|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
92-664 |
1.80e-125 |
|
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: 382.97 E-value: 1.80e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 92 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 170
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 171 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DVLYpyfmvekEMIPAQLPKGLMGRVvvwylqnclanlfagawEPRPegplpldipQASPQQVQRCVEILSRAKRPLLVL 330
Cdd:COG0028 163 DVQA-------AEAEEEPAPPELRGY-----------------RPRP---------APDPEAIEEAAELLAAAKRPVILA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 331 GSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSYG-R 402
Cdd:COG0028 210 GGGARRAGA-AEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALAEADLVLAVGARFDDRVTGNwD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 403 VLNRKSSIIIVNRNRDDMLLNsdifWKPQEAVQGDVGSFMIKLVEGLQGQTWS-SDWVEELRKADQQKEQTYRDKAllpv 481
Cdd:COG0028 289 EFAPDAKIIHIDIDPAEIGKN----YPVDLPIVGDAKAVLAALLEALEPRADDrAAWLARIAAWRAEYLAAYAADD---- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 482 pQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 561
Cdd:COG0028 361 -GPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 562 GAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDV-ACSLAYTDYHKAAMGLGAQGLilsR-DNEDQVVK 639
Cdd:COG0028 440 GGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKLAEAFGAKGE---RvETPEELEA 516
|
570 580
....*....|....*....|....*
gi 157823815 640 VLRDGQklcQEGHAVVVNILIGRTD 664
Cdd:COG0028 517 ALEEAL---ASDGPALIDVRVDPEE 538
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
93-626 |
1.33e-122 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 375.21 E-value: 1.33e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 93 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK05858 6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 LYPyfMVEKEMIPAQLPkglmgrvvvwylqnclanlfagawePRPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:PRK05858 166 AFS--MADDDGRPGALT-------------------------ELPAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIII 412
Cdd:PRK05858 213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 413 VnrnrDDMLLNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKADQQKEQtyRDKALL---PVPQHlnPVR 489
Cdd:PRK05858 291 V----DDAPPQRAHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARA--RDAAELaddRDPIH--PMR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 490 LLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 569
Cdd:PRK05858 363 VYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLM 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157823815 570 EFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVACSLA-YTDYHKAAMGLGAQG 626
Cdd:PRK05858 443 DVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHG 500
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
487-660 |
7.83e-63 |
|
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: 206.23 E-value: 7.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 487 PVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 566
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 567 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVP--RLGSDVACSLAYTDYHKAAMGLGAQGLILSRdnEDQVVKVLRDG 644
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLsyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTT--PEELKPALKRA 158
|
170
....*....|....*.
gi 157823815 645 QklcQEGHAVVVNILI 660
Cdd:cd02004 159 L---ASGKPALINVII 171
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
94-667 |
5.89e-59 |
|
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: 207.68 E-value: 5.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 173
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDVL 253
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 254 YPyfMVEKEMIPA-QLPKglmgrvvvwylqnclanlfAGAweprpegplpldipqASPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:TIGR02418 161 DS--PVSVKAIPAsYAPK-------------------LGA---------------APDDAIDEVAEAIQNAKLPVLLLGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirqnrsaalkkadvvvLAGAVCDFRLSYGRVLNRKSSIII 412
Cdd:TIGR02418 205 RASSPETTE-AVRRLLKKTQLPVVETFQGAGAVSRELEDH----------------FFGRVGLFRNQPGDRLLKQADLVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 413 V-------------NRNRDDMLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKADQQKEQT 472
Cdd:TIGR02418 268 TigydpieyeprnwNSENDATIVHIDVepaqidnNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQREAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 473 YRDKAlLPVPQHLNPVRLLQQVEETLPDNALLVVDGGDF-VATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLCQP 551
Cdd:TIGR02418 348 DRVPA-TLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHyIWMARYFRSYR-ARHLLISNGMQTLGVALPWAIGAALVRP 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 552 EAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILsr 631
Cdd:TIGR02418 426 NTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRV-- 503
|
570 580 590
....*....|....*....|....*....|....*.
gi 157823815 632 DNEDQVVKVLRdgQKLCQEGhAVVVNILIgrtDFRD 667
Cdd:TIGR02418 504 ESPDQLEPTLR--QAMEVEG-PVVVDIPV---DYSD 533
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
96-249 |
2.75e-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: 2.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 96 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 175
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823815 176 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELP 249
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
95-624 |
4.25e-58 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 205.21 E-value: 4.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 95 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 174
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 175 NAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLD 251
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 252 VlypyfMVEKemipaqlpkglmgrvvvwylqnclanlFAGAWEPRPEGPLPldiPQASPQQVQRCVEILSRAKRPLLVLG 331
Cdd:PRK07524 165 V-----LAAP---------------------------ADHLLPAPPTRPAR---PGPAPAALAQAAERLAAARRPLILAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 332 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRS-----AALKKADVVVLAG---AVCDFRLSYGRV 403
Cdd:PRK07524 210 GGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrALIAEADVVLAVGtelGETDYDVYFDGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 404 LNRKSSIIIVnrNRDDMLLNSdiFWKPQEAVQGDVGSFMIKLVEGLQGQTWSSDW----VEELRKAdQQKEQTyrdkall 479
Cdd:PRK07524 287 FPLPGELIRI--DIDPDQLAR--NYPPALALVGDARAALEALLARLPGQAAAADWgaarVAALRQA-LRAEWD------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 480 pvPQHLNPVRLLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLD-PGAFGTLGVGAGFALGAKLCQPEAEVWCL 558
Cdd:PRK07524 355 --PLTAAQVALLDTILAALPD-AIFVGDSTQPVYAGNLYFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPERPVVCL 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823815 559 FGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGA 624
Cdd:PRK07524 432 VGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGC 497
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
98-608 |
2.97e-57 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 203.68 E-value: 2.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 98 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 177
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 178 VAQSPVLLLGGAASTL---LQkRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDVLy 254
Cdd:PRK09259 96 TNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 255 pyfmveKEMIPAQLPKGLMGRVVvwylqnclanlfagaweprpeGPLPLDIPqaSPQQVQRCVEILSRAKRPLLVLGSQA 334
Cdd:PRK09259 174 ------AQTMDADEALTSLVKVV---------------------DPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 335 LLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGR--VLNRKSSIII 412
Cdd:PRK09259 225 AYAQADE-QIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgkTWGADKKFIQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 413 VNRNRDDMLLNSDIfwkpQEAVQGDVGSFMIKLVEGL--QGQTWSSDWVEELRKADQQKEQTYRDK-ALLPVP-QHLNPV 488
Cdd:PRK09259 304 IDIEPQEIDSNRPI----AAPVVGDIGSVMQALLAGLkqNTFKAPAEWLDALAERKEKNAAKMAEKlSTDTQPmNFYNAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 489 RLLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLcQPEAEVWCLFGDGAFGYSL 568
Cdd:PRK09259 380 GAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAV-ETGKPVVAIEGDSAFGFSG 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 157823815 569 IEFDTFVRHKVPVIALVGNDAGwtqISR--EQVPRLGSDVAC 608
Cdd:PRK09259 458 MEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSP 496
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
94-253 |
4.84e-57 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 190.52 E-value: 4.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQA-IDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLD 251
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 157823815 252 VL 253
Cdd:pfam02776 161 VL 162
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
94-634 |
4.82e-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: 4.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 LYPYFMVEKEMiPAQLPkglmgrvvvwylqnclanlfagAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:TIGR00118 163 TTAEIEYPYPE-KVNLP----------------------GYRPTVKG---------HPLQIKKAAELINLAKKPVILVGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLN 405
Cdd:TIGR00118 211 GVIIAGASE-ELKELAERIQIPVTTTLMGLGSFPEDHPLslgmlgmHGTKTANLAVHECDLIIAVGARFDDRVT-GNLAK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 406 RKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGL--QGQTWSSDWVEELR--KADQQKEQTYRDKAllpv 481
Cdd:TIGR00118 289 FAPNAKIIHIDIDPAEIGKNV--RVDIPIVGDARNVLEELLKKLfeLKERKESAWLEQINkwKKEYPLKMDYTEEG---- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 482 pqhLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 561
Cdd:TIGR00118 363 ---IKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGD 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823815 562 GAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQISREQvpRLGSdvACSLAYTDYHKAAMGLGAQGLILSRDNE 634
Cdd:TIGR00118 440 GSFQMNLQELSTAVQYDIPVKILILNNRylgmvrQWQELFYEE--RYSH--THMGSLPDFVKLAEAYGIKGIRIEKPEE 514
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
96-662 |
1.28e-54 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 196.76 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 96 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 175
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 176 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTpGPVFVELPLDVLYp 255
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYFY- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 256 yfmvekEMIPAQLPKglmgrvvvwylqnclanlfagaweprpegPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG---- 331
Cdd:PRK07525 168 ------GVIDVEIPQ-----------------------------PVRLERGAGGEQSLAEAAELLSEAKFPVILSGagvv 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 332 -SQALlpptpaNKLRAAVETLGVPCFLGGMSRGLLGRNHPLH---IRQNRSAA----LKKADVVVLAGAvcdfRLSYGRV 403
Cdd:PRK07525 213 lSDAI------EECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelIAKADVVLALGT----RLNPFGT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 404 LN--------RKSSIIIVNRNRDDMLLNsdifwKPQE-AVQGDVGSFMIKLVEGLQGQTWS---------------SDWV 459
Cdd:PRK07525 283 LPqygidywpKDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVARELLARLAERLAGdagreerkaliaaekSAWE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 460 EELRKADQQKEQ---TYRDKALLPVPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATA-AYLvQPRGPLRWLDPGAFGT 535
Cdd:PRK07525 358 QELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSIAnSYL-RFEKGRKYLAPGSFGN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 536 LGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSL-AYT 613
Cdd:PRK07525 437 CGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNV 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 157823815 614 DYHKAAMGLGAQGLILsrDNEDQVVKVLRDGQKLCQEGHAVVVNILIGR 662
Cdd:PRK07525 517 SYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
92-667 |
2.99e-50 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 183.90 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 92 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 171
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 172 AVKNAQVAQSPVLLLGGAA-STLLQKRgALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVkRADRLKR-THQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DVLYPyfMVEKEMI-PAQLPKglmgrvvvwylqnclanlfagaweprpEGPlpldipqASPQQVQRCVEILSRAKRPLLV 329
Cdd:PRK08617 164 DVVDA--PVTSKAIaPLSKPK---------------------------LGP-------ASPEDINYLAELIKNAKLPVLL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 330 LGSQALLPPTpANKLRAAVETLGVPCF-----LGGMSRGL---------LGRNHP---LhirqnrsaaLKKADVVVLAGa 392
Cdd:PRK08617 208 LGMRASSPEV-TAAIRRLLERTNLPVVetfqaAGVISRELedhffgrvgLFRNQPgdeL---------LKKADLVITIG- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 393 vcdfrlsYG------RVLNRKSSIIIVnrNRDDMLLNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKAD 466
Cdd:PRK08617 277 -------YDpieyepRNWNSEGDATII--HIDVLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 467 QQKEQtyRDKALLPVPQHL-NPVRLLQQVEETLPDNALLVVDGGDF---VATAAYLVQPRGPLrwldpgaFG----TLGV 538
Cdd:PRK08617 348 AQLEE--LAERPARLEEGAvHPLRIIRALQDIVTDDTTVTVDVGSHyiwMARYFRSYEPRHLL-------FSngmqTLGV 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 539 GAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKA 618
Cdd:PRK08617 419 ALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKY 498
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 157823815 619 AMGLGAQGliLSRDNEDQVVKVLRDGqkLCQEGhAVVVNILIgrtDFRD 667
Cdd:PRK08617 499 AESFGAKG--LRVTSPDELEPVLREA--LATDG-PVVIDIPV---DYSD 539
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
94-588 |
1.10e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 182.22 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHIspLLVACE---KLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 170
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAI--LNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 171 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DvlypyfmvekemIPAQLpkglmgrvvvwylqnclanlfaGAWEPRPEGPLPLDIP--QASPQQVQRCVEILSRAKRPLL 328
Cdd:PRK08527 163 D------------VTATL----------------------GEFEYPKEISLKTYKPtyKGNSRQIKKAAEAIKEAKKPLF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 329 VLGSQALLpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyG 401
Cdd:PRK08527 209 YLGGGAIL-SNASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDDRVT-G 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 402 RV--LNRKSSIIIVNRNRDDM--LLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQTWS--SDWVEELRKADQQKEQTYRD 475
Cdd:PRK08527 287 KLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELKEENPTtyKEWREILKRYNELHPLSYED 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 476 KALLPVPQHlnpvrLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEV 555
Cdd:PRK08527 361 SDEVLKPQW-----VIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVV 435
|
490 500 510
....*....|....*....|....*....|...
gi 157823815 556 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 588
Cdd:PRK08527 436 INFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
102-626 |
2.90e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 180.79 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 102 LRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQS 181
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 182 PVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVrDIVPTL-RAAMAAAQSGTPGPVFVELPLDVlypyfmve 260
Cdd:PRK08322 91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP-DNIPEVvREAFRLAEEERPGAVHLELPEDI-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 261 kemipaqlpkglmgrvvvwylqnclanlfagAWEPRPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 337
Cdd:PRK08322 162 -------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 338 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGavcdfrlsYGRV------L 404
Cdd:PRK08322 211 TA-SKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLSQGDYVHCAIEHADLIINVG--------HDVIekppffM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 405 NRKSSIIIVNRNRDDMLLNSDIFwkPQEAVQGDVGSFMIKLVEGL-QGQTWSSDWVEELRKA-DQQKEQTYRDKALLPVP 482
Cdd:PRK08322 282 NPNGDKKVIHINFLPAEVDPVYF--PQVEVVGDIANSLWQLKERLaDQPHWDFPRFLKIREAiEAHLEEGADDDRFPMKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 483 QhlnpvRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDG 562
Cdd:PRK08322 360 Q-----RIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDG 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823815 563 AFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQG 626
Cdd:PRK08322 435 GFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKG 498
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
94-585 |
1.91e-48 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 179.18 E-value: 1.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 173
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDVL 253
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 254 YPYFMVEKEMIPAQLPkgLMGrvvvwylqnclanlfagaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGSQ 333
Cdd:PRK06276 163 EGELDLEKYPIPAKID--LPG------------------YKPTTFG---------HPLQIKKAAELIAEAERPVILAGGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 334 ALLppTPANK-LRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGavCDFRlsyGRVLN 405
Cdd:PRK06276 214 VII--SGASEeLIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSVTESDVLIAIG--CRFS---DRTTG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 406 RKSSIIivnrnRDDMLLNSDIfwKPQE---------AVQGDVGSFMIKLVEGLQGQTWSSD--WVEELR--KADQQKEQT 472
Cdd:PRK06276 287 DISSFA-----PNAKIIHIDI--DPAEigknvrvdvPIVGDAKNVLRDLLAELMKKEIKNKseWLERVKklKKESIPRMD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 473 YRDKALlpVPQHLnpVRLLQQV--EETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQ 550
Cdd:PRK06276 360 FDDKPI--KPQRV--IKELMEVlrEIDPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAK 435
|
490 500 510
....*....|....*....|....*....|....*
gi 157823815 551 PEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALV 585
Cdd:PRK06276 436 PDANVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
94-626 |
3.16e-48 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 177.90 E-value: 3.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 171
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 172 AVKNAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVEL 248
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 249 PLDVlypyFMVEKEMIPAqlPKGlmgrvvvwylqnclanlfagawepRPEGPLPLDipqasPQQVQRCVEILSRAKRPLL 328
Cdd:PRK08266 166 PWDV----FGQRAPVAAA--PPL------------------------RPAPPPAPD-----PDAIAAAAALIAAAKNPMI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 329 VLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirQNRSAA---LKKADVVVLAGAVCDFRLSYGRVLN 405
Cdd:PRK08266 211 FVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG--LNFAAAyelWPQTDVVIGIGSRLELPTFRWPWRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 406 RKSSIIIVNRNRDDMllnsdIFWKPQEAVQGDVGSFMIKLVEGLQGQ-TWSSDWVEELRKADQQKEQtyRDKALLPVPQH 484
Cdd:PRK08266 286 DGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAgSKRPSRRAELRELKAAARQ--RIQAVQPQASY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 485 LNPVRllqqveETLPDNAlLVVDGGDFVATAAYLVQP-RGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 563
Cdd:PRK08266 359 LRAIR------EALPDDG-IFVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823815 564 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQG 626
Cdd:PRK08266 432 FMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLAESFGVAA 495
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
94-655 |
5.62e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 172.07 E-value: 5.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 173
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDVL 253
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 254 ---YPYFMVEKEMIPAQLPkglmgrvvvwylqnclanlfagawEPRPEgplpldipqasPQQVQRCVEILSRAKRPLLVL 330
Cdd:PRK06725 177 nekVTSFYNEVVEIPGYKP------------------------EPRPD-----------SMKLREVAKAISKAKRPLLYI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 331 GSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRV 403
Cdd:PRK06725 222 GG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAVTECDLLLALGVRFDDRVT-GKL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 404 --LNRKSSIIIVNRNRDDMLLNSDIfwkpQEAVQGDVGSFMIKLVEgLQGQTWSSDWVEELRKADQQKEQTYRDKallpv 481
Cdd:PRK06725 300 elFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKKALHMLLH-MSIHTQTDEWLQKVKTWKEEYPLSYKQK----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 482 PQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 561
Cdd:PRK06725 370 ESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 562 GAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQI---SREQVPRLGSdvacslayTDYHKAAMGLGAQGliLSRD 632
Cdd:PRK06725 450 ASFQMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS--------PDFVKVAEAYGVKG--LRAT 519
|
570 580
....*....|....*....|...
gi 157823815 633 NEDQVVKVLRDGqkLCQEGHAVV 655
Cdd:PRK06725 520 NSTEAKQVMLEA--FAHEGPVVV 540
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
94-634 |
1.60e-45 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 170.73 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 173
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDvl 253
Cdd:PRK06048 90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKD-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 254 ypyfmVEKEMIPAQLPKGLMGRvvvwylqnclanlfagAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL----- 328
Cdd:PRK06048 168 -----VTTAEIDFDYPDKVELR----------------GYKPTYKG---------NPQQIKRAAELIMKAERPIIyaggg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 329 VLGSQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFRLSyG 401
Cdd:PRK06048 218 VISSNA------SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARFDDRVT-G 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 402 RVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQTWsSDWVEELRKADQQKEQTYRDKALLPV 481
Cdd:PRK06048 291 KLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQYCDR-KEWLDKINQWKKEYPLKYKEREDVIK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 482 PQHlnpvrLLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 561
Cdd:PRK06048 368 PQY-----VIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGD 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823815 562 GAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQISREQvpRLGSdvACSLAYTDYHKAAMGLGAQGLILSRDNE 634
Cdd:PRK06048 442 GSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDK--RYSH--TCIKGSVDFVKLAEAYGALGLRVEKPSE 516
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
84-662 |
1.29e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 168.07 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 84 HKVDKTSIRHGGESVAAVLRAHGVRFVFtlvGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTG--TVGVAAVT 161
Cdd:PRK06154 12 HLPAEAKTMKVAEAVAEILKEEGVELLF---GFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 162 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTllqkrgALQAID----QMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQ 237
Cdd:PRK06154 89 YGPGAENAFGGVAQAYGDSVPVLFLPTGYPR------GSTDVApnfeSLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 238 SGTPGPVFVELPLDVLYpyfmvekemipaqlpkglmgrvvvwylqnclanlfagawEPRPEGPL-----PLDIPQASPQQ 312
Cdd:PRK06154 163 NGRPGPVVLELPVDVLA---------------------------------------EELDELPLdhrpsRRSRPGADPVE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 313 VQRCVEILSRAKRPLLVLGsQALLPPTPANKLRAAVETLGVPCF--LGGMSRglLGRNHPLHIRQNRSAA-------LKK 383
Cdd:PRK06154 204 VVEAAALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMttLNGKSA--FPEDHPLALGSGGRARpatvahfLRE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 384 ADVVVLAGavCDF-RLSYGRVLNRKSSIIIVnrNRDDMLLNSDIFWKpqEAVQGDVGSFMIKLVEGLQGQTW-----SSD 457
Cdd:PRK06154 281 ADVLFGIG--CSLtRSYYGLPMPEGKTIIHS--TLDDADLNKDYPID--HGLVGDAALVLKQMIEELRRRVGpdrgrAQQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 458 WVEELRKADQQKEQTYRDKaLLPVPQHLNPVRLLQQVEETL-PDNALLVVDGG---DFVATAAYLVQPRGPLRWldpGAF 533
Cdd:PRK06154 355 VAAEIEAVRAAWLAKWMPK-LTSDSTPINPYRVVWELQHAVdIKTVIITHDAGsprDQLSPFYVASRPGSYLGW---GKT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 534 GTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISREQVPRLGSDVACSLAYT 613
Cdd:PRK06154 431 TQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN-FSMGGYDKVMPVSTTKYRATDISG 509
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 157823815 614 DYHKAAMGLGAQGLILSRdnEDQVVKVLRDGQKLCQEGHAVVVNILIGR 662
Cdd:PRK06154 510 DYAAIARALGGYGERVED--PEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
94-647 |
1.47e-44 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 168.44 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 170
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGavlYIYDELYKQDK--IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 171 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DvlypyfmVEKEMIPAQLPKGLmgrvvvwylqnclanlfagawEPRPEGPlpldIPQASPQQVQRCVEILSRAKRPLLVL 330
Cdd:PRK06965 181 D-------VSKTPCEYEYPKSV---------------------EMRSYNP----VTKGHSGQIRKAVSLLLSAKRPYIYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 331 GSQALLpPTPANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRL- 398
Cdd:PRK06965 229 GGGVIL-ANASRELRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFDDRVi 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 399 ---SYGRVLNRKSSIIIVNRNRDDMLLNSDIfwkpqeAVQGDVGSFMIKLVEGLQ-----------GQTWSSdwVEELRK 464
Cdd:PRK06965 304 gnpAHFASRPRKIIHIDIDPSSISKRVKVDI------PIVGDVKEVLKELIEQLQtaehgpdadalAQWWKQ--IEGWRS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 465 ADQQKeqtYRDKALLPVPQHlnpvrllqqVEETLPD----NALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGA 540
Cdd:PRK06965 376 RDCLK---YDRESEIIKPQY---------VVEKLWEltdgDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGL 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 541 GFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV--IAL----VGNDAGWTQIsrEQVPRLGSDVACSLAytD 614
Cdd:PRK06965 444 PYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVkiISLnnryLGMVRQWQEI--EYSKRYSHSYMDALP--D 519
|
570 580 590
....*....|....*....|....*....|...
gi 157823815 615 YHKAAMGLGAQGLILSRDNEdqVVKVLRDGQKL 647
Cdd:PRK06965 520 FVKLAEAYGHVGMRIEKTSD--VEPALREALRL 550
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
94-591 |
1.65e-44 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 167.47 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAAST--LLQKRGAL-QAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELP 249
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 250 LDvlypyfmvekemipaqlpkgLMGRVVVWylqnclanlfagawePRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV 329
Cdd:PRK07064 165 ID--------------------IQAAEIEL---------------PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 330 LGSQALlppTPANKLRAAVEtLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAA----LKKADVVVLAGAvcDFR----LSY 400
Cdd:PRK07064 210 LGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAvealYKTCDLLLVVGS--RLRgnetLKY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 401 GRVLNRKSSIIIVNRNRDDMLLNSDIFwkpqeaVQGDVGSFMIKLVEGLQGQTW-SSDWVEELRKADQQKEQTYRDKall 479
Cdd:PRK07064 284 SLALPRPLIRVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLSvDPAFAADLRAAREAAVADLRKG--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 480 pvpqhLNPVRLL-QQVEETLPDNALLVVDGGdfVATAAY---LVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEV 555
Cdd:PRK07064 355 -----LGPYAKLvDALRAALPRDGNWVRDVT--ISNSTWgnrLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKT 426
|
490 500 510
....*....|....*....|....*....|....*.
gi 157823815 556 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 591
Cdd:PRK07064 427 VGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
94-634 |
1.07e-43 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 165.70 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFtlvGGHI-SPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFcasVRRVRD---IVPTLRAAMAAAQSGTPGPVFVELP 249
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 250 LDVLYPyfmvekemiPAQLPkglmgrvvvwylqnclanlfaGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV 329
Cdd:PRK06112 170 ADLLTA---------AAAAP---------------------AAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 330 LG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI------------RQNRSAALKKADVVVLAGA 392
Cdd:PRK06112 220 AGggvhiSGA------SAALAALQSLAGLPVATTNMGKGAVDETHPLSLgvvgslmgprspGRHLRDLVREADVVLLVGT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 393 VCDFRLSYGRVLNRKSSIII--------VNRNRDDMLLNSDifwkPQEAVQGdvgsfmikLVEGLQGQTWS--------- 455
Cdd:PRK06112 294 RTNQNGTDSWSLYPEQAQYIhidvdgeeVGRNYEALRLVGD----ARLTLAA--------LTDALRGRDLAaragrraal 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 456 SDWVEELRKADQQKEQTYRDKALLPVpqhlNPVRLLQQVEETLPDNALLVVDGG-DFVATAAYLVQPRGPLRWLDPGAFG 534
Cdd:PRK06112 362 EPAIAAGREAHREDSAPVALSDASPI----RPERIMAELQAVLTGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLA 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 535 TLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA--GWtQISREQVpRLGSDV-ACSLA 611
Cdd:PRK06112 438 GLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF-QKHAETV-KFGTHTdACHFA 515
|
570 580
....*....|....*....|...
gi 157823815 612 YTDYHKAAMGLGAQGLILSRDNE 634
Cdd:PRK06112 516 AVDHAAIARACGCDGVRVEDPAE 538
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
92-594 |
3.93e-42 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 160.81 E-value: 3.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 92 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 170
Cdd:PRK08199 8 RTGGQILVDALRANGVERVFCVPGESYLAVLDALhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 171 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:PRK08199 88 IGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DVLYpyfmvekemipaqlpkglmGRVVVwylqnclanlfAGAWEPRPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVL 330
Cdd:PRK08199 168 DVLS-------------------ETAEV-----------PDAPPYRRVAAAP------GAADLARLAELLARAERPLVIL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 331 G-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRS--AALKKADVVVLAGAvcdfRL 398
Cdd:PRK08199 212 GgsgwtEAA------VADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDlglgiNPAlaARIREADLVLAVGT----RL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 399 syGRVLNRKSSIIIVNRNRdDMLLNSDI-------FWKPQEAVQGDVGSF--MIKLVEGLQGQTWsSDWVEELRkadqqk 469
Cdd:PRK08199 282 --GEVTTQGYTLLDIPVPR-QTLVHVHPdaeelgrVYRPDLAIVADPAAFaaALAALEPPASPAW-AEWTAAAH------ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 470 eQTYRD-KALLPVPQHLNPVRLLQQVEETLPDNALLVVDGGDFvatAAYL---VQPRGPLRWLDPGAfGTLGVGAGFALG 545
Cdd:PRK08199 352 -ADYLAwSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNY---ATWLhrfFRFRRYRTQLAPTS-GSMGYGLPAAIA 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 157823815 546 AKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQI 594
Cdd:PRK08199 427 AKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
94-589 |
1.50e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 159.10 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 lypyfmvekemipaqlpkglmgrvvvwylQNCLANLfaGAWePRPEGPLPldIPQASPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:PRK08155 175 -----------------------------QTAVIEL--EAL-PAPAEKDA--APAFDEESIRDAAAMINAAKRPVLYLGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRlSYGRV-- 403
Cdd:PRK08155 221 GVINSGAPARARELA-EKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYILQEADLLIVLGARFDDR-AIGKTeq 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 404 LNRKSSIIIVNRNRDDMllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQTwSSDWVEelRKADQQKEQTyrdkalLPVPQ 483
Cdd:PRK08155 299 FCPNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQP-RAEWHQ--LVADLQREFP------CPIPK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 484 HLNPVR---LLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWC 557
Cdd:PRK08155 366 ADDPLShygLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPR---QWLTSGGLGTMGFGLPAAIGAALANPERKVLC 442
|
490 500 510
....*....|....*....|....*....|...
gi 157823815 558 LFGDGAFGYSLIEFDTFVRHKVPV-IALVGNDA 589
Cdd:PRK08155 443 FSGDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
94-597 |
4.27e-40 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 155.98 E-value: 4.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 169
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 170 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELP 249
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 250 LDV---LYPYFMVEkemiPAQL-PKGlmgrvvvwylqnclanlfagaWEPRPEGplpldipqaSPQQVQRCVEILSRAKR 325
Cdd:PRK07418 181 KDVgqeEFDYVPVE----PGSVkPPG---------------------YRPTVKG---------NPRQINAALKLIEEAER 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 326 PLLVLGSQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRL 398
Cdd:PRK07418 227 PLLYVGGGAISAGAHAE-LKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAVTECDLLIAVGARFDDRV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 399 --------SYGRVLNrkssIII----VNRNRddmllnsdifwKPQEAVQGDVGSFMIKLVEGLQGQTWS---SDWVEELr 463
Cdd:PRK07418 306 tgkldefaSRAKVIH----IDIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEPTTPprtQAWLERI- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 464 kadqqkeQTYRDKALLPVPQH---LNPVRLLQQVEETLPDnALLVVDGGDFVATAA-YLvqPRGPLRWLDPGAFGTLGVG 539
Cdd:PRK07418 370 -------NRWKQDYPLVVPPYegeIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAqFL--RNGPRRWISSAGLGTMGFG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 157823815 540 AGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISRE 597
Cdd:PRK07418 440 MPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQ 496
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
83-587 |
1.74e-39 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 153.44 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 83 MHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVT 161
Cdd:PRK07282 1 MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 162 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTP 241
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 242 GPVFVELPLDVlypyfmVEKEmipaqlpkglmgrvvVWYLQNclanlfagaweprPEGPLPLDIPQASPQ--QVQRCVEI 319
Cdd:PRK07282 161 GPVVIDLPKDV------SALE---------------TDFIYD-------------PEVNLPSYQPTLEPNdmQIKKILKQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 320 LSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGA 392
Cdd:PRK07282 207 LSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANIAMTEADFMINIGS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 393 VCDFRLSyGRVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKaDQQKEQT 472
Cdd:PRK07282 286 RFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLAEPTVHNNTEKWIEKVTK-DKNRVRS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 473 YRDKALLPVPQHlnpvrLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 552
Cdd:PRK07282 362 YDKKERVVQPQA-----VIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPD 436
|
490 500 510
....*....|....*....|....*....|....*.
gi 157823815 553 AEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 587
Cdd:PRK07282 437 KEVILFVGDGGFQMTNQELAILNIYKVPIkVVMLNN 472
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
94-626 |
2.95e-39 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 152.68 E-value: 2.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVA----CEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 169
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 170 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELP 249
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 250 LDVLYpyfmvEKemipaqlpkglMGRVVvwylqnclanlfagaWEPRPEGPLPLDIPQ-ASPQQVQRCVEILSRAKRPLL 328
Cdd:PRK06456 164 RDIFY-----EK-----------MEEIK---------------WPEKPLVKGYRDFPTrIDRLALKKAAEILINAERPII 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 329 VLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFR--LS 399
Cdd:PRK06456 213 LVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfTS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 400 YGRVLNRKSSIIIVNRNRDDmllnSDIFWKPQEAVQGDVGSF---MIKLVEGLQGQTWSSDWVEELRKADQQKEQTYRDK 476
Cdd:PRK06456 292 YDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIIlreLIKAITELGQKRDRSAWLKRVKEYKEYYSQFYYTE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 477 AllpvPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVW 556
Cdd:PRK06456 368 E----NGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVV 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823815 557 CLFGDGAFGYSLIEFDTFVRHKVPVIALVgNDAGWTQISReQVPRL-------GSDVACSlayTDYHKAAMGLGAQG 626
Cdd:PRK06456 444 DLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVR-QVQDLffgkrivGVDYGPS---PDFVKLAEAFGALG 515
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
94-581 |
1.45e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 150.74 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 LYPYFmvekeMIPAQLPKGLMGRvvvwylqnclanlfagAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:PRK08979 166 LNPAI-----LHPYEYPESIKMR----------------SYNPTTSG---------HKGQIKRGLQALLAAKKPVLYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLN 405
Cdd:PRK08979 216 GAIISGADKQILQLA-EKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNADLIFGIGVRFDDRTT-NNLEK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 406 RKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQTWSSD------WVEELRKADQQKEQTYrDKAll 479
Cdd:PRK08979 294 YCPNATILHIDIDPSSISKTV--RVDIPIVGSADKVLDSMLALLDESGETNDeaaiasWWNEIEVWRSRNCLAY-DKS-- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 480 pvPQHLNPvrllQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEV 555
Cdd:PRK08979 369 --SERIKP----QQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETV 442
|
490 500
....*....|....*....|....*.
gi 157823815 556 WCLFGDGAFGYSLIEFDTFVRHKVPV 581
Cdd:PRK08979 443 VCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
94-587 |
2.75e-38 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 149.65 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 173
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDVL 253
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 254 ypyfMVEKEMIPAQLPkglmgrvvvwylqnclanlfagaweprpegplPLDIPQASPQQVQRCVEILSRAKRPLLVLG-- 331
Cdd:PRK08978 163 ----LAEGELEPHLTT--------------------------------VENEPAFPAAELEQARALLAQAKKPVLYVGgg 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 332 ---SQAllppTPAnkLRAAVETLGVP--CFLGGMsrGLLGRNHP-----LHIRQNRSA--ALKKADVVVLAGAVCDFRLS 399
Cdd:PRK08978 207 vgmAGA----VPA--LREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDRVT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 400 yGRvLNR---KSSIIIVNRNRDDM--LLNSDIfwkpqeAVQGDvgsfMIKLVEGLQGQTWSSDWVEELRKADQQKEQTYR 474
Cdd:PRK08978 279 -GK-LNTfapHAKVIHLDIDPAEInkLRQAHV------ALQGD----LNALLPALQQPLNIDAWRQHCAQLRAEHAWRYD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 475 DKAllpvpQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAE 554
Cdd:PRK08978 347 HPG-----EAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDT 421
|
490 500 510
....*....|....*....|....*....|....
gi 157823815 555 VWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 587
Cdd:PRK08978 422 VICVSGDGSFMMNVQELGTIKRKQLPVkIVLLDN 455
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
94-660 |
2.98e-37 |
|
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: 146.90 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLL--VACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 171
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 172 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTpGPVFVELPLD 251
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 252 vlYPYFMVEKEMipaqlpkglmgrvvvWYLQNCLANLFAgaweprpegplpldIPQASPQQVQRCVEILSRAKRPLLVLG 331
Cdd:TIGR02720 160 --FGWQEIPDND---------------YYASSVSYQTPL--------------LPAPDVEAVTRAVQTLKAAERPVIYYG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 332 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlaGAVCDFRLSYGRvlNRKSSII 411
Cdd:TIGR02720 209 IGAR---KAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEA---LFQADLVLFVGN--NYPFAEV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 412 IVNRNRDDMLLNSDI----FWKPQE---AVQGDVGSFmIKLVEGLQGQTWSSDWVEElRKADQQKEQTYRDKALLPVPQH 484
Cdd:TIGR02720 281 SKAFKNTKYFIQIDIdpakLGKRHHtdiAVLADAKKA-LAAILAQVEPRESTPWWQA-NVANVKNWRAYLASLEDKTEGP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 485 LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 564
Cdd:TIGR02720 359 LQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 565 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGAQGLILsrDNEDQVVKV 640
Cdd:TIGR02720 439 SMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQedtnQPLIGVD----FNDADFAKIAEGVGAVGFRV--NKIEQLPAV 512
|
570 580
....*....|....*....|
gi 157823815 641 LRDGQKLcQEGHAVVVNILI 660
Cdd:TIGR02720 513 FEQAKAI-KQGKPVLIDAKI 531
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
94-584 |
6.03e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 146.15 E-value: 6.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 LYPYFmvekeMIPAQLPKGLMGRvvvwylqnclanlfagAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:PRK07979 166 LNPAN-----KLPYVWPESVSMR----------------SYNPTTQG---------HKGQIKRALQTLVAAKKPVVYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPAnKLRAAVETLGVPCF-----LGGM------SRGLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 401
Cdd:PRK07979 216 GAINAACHQ-QLKELVEKLNLPVVsslmgLGAFpathrqSLGMLG----MHGTYEANMTMHNADVIFAVGVRFDDRTTNN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 402 RVLNRKSSIII---VNRNRDDMLLNSDIfwkpqeAVQGDVGSFMIKLVEgLQGQTWSSDWVEELRKADQQKEQtYRDKAL 478
Cdd:PRK07979 291 LAKYCPNATVLhidIDPTSISKTVTADI------PIVGDARQVLEQMLE-LLSQESAHQPLDEIRDWWQQIEQ-WRARQC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 479 L---PVPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEV 555
Cdd:PRK07979 363 LkydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETV 442
|
490 500
....*....|....*....|....*....
gi 157823815 556 WCLFGDGAFGYSLIEFDTFVRHKVPVIAL 584
Cdd:PRK07979 443 VCVTGDGSIQMNIQELSTALQYELPVLVL 471
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
94-581 |
8.44e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 145.66 E-value: 8.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 170
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 171 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DVLYPYFMVEKEMipaqlPKGLMGRvvvwylqnclanlfagAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL-- 328
Cdd:PRK06466 164 DMTNPAEKFEYEY-----PKKVKLR----------------SYSPAVRG---------HSGQIRKAVEMLLAAKRPVIys 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 329 ----VLGSQALLPPTPANKLRAAVET--LGVPCFLGGMSR--GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrlsy 400
Cdd:PRK06466 214 gggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEANMAMHHADVILAVGARFD----- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 401 GRVLNRKSSII----IVNRNRDDMLLNSDIFWK-----PQEAVQGDVGSFMIKLVEGLQGQTWSSDW--VEELRKA-DQQ 468
Cdd:PRK06466 285 DRVTNGPAKFCpnakIIHIDIDPASISKTIKADipivgPVESVLTEMLAILKEIGEKPDKEALAAWWkqIDEWRGRhGLF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 469 KEQTYRDKALLPvpqhlnpvrllQQVEETLPD----NALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 544
Cdd:PRK06466 365 PYDKGDGGIIKP-----------QQVVETLYEvtngDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAM 433
|
490 500 510
....*....|....*....|....*....|....*..
gi 157823815 545 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 581
Cdd:PRK06466 434 GVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
81-588 |
2.19e-36 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 144.13 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 81 QLMHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAV 160
Cdd:PRK07710 5 RTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 161 TAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGT 240
Cdd:PRK07710 85 TSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 241 PGPVFVELPLDVLypyfmvekemipaqlpkglmgrvvvwylqnclanLFAGAWEPRPEGPLPLDIPQASPQ--QVQRCVE 318
Cdd:PRK07710 165 PGPVLIDIPKDMV----------------------------------VEEGEFCYDVQMDLPGYQPNYEPNllQIRKLVQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 319 ILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAG 391
Cdd:PRK07710 211 AVSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLflgmagmHGTYTANMALYECDLLINIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 392 AVCDFRLSyGRVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKADQQKEQ 471
Cdd:PRK07710 290 ARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWKEKYPL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 472 TYRDKAllpvpQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQP 551
Cdd:PRK07710 367 SYKRNS-----ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKP 441
|
490 500 510
....*....|....*....|....*....|....*..
gi 157823815 552 EAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 588
Cdd:PRK07710 442 DETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
94-588 |
6.35e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 143.13 E-value: 6.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGgIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 LYPYFmvekeMIPAQLPKGLMGRvvvwylqnclanlfagAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:PRK06882 166 VNPAN-----KFTYEYPEEVSLR----------------SYNPTVQG---------HKGQIKKALKALLVAKKPVLFVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTpANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 401
Cdd:PRK06882 216 GVITAEC-SEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEANNAMHESDLILGIGVRFDDRTTNN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 402 rvLNR---KSSIIIVNRNRDDMLLNSDIFWKPQEAVQGDVGSFMIKLVEG--LQGQTWSSDWVEELR--KADQQKEQTYR 474
Cdd:PRK06882 291 --LAKycpNAKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEEnlAKSQTDLTAWWQQINewKAKKCLEFDRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 475 DKALLPvpqhlnpvrllQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQ 550
Cdd:PRK06882 369 SDVIKP-----------QQVVEAIyrltNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAH 437
|
490 500 510
....*....|....*....|....*....|....*...
gi 157823815 551 PEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 588
Cdd:PRK06882 438 PEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
105-587 |
3.96e-35 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 140.60 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 105 HGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 180
Cdd:CHL00099 23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 181 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV---LYPYF 257
Cdd:CHL00099 103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 258 MVEKEMIPAQLPKglmgrvvvwylqnclanlfagaWEPrpegplpldIPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 337
Cdd:CHL00099 183 PPEPGNTIIKILG----------------------CRP---------IYKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 338 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLNRKSSI 410
Cdd:CHL00099 232 DA-HQEITELAELYKIPVTTTLMGKGIFDEDHPLclgmlgmHGTAYANFAVSECDLLIALGARFDDRVT-GKLDEFACNA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 411 IIV-----------NRNrddmllnsdifwkPQEAVQGDVGSFMIKLVEGL----------QGQTWssdwveelrkadQQK 469
Cdd:CHL00099 310 QVIhididpaeigkNRI-------------PQVAIVGDVKKVLQELLELLknspnlleseQTQAW------------RER 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 470 EQTYRDKALLPVPQH---LNPVRLLQQVEETLPDnALLVVDGGDFVATAAYL--VQPRgplRWLDPGAFGTLGVGAGFAL 544
Cdd:CHL00099 365 INRWRKEYPLLIPKPstsLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlkCKPR---KWLSSAGLGTMGYGLPAAI 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 157823815 545 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 587
Cdd:CHL00099 441 GAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIkIIIINN 484
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
94-587 |
2.73e-34 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 138.58 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLgiRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 170
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 171 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 251 DVLypyfmvekemiPAQLPkglmgrvvvwylqnclanlFagAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVL 330
Cdd:PRK07789 191 DAL-----------QAQTT-------------------F--SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 331 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDfrlsyGRV 403
Cdd:PRK07789 239 GGGVIRAEASA-ELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgmhgtvAAVAALQRSDLLIALGARFD-----DRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 404 LNRKSSI-----II--------VNRNRddmllNSDIFwkpqeaVQGDVGSFMIKLVEGLQ------GQTWSSDWVEELRK 464
Cdd:PRK07789 313 TGKLDSFapdakVIhadidpaeIGKNR-----HADVP------IVGDVKEVIAELIAALRaehaagGKPDLTAWWAYLDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 465 ADQQKEQTYRDkallPVPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 544
Cdd:PRK07789 382 WRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAM 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 157823815 545 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 587
Cdd:PRK07789 458 GAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINN 501
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
96-662 |
5.59e-33 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 134.34 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 96 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 173
Cdd:PRK11269 8 DAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDVL 253
Cdd:PRK11269 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 254 ypyfMVEKEmipaqlpkglmgrvvvwylqnclanlfagaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 333
Cdd:PRK11269 168 ----VAEIE------------------------------FDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 334 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL----------HIRQNrsAALKKADVVVLAGAvcdfrlsygRV 403
Cdd:PRK11269 213 GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATLLASDFVLGIGN---------RW 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 404 LNRKSSIIIVNRnRDDMLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQTWS------SDWVEEL--RKADQQ 468
Cdd:PRK11269 282 ANRHTGSVEVYT-KGRKFVHVDIeptqigrVFGPDLGIVSDAKAALELLVEVAREWKAAgrlpdrSAWVADCqeRKRTLL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 469 KEQTYRDkallpVPqhLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 548
Cdd:PRK11269 361 RKTHFDN-----VP--IKPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 549 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPrLGSDVACSLAY------------TDYH 616
Cdd:PRK11269 434 ADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRA-FDMDYCVQLAFeninspelngygVDHV 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 157823815 617 KAAMGLGAQGLILSRDNEdqVVKVLRDGQKLCQEGHA-VVVNILIGR 662
Cdd:PRK11269 513 KVAEGLGCKAIRVFKPED--IAPALEQAKALMAEFRVpVVVEVILER 557
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
94-581 |
6.84e-33 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 134.06 E-value: 6.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 lypYFMVEKEMIPAQLPkglmgrvvvwylqnclanlFAGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 332
Cdd:PRK09107 173 ---QFATGTYTPPQKAP-------------------VHVSYQPKVKG---------DAEAITEAVELLANAKRPVIYSGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 QALLPPTPANK-LRAAVETLGVP--CFLGGMSR---------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSy 400
Cdd:PRK09107 222 GVINSGPEASRlLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYEANMAMHDCDVMLCVGARFDDRIT- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 401 GRV-----LNRKSSIII----VNRNrddmlLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQTWSSD------WVEELRKA 465
Cdd:PRK09107 297 GRLdafspNSKKIHIDIdpssINKN-----VRVDV------PIIGDVGHVLEDMLRLWKARGKKPDkealadWWGQIARW 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 466 DQQKEQTYRDKALLPVPQHlnpvrLLQQVEE-TLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 544
Cdd:PRK09107 366 RARNSLAYTPSDDVIMPQY-----AIQRLYElTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAAL 440
|
490 500 510
....*....|....*....|....*....|....*..
gi 157823815 545 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 581
Cdd:PRK09107 441 GVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
102-591 |
3.48e-31 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 128.58 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 102 LRAHGVRFVFTLVGGHISPLLVACEK---LGIRVVDT---RHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 175
Cdd:PRK08327 17 LKELGVDYIFINSGTDYPPIIEAKARaraAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANALGGVHN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 176 AQVAQSPVLLLGGAASTLlqKRGAL-----------QAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPV 244
Cdd:PRK08327 97 AARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 245 FVELPLDVLypyfmVEKemipaqlpkglmgrvvvwylqnclanlfAGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAK 324
Cdd:PRK08327 175 YLTLPREVL-----AEE----------------------------VPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 325 RPLLV---LGSQALLPPTpankLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 401
Cdd:PRK08327 222 RPVIItwrAGRTAEGFAS----LRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLVLVVDSDVPWIPKKI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 402 RvLNRKSSIIIVnrnrDDMLLNSDI-FWK-PQE-AVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKADQQKEQTYRDKAL 478
Cdd:PRK08327 298 R-PDADARVIQI----DVDPLKSRIpLWGfPCDlCIQADTSTALDQLEERLKSLASAERRRARRRRAAVRELRIRQEAAK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 479 LPVPQHL------NPVRLLQQVEETLPDNALLVVDGGdFVATAAYLvqpRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 552
Cdd:PRK08327 373 RAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPGSYFGDGSAGGLGWALGAALGAKLATPD 448
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 157823815 553 AEVWCLFGDGAFGYSLIEFDTFV--RHKVPVIALVGNDAGW 591
Cdd:PRK08327 449 RLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
92-588 |
4.90e-30 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 125.23 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 92 RHGGESVAAVLRAHGVRFVFTLVGG-----HISPLLVACeklgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGL 166
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGasmeiHQALTRSNC----IRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 167 TNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFV 246
Cdd:PLN02470 89 TNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 247 ELPLDVlYPYFMVEKEMIPAQLPkGLMGRVvvwylqnclanlfagawePRPegplpldiPQASpqQVQRCVEILSRAKRP 326
Cdd:PLN02470 169 DIPKDI-QQQLAVPNWNQPMKLP-GYLSRL------------------PKP--------PEKS--QLEQIVRLISESKRP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 327 LLVLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDFRLS 399
Cdd:PLN02470 219 VVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANYAVDSADLLLAFGVRFDDRVT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 400 yGRV--LNRKSSIIIVNRNRDDMLLNSdifwKPQEAVQGDVG---SFMIKLVEGLQGQTWS-SDWVEELrkaDQQKEQ-- 471
Cdd:PLN02470 296 -GKLeaFASRASIVHIDIDPAEIGKNK----QPHVSVCADVKlalQGLNKLLEERKAKRPDfSAWRAEL---DEQKEKfp 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 472 -TYRDKALLPVPQHLnpvrlLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQ 550
Cdd:PLN02470 368 lSYPTFGDAIPPQYA-----IQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAAN 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 157823815 551 PEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 588
Cdd:PLN02470 443 PDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
507-658 |
1.80e-27 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 108.44 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 507 DGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVG 586
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157823815 587 NDAGWTQISREQVP----RLGSDVACSLAYTDYHKAAMGLGAQGliLSRDNEDQVVKVLRDGQKlcqEGHAVVVNI 658
Cdd:pfam02775 81 NNGGYGMTRGQQTPfgggRYSGPSGKILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEALE---HDGPALIDV 151
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
96-634 |
7.85e-27 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 115.31 E-value: 7.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 96 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 175
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 176 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSgTPGPVFVELPLDVLYp 255
Cdd:PRK06457 86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAIS-KRGVAHINLPVDILR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 256 yfmvekemipaqlpkglMGRvvvwylqnclanlfagawEPRPEGPLPLDIPQASPQqVQRCVEILSRAKRPLLVLGSQAL 335
Cdd:PRK06457 164 -----------------KSS------------------EYKGSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 336 LPPTPANKLraaVETLGVPCF----------------LGGMsrGLLGRNHPLhirqnrsAALKKADVVVLAGAVcdfrLS 399
Cdd:PRK06457 208 GLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI-------EAMDKADLLIMLGTS----FP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 400 YGRVLNRKSSIIIVNRNRDDM--LLNSDIfwkpqeAVQGDVGSFMI--------KLVEGLQGQtwSSDWVEELRKADQQk 469
Cdd:PRK06457 272 YVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLNidieeksdKFYEELKGK--KEDWLDSISKQENS- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 470 eqtyRDKALlpvpqhlNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 549
Cdd:PRK06457 343 ----LDKPM-------KPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 550 -QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGA 624
Cdd:PRK06457 412 vENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEWGVD----LYNPDFTKIAESIGF 487
|
570
....*....|
gi 157823815 625 QGLILSRDNE 634
Cdd:PRK06457 488 KGFRLEEPKE 497
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
482-663 |
1.23e-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: 101.82 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 482 PQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 561
Cdd:cd02013 1 GNPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 562 GAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSLAYTDYHKAAMGLGAQGLILsrDNEDQVVKV 640
Cdd:cd02013 81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPA 158
|
170 180
....*....|....*....|...
gi 157823815 641 LRDGQKLCQEGHAVVVNILIGRT 663
Cdd:cd02013 159 LQKAIAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
489-634 |
2.27e-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: 100.02 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 489 RLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 568
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157823815 569 IEFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQGLILSRDNE 634
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDPED 147
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
102-592 |
1.10e-23 |
|
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: 105.63 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 102 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 180
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLdAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 181 SPVLLLGGAASTLLQKRGAL--------QAIDQMSLFRPLCkfCASVR-----------RVrdivptLRAAMAAAQsgtp 241
Cdd:COG3961 94 VPVVHIVGAPGTRAQRRGPLlhhtlgdgDFDHFLRMFEEVT--VAQAVltpenaaaeidRV------LAAALREKR---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 242 gPVFVELPLDVlypyfmVEKEMipaqlpkglmgrvvvwylqnclanlfagawePRPEGPLPLDIPQASPQQVQRCV---- 317
Cdd:COG3961 162 -PVYIELPRDV------ADAPI-------------------------------EPPEAPLPLPPPASDPAALAAAVaaaa 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 318 EILSRAKRPLLVLGSQAL---LpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI--------RQNRSAALKKADV 386
Cdd:COG3961 204 ERLAKAKRPVILAGVEVHrfgL----QEELLALAEKTGIPVATTLLGKSVLDESHPQFIgtyagaasSPEVREYVENADC 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 387 VVLAGAV-CDFRL-SYGRVLNRKSSIIIvnrNRDDMLLNSDIFwkpqEAVQgdvgsfMIKLVEGLqgqtwssdwVEELRK 464
Cdd:COG3961 280 VLCLGVVfTDTNTgGFTAQLDPERTIDI---QPDSVRVGGHIY----PGVS------LADFLEAL---------AELLKK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 465 ADQQKEQTYRDKALLPVP--QHLNPVRLLQQVEETLPDNALLVVDGGD--FVATAAYLvqPRGpLRWLDPGAFGTLG--V 538
Cdd:COG3961 338 RSAPLPAPAPPPPPPPAApdAPLTQDRLWQRLQAFLDPGDIVVADTGTslFGAADLRL--PEG-ATFIAQPLWGSIGytL 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 157823815 539 GAgfALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWT 592
Cdd:COG3961 415 PA--ALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYT 466
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
95-252 |
5.33e-23 |
|
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: 96.08 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 95 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 173
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 174 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRR---VRDIVPT-LRAAMAaaqsgTPGPVFVELP 249
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPELLDRaIRTAIA-----KRGVAVLILP 157
|
...
gi 157823815 250 LDV 252
Cdd:cd07039 158 GDV 160
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
94-635 |
1.74e-22 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 102.00 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC--EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 171
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 172 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSgTPGPVFVELPLD 251
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 252 vlypyfmvekemIPAQLPKGLMGRVVVWYLQNclanlfagawEPRPegplpldipqaSPQQVQRCVEILSRAKRPLLVLG 331
Cdd:PRK08611 165 ------------LPAQKIKDTTNKTVDTFRPT----------VPSP-----------KPKDIKKAAKLINKAKKPVILAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 332 SQAllpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRSA--ALKKADVVVLAGAvcDFrlSYGRVL 404
Cdd:PRK08611 212 LGA---KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNlgkigTKPAyeAMQEADLLIMVGT--NY--PYVDYL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 405 NRKSSIIIVNRNRDDM--LLNSDIfwkpqeAVQGDVGSFM------IKLVEG---LQG-----QTWSSdWVEElrkaDQQ 468
Cdd:PRK08611 285 PKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALhqltenIKHVEDrrfLEAcqenmAKWWK-WMEE----DEN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 469 KEQTyrdkallPvpqhLNPVRLLQQVEETLPDNALLVVD-GGDFVATAAYL-VQPRGPL---RWLdpgafGTLGVGAGFA 543
Cdd:PRK08611 354 NAST-------P----IKPERVMAAIQKIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL-----GTMGCGLPGA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 544 LGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLG 623
Cdd:PRK08611 418 IAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACG 497
|
570
....*....|..
gi 157823815 624 AQGLILsRDNED 635
Cdd:PRK08611 498 GKGYRV-EKAEE 508
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
485-626 |
7.04e-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: 93.36 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 485 LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 564
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823815 565 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQG 626
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKG 143
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
98-249 |
3.39e-17 |
|
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: 78.93 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 98 VAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNA 176
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157823815 177 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPT-LRAAMAAAQSgtPGPVFVELP 249
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGiDHAIRTAYAS--QGPVVVRLP 153
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
313-445 |
3.73e-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: 75.68 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 313 VQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKAD 385
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGA-SEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157823815 386 VVVLAGAVCDFRLSYGRV--LNRKSSIIIVNRNRDDMLLNSdifwKPQEAVQGDVGSFMIKL 445
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLpeFAPDAKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
89-591 |
2.23e-15 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 79.23 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 89 TSIRHggeSVAAVLRAHGVRFVFTLVGGHISPLLVACEKlGIRVVDTRHEVTAVFAADAVARLTGTVGV----AAVTAGP 164
Cdd:PRK07092 12 TTVRD---ATIDLLRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFvnlhSAAGVGN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 165 GLTNTVTAVKNaqvaQSP-VLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGP 243
Cdd:PRK07092 88 AMGNLFTAFKN----HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 244 VFVELPLDvlypyfmvekemipaqlpkglmgrvvvwylqnclanlfagAWEpRPEGPLPL-DIPQA---SPQQVQRCVEI 319
Cdd:PRK07092 164 VFVSIPYD----------------------------------------DWD-QPAEPLPArTVSSAvrpDPAALARLGDA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 320 LSRAKRPLLVLGsqALLPPTPANKLRAAV-ETLGVPCFLGGMS-RGLLGRNHPLH------IRQNRSAALKKADVVVLAG 391
Cdd:PRK07092 203 LDAARRPALVVG--PAVDRAGAWDDAVRLaERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLVIG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 392 AVCdFRL---SYGRVLNRKSSIIIVNrnrDDMLLNSdifWKPQ-EAVQGDVGSFMIKLVEGLqgqtwssdwVEELRKADQ 467
Cdd:PRK07092 281 APV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVGDIRLALRDLLALL---------PPSARPAPP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 468 QKEqtyRDKALLPVPQHLNPVRLLQQVEETLPDNALLVVDggdfvATAAYLV-QPRgpLRWLDPGAF-----GTLGVGAG 541
Cdd:PRK07092 345 ARP---MPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEE-----APSTRPAmQEH--LPMRRQGSFytmasGGLGYGLP 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 157823815 542 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 591
Cdd:PRK07092 415 AAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
487-656 |
3.49e-15 |
|
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: 73.86 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 487 PVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 566
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 567 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSrdNEDQVVKVLRDGqk 646
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIE--SADDLLPVLERA-- 156
|
170
....*....|
gi 157823815 647 LCQEGHAVVV 656
Cdd:cd02010 157 LAADGVHVID 166
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
96-626 |
1.75e-14 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 76.57 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 96 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 174
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 175 NAQVAQSPVLLLggaASTLLQKR---GALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGtPGPVFVELPLD 251
Cdd:PRK06546 87 DAHRSGAPVLAI---ASHIPSAQigsGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 252 VlypyfmvekemipaqlpkglmgrvvvwylqnclanlfagAWEPRPEGPLPLDIPQA------SPQQVQRCVEILSRAKR 325
Cdd:PRK06546 163 I---------------------------------------ADEPAPEGFAPSVISPRrptvvpDPAEVRALADAINEAKK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 326 PLLVLGS---------QALlpptpANKLRAAV-ETLGVPCFLG-------GMSrGLLGRNHPlhirqnrSAALKKADVVV 388
Cdd:PRK06546 204 VTLFAGAgvrgahaevLAL-----AEKIKAPVgHSLRGKEWIQydnpfdvGMS-GLLGYGAA-------HEAMHEADLLI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 389 LAGAvcDFrlSYGRVLNRKsSIIIVNRNRDDMLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQTWSSDWVEELRKADQQ 468
Cdd:PRK06546 271 LLGT--DF--PYDQFLPDV-RTAQVDIDPEHLGRRTRV----DLAVHGDVAETIRALLPLVKEKTDRRFLDRMLKKHARK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 469 KEQ---TYRDKALLPVPQHlnPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLdpGAF--GTLGVGAGFA 543
Cdd:PRK06546 342 LEKvvgAYTRKVEKHTPIH--PEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVI--GSFrhGSMANALPHA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 544 LGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDVacslAYTDYHKAA 619
Cdd:PRK06546 418 IGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMlvdgLPDFGTDH----PPVDYAAIA 493
|
....*..
gi 157823815 620 MGLGAQG 626
Cdd:PRK06546 494 AALGIHA 500
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
102-637 |
1.08e-13 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 74.18 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 102 LRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVA 179
Cdd:PRK08273 13 LREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 180 QSPVLLLGGAastllQKRGAL-----QAIDQMSLFR----PLCKFCASVRRVRDIVP-TLRAAMAaaqsgTPGPVFVELP 249
Cdd:PRK08273 93 HVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVDrAVRTALA-----ERTVTAVILP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 250 LDVlypyfmveKEMiPAQLPKGLMGRVVvwylqnclanlfAGAWEPRPEgPLPldipqaSPQQVQRCVEILSRAKRPLLV 329
Cdd:PRK08273 163 NDV--------QEL-EYEPPPHAHGTVH------------SGVGYTRPR-VVP------YDEDLRRAAEVLNAGRKVAIL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 330 LGSQALlppTPANKLRAAVETLGvpcflGGMSRGLLGRnhplhirqnrsAALKKaDVVVLAGAVcdfrlsyGrVLNRKSS 409
Cdd:PRK08273 215 VGAGAL---GATDEVIAVAERLG-----AGVAKALLGK-----------AALPD-DLPWVTGSI-------G-LLGTKPS 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 410 iiivnrnrDDMLLNSDIF-----------WKPQE----AVQGDVGSFMIKL---VE-GLQG--------------QTWSS 456
Cdd:PRK08273 267 --------YELMRECDTLlmvgssfpyseFLPKEgqarGVQIDIDGRMLGLrypMEvNLVGdaaetlrallplleRKKDR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 457 DWVEELRKADQQKEQTYRDKALLPvPQHLNPVRLLQQVEETLPDNALLVVDGGDfVAT--AAYLVQPRGPLRWLDpGAFG 534
Cdd:PRK08273 339 SWRERIEKWVARWWETLEARAMVP-ADPVNPQRVFWELSPRLPDNAILTADSGS-CANwyARDLRMRRGMMASLS-GTLA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 535 TLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS-LIEFDTFVRH-----KVPVIALVGNDAGWTQISREQVPRLGS---D 605
Cdd:PRK08273 416 TMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDPRLIVLVLNNRDLNQVTWEQRVMEGDpkfE 495
|
570 580 590
....*....|....*....|....*....|..
gi 157823815 606 VACSLAYTDYHKAAMGLGAQGLILsrDNEDQV 637
Cdd:PRK08273 496 ASQDLPDVPYARFAELLGLKGIRV--DDPEQL 525
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
485-660 |
1.55e-12 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 66.46 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 485 LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 564
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 565 GYSLIEFDTFVRHKVPVIALVGNDAGWtQISREQVPRLGSDVACSLAY---------TDYHKAAMGLGAQGLILSRDNEd 635
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVETPEE- 157
|
170 180
....*....|....*....|....*
gi 157823815 636 qVVKVLRDGQklcQEGHAVVVNILI 660
Cdd:cd02002 158 -LDEALREAL---AEGGPALIEVVV 178
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
489-664 |
2.34e-12 |
|
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: 66.02 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 489 RLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 568
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 569 IEFDTFVRHKVPVIALVGNDAGWT---QISREQVPrlgsdvacslaYTD-----YHKAAMGLGAQGLILSRD--NEDQVV 638
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFRvkTEGELD 153
|
170 180
....*....|....*....|....*.
gi 157823815 639 KVLRDGQKLCqeGHAVVVNILIGRTD 664
Cdd:cd02005 154 EALKDALFNR--DKLSLIEVILPKDD 177
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
102-249 |
9.02e-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: 63.67 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 102 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 180
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLdAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 181 SPVLLLGGAASTLLQKRGA-----LQAID---QMSLFRPLCkfCASVRRVRDIVPT------LRAAMAAAQsgtpgPVFV 246
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGLllhhtLGDGDfdvFLKMFEEIT--CAAARLTDPENAAeeidrvLRTALRESR-----PVYI 158
|
...
gi 157823815 247 ELP 249
Cdd:cd07038 159 EIP 161
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
485-587 |
1.27e-11 |
|
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: 64.06 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 485 LNPVRLLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 561
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQhqmWAAQYYRFKKPR---SWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
|
90 100
....*....|....*....|....*.
gi 157823815 562 GAFGYSLIEFDTFVRHKVPVIALVGN 587
Cdd:cd02015 78 GSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
98-589 |
3.43e-11 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 66.16 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 98 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNA 176
Cdd:PRK09124 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 177 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAqSGTPGPVFVELPLDVlypy 256
Cdd:PRK09124 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDV---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 257 fmvekemipaqlpkglmgrvvvwylqnclanLFAGAWEPRPEGPLPLDIPQASP--QQVQRCVEILSRAKRPLLVLGS-- 332
Cdd:PRK09124 164 -------------------------------ALKPAPERATPHWYHAPQPVVTPaeEELRKLAALLNGSSNITLLCGSgc 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 333 -QAllpptpANKLRAAVETLGVPC---------------FLGGMSrGLLGRNHPLHirqnrsaALKKADVVVLAGavCDF 396
Cdd:PRK09124 213 aGA------HDELVALAETLKAPIvhalrgkehveydnpYDVGMT-GLIGFSSGYH-------AMMNCDTLLMLG--TDF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 397 rlSYGRVLNRKSSIIIVNRN--------RDDMllnsdifwkpqeAVQGDVGSFMIKLVEGLQGQTWSSdwveELRKADQQ 468
Cdd:PRK09124 277 --PYRQFYPTDAKIIQIDINpgslgrrsPVDL------------GLVGDVKATLAALLPLLEEKTDRK----FLDKALEH 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 469 KEQTYRDKALLPVPQH----LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 544
Cdd:PRK09124 339 YRKARKGLDDLAVPSDggkpIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQAL 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 157823815 545 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA 589
Cdd:PRK09124 419 GAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
94-625 |
5.27e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 65.66 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVL-LLGGAASTLLQKRGALQAiDQMSLFRPLCKFcasVRRVRD---IVPTLRAAMAAAQSGTPGPVFVEL 248
Cdd:PRK12474 87 LHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASagaVDSDVARAVQAAQSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 249 PLDVlypyfmvekemipaqlpkglmgrvvvwylqnclanlfagAWEPRPEGPLPL-DIPQA--SPQQVQRCVEILSRAKR 325
Cdd:PRK12474 163 PADV---------------------------------------AWNEAAYAAQPLrGIGPApvAAETVERIAALLRNGKK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 326 PLLVLGSQALL--PPTPANKLRAAVetlGVPCFLGGMS-RGLLGRNH-PL----HIRQNRSAALKKADVVVLAGAvcDFR 397
Cdd:PRK12474 204 SALLLRGSALRgaPLEAAGRIQAKT---GVRLYCDTFApRIERGAGRvPIeripYFHEQITAFLKDVEQLVLVGA--KPP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 398 LSYGRVLNRKSsiiivnrnrddmllnsdifWKPQEavqgdvGSFMIKLV----EGLQGQTWSSDWVeelrkaDQQKEQTY 473
Cdd:PRK12474 279 VSFFAYPGKPS-------------------WGAPP------GCEIVYLAqpdeDLAQALQDLADAV------DAPAEPAA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 474 RDKALLPVPQH--LNPVRLLQQVEETLPDNAlLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQP 551
Cdd:PRK12474 328 RTPLALPALPKgaLNSLGVAQLIAHRTPDQA-IYADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 552 EAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREqVPRLGSDVACSLAYT---------DYHKAAMGL 622
Cdd:PRK12474 407 DRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGE-LQRVGAQGAGRNALSmldlhnpelNWMKIAEGL 485
|
...
gi 157823815 623 GAQ 625
Cdd:PRK12474 486 GVE 488
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
94-392 |
2.63e-10 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 63.32 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 94 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 172
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 173 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPLDV 252
Cdd:PRK07586 83 LHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 253 lypyfmvekemipaqlpkglmgrvvvwylqnclanlfagAWEP--RPEGPLPL-DIPQASPQQVQRCVEILSRAKRPLLV 329
Cdd:PRK07586 163 ---------------------------------------AWSEggPPAPPPPApAPAAVDPAAVEAAAAALRSGEPTVLL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 330 LGSQALLPPTPANKLRAAVET---LGVPCFLGGMSRGlLGRNH----PLHIRQNRsAALKKADVVVLAGA 392
Cdd:PRK07586 204 LGGRALRERGLAAAARIAAATgarLLAETFPARMERG-AGRPAverlPYFAEQAL-AQLAGVRHLVLVGA 271
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
485-662 |
4.74e-07 |
|
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: 50.74 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 485 LNPVRLLQQVEETL-PDNALLVVDGGDFVATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 563
Cdd:cd02006 8 IKPQRVYEEMNKAFgRDVRYVTTIGLSQIAGAQMLHVYK-PRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 564 FGYSLIEFDTFVRHKVPVIALVGNDAgWTQISREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQGLILSR 631
Cdd:cd02006 87 FQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIRQAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTK 165
|
170 180 190
....*....|....*....|....*....|..
gi 157823815 632 DNEdqVVKVLRDGQKLCQEGHA-VVVNILIGR 662
Cdd:cd02006 166 PEE--LAAAFEQAKKLMAEHRVpVVVEAILER 195
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
102-250 |
2.61e-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: 44.80 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157823815 102 LRAHGVRFVFTLVGGHISPLLVACEKLG-IRV---VDTRhevTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 177
Cdd:cd07037 7 LKRLGVRDVVISPGSRSAPLALAAAEHPeFRLhvrVDER---SAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157823815 178 VAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVR------RVRDIVPTLRAAMAAAQSGTPGPVFVELPL 250
Cdd:cd07037 84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
307-368 |
1.33e-03 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 39.93 E-value: 1.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157823815 307 QASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAVETLGVP-CFLGGMSRGLLGRN 368
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| |
