|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
52-624 |
1.94e-127 |
|
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: 386.44 E-value: 1.94e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 52 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 130
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 131 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 211 DVLYpyfmvekEMIPTKLPNSLMGRVvvwylqnclanlfvgawEPRPegplpldipQASPQQVQRCVEILSRAKRPLLVL 290
Cdd:COG0028 163 DVQA-------AEAEEEPAPPELRGY-----------------RPRP---------APDPEAIEEAAELLAAAKRPVILA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 291 GSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSYG-R 362
Cdd:COG0028 210 GGGARRAGA-AEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALAEADLVLAVGARFDDRVTGNwD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 363 VLNRKSSIIIVNRNRDDLLLNsdifWKPQEAVQGDVGSFMIKLVEGLQGQMWS-SDWAEELRKADQQKEQTYRDKAlmpv 441
Cdd:COG0028 289 EFAPDAKIIHIDIDPAEIGKN----YPVDLPIVGDAKAVLAALLEALEPRADDrAAWLARIAAWRAEYLAAYAADD---- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 442 lQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 521
Cdd:COG0028 361 -GPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 522 GAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDV-ACSLAYTDYHKAAMGLGAQGLilsR-DNKDQVVK 599
Cdd:COG0028 440 GGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKLAEAFGAKGE---RvETPEELEA 516
|
570 580
....*....|....*....|....*
gi 755534354 600 VLREGQqlcQDGHAVVVNILIGRTD 624
Cdd:COG0028 517 ALEEAL---ASDGPALIDVRVDPEE 538
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
53-586 |
1.62e-120 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 368.66 E-value: 1.62e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 53 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK05858 6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 LYPyfMVEKEMIPTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:PRK05858 166 AFS--MADDDGRPGALTEL-------------------------PAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIII 372
Cdd:PRK05858 213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 373 VNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKEQtyRDKALM-----PvlqhLNP 447
Cdd:PRK05858 291 VDDAPPQR----AHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARA--RDAAELaddrdP----IHP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 448 VWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS 527
Cdd:PRK05858 361 MRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFS 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534354 528 LIEFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVACSLA-YTDYHKAAMGLGAQG 586
Cdd:PRK05858 441 LMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHG 500
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
450-620 |
1.56e-62 |
|
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: 204.69 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 450 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 529
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 530 EFDTFVRHKVPVIALVGNDAGWTQISREQVP--RLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQL 607
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLsyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTP--EELKPALKRALAS 161
|
170
....*....|...
gi 755534354 608 cqdGHAVVVNILI 620
Cdd:cd02004 162 ---GKPALINVII 171
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
56-209 |
1.25e-58 |
|
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: 193.52 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 56 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755534354 136 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 209
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
55-584 |
1.50e-58 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 205.59 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 55 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 134
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 135 NAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 211
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 212 VlypyfMVEKemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG 291
Cdd:PRK07524 165 V-----LAAP------------------------------ADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 292 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRS-----AALKKADVVVLAG---AVCDFRLSYGRV 363
Cdd:PRK07524 210 GGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrALIAEADVVLAVGtelGETDYDVYFDGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 364 LNRKSSIIIVNRNRDDLLLNsdifWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEElRKADQQKEQTYRDKALMPVLQ 443
Cdd:PRK07524 287 FPLPGELIRIDIDPDQLARN----YPPALALVGDARAALEALLARLPGQAAAADWGAA-RVAALRQALRAEWDPLTAAQV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 444 HLnpvwvLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLD-PGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDG 522
Cdd:PRK07524 362 AL-----LDTILAALPD-AIFVGDSTQPVYAGNLYFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPERPVVCLVGDG 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534354 523 AFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGA 584
Cdd:PRK07524 436 GLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGC 497
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
54-213 |
6.89e-58 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 192.06 E-value: 6.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQA-IDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 211
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 755534354 212 VL 213
Cdd:pfam02776 161 VL 162
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
54-627 |
7.75e-58 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 203.44 E-value: 7.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 133
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 213
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 214 YPyfMVEKEMIPtklpnslmgrvvvwylqnclanlfvgaweprpegplPLDIPQ---ASPQQVQRCVEILSRAKRPLLVL 290
Cdd:TIGR02418 161 DS--PVSVKAIP------------------------------------ASYAPKlgaAPDDAIDEVAEAIQNAKLPVLLL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 291 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirqnrsaalkkadvvvLAGAVCDFRLSYGRVLNRKSSI 370
Cdd:TIGR02418 203 GLRASSPETTE-AVRRLLKKTQLPVVETFQGAGAVSRELEDH----------------FFGRVGLFRNQPGDRLLKQADL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 371 IIV-------------NRNRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKE 430
Cdd:TIGR02418 266 VITigydpieyeprnwNSENDATIVHIDVepaqidnNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQRE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 431 QTYRDKAlMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDF-VATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLC 509
Cdd:TIGR02418 346 ALDRVPA-TLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHyIWMARYFRSYR-ARHLLISNGMQTLGVALPWAIGAALV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 510 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLIL 589
Cdd:TIGR02418 424 RPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRV 503
|
570 580 590
....*....|....*....|....*....|....*...
gi 755534354 590 srDNKDQVVKVLREGQQLcqDGhAVVVNILIgrtDFRD 627
Cdd:TIGR02418 504 --ESPDQLEPTLRQAMEV--EG-PVVVDIPV---DYSD 533
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
56-622 |
1.52e-55 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 198.30 E-value: 1.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 56 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 136 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLDvlYP 215
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 216 YFMVEKEmIPTklpnslmgrvvvwylqnclanlfvgaweprpegPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG---- 291
Cdd:PRK07525 167 YGVIDVE-IPQ---------------------------------PVRLERGAGGEQSLAEAAELLSEAKFPVILSGagvv 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 292 -SQALlpptpaNKLRAAVETLGVPCFLGGMSRGLLGRNHPLH---IRQNRSAA----LKKADVVVLAGAvcdfRLSYGRV 363
Cdd:PRK07525 213 lSDAI------EECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelIAKADVVLALGT----RLNPFGT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 364 LN--------RKSSIIIVNRNRDDLLLNsdifwKPQE-AVQGDVGSFMIKLVEGLQGQMWS---------------SDWA 419
Cdd:PRK07525 283 LPqygidywpKDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVARELLARLAERLAGdagreerkaliaaekSAWE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 420 EELRKADQQKEQ---TYRDKALMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATA-AYLvQPRGPLRWLDPGAFGT 495
Cdd:PRK07525 358 QELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSIAnSYL-RFEKGRKYLAPGSFGN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 496 LGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSL-AYT 573
Cdd:PRK07525 437 CGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNV 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 755534354 574 DYHKAAMGLGAQGLILsrDNKDQVVKVLREGQQLCQDGHAVVVNILIGR 622
Cdd:PRK07525 517 SYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
58-568 |
2.71e-55 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 197.52 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 58 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 137
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 138 VAQSPVLLLGGAASTL---LQkRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVLY 214
Cdd:PRK09259 96 TNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 215 PYFMVEKemiptklpnslmGRVVVWylqnclanlfvgawepRPEGPLPLDIPqaSPQQVQRCVEILSRAKRPLLVLGSQA 294
Cdd:PRK09259 175 QTMDADE------------ALTSLV----------------KVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 295 LLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGR--VLNRKSSIII 372
Cdd:PRK09259 225 AYAQADE-QIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgkTWGADKKFIQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 373 VnrnrddlllnsDIfwKPQEA---------VQGDVGSFMIKLVEGLQGQmW---SSDWAEEL--RKADQQKEQTYRDKAL 438
Cdd:PRK09259 304 I-----------DI--EPQEIdsnrpiaapVVGDIGSVMQALLAGLKQN-TfkaPAEWLDALaeRKEKNAAKMAEKLSTD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 439 MPVLQHLNPVWVLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLcQPEAEVWCL 518
Cdd:PRK09259 370 TQPMNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAV-ETGKPVVAI 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 755534354 519 FGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGwtqISR--EQVPRLGSDVAC 568
Cdd:PRK09259 448 EGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSP 496
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
54-549 |
2.80e-55 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 197.25 E-value: 2.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 LYPYFMVEkemIPTKLpnSLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:TIGR00118 163 TTAEIEYP---YPEKV--NLPG------------------YRPTVKG---------HPLQIKKAAELINLAKKPVILVGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLN 365
Cdd:TIGR00118 211 GVIIAGASE-ELKELAERIQIPVTTTLMGLGSFPEDHPLslgmlgmHGTKTANLAVHECDLIIAVGARFDDRVT-GNLAK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 366 RKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGL--QGQMWSSDWAEELR--KADQQKEQTYRDKALMPv 441
Cdd:TIGR00118 289 FAPNAKIIHIDIDPAEIGKNV--RVDIPIVGDARNVLEELLKKLfeLKERKESAWLEQINkwKKEYPLKMDYTEEGIKP- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 442 lQHlnpvwVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 521
Cdd:TIGR00118 366 -QQ-----VIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGD 439
|
490 500
....*....|....*....|....*...
gi 755534354 522 GAFGYSLIEFDTFVRHKVPVIALVGNDA 549
Cdd:TIGR00118 440 GSFQMNLQELSTAVQYDIPVKILILNNR 467
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
54-548 |
1.92e-52 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 189.54 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHIspLLVACE---KLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 130
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAI--LNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 131 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 211 DV-------LYPyfmvEKEMIPTKLPNslmgrvvvwYLQNclanlfvgaweprpegplpldipqasPQQVQRCVEILSRA 283
Cdd:PRK08527 163 DVtatlgefEYP----KEISLKTYKPT---------YKGN--------------------------SRQIKKAAEAIKEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 284 KRPLLVLGSQALLpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDF 356
Cdd:PRK08527 204 KKPLFYLGGGAIL-SNASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 357 RLSyGRV--LNRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQMWS--SDWAEELRKADQQKE 430
Cdd:PRK08527 283 RVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELKEENPTtyKEWREILKRYNELHP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 431 QTYRDKALMpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQ 510
Cdd:PRK08527 356 LSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAV 430
|
490 500 510
....*....|....*....|....*....|....*...
gi 755534354 511 PEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 548
Cdd:PRK08527 431 PDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
52-627 |
3.76e-50 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 182.75 E-value: 3.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 52 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 131
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 132 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 211
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 212 VLYPyfmvekemiPTKLPNslmgrvvvwylqnclanlfVGAWEPRPEGPlpldipqASPQQVQRCVEILSRAKRPLLVLG 291
Cdd:PRK08617 165 VVDA---------PVTSKA-------------------IAPLSKPKLGP-------ASPEDINYLAELIKNAKLPVLLLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 292 SQALLPPTpANKLRAAVETLGVPCF-----LGGMSRGL---------LGRNHP---LhirqnrsaaLKKADVVVLAGavc 354
Cdd:PRK08617 210 MRASSPEV-TAAIRRLLERTNLPVVetfqaAGVISRELedhffgrvgLFRNQPgdeL---------LKKADLVITIG--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 355 dfrlsYG------RVLNRKSSIIIVnrNRDDLLLNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQ 428
Cdd:PRK08617 277 -----YDpieyepRNWNSEGDATII--HIDVLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELRAQ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 429 KEQTYRDKALMPVlQHLNPVWVLQQVEETLPDNALLVVDGGDF---VATAAYLVQPRGPLrwldpgaFG----TLGVGAG 501
Cdd:PRK08617 350 LEELAERPARLEE-GAVHPLRIIRALQDIVTDDTTVTVDVGSHyiwMARYFRSYEPRHLL-------FSngmqTLGVALP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 502 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMG 581
Cdd:PRK08617 422 WAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAES 501
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 755534354 582 LGAQGliLSRDNKDQVVKVLREGqqLCQDGhAVVVNILIgrtDFRD 627
Cdd:PRK08617 502 FGAKG--LRVTSPDELEPVLREA--LATDG-PVVIDIPV---DYSD 539
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
54-586 |
6.38e-49 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 179.05 E-value: 6.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 131
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 132 AVKNAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVEL 208
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 209 PLDVLYpyfMVEKEMIPTKLpnslmgrvvvwylqnclanlfvgawepRPEGPLPLDipqasPQQVQRCVEILSRAKRPLL 288
Cdd:PRK08266 166 PWDVFG---QRAPVAAAPPL---------------------------RPAPPPAPD-----PDAIAAAAALIAAAKNPMI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 289 VLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirQNRSAA---LKKADVVVLAGAVCDFRLSYGRVLN 365
Cdd:PRK08266 211 FVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG--LNFAAAyelWPQTDVVIGIGSRLELPTFRWPWRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 366 RKSSIIIVNRNRDDLllnsdIFWKPQEAVQGDVGSFMIKLVEGLQGQM-WSSDWAEELRKADQQKEQtyRDKALMPVLQH 444
Cdd:PRK08266 286 DGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAGsKRPSRRAELRELKAAARQ--RIQAVQPQASY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 445 LNpvwvlqQVEETLPDNAlLVVDGGDFVATAAYLVQP-RGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 523
Cdd:PRK08266 359 LR------AIREALPDDG-IFVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755534354 524 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQG 586
Cdd:PRK08266 432 FMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLAESFGVAA 495
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
62-615 |
2.15e-48 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 177.71 E-value: 2.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 62 LRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQS 141
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 142 PVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVrDIVPTL-RTAIAAAQSGTPGPVFVELPLDVlypyfmve 220
Cdd:PRK08322 91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP-DNIPEVvREAFRLAEEERPGAVHLELPEDI-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 221 kemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 297
Cdd:PRK08322 162 -------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 298 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGavcdfrlsYGRV------L 364
Cdd:PRK08322 211 TA-SKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLSQGDYVHCAIEHADLIINVG--------HDVIekppffM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 365 NRKSSIIIVNRNRDDLLLNSDIFwkPQEAVQGDVGSFMIKLVEGL-QGQMWSSDWAEELRKADQQKEQTYRDKALMPVLq 443
Cdd:PRK08322 282 NPNGDKKVIHINFLPAEVDPVYF--PQVEVVGDIANSLWQLKERLaDQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 444 hlnPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 523
Cdd:PRK08322 359 ---PQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 524 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLRE 603
Cdd:PRK08322 436 FMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESA--DDLLPTLEE 513
|
570
....*....|..
gi 755534354 604 GqqLCQDGHAVV 615
Cdd:PRK08322 514 A--LAQPGVHVI 523
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
54-545 |
1.01e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 176.48 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 213
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 214 YPYFMVEKEMIPTKLPnsLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGSQ 293
Cdd:PRK06276 163 EGELDLEKYPIPAKID--LPG------------------YKPTTFG---------HPLQIKKAAELIAEAERPVILAGGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 294 ALLppTPANK-LRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGavCDFRlsyGRVLN 365
Cdd:PRK06276 214 VII--SGASEeLIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSVTESDVLIAIG--CRFS---DRTTG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 366 RKSS------IIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQMWSSD--WAEELR--KADQQKEQTYRD 435
Cdd:PRK06276 287 DISSfapnakIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNKseWLERVKklKKESIPRMDFDD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 436 KALMPvlQHLnpVWVLQQV--EETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEA 513
Cdd:PRK06276 363 KPIKP--QRV--IKELMEVlrEIDPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDA 438
|
490 500 510
....*....|....*....|....*....|..
gi 755534354 514 EVWCLFGDGAFGYSLIEFDTFVRHKVPVIALV 545
Cdd:PRK06276 439 NVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
54-622 |
2.97e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 171.88 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDvl 213
Cdd:PRK06048 90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKD-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 214 ypyfmVEKEMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL----- 288
Cdd:PRK06048 168 -----VTTAEIDFDYPDKVELR----------------GYKPTYKG---------NPQQIKRAAELIMKAERPIIyaggg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 289 VLGSQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFRLSyG 361
Cdd:PRK06048 218 VISSNA------SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARFDDRVT-G 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 362 RVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQgqmwSSDWAEELRKADQQKEQ-----TYRDK 436
Cdd:PRK06048 291 KLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQ----YCDRKEWLDKINQWKKEyplkyKERED 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 437 ALMpvlqhlnPVWVLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVW 516
Cdd:PRK06048 365 VIK-------PQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 517 CLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQISREQvpRLGSdvACSLAYTDYHKAAMGLGAQGLILS 590
Cdd:PRK06048 437 DIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDK--RYSH--TCIKGSVDFVKLAEAYGALGLRVE 512
|
570 580 590
....*....|....*....|....*....|..
gi 755534354 591 RDNkdQVVKVLREGQQLcqdGHAVVVNILIGR 622
Cdd:PRK06048 513 KPS--EVRPAIEEAVAS---DRPVVIDFIVEC 539
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
44-622 |
1.77e-45 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 169.99 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 44 HKVDKTSIRHGGESVAAVLRAHGVRFVFtlvGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTG--TVGVAAVT 121
Cdd:PRK06154 12 HLPAEAKTMKVAEAVAEILKEEGVELLF---GFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 122 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTllqkrgALQAID----QMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQ 197
Cdd:PRK06154 89 YGPGAENAFGGVAQAYGDSVPVLFLPTGYPR------GSTDVApnfeSLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 198 SGTPGPVFVELPLDVLYpyfmvekemipTKLPNSlmgrvvvwylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCV 277
Cdd:PRK06154 163 NGRPGPVVLELPVDVLA-----------EELDEL-----------------------PLDHRPSRRSRPGADPVEVVEAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 278 EILSRAKRPLLVLGsQALLPPTPANKLRAAVETLGVPCF--LGGMSRglLGRNHPLHIRQNRSAA-------LKKADVVV 348
Cdd:PRK06154 209 ALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMttLNGKSA--FPEDHPLALGSGGRARpatvahfLREADVLF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 349 LAGavCDF-RLSYGRVLNRKSSIIIVnrNRDDLLLNSDIFWKpqEAVQGDVGSFMIKLVEGLQGQMW-----SSDWAEEL 422
Cdd:PRK06154 286 GIG--CSLtRSYYGLPMPEGKTIIHS--TLDDADLNKDYPID--HGLVGDAALVLKQMIEELRRRVGpdrgrAQQVAAEI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 423 RKADQQKEQTYRDKaLMPVLQHLNPVWVLQQVEETL-PDNALLVVDGG---DFVATAAYLVQPRGPLRWldpGAFGTLGV 498
Cdd:PRK06154 360 EAVRAAWLAKWMPK-LTSDSTPINPYRVVWELQHAVdIKTVIITHDAGsprDQLSPFYVASRPGSYLGW---GKTTQLGY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 499 GAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISREQVPRLGSDVACSLAYTDYHKA 578
Cdd:PRK06154 436 GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN-FSMGGYDKVMPVSTTKYRATDISGDYAAI 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 755534354 579 AMGLGAQGLILSRdnKDQVVKVLREGQQLCQDGHAVVVNILIGR 622
Cdd:PRK06154 515 ARALGGYGERVED--PEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
54-551 |
2.05e-45 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 169.40 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAAST--LLQKRGAL-QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 209
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 210 LDvlypyfmvekemiptklpnsLMGRVVVWylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV 289
Cdd:PRK07064 165 ID--------------------IQAAEIEL---------------PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 290 LGSQALlppTPANKLRAAVEtLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAA----LKKADVVVLAGAvcDFR----LSY 360
Cdd:PRK07064 210 LGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAvealYKTCDLLLVVGS--RLRgnetLKY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 361 GRVLNRKSSIIIVNRNRDDLLLNSDIFwkpqeaVQGDVGSFMIKLVEGLQGQMW-SSDWAEELRKADQQKEQTYRDKalm 439
Cdd:PRK07064 284 SLALPRPLIRVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLSvDPAFAADLRAAREAAVADLRKG--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 440 pvlqhLNPVWVL-QQVEETLPDNALLVVDGGdfVATAAY---LVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEV 515
Cdd:PRK07064 355 -----LGPYAKLvDALRAALPRDGNWVRDVT--ISNSTWgnrLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKT 426
|
490 500 510
....*....|....*....|....*....|....*.
gi 755534354 516 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 551
Cdd:PRK07064 427 VGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
54-615 |
1.39e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 167.45 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 213
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 214 ---YPYFMVEKEMIPTKLPnslmgrvvvwylqnclanlfvgawEPRPEgplpldipqasPQQVQRCVEILSRAKRPLLVL 290
Cdd:PRK06725 177 nekVTSFYNEVVEIPGYKP------------------------EPRPD-----------SMKLREVAKAISKAKRPLLYI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 291 GSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRV 363
Cdd:PRK06725 222 GG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAVTECDLLLALGVRFDDRVT-GKL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 364 --LNRKSSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEgLQGQMWSSDWAEELRKADQQKEQTYRDKAlmpv 441
Cdd:PRK06725 300 elFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKKALHMLLH-MSIHTQTDEWLQKVKTWKEEYPLSYKQKE---- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 442 lQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 521
Cdd:PRK06725 371 -SELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 522 GAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQI---SREQVPRLGSdvacslayTDYHKAAMGLGAQGliLSRD 592
Cdd:PRK06725 450 ASFQMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS--------PDFVKVAEAYGVKG--LRAT 519
|
570 580
....*....|....*....|...
gi 755534354 593 NKDQVVKVLREGqqLCQDGHAVV 615
Cdd:PRK06725 520 NSTEAKQVMLEA--FAHEGPVVV 540
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
54-607 |
7.24e-44 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 165.75 E-value: 7.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 130
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGavlYIYDELYKQDK--IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 131 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 211 DvlypyfmVEKEMIPTKLPNSLmgrvvvwylqnclanlfvgawEPRPEGPlpldIPQASPQQVQRCVEILSRAKRPLLVL 290
Cdd:PRK06965 181 D-------VSKTPCEYEYPKSV---------------------EMRSYNP----VTKGHSGQIRKAVSLLLSAKRPYIYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 291 GSQALLpPTPANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrls 359
Cdd:PRK06965 229 GGGVIL-ANASRELRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFD---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 360 yGRVLNRKSSIIIVNRNrddlLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQ-----------GQMWSSdwAEE 421
Cdd:PRK06965 300 -DRVIGNPAHFASRPRK----IIHIDIdpssiskRVKVDIPIVGDVKEVLKELIEQLQtaehgpdadalAQWWKQ--IEG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 422 LRKADQQKEQTYRDKalmpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAG 501
Cdd:PRK06965 373 WRSRDCLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 502 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV--IAL----VGNDAGWTQIsrEQVPRLGSDVACSLAytDY 575
Cdd:PRK06965 445 YAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVkiISLnnryLGMVRQWQEI--EYSKRYSHSYMDALP--DF 520
|
570 580 590
....*....|....*....|....*....|..
gi 755534354 576 HKAAMGLGAQGLILSRdnKDQVVKVLREGQQL 607
Cdd:PRK06965 521 VKLAEAYGHVGMRIEK--TSDVEPALREALRL 550
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
54-591 |
5.25e-42 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 160.31 E-value: 5.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFtlvGGHI-SPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVELP 209
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 210 LDVLypyfmvEKEMIPTKLPNSlmgrvvvwylqnclANLfvGAWeprpegplPLDIPQASPQQVQRCVEILSRAKRPLLV 289
Cdd:PRK06112 170 ADLL------TAAAAAPAAPRS--------------NSL--GHF--------PLDRTVPAPQRLAEAASLLAQAQRPVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 290 LG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI------------RQNRSAALKKADVVVLAGA 352
Cdd:PRK06112 220 AGggvhiSGA------SAALAALQSLAGLPVATTNMGKGAVDETHPLSLgvvgslmgprspGRHLRDLVREADVVLLVGT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 353 VCDFRLSYGRVLNRKSSIII--------VNRNRDDLLLNSDifwkPQEAVQGDVGSFMIKLVEGLQGQMWS-SDWAEELR 423
Cdd:PRK06112 294 RTNQNGTDSWSLYPEQAQYIhidvdgeeVGRNYEALRLVGD----ARLTLAALTDALRGRDLAARAGRRAAlEPAIAAGR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 424 KADQQKEQTYRDKALMPVlqhlNPVWVLQQVEETLPDNALLVVDGG-DFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 502
Cdd:PRK06112 370 EAHREDSAPVALSDASPI----RPERIMAELQAVLTGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLAGLGWGVPM 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 503 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA--GWtQISREQVpRLGSDV-ACSLAYTDYHKAA 579
Cdd:PRK06112 446 AIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF-QKHAETV-KFGTHTdACHFAAVDHAAIA 523
|
570
....*....|..
gi 755534354 580 MGLGAQGLILSR 591
Cdd:PRK06112 524 RACGCDGVRVED 535
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
54-549 |
2.27e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 158.33 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 lypyfmvekemiptklpnslmgrvvvwylQNclANLFVGAWePRPEGPLPldIPQASPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:PRK08155 175 -----------------------------QT--AVIELEAL-PAPAEKDA--APAFDEESIRDAAAMINAAKRPVLYLGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRlSYGRV-- 363
Cdd:PRK08155 221 GVINSGAPARARELA-EKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYILQEADLLIVLGARFDDR-AIGKTeq 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 364 LNRKSSIIIVNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMwSSDWAEelRKADQQKEQTYRdkalMPVLQ 443
Cdd:PRK08155 299 FCPNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQP-RAEWHQ--LVADLQREFPCP----IPKAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 444 H-LNPVWVLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLF 519
Cdd:PRK08155 368 DpLSHYGLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPR---QWLTSGGLGTMGFGLPAAIGAALANPERKVLCFS 444
|
490 500 510
....*....|....*....|....*....|.
gi 755534354 520 GDGAFGYSLIEFDTFVRHKVPV-IALVGNDA 549
Cdd:PRK08155 445 GDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
52-554 |
8.12e-41 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 156.57 E-value: 8.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 52 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 130
Cdd:PRK08199 8 RTGGQILVDALRANGVERVFCVPGESYLAVLDALhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 131 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:PRK08199 88 IGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 211 DVLYpyfmvekemiptklpnslmGRVVVwylqnclanlfvgaweprPEGPlPLDIPQASP--QQVQRCVEILSRAKRPLL 288
Cdd:PRK08199 168 DVLS-------------------ETAEV------------------PDAP-PYRRVAAAPgaADLARLAELLARAERPLV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 289 VLG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLH-----IRQNRS--AALKKADVVVLAGAvcdf 356
Cdd:PRK08199 210 ILGgsgwtEAA------VADLRAFAERWGLPVACAFRRQDLFDNRHPNYagdlgLGINPAlaARIREADLVLAVGT---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 357 RLsyGRVLNRKSSIIIVNRNRDDLL--------LNSdiFWKPQEAVQGDVGSF--MIKLVEGLQGQMWsSDWAEELRkAD 426
Cdd:PRK08199 280 RL--GEVTTQGYTLLDIPVPRQTLVhvhpdaeeLGR--VYRPDLAIVADPAAFaaALAALEPPASPAW-AEWTAAAH-AD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 427 QQKEQTYRdkalmPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFvatAAYL---VQPRGPLRWLDPGAfGTLGVGAGFA 503
Cdd:PRK08199 354 YLAWSAPL-----PGPGAVQLGEVMAWLRERLPADAIITNGAGNY---ATWLhrfFRFRRYRTQLAPTS-GSMGYGLPAA 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 755534354 504 LGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQI 554
Cdd:PRK08199 425 IAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
54-547 |
2.50e-39 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 151.96 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 213
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 214 ypyfmvekemiptklpnslmgrvvvwylqncLANLFVGAWEPRPEGPlpldiPQASPQQVQRCVEILSRAKRPLLVLG-- 291
Cdd:PRK08978 163 -------------------------------LAEGELEPHLTTVENE-----PAFPAAELEQARALLAQAKKPVLYVGgg 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 292 ---SQAllppTPAnkLRAAVETLGVP--CFLGGMsrGLLGRNHP-----LHIRQNRSA--ALKKADVVVLAGAVCDFRLS 359
Cdd:PRK08978 207 vgmAGA----VPA--LREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDRVT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 360 yGRvLNR---KSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDvgsfMIKLVEGLQGQMWSSDWAEELRKADQQKEQTYR 434
Cdd:PRK08978 279 -GK-LNTfapHAKVIHLDIDPAEInkLRQAHV------ALQGD----LNALLPALQQPLNIDAWRQHCAQLRAEHAWRYD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 435 DKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAE 514
Cdd:PRK08978 347 HPG-----EAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDT 421
|
490 500 510
....*....|....*....|....*....|....
gi 755534354 515 VWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 547
Cdd:PRK08978 422 VICVSGDGSFMMNVQELGTIKRKQLPVkIVLLDN 455
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
43-547 |
3.02e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 149.20 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 43 MHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVT 121
Cdd:PRK07282 1 MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 122 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTP 201
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 202 GPVFVELPLDVlypyfmVEKEmipTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPLDIPQASPQ--QVQRCVEI 279
Cdd:PRK07282 161 GPVVIDLPKDV------SALE---TDFIYD-------------------------PEVNLPSYQPTLEPNdmQIKKILKQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 280 LSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGA 352
Cdd:PRK07282 207 LSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANIAMTEADFMINIGS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 353 VCDFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKaDQQKEQT 432
Cdd:PRK07282 286 RFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLAEPTVHNNTEKWIEKVTK-DKNRVRS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 433 YRDKALMpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 512
Cdd:PRK07282 362 YDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPD 436
|
490 500 510
....*....|....*....|....*....|....*.
gi 755534354 513 AEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 547
Cdd:PRK07282 437 KEVILFVGDGGFQMTNQELAILNIYKVPIkVVMLNN 472
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
54-586 |
3.41e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 149.22 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVA----CEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 129
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 130 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 209
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 210 LDVLYpyfmvEKemiptklpnslMGRVVvwylqnclanlfvgaWEPRPEGPLPLDIPQ-ASPQQVQRCVEILSRAKRPLL 288
Cdd:PRK06456 164 RDIFY-----EK-----------MEEIK---------------WPEKPLVKGYRDFPTrIDRLALKKAAEILINAERPII 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 289 VLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFR--LS 359
Cdd:PRK06456 213 LVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfTS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 360 YGRVLNRKSSIIIVNRNRDDlllnSDIFWKPQEAVQGDVGSF---MIKLVEGLQGQMWSSDWAEELRKADQQKEQTY--- 433
Cdd:PRK06456 292 YDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIIlreLIKAITELGQKRDRSAWLKRVKEYKEYYSQFYyte 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 434 RDKALMPvlqhlnpvW-VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 512
Cdd:PRK06456 368 ENGKLKP--------WkIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 513 AEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVgNDAGWTQISReQVPRL-------GSDVACSlayTDYHKAAMGLGAQ 585
Cdd:PRK06456 440 KVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVR-QVQDLffgkrivGVDYGPS---PDFVKLAEAFGAL 514
|
.
gi 755534354 586 G 586
Cdd:PRK06456 515 G 515
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
54-622 |
3.51e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 149.82 E-value: 3.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 129
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 130 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 209
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 210 LDV---LYPYFMVEKEMIptKLPnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 286
Cdd:PRK07418 181 KDVgqeEFDYVPVEPGSV--KPP----------------------GYRPTVKG---------NPRQINAALKLIEEAERP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 287 LLVLGSQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRL- 358
Cdd:PRK07418 228 LLYVGGGAISAGAHAE-LKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAVTECDLLIAVGARFDDRVt 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 359 -------SYGRVLNrkssIII----VNRNRddlllnsdifwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQ 427
Cdd:PRK07418 307 gkldefaSRAKVIH----IDIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 428 QKEqtyrDKALM--PVLQHLNPVWVLQQVEETLPDnALLVVDGGDFVATAA-YLvqPRGPLRWLDPGAFGTLGVGAGFAL 504
Cdd:PRK07418 372 WKQ----DYPLVvpPYEGEIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAqFL--RNGPRRWISSAGLGTMGFGMPAAM 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 505 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISRE-QVPRLG-----SDVACSLAytDYHKA 578
Cdd:PRK07418 445 GVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQwQESFYGerysaSNMEPGMP--DFVKL 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 755534354 579 AMGLGAQGLILSrdNKDQVVKVLREgqQLCQDGhAVVVNILIGR 622
Cdd:PRK07418 522 AEAFGVKGMVIS--ERDQLKDAIAE--ALAHDG-PVLIDVHVRR 560
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
54-541 |
3.76e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 149.20 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:PRK08979 166 LNPAI-----LHPYEYPESIKMR----------------SYNPTTSG---------HKGQIKRGLQALLAAKKPVLYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGAVCDFRLSygrvln 365
Cdd:PRK08979 216 GAIISGADKQILQLA-EKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNADLIFGIGVRFDDRTT------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 366 rkssiiivnRNRDDLLLNSDIFW---KP---QEAVQGD---VGSF------MIKLVEGlQGQMWSSD----WAEELRKAD 426
Cdd:PRK08979 289 ---------NNLEKYCPNATILHidiDPssiSKTVRVDipiVGSAdkvldsMLALLDE-SGETNDEAaiasWWNEIEVWR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 427 QQKEQTYRDKAlmpvlQHLNPvwvlQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 502
Cdd:PRK08979 359 SRNCLAYDKSS-----ERIKP----QQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPA 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 755534354 503 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 541
Cdd:PRK08979 430 AMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
54-620 |
3.92e-38 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 149.22 E-value: 3.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLL--VACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 131
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 132 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLD 211
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 212 vlYPYFMVEKEMiptklpnslmgrvvvWYLQNCLANLFVgaweprpegplpldIPQASPQQVQRCVEILSRAKRPLLVLG 291
Cdd:TIGR02720 160 --FGWQEIPDND---------------YYASSVSYQTPL--------------LPAPDVEAVTRAVQTLKAAERPVIYYG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 292 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlaGAVCDFRLSYGRvlNRKSSII 371
Cdd:TIGR02720 209 IGAR---KAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEA---LFQADLVLFVGN--NYPFAEV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 372 IVNRNRDDLLLNSDI----FWKPQE---AVQGDVGSFmIKLVEGLQGQMWSSDWAEElRKADQQKEQTYRDKALMPVLQH 444
Cdd:TIGR02720 281 SKAFKNTKYFIQIDIdpakLGKRHHtdiAVLADAKKA-LAAILAQVEPRESTPWWQA-NVANVKNWRAYLASLEDKTEGP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 445 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 524
Cdd:TIGR02720 359 LQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 525 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGAQGLILsrDNKDQVVKV 600
Cdd:TIGR02720 439 SMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQedtnQPLIGVD----FNDADFAKIAEGVGAVGFRV--NKIEQLPAV 512
|
570 580
....*....|....*....|
gi 755534354 601 LREGQQLCQdGHAVVVNILI 620
Cdd:TIGR02720 513 FEQAKAIKQ-GKPVLIDAKI 531
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
54-544 |
1.06e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 147.69 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:PRK07979 166 LNPAN-----KLPYVWPESVSMR----------------SYNPTTQG---------HKGQIKRALQTLVAAKKPVVYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTPAnKLRAAVETLGVPCF-----LGGM------SRGLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 361
Cdd:PRK07979 216 GAINAACHQ-QLKELVEKLNLPVVsslmgLGAFpathrqSLGMLG----MHGTYEANMTMHNADVIFAVGVRFDDRTTNN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 362 RVLNRKSSIII---VNRNRDDLLLNSDIfwkpqeAVQGDVGSFMIKLVEgLQGQMWSSDWAEELRKADQQKEQTYRDKAL 438
Cdd:PRK07979 291 LAKYCPNATVLhidIDPTSISKTVTADI------PIVGDARQVLEQMLE-LLSQESAHQPLDEIRDWWQQIEQWRARQCL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 439 M--PVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVW 516
Cdd:PRK07979 364 KydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVV 443
|
490 500
....*....|....*....|....*...
gi 755534354 517 CLFGDGAFGYSLIEFDTFVRHKVPVIAL 544
Cdd:PRK07979 444 CVTGDGSIQMNIQELSTALQYELPVLVL 471
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
54-541 |
2.25e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 143.73 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 130
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 131 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 211 DVLYPYFMVEKEMiPTKlpnslmgrvvvwylqnclanLFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL-- 288
Cdd:PRK06466 164 DMTNPAEKFEYEY-PKK--------------------VKLRSYSPAVRG---------HSGQIRKAVEMLLAAKRPVIys 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 289 ----VLGSQALLPPTPANKLRAAVET--LGVPCFLGGMSR--GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrlsy 360
Cdd:PRK06466 214 gggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEANMAMHHADVILAVGARFD----- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 361 GRVLNRKSSII----IVNRNRDDLLLNSDIFWK-----PQEAVQGDVGSFMIKLVEGLQGQMWSSDWAE--ELRKA-DQQ 428
Cdd:PRK06466 285 DRVTNGPAKFCpnakIIHIDIDPASISKTIKADipivgPVESVLTEMLAILKEIGEKPDKEALAAWWKQidEWRGRhGLF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 429 KEQTYRDKALMPvlqhlnpvwvlQQVEETLPD----NALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 504
Cdd:PRK06466 365 PYDKGDGGIIKP-----------QQVVETLYEvtngDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAM 433
|
490 500 510
....*....|....*....|....*....|....*..
gi 755534354 505 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 541
Cdd:PRK06466 434 GVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
54-548 |
8.23e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 142.36 E-value: 8.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGgIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:PRK06882 166 VNPAN-----KFTYEYPEEVSLR----------------SYNPTVQG---------HKGQIKKALKALLVAKKPVLFVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTpANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLS-- 359
Cdd:PRK06882 216 GVITAEC-SEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEANNAMHESDLILGIGVRFDDRTTnn 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 360 ------YGRVL-----------NRKSSIIIVNRNRDDL-----LLNSDIFWKPQEAVqgdvgsfmiklveglqgqmwsSD 417
Cdd:PRK06882 291 lakycpNAKVIhididptsiskNVPAYIPIVGSAKNVLeeflsLLEEENLAKSQTDL---------------------TA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 418 WAEELR--KADQQKEQTYRDKALMPvlqhlnpvwvlQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPG 491
Cdd:PRK06882 350 WWQQINewKAKKCLEFDRTSDVIKP-----------QQVVEAIyrltNGDAYVASDVGQHQMFAALHYPFDKPRRWINSG 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 755534354 492 AFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 548
Cdd:PRK06882 419 GAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
41-548 |
1.32e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 141.44 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 41 QLMHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAV 120
Cdd:PRK07710 5 RTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 121 TAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGT 200
Cdd:PRK07710 85 TSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 201 PGPVFVELPLDVLYP--YFMVEKEM-----IPTKLPNSLmgrvvvwylqnclanlfvgaweprpegplpldipqaspqQV 273
Cdd:PRK07710 165 PGPVLIDIPKDMVVEegEFCYDVQMdlpgyQPNYEPNLL---------------------------------------QI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 274 QRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADV 346
Cdd:PRK07710 206 RKLVQAVSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLflgmagmHGTYTANMALYECDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 347 VVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKAD 426
Cdd:PRK07710 285 LINIGARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 427 QQKEQTYRDKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGA 506
Cdd:PRK07710 362 EKYPLSYKRNS-----ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGA 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 755534354 507 KLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 548
Cdd:PRK07710 437 QLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
54-547 |
9.76e-35 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 139.35 E-value: 9.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLgiRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 130
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 131 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 211 DVLypyfmvEKEMiptklpnslmgrvvvwylqnclanLFvgAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVL 290
Cdd:PRK07789 191 DAL------QAQT------------------------TF--SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 291 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDfrlsyGRV 363
Cdd:PRK07789 239 GGGVIRAEASA-ELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgmhgtvAAVAALQRSDLLIALGARFD-----DRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 364 LNRKSSI-----II--------VNRNRddlllNSDIFwkpqeaVQGDVGSFMIKLVEGLQ------GQMWSSDWAEELRK 424
Cdd:PRK07789 313 TGKLDSFapdakVIhadidpaeIGKNR-----HADVP------IVGDVKEVIAELIAALRaehaagGKPDLTAWWAYLDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 425 ADQQKEQTYRDkalmPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 504
Cdd:PRK07789 382 WRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAM 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 755534354 505 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 547
Cdd:PRK07789 458 GAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINN 501
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
65-547 |
2.44e-34 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 137.91 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 65 HGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 140
Cdd:CHL00099 23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 141 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV---LYPYF 217
Cdd:CHL00099 103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 218 MVEKEMIPTKLPnslmgrvvvwylqnclanlfvgAWEPrpegplpldIPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 297
Cdd:CHL00099 183 PPEPGNTIIKIL----------------------GCRP---------IYKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 298 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLNRKSSI 370
Cdd:CHL00099 232 DA-HQEITELAELYKIPVTTTLMGKGIFDEDHPLclgmlgmHGTAYANFAVSECDLLIALGARFDDRVT-GKLDEFACNA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 371 IIV-----------NRNrddlllnsdifwkPQEAVQGDVGSFMIKLVEglqgqmwSSDWAEELRKADQQ---KEQTYRDK 436
Cdd:CHL00099 310 QVIhididpaeigkNRI-------------PQVAIVGDVKKVLQELLE-------LLKNSPNLLESEQTqawRERINRWR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 437 ALMPVL-----QHLNPVWVLQQVEETLPDnALLVVDGGDFVATAAYL--VQPRgplRWLDPGAFGTLGVGAGFALGAKLC 509
Cdd:CHL00099 370 KEYPLLipkpsTSLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlkCKPR---KWLSSAGLGTMGYGLPAAIGAQIA 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 755534354 510 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 547
Cdd:CHL00099 446 HPNELVICISGDASFQMNLQELGTIAQYNLPIkIIIINN 484
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
62-551 |
1.88e-33 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 135.13 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 62 LRAHGVRFVFTLVGGHISPLLVACEK---LGIRVVDT---RHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:PRK08327 17 LKELGVDYIFINSGTDYPPIIEAKARaraAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANALGGVHN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 136 AQVAQSPVLLLGGAASTLlqKRGAL-----------QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPV 204
Cdd:PRK08327 97 AARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 205 FVELPLDVLypyfmVEKemiptklpnslmgrvvvwylqnclanlfVGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAK 284
Cdd:PRK08327 175 YLTLPREVL-----AEE----------------------------VPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 285 RPLLV---LGSQALLPPTpankLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlagavcdfrlsyg 361
Cdd:PRK08327 222 RPVIItwrAGRTAEGFAS----LRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLV-------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 362 rvlnrkssiiivnrnrddLLLNSDIFWKPQE------------------------------AVQGDVGSFMIKLVEGLQG 411
Cdd:PRK08327 284 ------------------LVVDSDVPWIPKKirpdadarviqidvdplksriplwgfpcdlCIQADTSTALDQLEERLKS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 412 QMWSSDWAEELRKADQQKEQTYRDKALMPVLQHL------NPVWVLQQVEETLPDNALLVVDGGdFVATAAYLvqpRGPL 485
Cdd:PRK08327 346 LASAERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPG 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755534354 486 RWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFV--RHKVPVIALVGNDAGW 551
Cdd:PRK08327 422 SYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
54-541 |
2.41e-33 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 135.22 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 lypYFMVEKEMIPTKLPnslmgrvvvwylqnclanlFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 292
Cdd:PRK09107 173 ---QFATGTYTPPQKAP-------------------VHVSYQPKVKG---------DAEAITEAVELLANAKRPVIYSGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 293 QALLPPTPANK-LRAAVETLGVP--CFLGGMSR---------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSy 360
Cdd:PRK09107 222 GVINSGPEASRlLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYEANMAMHDCDVMLCVGARFDDRIT- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 361 GRV-----LNRKSSIII----VNRN-RDDLllnsdifwkpqeAVQGDVGSFMIKLVEGLQGQMWSSD------WAEELRK 424
Cdd:PRK09107 297 GRLdafspNSKKIHIDIdpssINKNvRVDV------------PIIGDVGHVLEDMLRLWKARGKKPDkealadWWGQIAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 425 ADQQKEQTYR--DKALMPvlQHlnpvwVLQQVEE-TLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAG 501
Cdd:PRK09107 365 WRARNSLAYTpsDDVIMP--QY-----AIQRLYElTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 755534354 502 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 541
Cdd:PRK09107 438 AALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
56-622 |
3.67e-31 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 128.56 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 56 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK11269 8 DAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 213
Cdd:PRK11269 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 214 ypyfMVEKEmiptklpnslmgrvvvwylqnclanlfvgaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 293
Cdd:PRK11269 168 ----VAEIE------------------------------FDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 294 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL----------HIRQNrsAALKKADVVVLAGAvcdfrlsygRV 363
Cdd:PRK11269 213 GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATLLASDFVLGIGN---------RW 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 364 LNRKSSIIIVNRnRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWS------SDWAEEL--RKADQQ 428
Cdd:PRK11269 282 ANRHTGSVEVYT-KGRKFVHVDIeptqigrVFGPDLGIVSDAKAALELLVEVAREWKAAgrlpdrSAWVADCqeRKRTLL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 429 KEQTYRDkalMPVlqhlNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 508
Cdd:PRK11269 361 RKTHFDN---VPI----KPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 509 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPrLGSDVACSLAY------------TDYH 576
Cdd:PRK11269 434 ADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRA-FDMDYCVQLAFeninspelngygVDHV 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 755534354 577 KAAMGLGAQGLILSRdnKDQVVKVLREGQQLCQDGHA-VVVNILIGR 622
Cdd:PRK11269 513 KVAEGLGCKAIRVFK--PEDIAPALEQAKALMAEFRVpVVVEVILER 557
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
52-548 |
1.06e-28 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 121.00 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 52 RHGGESVAAVLRAHGVRFVFTLVGG-----HISPLLVACeklgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGL 126
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGasmeiHQALTRSNC----IRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 127 TNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFV 206
Cdd:PLN02470 89 TNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 207 ELPLDVlypyfmvEKEM-IPT-KLPNSLMGrvvvwYLQNClanlfvgawePRPegplpldiPQASpqQVQRCVEILSRAK 284
Cdd:PLN02470 169 DIPKDI-------QQQLaVPNwNQPMKLPG-----YLSRL----------PKP--------PEKS--QLEQIVRLISESK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 285 RPLLVLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDFR 357
Cdd:PLN02470 217 RPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANYAVDSADLLLAFGVRFDDR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 358 LSyGRV--LNRKSSIIIVNRNRDDLLLNSdifwKPQEAVQGDVG---SFMIKLVEGLQGQMWS-SDWAEELrkaDQQKEQ 431
Cdd:PLN02470 294 VT-GKLeaFASRASIVHIDIDPAEIGKNK----QPHVSVCADVKlalQGLNKLLEERKAKRPDfSAWRAEL---DEQKEK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 432 ---TYRDKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 508
Cdd:PLN02470 366 fplSYPTFG-----DAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAA 440
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 755534354 509 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 548
Cdd:PLN02470 441 ANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
467-616 |
2.15e-28 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 110.75 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 467 DGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVG 546
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755534354 547 NDAGWTQISREQVP----RLGSDVACSLAYTDYHKAAMGLGAQGliLSRDNKDQVVKVLREGqqLCQDGHAVVV 616
Cdd:pfam02775 81 NNGGYGMTRGQQTPfgggRYSGPSGKILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEA--LEHDGPALID 150
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
56-594 |
2.79e-26 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 113.39 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 56 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 136 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLDVLYp 215
Cdd:PRK06457 86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAIS-KRGVAHINLPVDILR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 216 yfmvekemiptklpnslMGRvvvwylqnclanlfvgawEPRPEGPLPLDIPQASPQqVQRCVEILSRAKRPLLVLGSQAL 295
Cdd:PRK06457 164 -----------------KSS------------------EYKGSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 296 LPPTPANKLraaVETLGVPCF----------------LGGMsrGLLGRNHPLhirqnrsAALKKADVVVLAGAVcdfrLS 359
Cdd:PRK06457 208 GLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI-------EAMDKADLLIMLGTS----FP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 360 YGRVLNRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFMI--------KLVEGLQGQMwsSDWAEELRKADQQk 429
Cdd:PRK06457 272 YVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLNidieeksdKFYEELKGKK--EDWLDSISKQENS- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 430 eqtyRDKALmpvlqhlNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 509
Cdd:PRK06457 343 ----LDKPM-------KPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 510 -QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGA 584
Cdd:PRK06457 412 vENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEWGVD----LYNPDFTKIAESIGF 487
|
570
....*....|
gi 755534354 585 QGLILSRDNK 594
Cdd:PRK06457 488 KGFRLEEPKE 497
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
445-623 |
2.89e-24 |
|
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: 100.66 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 445 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 524
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 525 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLRE 603
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
|
170 180
....*....|....*....|
gi 755534354 604 GQQLCQDGHAVVVNILIGRT 623
Cdd:cd02013 162 AIAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
450-616 |
2.96e-24 |
|
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: 99.64 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 450 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 529
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 530 EFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQlc 608
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDP--EDLEAALAEALA-- 157
|
....*...
gi 755534354 609 QDGHAVVV 616
Cdd:cd00568 158 AGGPALIE 165
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
55-212 |
6.38e-24 |
|
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: 98.39 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 55 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 133
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 134 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRR---VRDIVPT-LRTAIAaaqsgTPGPVFVELP 209
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPELLDRaIRTAIA-----KRGVAVLILP 157
|
...
gi 755534354 210 LDV 212
Cdd:cd07039 158 GDV 160
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
62-552 |
1.61e-22 |
|
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: 101.77 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 62 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 140
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLdAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 141 SPVLLLGGAASTLLQKRGAL--------QAIDQMSLFRPLCkfCASVR-----------RVrdivptLRTAIAAAQsgtp 201
Cdd:COG3961 94 VPVVHIVGAPGTRAQRRGPLlhhtlgdgDFDHFLRMFEEVT--VAQAVltpenaaaeidRV------LAAALREKR---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 202 gPVFVELPLDVlypyfmVEKEMiptklpnslmgrvvvwylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCV---- 277
Cdd:COG3961 162 -PVYIELPRDV------ADAPI-------------------------------EPPEAPLPLPPPASDPAALAAAVaaaa 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 278 EILSRAKRPLLVLGSQAL---LpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI--------RQNRSAALKKADV 346
Cdd:COG3961 204 ERLAKAKRPVILAGVEVHrfgL----QEELLALAEKTGIPVATTLLGKSVLDESHPQFIgtyagaasSPEVREYVENADC 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 347 VVLAGAV-CDFRL-SYGRVLNRKSSIIIvnrNRDDLLLNSDIFwkpqEAVQgdvgsfMIKLVEGLQGQMWSSDWAEELRK 424
Cdd:COG3961 280 VLCLGVVfTDTNTgGFTAQLDPERTIDI---QPDSVRVGGHIY----PGVS------LADFLEALAELLKKRSAPLPAPA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 425 ADQQKEQTYRDKALMpvlqhLNPVWvlQQVEETLPDNALLVVDGGD--FVATAAYLvqPRGpLRWLDPGAFGTLG--VGA 500
Cdd:COG3961 347 PPPPPPPAAPDAPLT-----QDRLW--QRLQAFLDPGDIVVADTGTslFGAADLRL--PEG-ATFIAQPLWGSIGytLPA 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 755534354 501 gfALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWT 552
Cdd:COG3961 417 --ALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYT 466
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
445-620 |
2.00e-22 |
|
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: 94.90 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 445 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 524
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 525 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLREG 604
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
|
170
....*....|....*.
gi 755534354 605 QQlcQDGhAVVVNILI 620
Cdd:cd02014 160 LA--ADG-PVVIDVVT 172
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
54-586 |
5.09e-22 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 100.46 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC--EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 131
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 132 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLD 211
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 212 VLypyfmVEKEMIPTKLPNSLMgrvvvwylqnclanlfvgaweprpegplPLDIPQASPQQVQRCVEILSRAKRPLLVLG 291
Cdd:PRK08611 165 LP-----AQKIKDTTNKTVDTF----------------------------RPTVPSPKPKDIKKAAKLINKAKKPVILAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 292 SQAllpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRSA--ALKKADVVVLAGAvcDFrlSYGRVL 364
Cdd:PRK08611 212 LGA---KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNlgkigTKPAyeAMQEADLLIMVGT--NY--PYVDYL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 365 NRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFM------IKLVE------GLQGQMwsSDWAEELRKADQQKE 430
Cdd:PRK08611 285 PKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALhqltenIKHVEdrrfleACQENM--AKWWKWMEEDENNAS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 431 QTYRDKALMPVLQhlnpvwvlqqveETLPDNALLVVD-GGDFVATAAYL-VQPRGPL---RWLdpgafGTLGVGAGFALG 505
Cdd:PRK08611 357 TPIKPERVMAAIQ------------KIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL-----GTMGCGLPGAIA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 506 AKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQ 585
Cdd:PRK08611 420 AKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGK 499
|
.
gi 755534354 586 G 586
Cdd:PRK08611 500 G 500
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
58-209 |
6.17e-18 |
|
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: 81.24 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 58 VAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNA 136
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534354 137 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELP 209
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLP 153
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
273-405 |
2.58e-16 |
|
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: 76.06 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 273 VQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKAD 345
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGA-SEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755534354 346 VVVLAGAVCDFRLSYGRV--LNRKSSIIIVNRNRDDLLLNSdifwKPQEAVQGDVGSFMIKL 405
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLpeFAPDAKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
49-551 |
3.14e-15 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 78.84 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 49 TSIRHggeSVAAVLRAHGVRFVFTLVGGHISPLLVACEKlGIRVVDTRHEVTAVFAADAVARLTGTVGV----AAVTAGP 124
Cdd:PRK07092 12 TTVRD---ATIDLLRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFvnlhSAAGVGN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 125 GLTNTVTAVKNaqvaQSP-VLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGP 203
Cdd:PRK07092 88 AMGNLFTAFKN----HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 204 VFVELPLDvlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEpRPEGPLPL-DIPQA---SPQQVQRCVEI 279
Cdd:PRK07092 164 VFVSIPYD----------------------------------------DWD-QPAEPLPArTVSSAvrpDPAALARLGDA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 280 LSRAKRPLLVLGsqALLPPTPANKLRAAV-ETLGVPCFLGGMS-RGLLGRNHPLH------IRQNRSAALKKADVVVLAG 351
Cdd:PRK07092 203 LDAARRPALVVG--PAVDRAGAWDDAVRLaERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLVIG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 352 AVCdFRL---SYGRVLNRKSSIIIVNrnrDDLLLNSdifWKPQ-EAVQGDVGSFMIKLVEGLqgqmwssdwAEELRKADQ 427
Cdd:PRK07092 281 APV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVGDIRLALRDLLALL---------PPSARPAPP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 428 QKEQTYRDKALMPVlqhLNPVWVLQQVEETLPDNALLVVDggdfvATAAYLV-QPRgpLRWLDPGAF-----GTLGVGAG 501
Cdd:PRK07092 345 ARPMPPPAPAPGEP---LSVAFVLQTLAALRPADAIVVEE-----APSTRPAmQEH--LPMRRQGSFytmasGGLGYGLP 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 755534354 502 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 551
Cdd:PRK07092 415 AAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
56-615 |
7.57e-15 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 77.72 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 56 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 134
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 135 NAQVAQSPVLLLggaASTLLQKR---GALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELPLD 211
Cdd:PRK06546 87 DAHRSGAPVLAI---ASHIPSAQigsGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 212 VlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLDIPQA------SPQQVQRCVEILSRAKR 285
Cdd:PRK06546 163 I---------------------------------------ADEPAPEGFAPSVISPRrptvvpDPAEVRALADAINEAKK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 286 PLLVLGS---------QALlpptpANKLRAAV-ETLGVPCFLG-------GMSrGLLGRNHPlhirqnrSAALKKADVVV 348
Cdd:PRK06546 204 VTLFAGAgvrgahaevLAL-----AEKIKAPVgHSLRGKEWIQydnpfdvGMS-GLLGYGAA-------HEAMHEADLLI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 349 LAGAvcDFrlSYGRVLNRKsSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQ 428
Cdd:PRK06546 271 LLGT--DF--PYDQFLPDV-RTAQVDIDPEHLGRRTRV----DLAVHGDVAETIRALLPLVKEKTDRRFLDRMLKKHARK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 429 KEQ---TYRDKalmpVLQH--LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLdpGAF--GTLGVGAG 501
Cdd:PRK06546 342 LEKvvgAYTRK----VEKHtpIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVI--GSFrhGSMANALP 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 502 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDVacslAYTDYHK 577
Cdd:PRK06546 416 HAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMlvdgLPDFGTDH----PPVDYAA 491
|
570 580 590
....*....|....*....|....*....|....*...
gi 755534354 578 AAMGLGAQGLILSrDNKDqVVKVLREGqqLCQDGHAVV 615
Cdd:PRK06546 492 IAAALGIHAVRVE-DPKD-VRGALREA--FAHPGPALV 525
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
447-616 |
1.56e-14 |
|
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: 71.94 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 447 PVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 526
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 527 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSrdNKDQVVKVLREGqq 606
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIE--SADDLLPVLERA-- 156
|
170
....*....|
gi 755534354 607 LCQDGHAVVV 616
Cdd:cd02010 157 LAADGVHVID 166
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
445-620 |
9.30e-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: 69.93 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 445 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 524
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 525 GYSLIEFDTFVRHKVPVIALVGNDAGWtQISREQVPRLGSDVACSLAY---------TDYHKAAMGLGAQGLILSRdnKD 595
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVET--PE 156
|
170 180
....*....|....*....|....*
gi 755534354 596 QVVKVLREGQqlcQDGHAVVVNILI 620
Cdd:cd02002 157 ELDEALREAL---AEGGPALIEVVV 178
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
62-524 |
1.05e-13 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 74.18 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 62 LRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVA 139
Cdd:PRK08273 13 LREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 140 QSPVLLLGGAastllQKRGAL-----QAIDQMSLFR----PLCKFCASVRRVRDIVP-TLRTAIAaaqsgTPGPVFVELP 209
Cdd:PRK08273 93 HVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVDrAVRTALA-----ERTVTAVILP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 210 LDVL---YPYFMVEKEMIPTKLPNSlMGRVVvwylqnclanlfvgawePRPEgplpldipqaspqQVQRCVEILSRAKRP 286
Cdd:PRK08273 163 NDVQeleYEPPPHAHGTVHSGVGYT-RPRVV-----------------PYDE-------------DLRRAAEVLNAGRKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 287 LLVLGSQALlppTPANKLRAAVETLGvpcflGGMSRGLLGRnhplhirqnrsAALKKaDVVVLAGAVcdfrlsyGrVLNR 366
Cdd:PRK08273 212 AILVGAGAL---GATDEVIAVAERLG-----AGVAKALLGK-----------AALPD-DLPWVTGSI-------G-LLGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 367 KSSIIIVnRNRDDLLLNSDIF----WKPQE----AVQGDVGSFMIKL---VE-GLQG--------------QMWSSDWAE 420
Cdd:PRK08273 264 KPSYELM-RECDTLLMVGSSFpyseFLPKEgqarGVQIDIDGRMLGLrypMEvNLVGdaaetlrallplleRKKDRSWRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 421 ELRKADQQKEQTYRDKALMPVlQHLNPVWVLQQVEETLPDNALLVVDGGDfVAT--AAYLVQPRGPLRWLDpGAFGTLGV 498
Cdd:PRK08273 343 RIEKWVARWWETLEARAMVPA-DPVNPQRVFWELSPRLPDNAILTADSGS-CANwyARDLRMRRGMMASLS-GTLATMGP 419
|
490 500
....*....|....*....|....*.
gi 755534354 499 GAGFALGAKLCQPEAEVWCLFGDGAF 524
Cdd:PRK08273 420 AVPYAIAAKFAHPDRPVIALVGDGAM 445
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
445-547 |
4.28e-13 |
|
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: 67.91 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 445 LNPVWVLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 521
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQhqmWAAQYYRFKKPR---SWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
|
90 100
....*....|....*....|....*.
gi 755534354 522 GAFGYSLIEFDTFVRHKVPVIALVGN 547
Cdd:cd02015 78 GSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
62-209 |
3.24e-12 |
|
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: 64.82 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 62 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 140
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLdAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 141 SPVLLLGGAASTLLQKRGA-----LQAID---QMSLFRPLCkfCASVRRVRDIVPT------LRTAIAAAQsgtpgPVFV 206
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGLllhhtLGDGDfdvFLKMFEEIT--CAAARLTDPENAAeeidrvLRTALRESR-----PVYI 158
|
...
gi 755534354 207 ELP 209
Cdd:cd07038 159 EIP 161
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
449-624 |
1.11e-11 |
|
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: 63.71 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 449 WVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 528
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 529 IEFDTFVRHKVPVIALVGNDAGWT---QISREQVPrlgsdvacslaYTD-----YHKAAMGLGAQGLILSRD--NKDQVV 598
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFRvkTEGELD 153
|
170 180
....*....|....*....|....*.
gi 755534354 599 KVLREGQQLCqdGHAVVVNILIGRTD 624
Cdd:cd02005 154 EALKDALFNR--DKLSLIEVILPKDD 177
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
54-585 |
4.89e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 65.66 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVL-LLGGAASTLLQKRGALQAiDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVEL 208
Cdd:PRK12474 87 LHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASagaVDSDVARAVQAAQSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 209 PLDVlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPL-DIPQA--SPQQVQRCVEILSRAKR 285
Cdd:PRK12474 163 PADV---------------------------------------AWNEAAYAAQPLrGIGPApvAAETVERIAALLRNGKK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 286 PLLVLGSQALL--PPTPANKLRAAVetlGVPCFLGGMS-RGLLGRNH-PL----HIRQNRSAALKKADVVVLAGAvcDFR 357
Cdd:PRK12474 204 SALLLRGSALRgaPLEAAGRIQAKT---GVRLYCDTFApRIERGAGRvPIeripYFHEQITAFLKDVEQLVLVGA--KPP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 358 LSYGRVLNRKSSIIIVNRNRDDLLlnsdifwKPQEavqgdvgsfmiKLVEGLQgqmwssDWAEELrkaDQQKEQTYRDKA 437
Cdd:PRK12474 279 VSFFAYPGKPSWGAPPGCEIVYLA-------QPDE-----------DLAQALQ------DLADAV---DAPAEPAARTPL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 438 LMPVLQH--LNPVWVLQQVEETLPDNAlLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEV 515
Cdd:PRK12474 332 ALPALPKgaLNSLGVAQLIAHRTPDQA-IYADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKV 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534354 516 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREqVPRLGSDVACSLAYT---------DYHKAAMGLGAQ 585
Cdd:PRK12474 411 VCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGE-LQRVGAQGAGRNALSmldlhnpelNWMKIAEGLGVE 488
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
54-352 |
1.11e-10 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 64.48 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 54 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 133 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 212
Cdd:PRK07586 83 LHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 213 lypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEP--RPEGPLPL-DIPQASPQQVQRCVEILSRAKRPLLV 289
Cdd:PRK07586 163 ---------------------------------------AWSEggPPAPPPPApAPAAVDPAAVEAAAAALRSGEPTVLL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 290 LGSQALLPPTPANKLRAAVET---LGVPCFLGGMSRGlLGRNH----PLHIRQNRsAALKKADVVVLAGA 352
Cdd:PRK07586 204 LGGRALRERGLAAAARIAAATgarLLAETFPARMERG-AGRPAverlPYFAEQAL-AQLAGVRHLVLVGA 271
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
58-549 |
5.56e-10 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 62.31 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 58 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNA 136
Cdd:PRK09124 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 137 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAqSGTPGPVFVELPLDVLYpy 216
Cdd:PRK09124 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDVAL-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 217 fmvekEMIPTKLPnslmgrvVVWYlqnclanlfvgaweprpEGPLPLDIPQASpqQVQRCVEILSRAKRPLLVLGS---Q 293
Cdd:PRK09124 166 -----KPAPERAT-------PHWY-----------------HAPQPVVTPAEE--ELRKLAALLNGSSNITLLCGSgcaG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 294 AllpptpANKLRAAVETLGVPC---------------FLGGMSrGLLGRNHPLHirqnrsaALKKADVVVLAGavCDFrl 358
Cdd:PRK09124 215 A------HDELVALAETLKAPIvhalrgkehveydnpYDVGMT-GLIGFSSGYH-------AMMNCDTLLMLG--TDF-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 359 SYGRVLNRKSSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQgqmwssdwaeelRKADqqkeQTYRDKAL 438
Cdd:PRK09124 277 PYRQFYPTDAKIIQIDINPGSLGRRSPV----DLGLVGDVKATLAALLPLLE------------EKTD----RKFLDKAL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 439 M----------------PVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 502
Cdd:PRK09124 337 EhyrkarkglddlavpsDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQ 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 755534354 503 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA 549
Cdd:PRK09124 417 ALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
475-622 |
1.08e-05 |
|
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: 46.89 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 475 AAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAgWTQI 554
Cdd:cd02006 38 GAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 555 SREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQGLILSRDNkdQVVKVLREGQQLCQDGHA-VVVNILIG 621
Cdd:cd02006 117 IRQAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPE--ELAAAFEQAKKLMAEHRVpVVVEAILE 194
|
.
gi 755534354 622 R 622
Cdd:cd02006 195 R 195
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
62-210 |
1.88e-05 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) 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. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 45.18 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755534354 62 LRAHGVRFVFTLVGGHISPLLVACEKLG-IRV---VDTRhevTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 137
Cdd:cd07037 7 LKRLGVRDVVISPGSRSAPLALAAAEHPeFRLhvrVDER---SAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755534354 138 VAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVR------RVRDIVPTLRTAIAAAQSGTPGPVFVELPL 210
Cdd:cd07037 84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
267-328 |
1.24e-03 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 39.93 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755534354 267 QASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAVETLGVP-CFLGGMSRGLLGRN 328
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| |
