTQi 489
Cdd:PRK08273 423 yAIAAKFAHPDRPVIALVGDGAMQMNgMAELitvAKYWRQWSDPrlIVLVLNN----------------RDLNQVTWEQ- 485
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2216604589 490 pQALSLDPQAEC--------Y------------RVSEAEQLADVLEKVAHHERLSLIEVMLpKADIPPL 538
Cdd:PRK08273 486 -RVMEGDPKFEAsqdlpdvpYarfaellglkgiRVDDPEQLGAAWDEALAADRPVVLEVKT-DPNVPPL 552
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
8-462 |
2.08e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 69.61 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSpDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGI 86
Cdd:PRK06725 18 AGHVIQCLKKLGVTTVFGYPGGAILPVYDALYES-GLKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVGAP-----GMASQQRGELLHHTLgdgefrhfyhmsePITAAQAILTEQNACYEIDRVLTTMLRERR 161
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVatpliGKDGFQEADVVGITV-------------PVTKHNYQVRDVNQLSRIVQEAFYIAESGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 162 PGYLM--VPADVAKKAATPPVNALTLQPA-----DADNACLKAFRDAARvrlaMAQRTALLADFLVLRHGLKPALQKWVK 234
Cdd:PRK06725 164 PGPVLidIPKDVQNEKVTSFYNEVVEIPGykpepRPDSMKLREVAKAIS----KAKRPLLYIGGGVIHSGGSEELIEFAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 235 EVPMAHATMLMGKGIFDERQA------GFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQ 308
Cdd:PRK06725 240 ENRIPVVSTLMGLGAYPPGDPlflgmlGMHGTYAANM-------AVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHID 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 309 PHASR-----------VGDV---WFTGIPMIQAIETLAELCKEHVHDSPAPfvnndIAWPTEGGSLTQESFWSTLQTFIR 374
Cdd:PRK06725 313 IDPSEfhknvaveypvVGDVkkaLHMLLHMSIHTQTDEWLQKVKTWKEEYP-----LSYKQKESELKPQHVINLVSELTN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 PGDIILADQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQ 453
Cdd:PRK06725 388 GEAIVTTEVGQhQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNI 467
|
....*....
gi 2216604589 454 RPVILVLNN 462
Cdd:PRK06725 468 PVKVFIINN 476
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
8-463 |
5.57e-12 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 68.20 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAA-LLTTFGVGELSAMNGI 86
Cdd:PRK09107 14 AEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGvVLVTSGPGATNAVTPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVGapgmasqqrgELLHHTLGDGEFRH--FYHMSEPITAAQAILTEQN----ACYEIDRVLTTmlreR 160
Cdd:PRK09107 94 QDALMDSIPLVCITG----------QVPTHLIGSDAFQEcdTVGITRPCTKHNWLVKDVNdlarVIHEAFHVATS----G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 161 RPGYLMV--PADV--AKKAATPPVNALTL---QPADADNAclKAFRDAARVrLAMAQRTALLADFLVLRHGlkPALQKWV 233
Cdd:PRK09107 160 RPGPVVVdiPKDVqfATGTYTPPQKAPVHvsyQPKVKGDA--EAITEAVEL-LANAKRPVIYSGGGVINSG--PEASRLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 234 KEvpMAHAT------MLMGKGIFDER------QAGFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTA 301
Cdd:PRK09107 235 RE--LVELTgfpitsTLMGLGAYPASgknwlgMLGMHGTYEANM-------AMHDCDVMLCVGARFDDRITGRLDAFSPN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 302 AQTIEVQPHASRVGDVWFTGIPMI-QAIETLAELCKEHVHDSPAPFVNNDIAWpteggsLTQESFWSTLQ--TFIRPGDI 378
Cdd:PRK09107 306 SKKIHIDIDPSSINKNVRVDVPIIgDVGHVLEDMLRLWKARGKKPDKEALADW------WGQIARWRARNslAYTPSDDV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 379 ILADQGTSAFGAI----DLRLPAEV-----------NFIVQPLW------GSIGYTLAAAFGAQTACPNRRVIVLTGDGA 437
Cdd:PRK09107 380 IMPQYAIQRLYELtkgrDTYITTEVgqhqmwaaqffGFEEPNRWmtsgglGTMGYGLPAALGVQIAHPDALVIDIAGDAS 459
|
490 500
....*....|....*....|....*..
gi 2216604589 438 AQLTIQEMGSMLRDKQrPV-ILVLNNE 463
Cdd:PRK09107 460 IQMCIQEMSTAVQYNL-PVkIFILNNQ 485
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
367-530 |
6.19e-12 |
|
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: 64.09 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 367 STLQTFIRPGDIILADQG-TSAFGA--IDLRLPAEVnfivqpL----WGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQ 439
Cdd:cd02004 6 HELQEALPDDAIIVSDGGnTMDWARyiLRPRKPRHR------LdagtFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 440 LTIQEMGSMLRDKQRPVILVLNNEGYtveraihgpeQRYNDIALWNWTQIPQALSLDPQAE-----------CYRVSEAE 508
Cdd:cd02004 80 FSGMELETAVRYNLPIVVVVGNNGGW----------YQGLDGQQLSYGLGLPVTTLLPDTRydlvaeafggkGELVTTPE 149
|
170 180
....*....|....*....|..
gi 2216604589 509 QLADVLEKVAHHERLSLIEVML 530
Cdd:cd02004 150 ELKPALKRALASGKPALINVII 171
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
8-463 |
2.13e-11 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 66.32 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSpDICWVGCANELNASYAADGYARCKGF-AALLTTFGVGELSAMNGI 86
Cdd:PRK07710 19 AQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDC-GIPHILTRHEQGAIHAAEGYARISGKpGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVGAP-----GMASQQRGELLHHTLGDGefRHFYHMSEPITAAQAIlteqnacYEIDRVLTTmlreRR 161
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVatsviGSDAFQEADIMGITMPVT--KHNYQVRKASDLPRII-------KEAFHIATT----GR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 162 PGYLMV--PADVAKKAAT----PPVNALTLQPADADNAC-LKAFRDAarvrLAMAQRTALLADFLVLRHGLKPALQKWVK 234
Cdd:PRK07710 165 PGPVLIdiPKDMVVEEGEfcydVQMDLPGYQPNYEPNLLqIRKLVQA----VSVAKKPVILAGAGVLHAKASKELTSYAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 235 --EVPMAHAtmLMGKGIFDERQ------AGFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIE 306
Cdd:PRK07710 241 qqEIPVVHT--LLGLGGFPADHplflgmAGMHGTYTANM-------ALYECDLLINIGARFDDRVTGNLAYFAKEATVAH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 307 VQPHASRVGDVWFTGIPMI-QAIETLAELCK-----EHVHDSPAPFVNNDIAWP----TEGGSLTQESFWSTLQTFIRPG 376
Cdd:PRK07710 312 IDIDPAEIGKNVPTEIPIVaDAKQALQVLLQqegkkENHHEWLSLLKNWKEKYPlsykRNSESIKPQKAIEMLYEITKGE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 377 DIILADQGTSAFGAID---LRLPAEvnFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMgSMLRDKQ 453
Cdd:PRK07710 392 AIVTTDVGQHQMWAAQyypFKTPDK--WVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQEL-SVIKELS 468
|
490
....*....|.
gi 2216604589 454 RPV-ILVLNNE 463
Cdd:PRK07710 469 LPVkVVILNNE 479
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
7-541 |
2.43e-11 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 66.16 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNG 85
Cdd:PRK09124 5 VADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGeLAVCAGSCGPGNLHLING 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIvgAPGMASQQRG----------ELlhhtlgdgeFRHFYHMSEPITAAQailteqnacyEIDRVLTT 155
Cdd:PRK09124 85 LFDCHRNHVPVLAI--AAHIPSSEIGsgyfqethpqEL---------FRECSHYCELVSNPE----------QLPRVLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 156 MLR----ERRPGYLMVPADVAKKAA-------TPPVNALTLQPADADNACLKA-FRDAARVRLAMAQRTALLADFLVlrh 223
Cdd:PRK09124 144 AMRkailNRGVAVVVLPGDVALKPAperatphWYHAPQPVVTPAEEELRKLAAlLNGSSNITLLCGSGCAGAHDELV--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 224 GLKPALQkwvkeVPMAHAtmLMGK------GIFDERQAGFYGTYSGSasaapvkEAIEGADTVLCIGTRFtdTLTAGFTH 297
Cdd:PRK09124 221 ALAETLK-----APIVHA--LRGKehveydNPYDVGMTGLIGFSSGY-------HAMMNCDTLLMLGTDF--PYRQFYPT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 298 QLTAAQtIEVQPHA--SR-------VGDVWFTG---IPMIQAIETLAELCKEHVHDSPAPFVNNDIAWPTEGGSLTQESF 365
Cdd:PRK09124 285 DAKIIQ-IDINPGSlgRRspvdlglVGDVKATLaalLPLLEEKTDRKFLDKALEHYRKARKGLDDLAVPSDGGKPIHPQY 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 366 WSTLQTFIRPGDIIL-ADQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGA-AQLti 442
Cdd:PRK09124 364 LARQISEFAADDAIFtCDVGTpTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGfSML-- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 443 qeMGSMLRDKQR--PV-ILVLNNE------------GY-TVERAIHGPeqryndialwNWTQIPQALSLdpqaECYRVSE 506
Cdd:PRK09124 442 --MGDFLSLVQLklPVkIVVFNNSvlgfvamemkagGYlTDGTDLHNP----------DFAAIAEACGI----TGIRVEK 505
|
570 580 590
....*....|....*....|....*....|....*..
gi 2216604589 507 AEQLADVLEKVAHHERLSLIEVMLPKAD--IPPLLGA 541
Cdd:PRK09124 506 ASELDGALQRAFAHDGPALVDVVTAKQElaMPPQIKL 542
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
8-462 |
7.88e-11 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 64.47 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVID---SPDICWVGCANELNASYAADGYARCKGFAALLT-TFGVGELSAM 83
Cdd:PRK06456 5 ARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlaNGELRHVLMRHEQAAAHAADGYARASGVPGVCTaTSGPGTTNLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 84 NGIAGSFAEHVPVLHIVG-----APGMASQQRGELLhhtlgdGEFRHFYHMSEPITAAQAI-LTEQNACYeidrVLTTml 157
Cdd:PRK06456 85 TGLITAYWDSSPVIAITGqvprsVMGKMAFQEADAM------GVFENVTKYVIGIKRIDEIpQWIKNAFY----IATT-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 158 reRRPGYLMV--PADV-------AKKAATPPVNALTLQPADADNACLKafrDAARVrLAMAQRTALLADFLVLRHGLKPA 228
Cdd:PRK06456 153 --GRPGPVVIdiPRDIfyekmeeIKWPEKPLVKGYRDFPTRIDRLALK---KAAEI-LINAERPIILVGTGVVWSNATPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 229 LQKWVKEVPMAHATMLMGKGIFDERQAGFYGT--YSGSASAApvKEAIEgADTVLCIGTRFTD-TLTAGFTHQLTAAQTI 305
Cdd:PRK06456 227 VLELAELLHIPIVSTFPGKTAIPHDHPLYFGPmgYYGRAEAS--MAALE-SDAMLVVGARFSDrTFTSYDEMVETRKKFI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 306 EV-----------QPHASRVGDVWFTGIPMIQAIetlAELCKEHVHDSPAPFVN------NDIAWPTEGGSLTQesfWST 368
Cdd:PRK06456 304 MVnidptdgekaiKVDVGIYGNAKIILRELIKAI---TELGQKRDRSAWLKRVKeykeyySQFYYTEENGKLKP---WKI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 369 LQTfIR---PGDIILadqgTSAFGaiDLRLPAEV--------NFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGA 437
Cdd:PRK06456 378 MKT-IRqalPRDAIV----TTGVG--QHQMWAEVfwevleprTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGS 450
|
490 500
....*....|....*....|....*
gi 2216604589 438 AQLTIQEMGSMLrDKQRPVILVLNN 462
Cdd:PRK06456 451 FLMTGTNLATAV-DEHIPVISVIFD 474
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
10-463 |
5.69e-10 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 62.03 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 10 YLLDRLtdcGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNGIAG 88
Cdd:PRK08155 21 RLLERQ---GIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVcMACSGPGATNLVTAIAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 89 SFAEHVPVLHIVG--APGMasqqrgellhhtLGDGEFRHF--YHMSEPITAAQAILTEQNacyEIDRVLTTMLR---ERR 161
Cdd:PRK08155 98 ARLDSIPLVCITGqvPASM------------IGTDAFQEVdtYGISIPITKHNYLVRDIE---ELPQVISDAFRiaqSGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 162 PGYLMV--PADVakKAATPPVNALTlQPADADNAC---LKAFRDAARVrLAMAQRTALLADFLVLRHGLKPALQKWVKEV 236
Cdd:PRK08155 163 PGPVWIdiPKDV--QTAVIELEALP-APAEKDAAPafdEESIRDAAAM-INAAKRPVLYLGGGVINSGAPARARELAEKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 237 PMAHATMLMGKGIFDERQAGFYGTYsGSASAAPVKEAIEGADTVLCIGTRFTDTLTaGFTHQLTA-AQTIEV-------- 307
Cdd:PRK08155 239 QLPTTMTLMALGMLPKAHPLSLGML-GMHGARSTNYILQEADLLIVLGARFDDRAI-GKTEQFCPnAKIIHVdidraelg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 308 ---QPH---ASRVGDVWFTGIPMIQA------IETLAELCKEHvhdspaPFvnndiAWPTEGGSLTQESFWSTLQTFIRP 375
Cdd:PRK08155 317 kikQPHvaiQADVDDVLAQLLPLVEAqpraewHQLVADLQREF------PC-----PIPKADDPLSHYGLINAVAACVDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 376 GDIILADQGTSAF---GAIDLRLPAEvnfivqplW------GSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMG 446
Cdd:PRK08155 386 NAIITTDVGQHQMwtaQAYPLNRPRQ--------WltsgglGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMA 457
|
490
....*....|....*..
gi 2216604589 447 SMLRDKQRPVILVLNNE 463
Cdd:PRK08155 458 TAAENQLDVKIILMNNE 474
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
8-462 |
1.12e-09 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 60.97 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 8 ADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNGI 86
Cdd:PRK06965 24 AEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGkVGVALVTSGPGVTNAVTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 87 AGSFAEHVPVLHIVG-----APGMASQQRGEllhhTLGdgefrhfyhMSEPITAAQAILTEQNACYEIDRVLTTMLRERR 161
Cdd:PRK06965 104 ATAYMDSIPMVVISGqvptaAIGQDAFQECD----TVG---------ITRPIVKHNFLVKDVRDLAETVKKAFYIARTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 162 PGYLMV--PADVAKKAA--TPP--VNALTLQPADADNAclKAFRDAARVRLAmAQRTALLADFLVLRHGLKPALQKWVKE 235
Cdd:PRK06965 171 PGPVVVdiPKDVSKTPCeyEYPksVEMRSYNPVTKGHS--GQIRKAVSLLLS-AKRPYIYTGGGVILANASRELRQLADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 236 VPMAHATMLMGKGIF---DER---QAGFYGTYSGSasaapvkEAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTI---E 306
Cdd:PRK06965 248 LGYPVTNTLMGLGAYpasDKKflgMLGMHGTYEAN-------MAMQHCDVLIAIGARFDDRVIGNPAHFASRPRKIihiD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 307 VQPH--ASRVGdvwfTGIPMIQAI-ETLAELCKEHVHDSPAPfvnndiawptEGGSLTQesFWSTLQ--------TFIRP 375
Cdd:PRK06965 321 IDPSsiSKRVK----VDIPIVGDVkEVLKELIEQLQTAEHGP----------DADALAQ--WWKQIEgwrsrdclKYDRE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 376 GDII-----------LADQG---TSAFGAIDLRLPAEVNFIVQPLW------GSIGYTLAAAFGAQTACPNRRVIVLTGD 435
Cdd:PRK06965 385 SEIIkpqyvveklweLTDGDafvCSDVGQHQMWAAQFYRFNEPRRWinsgglGTMGVGLPYAMGIKMAHPDDDVVCITGE 464
|
490 500
....*....|....*....|....*..
gi 2216604589 436 GAAQLTIQEMGSMLRDKQRPVILVLNN 462
Cdd:PRK06965 465 GSIQMCIQELSTCLQYDTPVKIISLNN 491
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
7-462 |
2.03e-09 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 60.23 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDyNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNG 85
Cdd:PRK06457 4 VAEVIIRVLEDNGIQRIYGIPGD-SIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGkPSACMGTSGPGSIHLLNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIVGapgmasQQRGELLHHTLGDgEFRHFYHMSEPITAAQAILTEQNACYEIDRVLTTMLRERRPGYL 165
Cdd:PRK06457 83 LYDAKMDHAPVIALTG------QVESDMIGHDYFQ-EVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKRGVAHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 166 MVPADVAKKAA--TPPVNALTLQP---ADADNAclKAFRDAARVRLAMAQRTAlladflvlrHGLKPALQKWVKEV--PM 238
Cdd:PRK06457 156 NLPVDILRKSSeyKGSKNTEVGKVkysIDFSRA--KELIKESEKPVLLIGGGT---------RGLGKEINRFAEKIgaPI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 239 AHAtmLMGKGIFDERQAGFYGTYsGSASAAPVKEAIEGADTVLCIGTRFTdtlTAGFTHQltAAQTIEVQPHASRVGDVW 318
Cdd:PRK06457 225 IYT--LNGKGILPDLDPKVMGGI-GLLGTKPSIEAMDKADLLIMLGTSFP---YVNFLNK--SAKVIQVDIDNSNIGKRL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 319 FTGIPMIQaieTLAELCKEHVHDSPAPF---VNNDIA-WPTEggsltQESFWSTLQTFIRP-------------GDIILA 381
Cdd:PRK06457 297 DVDLSYPI---PVAEFLNIDIEEKSDKFyeeLKGKKEdWLDS-----ISKQENSLDKPMKPqrvayivsqkckkDAVIVT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 382 DQGT-SAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPN-RRVIVLTGDGAAQLTIQEMGSMlRDKQRPV-IL 458
Cdd:PRK06457 369 DTGNvTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVENkRQVISFVGDGGFTMTMMELITA-KKYDLPVkII 447
|
....
gi 2216604589 459 VLNN 462
Cdd:PRK06457 448 IYNN 451
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
375-516 |
4.10e-09 |
|
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: 56.36 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 375 PGDIILA-DQG-TSAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDK 452
Cdd:cd02013 18 PEDAIVStDIGnICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMMEIMTAVRHK 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2216604589 453 QRPVILVLNNEGYTVERAihgpeqryNDIALWN----WTQIPqALSLDPQAECY-----RVSEAEQLADVLEK 516
Cdd:cd02013 98 LPVTAVVFRNRQWGAEKK--------NQVDFYNnrfvGTELE-SESFAKIAEACgakgiTVDKPEDVGPALQK 161
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
19-530 |
5.34e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 58.57 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 19 GADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGELSAMNGIAGSFAEHVPVL 97
Cdd:PRK08527 17 GVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVaIVTSGPGFTNAVTGLATAYMDSIPLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 98 HIVGAPGMAsqqrgellhhTLGDGEFRHF--YHMSEPITAAQAILTEQNacyEIDRVLTT---MLRERRPG--YLMVPAD 170
Cdd:PRK08527 97 LISGQVPNS----------LIGTDAFQEIdaVGISRPCVKHNYLVKSIE---ELPRILKEafyIARSGRPGpvHIDIPKD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 171 V----AKKAATPPVNALTLQPADADNAclKAFRDAARVrLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHATMLMG 246
Cdd:PRK08527 164 VtatlGEFEYPKEISLKTYKPTYKGNS--RQIKKAAEA-IKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 247 KGIFDERQ------AGFYGTYSGSAsaapvkeAIEGADTVLCIGTRFTDTLTAGFTHQLTAAQTIEVQPHASRVGDVWFT 320
Cdd:PRK08527 241 RGVLRSDDplllgmLGMHGSYAANM-------AMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 321 GIPMI----QAIETLAELCKEHVHDSPAPFV----------------NNDIAWPTeggsltqesfWSTLQTFIRPGD--I 378
Cdd:PRK08527 314 DYPIVgdlkNVLKEMLEELKEENPTTYKEWReilkrynelhplsyedSDEVLKPQ----------WVIERVGELLGDdaI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 379 ILADQG-----TSAFGAIDLrlPAEvnFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLrDKQ 453
Cdd:PRK08527 384 ISTDVGqhqmwVAQFYPFNY--PRQ--LATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAV-EYK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 454 RPVI-LVLNNE--GYTVERAIHGPEQRYN--DIALW-NWTQIPQALSldpqAECYRVSEAEQLADVLEKVAHHERLSLIE 527
Cdd:PRK08527 459 IPVInIILNNNflGMVRQWQTFFYEERYSetDLSTQpDFVKLAESFG----GIGFRVTTKEEFDKALKEALESDKVALID 534
|
...
gi 2216604589 528 VML 530
Cdd:PRK08527 535 VKI 537
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
7-537 |
6.63e-09 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 58.46 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 7 VADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKG-FAALLTTFGVGELSAMNG 85
Cdd:PRK06546 5 VAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGkLAVCAGSCGPGNLHLING 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 86 IAGSFAEHVPVLHIvgAPGMASQQRG-ELLHHTLGDGEFRHFYHMSEPI-TAAQAilteqnacyeiDRVLTTMLRER--R 161
Cdd:PRK06546 85 LYDAHRSGAPVLAI--ASHIPSAQIGsGFFQETHPDRLFVECSGYCEMVsSAEQA-----------PRVLHSAIQHAvaG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 162 PGY--LMVPADVA-KKAATPPVNAL------TLQPADADNACL-KAFRDAARVRLAMAQRTALLADFLVlrhglkpALQK 231
Cdd:PRK06546 152 GGVsvVTLPGDIAdEPAPEGFAPSVisprrpTVVPDPAEVRALaDAINEAKKVTLFAGAGVRGAHAEVL-------ALAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 232 WVKeVPMAHAtmLMGKGI------FDERQAGFYGtYsGSASaapvkEAIEGADTVLCIGTRFTDTltaGFTHQLTAAQtI 305
Cdd:PRK06546 225 KIK-APVGHS--LRGKEWiqydnpFDVGMSGLLG-Y-GAAH-----EAMHEADLLILLGTDFPYD---QFLPDVRTAQ-V 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 306 EVQP-HASR--------VGDVWFTG---IPMIQAIET---LAELCKEHvhdspAPFVNNDI-AWPTEGGSLT---QESFW 366
Cdd:PRK06546 291 DIDPeHLGRrtrvdlavHGDVAETIralLPLVKEKTDrrfLDRMLKKH-----ARKLEKVVgAYTRKVEKHTpihPEYVA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 367 STLQTFIRPGDIILADQG-TSAFGAIDLRLPAEVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTiqeM 445
Cdd:PRK06546 366 SILDELAADDAVFTVDTGmCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSML---L 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 446 GSMLRDKQR--PV-ILVLNNEGY---TVERAIHGPEQRYNDIALWNWTQIPQALSLdpqaECYRVSEAEQLADVLEKVAH 519
Cdd:PRK06546 443 GELLTVKLYdlPVkVVVFNNSTLgmvKLEMLVDGLPDFGTDHPPVDYAAIAAALGI----HAVRVEDPKDVRGALREAFA 518
|
570 580
....*....|....*....|
gi 2216604589 520 HERLSLIEVML-PKA-DIPP 537
Cdd:PRK06546 519 HPGPALVDVVTdPNAlSIPP 538
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
409-528 |
1.41e-08 |
|
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: 54.60 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 409 SIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVER---AIHGPEQRYNDIALWN 485
Cdd:cd02010 49 TMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGYGLIKwkqEKEYGRDSGVDFGNPD 128
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2216604589 486 WTQIPQALSldpqAECYRVSEAEQLADVLEKVAHHERLSLIEV 528
Cdd:cd02010 129 FVKYAESFG----AKGYRIESADDLLPVLERALAADGVHVIDC 167
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
52-482 |
2.31e-08 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 56.65 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 52 ELNASYAADGYA---RCKGFAALltTFGVGELSAMNGIAGSFAEHVPVLhIVGapGMASQQRgellhhtLGDGEFRHFYH 128
Cdd:PRK05858 51 EQTAAFAAEAWAkltRVPGVAVL--TAGPGVTNGMSAMAAAQFNQSPLV-VLG--GRAPALR-------WGMGSLQEIDH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 129 --MSEPITA-AQAILTEQNACYEIDRVLTTMLRERR-PGYLMVPADVAKKAATPPVNALTLQPADADNACLKAFRDAARV 204
Cdd:PRK05858 119 vpFVAPVTKfAATAQSAENAGRLVDQALQAAVTPHRgPVFVDFPMDHAFSMADDDGRPGALTELPAGPTPDPDALARAAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 205 RLAMAQRTALLADFLVLRHGLKPALQKWVKEVPMAHATMLMGKGIF--DERQAgfygtYSGSASAApvkeaIEGADTVLC 282
Cdd:PRK05858 199 LLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVpaDHPLA-----FSRARGKA-----LGEADVVLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 283 IGTRFTDTLtaGFTHQLTAAQTIEV-----------QPHASRVGDvwftgipMIQAIETLAELCKEHVhdSPAPFVNN-- 349
Cdd:PRK05858 269 VGVPMDFRL--GFGVFGGTAQLVHVddappqrahhrPVAAGLYGD-------LSAILSALAGAGGDRT--DHQGWIEElr 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 350 ---DIAWPTEGGSLTQES-------FWSTLQTFIRPGDIILADQGTsaFGA-----IDLRLPAevNFIVQPLWGSIGYTL 414
Cdd:PRK05858 338 taeTAARARDAAELADDRdpihpmrVYGELAPLLDRDAIVIGDGGD--FVSyagryIDPYRPG--CWLDPGPFGCLGTGP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 415 AAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVE----RAIHG--------PEQRYNDIA 482
Cdd:PRK05858 414 GYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEkhpmEALYGydvaadlrPGTRYDEVV 493
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
368-537 |
4.85e-08 |
|
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: 53.46 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 368 TLQTFIRPGDIILADQGTsafgaidlrLPAEVnfivQPLWGS--------------IGYTLAAAFGAQTACPNRRVIVLT 433
Cdd:cd02003 7 ALNEAIGDDDVVINAAGS---------LPGDL----HKLWRArtpggyhleygyscMGYEIAAGLGAKLAKPDREVYVLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 434 GDGAAQLTIQEMGSMLRDKQRPVILVLNNEGYTVERAI---HGPEQRYNDIALWNWTQIPQALSLDP----------QAE 500
Cdd:cd02003 74 GDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLqesTGSGSFGTEFRDRDQESGQLDGALLPvdfaanarslGAR 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2216604589 501 CYRVSEAEQLADVLEKVAHHERLSLIEV-MLPKADIPP 537
Cdd:cd02003 154 VEKVKTIEELKAALAKAKASDRTTVIVIkTDPKSMTPG 191
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
351-532 |
1.74e-05 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 47.69 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 351 IAWPTEGGSLTQESFWSTLQTFIRPGDIILADQGTSaFGAIDLRLPAEvnFIVQPLWGSIGYTLAAAFGAQTACPNRRVI 430
Cdd:PRK08327 376 IERLKDRGPITPAYLSYCLGEVADEYDAIVTEYPFV-PRQARLNKPGS--YFGDGSAGGLGWALGAALGAKLATPDRLVI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 431 VLTGDGAAQLTIQEMGSMLRDKQR-PV-ILVLNNEGY-TVERAIHG--PE---QRYNDialwnwtqIPQAlSLDPQ---- 498
Cdd:PRK08327 453 ATVGDGSFIFGVPEAAHWVAERYGlPVlVVVFNNGGWlAVKEAVLEvyPEgyaARKGT--------FPGT-DFDPRpdfa 523
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2216604589 499 --AECY-----RVSEAEQLADVL----EKVAHHERLSLIEVMLPK 532
Cdd:PRK08327 524 kiAEAFggygeRVEDPEELKGALrralAAVRKGRRSAVLDVIVDR 568
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-238 |
2.11e-05 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 47.16 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 1 MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPdICWVGCANELNASYAADGYARCKGFAAL-LTTFGVGE 79
Cdd:PRK08617 1 TDKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSG-PELIVTRHEQNAAFMAAAIGRLTGKPGVvLVTSGPGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 80 LSAMNGIAGSFAEHVPVLHIVGApgmasQQRGELLHHTlgdgefrhfyHMS-------EPITAAQAILTEQNAcyeIDRV 152
Cdd:PRK08617 80 SNLATGLVTATAEGDPVVAIGGQ-----VKRADRLKRT----------HQSmdnvalfRPITKYSAEVQDPDN---LSEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 153 LTTMLRER---RPG--YLMVPADV----AKKAATPPVNALTLQPADADNAclkafrDAARVRLAMAQRTALLADFLVLRH 223
Cdd:PRK08617 142 LANAFRAAesgRPGaaFVSLPQDVvdapVTSKAIAPLSKPKLGPASPEDI------NYLAELIKNAKLPVLLLGMRASSP 215
|
250
....*....|....*
gi 2216604589 224 GLKPALQKWVKEVPM 238
Cdd:PRK08617 216 EVTAAIRRLLERTNL 230
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
406-515 |
5.97e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 41.12 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 406 LWGSIGYTLAAAFGAQTACPnRRVIVLTGDGaAQLTiqEMGSMLR-DKQRP---VILVLNNEGYtverAIHGPEQRYNDI 481
Cdd:cd03372 40 MLGSMGLASSIGLGLALAQP-RKVIVIDGDG-SLLM--NLGALATiAAEKPknlIIVVLDNGAY----GSTGNQPTHAGK 111
|
90 100 110
....*....|....*....|....*....|....
gi 2216604589 482 ALwNWTQIPQALSLDpqaECYRVSEAEQLADVLE 515
Cdd:cd03372 112 KT-DLEAVAKACGLD---NVATVASEEAFEKAVE 141
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
408-465 |
7.92e-04 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 41.11 E-value: 7.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2216604589 408 GSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQEMGSMLRDKQrPVILVLNNEGY 465
Cdd:cd02006 57 GPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRI-PYIHVLVNNAY 113
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
408-528 |
4.15e-03 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 38.45 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216604589 408 GSIGYTLAAAFGAQTACPNRRVIVLTGDGAAqltIQEMGSM-LRDKQRP---VILVLNNEGY-------TVERAIhgpeq 476
Cdd:cd03371 48 GSMGHASQIALGIALARPDRKVVCIDGDGAA---LMHMGGLaTIGGLAPanlIHIVLNNGAHdsvggqpTVSFDV----- 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2216604589 477 ryndialwNWTQIPQAlsldpqaeC-----YRVSEAEQLADVLEKVAHHERLSLIEV 528
Cdd:cd03371 120 --------SLPAIAKA--------CgyravYEVPSLEELVAALAKALAADGPAFIEV 160
|
|
| |
