|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05858 |
PRK05858 |
acetolactate synthase; |
63-596 |
1.38e-120 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 369.05 E-value: 1.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 63 HGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK05858 6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPyfMVEKEMIPTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK05858 166 AFS--MADDDGRPGALTEL-------------------------PAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIII 382
Cdd:PRK05858 213 DVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVH 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 383 VNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKEQtyRDKALM-----PvlqhLNP 457
Cdd:PRK05858 291 VDDAPPQR----AHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAETAARA--RDAAELaddrdP----IHP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 458 VWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS 537
Cdd:PRK05858 361 MRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFS 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318663320 538 LIEFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVACSLA-YTDYHKAAMGLGAQG 596
Cdd:PRK05858 441 LMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHG 500
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
62-630 |
8.08e-112 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 223107 [Multi-domain] Cd Length: 550 Bit Score: 346.56 E-value: 8.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:COG0028 2 MTGAEALVEALEANGVDTVFGIPGGSILPLYDALYDSGIRHILVRHEQGAAFAADGYARATGKPGVCLVTSGPGATNLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:COG0028 82 GLADAYMDSVPLLAITGQVPTSLIGTDAFQEVDQVGLFRPITKYNFEVRSPEDIPEVVARAFRIALSGRPGPVVVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLypyfmveKEMIPTKLPnslmgrvvvwylqnclanlfvGAWEPRPEGPLPldipqASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:COG0028 162 VL-------AAEAEEPGP---------------------EPAILPPYRPAP-----PPPEAIRKAAELLAEAKRPVILAG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPLH-----IRQNRSA--ALKKADVVVLAGAVCDFRLSYGRVL 374
Cdd:COG0028 209 GGVRRAGASEE-LRELAEKLGAPVVTTLMGKGAVPEDHPLSlgmlgMHGTKAAneALEEADLLLAVGARFDDRVTGYSGF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQmwSSDWAEELRKADQQKEQTYRDKALMPVlqh 454
Cdd:COG0028 288 APPAAIIHIDIDPAEI----GKNYPVDVPIVGDAKATLEALLEELKPE--RAAWLEELLEARAAYRDLALEELADDG--- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:COG0028 359 IKPQYVIKVLRELLPDDAIVVTDVGQHQMWAARYFDFYRPRRFLTSGGLGTMGFGLPAAIGAKLAAPDRKVVAIAGDGGF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLG-SDVACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLRE 613
Cdd:COG0028 439 MMNGQELETAVRYGLPVKIVVLNNGGYGMVRQWQELFYGgRYSGTDLGNPDFVKLAEAYGAKGIRV--ETPEELEEALEE 516
|
570
....*....|....*..
gi 1318663320 614 GqqLCQDGhAVVVNILI 630
Cdd:COG0028 517 A--LASDG-PVLIDVVV 530
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
460-630 |
1.68e-62 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 204.69 E-value: 1.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 460 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 539
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 540 EFDTFVRHKVPVIALVGNDAGWTQISREQVP--RLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQL 617
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLsyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTP--EELKPALKRALAS 161
|
170
....*....|...
gi 1318663320 618 cqdGHAVVVNILI 630
Cdd:cd02004 162 ---GKPALINVII 171
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
66-219 |
1.05e-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: 193.90 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 146 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
65-594 |
1.24e-58 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 205.98 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 65 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 144
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 145 NAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VlypyfMVEKemiptklpnslmgrvvvwylqnclanlFVGAWEPRPEGPLPldiPQASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:PRK07524 165 V-----LAAP---------------------------ADHLLPAPPTRPAR---PGPAPAALAQAAERLAAARRPLILAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRS-----AALKKADVVVLAG---AVCDFRLSYGRV 373
Cdd:PRK07524 210 GGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrALIAEADVVLAVGtelGETDYDVYFDGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSIIIVNRNRDDLLLNsdifWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEElRKADQQKEQTYRDKALMPVLQ 453
Cdd:PRK07524 287 FPLPGELIRIDIDPDQLARN----YPPALALVGDARAALEALLARLPGQAAAADWGAA-RVAALRQALRAEWDPLTAAQV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 454 HLnpvwvLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLD-PGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDG 532
Cdd:PRK07524 362 AL-----LDTILAALPD-AIFVGDSTQPVYAGNLYFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPERPVVCLVGDG 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1318663320 533 AFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGA 594
Cdd:PRK07524 436 GLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGC 497
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
64-637 |
6.09e-58 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 204.21 E-value: 6.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 YPyfMVEKEMIPtklpnslmgrvvvwylqnclanlfvgaweprpegplPLDIPQ---ASPQQVQRCVEILSRAKRPLLVL 300
Cdd:TIGR02418 161 DS--PVSVKAIP------------------------------------ASYAPKlgaAPDDAIDEVAEAIQNAKLPVLLL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirqnrsaalkkadvvvLAGAVCDFRLSYGRVLNRKSSI 380
Cdd:TIGR02418 203 GLRASSPETTE-AVRRLLKKTQLPVVETFQGAGAVSRELEDH----------------FFGRVGLFRNQPGDRLLKQADL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIV-------------NRNRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQKE 440
Cdd:TIGR02418 266 VITigydpieyeprnwNSENDATIVHIDVepaqidnNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQRE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKAlMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDF-VATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:TIGR02418 346 ALDRVPA-TLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHyIWMARYFRSYR-ARHLLISNGMQTLGVALPWAIGAALV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLIL 599
Cdd:TIGR02418 424 RPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRV 503
|
570 580 590
....*....|....*....|....*....|....*...
gi 1318663320 600 srDNKDQVVKVLREGQQLcqDGhAVVVNILIgrtDFRD 637
Cdd:TIGR02418 504 --ESPDQLEPTLRQAMEV--EG-PVVVDIPV---DYSD 533
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
64-223 |
1.58e-57 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 426975 [Multi-domain] Cd Length: 169 Bit Score: 191.30 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGTILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQA-IDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:pfam02776 81 LANAYVDSVPLIVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSPDEIPEVLRRAFRAAMSGRPGPVYLEIPLD 160
|
..
gi 1318663320 222 VL 223
Cdd:pfam02776 161 VL 162
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
66-632 |
1.18e-55 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 199.07 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 146 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLDvlYP 225
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 226 YFMVEKEmIPTklpnslmgrvvvwylqnclanlfvgaweprpegPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG---- 301
Cdd:PRK07525 167 YGVIDVE-IPQ---------------------------------PVRLERGAGGEQSLAEAAELLSEAKFPVILSGagvv 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 -SQALlpptpaNKLRAAVETLGVPCFLGGMSRGLLGRNHPLH---IRQNRSAA----LKKADVVVLAGAvcdfRLSYGRV 373
Cdd:PRK07525 213 lSDAI------EECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelIAKADVVLALGT----RLNPFGT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LN--------RKSSIIIVNRNRDDLLLNsdifwKPQE-AVQGDVGSFMIKLVEGLQGQMWS---------------SDWA 429
Cdd:PRK07525 283 LPqygidywpKDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVARELLARLAERLAGdagreerkaliaaekSAWE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 430 EELRKADQQKEQ---TYRDKALMPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATA-AYLvQPRGPLRWLDPGAFGT 505
Cdd:PRK07525 358 QELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSIAnSYL-RFEKGRKYLAPGSFGN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 506 LGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSL-AYT 583
Cdd:PRK07525 437 CGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNV 516
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1318663320 584 DYHKAAMGLGAQGLILsrDNKDQVVKVLREGQQLCQDGHAVVVNILIGR 632
Cdd:PRK07525 517 SYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
64-559 |
1.65e-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: 198.02 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFMVEkemIPTKLpnSLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:TIGR00118 163 TTAEIEYP---YPEKV--NLPG------------------YRPTVKG---------HPLQIKKAAELINLAKKPVILVGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLN 375
Cdd:TIGR00118 211 GVIIAGASE-ELKELAERIQIPVTTTLMGLGSFPEDHPLslgmlgmHGTKTANLAVHECDLIIAVGARFDDRVT-GNLAK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 RKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGL--QGQMWSSDWAEELR--KADQQKEQTYRDKALMPv 451
Cdd:TIGR00118 289 FAPNAKIIHIDIDPAEIGKNV--RVDIPIVGDARNVLEELLKKLfeLKERKESAWLEQINkwKKEYPLKMDYTEEGIKP- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 452 lQHlnpvwVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 531
Cdd:TIGR00118 366 -QQ-----VIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGD 439
|
490 500
....*....|....*....|....*...
gi 1318663320 532 GAFGYSLIEFDTFVRHKVPVIALVGNDA 559
Cdd:TIGR00118 440 GSFQMNLQELSTAVQYDIPVKILILNNR 467
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
68-578 |
1.70e-55 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 197.90 E-value: 1.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 68 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 147
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 148 VAQSPVLLLGGAASTL---LQkRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVLY 224
Cdd:PRK09259 96 TNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 225 PYFMVEKemiptklpnslmGRVVVWylqnclanlfvgawepRPEGPLPLDIPqaSPQQVQRCVEILSRAKRPLLVLGSQA 304
Cdd:PRK09259 175 QTMDADE------------ALTSLV----------------KVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 305 LLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVVLAGAVCDFRLSYGR--VLNRKSSIII 382
Cdd:PRK09259 225 AYAQADE-QIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgkTWGADKKFIQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 383 VnrnrddlllnsDIfwKPQEA---------VQGDVGSFMIKLVEGLQGQmW---SSDWAEEL--RKADQQKEQTYRDKAL 448
Cdd:PRK09259 304 I-----------DI--EPQEIdsnrpiaapVVGDIGSVMQALLAGLKQN-TfkaPAEWLDALaeRKEKNAAKMAEKLSTD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 MPVLQHLNPVWVLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC--QPeaeVW 526
Cdd:PRK09259 370 TQPMNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VV 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 527 CLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGwtqISR--EQVPRLGSDVAC 578
Cdd:PRK09259 446 AIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSP 496
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
64-558 |
2.15e-52 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 189.54 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHIspLLVACE---KLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAI--LNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DV-------LYPyfmvEKEMIPTKLPNslmgrvvvwYLQNclanlfvgaweprpegplpldipqasPQQVQRCVEILSRA 293
Cdd:PRK08527 163 DVtatlgefEYP----KEISLKTYKPT---------YKGN--------------------------SRQIKKAAEAIKEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 294 KRPLLVLGSQALLpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDF 366
Cdd:PRK08527 204 KKPLFYLGGGAIL-SNASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 367 RLSyGRV--LNRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQMWS--SDWAEELRKADQQKE 440
Cdd:PRK08527 283 RVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELKEENPTtyKEWREILKRYNELHP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKALMpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQ 520
Cdd:PRK08527 356 LSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAV 430
|
490 500 510
....*....|....*....|....*....|....*...
gi 1318663320 521 PEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PRK08527 431 PDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
62-637 |
2.40e-50 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 183.52 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLD 221
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLYPyfmvekemiPTKLPNslmgrvvvwylqnclanlfVGAWEPRPEGPlpldipqASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:PRK08617 165 VVDA---------PVTSKA-------------------IAPLSKPKLGP-------ASPEDINYLAELIKNAKLPVLLLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALLPPTpANKLRAAVETLGVPCF-----LGGMSRGL---------LGRNHP---LhirqnrsaaLKKADVVVLAGavc 364
Cdd:PRK08617 210 MRASSPEV-TAAIRRLLERTNLPVVetfqaAGVISRELedhffgrvgLFRNQPgdeL---------LKKADLVITIG--- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 365 dfrlsYG------RVLNRKSSIIIVnrNRDDLLLNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQ 438
Cdd:PRK08617 277 -----YDpieyepRNWNSEGDATII--HIDVLPAEIDNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEILEELRAQ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQTYRDKALMPVlQHLNPVWVLQQVEETLPDNALLVVDGGDF---VATAAYLVQPRGPLrwldpgaFG----TLGVGAG 511
Cdd:PRK08617 350 LEELAERPARLEE-GAVHPLRIIRALQDIVTDDTTVTVDVGSHyiwMARYFRSYEPRHLL-------FSngmqTLGVALP 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMG 591
Cdd:PRK08617 422 WAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAES 501
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1318663320 592 LGAQGliLSRDNKDQVVKVLREGqqLCQDGhAVVVNILIgrtDFRD 637
Cdd:PRK08617 502 FGAKG--LRVTSPDELEPVLREA--LATDG-PVVIDIPV---DYSD 539
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
64-596 |
3.82e-49 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 179.82 E-value: 3.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGG--AASTLLQKRGALQAI-DQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVEL 218
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 219 PLDVLYpyfMVEKEMIPTKLpnslmgrvvvwylqnclanlfvgawepRPEGPLPLDipqasPQQVQRCVEILSRAKRPLL 298
Cdd:PRK08266 166 PWDVFG---QRAPVAAAPPL---------------------------RPAPPPAPD-----PDAIAAAAALIAAAKNPMI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 VLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHirQNRSAA---LKKADVVVLAGAVCDFRLSYGRVLN 375
Cdd:PRK08266 211 FVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLG--LNFAAAyelWPQTDVVIGIGSRLELPTFRWPWRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 RKSSIIIVNRNRDDLllnsdIFWKPQEAVQGDVGSFMIKLVEGLQGQM-WSSDWAEELRKADQQKEQtyRDKALMPVLQH 454
Cdd:PRK08266 286 DGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAGsKRPSRRAELRELKAAARQ--RIQAVQPQASY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNpvwvlqQVEETLPDNAlLVVDGGDFVATAAYLVQP-RGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 533
Cdd:PRK08266 359 LR------AIREALPDDG-IFVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 534 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQG 596
Cdd:PRK08266 432 FMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLAESFGVAA 495
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
72-625 |
1.93e-48 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 178.10 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 72 LRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQS 151
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 152 PVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVrDIVPTL-RTAIAAAQSGTPGPVFVELPLDVlypyfmve 230
Cdd:PRK08322 91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP-DNIPEVvREAFRLAEEERPGAVHLELPEDI-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 231 kemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 307
Cdd:PRK08322 162 -------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 308 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGavcdfrlsYGRV------L 374
Cdd:PRK08322 211 TA-SKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLSQGDYVHCAIEHADLIINVG--------HDVIekppffM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDLLLNSDIFwkPQEAVQGDVGSFMIKLVEGL-QGQMWSSDWAEELRKADQQKEQTYRDKALMPVLq 453
Cdd:PRK08322 282 NPNGDKKVIHINFLPAEVDPVYF--PQVEVVGDIANSLWQLKERLaDQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 454 hlnPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 533
Cdd:PRK08322 359 ---PQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 534 FGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLRE 613
Cdd:PRK08322 436 FMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESA--DDLLPTLEE 513
|
570
....*....|..
gi 1318663320 614 GqqLCQDGHAVV 625
Cdd:PRK08322 514 A--LAQPGVHVI 523
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
64-555 |
1.08e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 176.87 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 YPYFMVEKEMIPTKLPnsLMGrvvvwylqnclanlfvgaWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGSQ 303
Cdd:PRK06276 163 EGELDLEKYPIPAKID--LPG------------------YKPTTFG---------HPLQIKKAAELIAEAERPVILAGGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 ALLppTPANK-LRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGavCDFRlsyGRVLN 375
Cdd:PRK06276 214 VII--SGASEeLIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSVTESDVLIAIG--CRFS---DRTTG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 RKSS------IIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQMWSSD--WAEELR--KADQQKEQTYRD 445
Cdd:PRK06276 287 DISSfapnakIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNKseWLERVKklKKESIPRMDFDD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 446 KALMPvlQHLnpVWVLQQV--EETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEA 523
Cdd:PRK06276 363 KPIKP--QRV--IKELMEVlrEIDPSKNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDA 438
|
490 500 510
....*....|....*....|....*....|..
gi 1318663320 524 EVWCLFGDGAFGYSLIEFDTFVRHKVPVIALV 555
Cdd:PRK06276 439 NVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
64-632 |
2.01e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 172.65 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK06048 90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 -------YPyfmvEKEMIPtklpnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 296
Cdd:PRK06048 170 taeidfdYP----DKVELR--------------------------GYKPTYKG---------NPQQIKRAAELIMKAERP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LL-----VLGSQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVC 364
Cdd:PRK06048 211 IIyagggVISSNA------SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 365 DFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQgqmwSSDWAEELRKADQQKEQ--- 441
Cdd:PRK06048 285 DDRVT-GKLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQ----YCDRKEWLDKINQWKKEypl 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 442 --TYRDKALMpvlqhlnPVWVLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:PRK06048 358 kyKEREDVIK-------PQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQISREQvpRLGSdvACSLAYTDYHKAAMGLG 593
Cdd:PRK06048 430 KPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDK--RYSH--TCIKGSVDFVKLAEAYG 505
|
570 580 590
....*....|....*....|....*....|....*....
gi 1318663320 594 AQGLILSRDNkdQVVKVLREGQQLcqdGHAVVVNILIGR 632
Cdd:PRK06048 506 ALGLRVEKPS--EVRPAIEEAVAS---DRPVVIDFIVEC 539
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
54-632 |
8.91e-46 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 170.76 E-value: 8.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 54 HKVDKTSIRHGGESVAAVLRAHGVRFVFtlvGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTG--TVGVAAVT 131
Cdd:PRK06154 12 HLPAEAKTMKVAEAVAEILKEEGVELLF---GFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 132 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTllqkrgALQAID----QMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQ 207
Cdd:PRK06154 89 YGPGAENAFGGVAQAYGDSVPVLFLPTGYPR------GSTDVApnfeSLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 208 SGTPGPVFVELPLDVLYpyfmvekemipTKLPNSlmgrvvvwylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCV 287
Cdd:PRK06154 163 NGRPGPVVLELPVDVLA-----------EELDEL-----------------------PLDHRPSRRSRPGADPVEVVEAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 288 EILSRAKRPLLVLGsQALLPPTPANKLRAAVETLGVPCF--LGGMSRglLGRNHPLHIRQNRSAA-------LKKADVVV 358
Cdd:PRK06154 209 ALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMttLNGKSA--FPEDHPLALGSGGRARpatvahfLREADVLF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 359 LAGavCDF-RLSYGRVLNRKSSIIIVnrNRDDLLLNSDIFWKpqEAVQGDVGSFMIKLVEGLQGQMW-----SSDWAEEL 432
Cdd:PRK06154 286 GIG--CSLtRSYYGLPMPEGKTIIHS--TLDDADLNKDYPID--HGLVGDAALVLKQMIEELRRRVGpdrgrAQQVAAEI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 433 RKADQQKEQTYRDKaLMPVLQHLNPVWVLQQVEETL-PDNALLVVDGG---DFVATAAYLVQPRGPLRWldpGAFGTLGV 508
Cdd:PRK06154 360 EAVRAAWLAKWMPK-LTSDSTPINPYRVVWELQHAVdIKTVIITHDAGsprDQLSPFYVASRPGSYLGW---GKTTQLGY 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 509 GAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISREQVPRLGSDVACSLAYTDYHKA 588
Cdd:PRK06154 436 GLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN-FSMGGYDKVMPVSTTKYRATDISGDYAAI 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1318663320 589 AMGLGAQGLILSRdnKDQVVKVLREGQQLCQDGHAVVVNILIGR 632
Cdd:PRK06154 515 ARALGGYGERVED--PEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
64-561 |
1.61e-45 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 169.79 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAAST--LLQKRGAL-QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDvlypyfmvekemiptklpnsLMGRVVVWylqnclanlfvgawePRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV 299
Cdd:PRK07064 165 ID--------------------IQAAEIEL---------------PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 300 LGSQALlppTPANKLRAAVEtLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAA----LKKADVVVLAGAvcDFR----LSY 370
Cdd:PRK07064 210 LGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAvealYKTCDLLLVVGS--RLRgnetLKY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 371 GRVLNRKSSIIIVNRNRDDLLLNSDIFwkpqeaVQGDVGSFMIKLVEGLQGQMW-SSDWAEELRKADQQKEQTYRDKalm 449
Cdd:PRK07064 284 SLALPRPLIRVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLSvDPAFAADLRAAREAAVADLRKG--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 450 pvlqhLNPVWVL-QQVEETLPDNALLVVDGGdfVATAAY---LVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEV 525
Cdd:PRK07064 355 -----LGPYAKLvDALRAALPRDGNWVRDVT--ISNSTWgnrLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKT 426
|
490 500 510
....*....|....*....|....*....|....*.
gi 1318663320 526 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 561
Cdd:PRK07064 427 VGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
64-625 |
9.00e-45 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 168.22 E-value: 9.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ---YPYFMVEKEMIPTKLPnslmgrvvvwylqnclanlfvgawEPRPEgplpldipqasPQQVQRCVEILSRAKRPLLVL 300
Cdd:PRK06725 177 nekVTSFYNEVVEIPGYKP------------------------EPRPD-----------SMKLREVAKAISKAKRPLLYI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRV 373
Cdd:PRK06725 222 GG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAVTECDLLLALGVRFDDRVT-GKL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 --LNRKSSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEgLQGQMWSSDWAEELRKADQQKEQTYRDKAlmpv 451
Cdd:PRK06725 300 elFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKKALHMLLH-MSIHTQTDEWLQKVKTWKEEYPLSYKQKE---- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 452 lQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 531
Cdd:PRK06725 371 -SELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 532 GAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQI---SREQVPRLGSdvacslayTDYHKAAMGLGAQGliLSRD 602
Cdd:PRK06725 450 ASFQMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS--------PDFVKVAEAYGVKG--LRAT 519
|
570 580
....*....|....*....|...
gi 1318663320 603 NKDQVVKVLREGqqLCQDGHAVV 625
Cdd:PRK06725 520 NSTEAKQVMLEA--FAHEGPVVV 540
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
64-617 |
6.11e-44 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 166.13 E-value: 6.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGavlYIYDELYKQDK--IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DvlypyfmVEKEMIPTKLPNSLmgrvvvwylqnclanlfvgawEPRPEGPlpldIPQASPQQVQRCVEILSRAKRPLLVL 300
Cdd:PRK06965 181 D-------VSKTPCEYEYPKSV---------------------EMRSYNP----VTKGHSGQIRKAVSLLLSAKRPYIYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLpPTPANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrls 369
Cdd:PRK06965 229 GGGVIL-ANASRELRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFD---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 yGRVLNRKSSIIIVNRNrddlLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQ-----------GQMWSSdwAEE 431
Cdd:PRK06965 300 -DRVIGNPAHFASRPRK----IIHIDIdpssiskRVKVDIPIVGDVKEVLKELIEQLQtaehgpdadalAQWWKQ--IEG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 432 LRKADQQKEQTYRDKalmpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAG 511
Cdd:PRK06965 373 WRSRDCLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV--IAL----VGNDAGWTQIsrEQVPRLGSDVACSLAytDY 585
Cdd:PRK06965 445 YAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVkiISLnnryLGMVRQWQEI--EYSKRYSHSYMDALP--DF 520
|
570 580 590
....*....|....*....|....*....|..
gi 1318663320 586 HKAAMGLGAQGLILSRdnKDQVVKVLREGQQL 617
Cdd:PRK06965 521 VKLAEAYGHVGMRIEK--TSDVEPALREALRL 550
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
64-601 |
3.14e-42 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 161.08 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFtlvGGHI-SPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDVLypyfmvEKEMIPTKLPNSlmgrvvvwylqnclANLfvGAWeprpegplPLDIPQASPQQVQRCVEILSRAKRPLLV 299
Cdd:PRK06112 170 ADLL------TAAAAAPAAPRS--------------NSL--GHF--------PLDRTVPAPQRLAEAASLLAQAQRPVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 300 LG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI------------RQNRSAALKKADVVVLAGA 362
Cdd:PRK06112 220 AGggvhiSGA------SAALAALQSLAGLPVATTNMGKGAVDETHPLSLgvvgslmgprspGRHLRDLVREADVVLLVGT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 363 VCDFRLSYGRVLNRKSSIII--------VNRNRDDLLLNSDifwkPQEAVQGDVGSFMIKLVEGLQGQMWS-SDWAEELR 433
Cdd:PRK06112 294 RTNQNGTDSWSLYPEQAQYIhidvdgeeVGRNYEALRLVGD----ARLTLAALTDALRGRDLAARAGRRAAlEPAIAAGR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 434 KADQQKEQTYRDKALMPVlqhlNPVWVLQQVEETLPDNALLVVDGG-DFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 512
Cdd:PRK06112 370 EAHREDSAPVALSDASPI----RPERIMAELQAVLTGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLAGLGWGVPM 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 513 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA--GWtQISREQVpRLGSDV-ACSLAYTDYHKAA 589
Cdd:PRK06112 446 AIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF-QKHAETV-KFGTHTdACHFAAVDHAAIA 523
|
570
....*....|..
gi 1318663320 590 MGLGAQGLILSR 601
Cdd:PRK06112 524 RACGCDGVRVED 535
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
64-559 |
1.78e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 158.72 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 lypyfmvekemiptklpnslmgrvvvwylQNclANLFVGAWePRPEGPLPldIPQASPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK08155 175 -----------------------------QT--AVIELEAL-PAPAEKDA--APAFDEESIRDAAAMINAAKRPVLYLGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRlSYGRV-- 373
Cdd:PRK08155 221 GVINSGAPARARELA-EKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYILQEADLLIVLGARFDDR-AIGKTeq 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSIIIVNRNRDDLllnsDIFWKPQEAVQGDVGSFMIKLVEGLQGQMwSSDWAEelRKADQQKEQTYRdkalMPVLQ 453
Cdd:PRK08155 299 FCPNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQP-RAEWHQ--LVADLQREFPCP----IPKAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 454 H-LNPVWVLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLF 529
Cdd:PRK08155 368 DpLSHYGLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPR---QWLTSGGLGTMGFGLPAAIGAALANPERKVLCFS 444
|
490 500 510
....*....|....*....|....*....|.
gi 1318663320 530 GDGAFGYSLIEFDTFVRHKVPV-IALVGNDA 559
Cdd:PRK08155 445 GDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
62-564 |
6.14e-41 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 156.96 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 62 RHGGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK08199 8 RTGGQILVDALRANGVERVFCVPGESYLAVLDALhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK08199 88 IGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLYpyfmvekemiptklpnslmGRVVVwylqnclanlfvgaweprPEGPlPLDIPQASP--QQVQRCVEILSRAKRPLL 298
Cdd:PRK08199 168 DVLS-------------------ETAEV------------------PDAP-PYRRVAAAPgaADLARLAELLARAERPLV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 VLG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRS--AALKKADVVVLAGAvcdf 366
Cdd:PRK08199 210 ILGgsgwtEAA------VADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDlglgiNPAlaARIREADLVLAVGT---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 367 RLsyGRVLNRKSSIIIVNRNRDDLL--------LNSdiFWKPQEAVQGDVGSF--MIKLVEGLQGQMWsSDWAEELRkAD 436
Cdd:PRK08199 280 RL--GEVTTQGYTLLDIPVPRQTLVhvhpdaeeLGR--VYRPDLAIVADPAAFaaALAALEPPASPAW-AEWTAAAH-AD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 437 QQKEQTYRdkalmPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFvatAAYL---VQPRGPLRWLDPGAfGTLGVGAGFA 513
Cdd:PRK08199 354 YLAWSAPL-----PGPGAVQLGEVMAWLRERLPADAIITNGAGNY---ATWLhrfFRFRRYRTQLAPTS-GSMGYGLPAA 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1318663320 514 LGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQI 564
Cdd:PRK08199 425 IAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
64-557 |
2.21e-39 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 152.34 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ypyfmvekemiptklpnslmgrvvvwylqncLANLFVGAWEPRPEGPlpldiPQASPQQVQRCVEILSRAKRPLLVLG-- 301
Cdd:PRK08978 163 -------------------------------LAEGELEPHLTTVENE-----PAFPAAELEQARALLAQAKKPVLYVGgg 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 ---SQAllppTPAnkLRAAVETLGVP--CFLGGMsrGLLGRNHP-----LHIRQNRSA--ALKKADVVVLAGAVCDFRLS 369
Cdd:PRK08978 207 vgmAGA----VPA--LREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDRVT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 yGRvLNR---KSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDvgsfMIKLVEGLQGQMWSSDWAEELRKADQQKEQTYR 444
Cdd:PRK08978 279 -GK-LNTfapHAKVIHLDIDPAEInkLRQAHV------ALQGD----LNALLPALQQPLNIDAWRQHCAQLRAEHAWRYD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 445 DKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAE 524
Cdd:PRK08978 347 HPG-----EAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDT 421
|
490 500 510
....*....|....*....|....*....|....
gi 1318663320 525 VWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:PRK08978 422 VICVSGDGSFMMNVQELGTIKRKQLPVkIVLLDN 455
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
64-632 |
2.60e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 150.20 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 139
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 140 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDV---LYPYFMVEKEMIptKLPnslmgrvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRP 296
Cdd:PRK07418 181 KDVgqeEFDYVPVEPGSV--KPP----------------------GYRPTVKG---------NPRQINAALKLIEEAERP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LLVLGSQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRL- 368
Cdd:PRK07418 228 LLYVGGGAISAGAHAE-LKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAVTECDLLIAVGARFDDRVt 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 369 -------SYGRVLNrkssIII----VNRNRddlllnsdifwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQ 437
Cdd:PRK07418 307 gkldefaSRAKVIH----IDIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERINR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 438 QKEqtyrDKALM--PVLQHLNPVWVLQQVEETLPDnALLVVDGGDFVATAA-YLvqPRGPLRWLDPGAFGTLGVGAGFAL 514
Cdd:PRK07418 372 WKQ----DYPLVvpPYEGEIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAqFL--RNGPRRWISSAGLGTMGFGMPAAM 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 515 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISRE-QVPRLG-----SDVACSLAytDYHKA 588
Cdd:PRK07418 445 GVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQwQESFYGerysaSNMEPGMP--DFVKL 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1318663320 589 AMGLGAQGLILSrdNKDQVVKVLREgqQLCQDGhAVVVNILIGR 632
Cdd:PRK07418 522 AEAFGVKGMVIS--ERDQLKDAIAE--ALAHDG-PVLIDVHVRR 560
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
53-557 |
3.19e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 149.20 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 53 MHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVT 131
Cdd:PRK07282 1 MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 132 AGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTP 211
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 212 GPVFVELPLDVlypyfmVEKEmipTKLPNSlmgrvvvwylqnclanlfvgaweprPEGPLPLDIPQASPQ--QVQRCVEI 289
Cdd:PRK07282 161 GPVVIDLPKDV------SALE---TDFIYD-------------------------PEVNLPSYQPTLEPNdmQIKKILKQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 290 LSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGA 362
Cdd:PRK07282 207 LSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANIAMTEADFMINIGS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 363 VCDFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKaDQQKEQT 442
Cdd:PRK07282 286 RFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLAEPTVHNNTEKWIEKVTK-DKNRVRS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 443 YRDKALMpvlqhLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 522
Cdd:PRK07282 362 YDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPD 436
|
490 500 510
....*....|....*....|....*....|....*.
gi 1318663320 523 AEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:PRK07282 437 KEVILFVGDGGFQMTNQELAILNIYKVPIkVVMLNN 472
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
64-596 |
3.89e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 149.22 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVA----CEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNT 139
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 140 VTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELP 219
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDVLYpyfmvEKemiptklpnslMGRVVvwylqnclanlfvgaWEPRPEGPLPLDIPQ-ASPQQVQRCVEILSRAKRPLL 298
Cdd:PRK06456 164 RDIFY-----EK-----------MEEIK---------------WPEKPLVKGYRDFPTrIDRLALKKAAEILINAERPII 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 VLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPLHI-------RQNRSAALKKADVVVLAGAVCDFR--LS 369
Cdd:PRK06456 213 LVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfTS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 YGRVLNRKSSIIIVNRNRDDlllnSDIFWKPQEAVQGDVGSF---MIKLVEGLQGQMWSSDWAEELRKADQQKEQTY--- 443
Cdd:PRK06456 292 YDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIIlreLIKAITELGQKRDRSAWLKRVKEYKEYYSQFYyte 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 444 RDKALMPvlqhlnpvW-VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPE 522
Cdd:PRK06456 368 ENGKLKP--------WkIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 523 AEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVgNDAGWTQISReQVPRL-------GSDVACSlayTDYHKAAMGLGAQ 595
Cdd:PRK06456 440 KVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVR-QVQDLffgkrivGVDYGPS---PDFVKLAEAFGAL 514
|
.
gi 1318663320 596 G 596
Cdd:PRK06456 515 G 515
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
64-551 |
3.97e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 149.20 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK08979 166 LNPAI-----LHPYEYPESIKMR----------------SYNPTTSG---------HKGQIKRGLQALLAAKKPVLYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKADVVVLAGAVCDFRLSygrvln 375
Cdd:PRK08979 216 GAIISGADKQILQLA-EKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNADLIFGIGVRFDDRTT------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 376 rkssiiivnRNRDDLLLNSDIFW---KP---QEAVQGD---VGSF------MIKLVEGlQGQMWSSD----WAEELRKAD 436
Cdd:PRK08979 289 ---------NNLEKYCPNATILHidiDPssiSKTVRVDipiVGSAdkvldsMLALLDE-SGETNDEAaiasWWNEIEVWR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 437 QQKEQTYRDKAlmpvlQHLNPvwvlQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 512
Cdd:PRK08979 359 SRNCLAYDKSS-----ERIKP----QQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPA 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 1318663320 513 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 551
Cdd:PRK08979 430 AMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
64-630 |
4.14e-38 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 149.22 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLL--VACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTpGPVFVELPLD 221
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 vlYPYFMVEKEMiptklpnslmgrvvvWYLQNCLANLFVgaweprpegplpldIPQASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:TIGR02720 160 --FGWQEIPDND---------------YYASSVSYQTPL--------------LPAPDVEAVTRAVQTLKAAERPVIYYG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlaGAVCDFRLSYGRvlNRKSSII 381
Cdd:TIGR02720 209 IGAR---KAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEA---LFQADLVLFVGN--NYPFAEV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 382 IVNRNRDDLLLNSDI----FWKPQE---AVQGDVGSFmIKLVEGLQGQMWSSDWAEElRKADQQKEQTYRDKALMPVLQH 454
Cdd:TIGR02720 281 SKAFKNTKYFIQIDIdpakLGKRHHtdiAVLADAKKA-LAAILAQVEPRESTPWWQA-NVANVKNWRAYLASLEDKTEGP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:TIGR02720 359 LQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAF 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGAQGLILsrDNKDQVVKV 610
Cdd:TIGR02720 439 SMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQedtnQPLIGVD----FNDADFAKIAEGVGAVGFRV--NKIEQLPAV 512
|
570 580
....*....|....*....|
gi 1318663320 611 LREGQQLCQdGHAVVVNILI 630
Cdd:TIGR02720 513 FEQAKAIKQ-GKPVLIDAKI 531
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
64-554 |
9.17e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 148.07 E-value: 9.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK07979 166 LNPAN-----KLPYVWPESVSMR----------------SYNPTTQG---------HKGQIKRALQTLVAAKKPVVYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPAnKLRAAVETLGVPCF-----LGGM------SRGLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSYG 371
Cdd:PRK07979 216 GAINAACHQ-QLKELVEKLNLPVVsslmgLGAFpathrqSLGMLG----MHGTYEANMTMHNADVIFAVGVRFDDRTTNN 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 372 RVLNRKSSIII---VNRNRDDLLLNSDIfwkpqeAVQGDVGSFMIKLVEgLQGQMWSSDWAEELRKADQQKEQTYRDKAL 448
Cdd:PRK07979 291 LAKYCPNATVLhidIDPTSISKTVTADI------PIVGDARQVLEQMLE-LLSQESAHQPLDEIRDWWQQIEQWRARQCL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 M--PVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVW 526
Cdd:PRK07979 364 KydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVV 443
|
490 500
....*....|....*....|....*...
gi 1318663320 527 CLFGDGAFGYSLIEFDTFVRHKVPVIAL 554
Cdd:PRK07979 444 CVTGDGSIQMNIQELSTALQYELPVLVL 471
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
64-551 |
1.71e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 144.12 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLYPYFMVEKEMiPTKlpnslmgrvvvwylqnclanLFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLL-- 298
Cdd:PRK06466 164 DMTNPAEKFEYEY-PKK--------------------VKLRSYSPAVRG---------HSGQIRKAVEMLLAAKRPVIys 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 299 ----VLGSQALLPPTPANKLRAAVET--LGVPCFLGGMSR--GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDfrlsy 370
Cdd:PRK06466 214 gggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEANMAMHHADVILAVGARFD----- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 371 GRVLNRKSSII----IVNRNRDDLLLNSDIFWK-----PQEAVQGDVGSFMIKLVEGLQGQMWSSDWAE--ELRKA-DQQ 438
Cdd:PRK06466 285 DRVTNGPAKFCpnakIIHIDIDPASISKTIKADipivgPVESVLTEMLAILKEIGEKPDKEALAAWWKQidEWRGRhGLF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQTYRDKALMPvlqhlnpvwvlQQVEETLPD----NALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 514
Cdd:PRK06466 365 PYDKGDGGIIKP-----------QQVVETLYEvtngDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAM 433
|
490 500 510
....*....|....*....|....*....|....*..
gi 1318663320 515 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 551
Cdd:PRK06466 434 GVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
64-558 |
6.13e-36 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 142.75 E-value: 6.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGgIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPYFmvekeMIPTKLPNSLMGRvvvwylqnclanlfvgAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK06882 166 VNPAN-----KFTYEYPEEVSLR----------------SYNPTVQG---------HKGQIKKALKALLVAKKPVLFVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTpANKLRAAVETLGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLS-- 369
Cdd:PRK06882 216 GVITAEC-SEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEANNAMHESDLILGIGVRFDDRTTnn 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 ------YGRVL-----------NRKSSIIIVNRNRDDL-----LLNSDIFWKPQEAVqgdvgsfmiklveglqgqmwsSD 427
Cdd:PRK06882 291 lakycpNAKVIhididptsiskNVPAYIPIVGSAKNVLeeflsLLEEENLAKSQTDL---------------------TA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 428 WAEELR--KADQQKEQTYRDKALMPvlqhlnpvwvlQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPG 501
Cdd:PRK06882 350 WWQQINewKAKKCLEFDRTSDVIKP-----------QQVVEAIyrltNGDAYVASDVGQHQMFAALHYPFDKPRRWINSG 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1318663320 502 AFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PRK06882 419 GAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
51-558 |
7.41e-36 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 142.21 E-value: 7.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 51 QLMHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAV 130
Cdd:PRK07710 5 RTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 131 TAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGT 210
Cdd:PRK07710 85 TSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 211 PGPVFVELPLDVLYP--YFMVEKEM-----IPTKLPNSLmgrvvvwylqnclanlfvgaweprpegplpldipqaspqQV 283
Cdd:PRK07710 165 PGPVLIDIPKDMVVEegEFCYDVQMdlpgyQPNYEPNLL---------------------------------------QI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 284 QRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADV 356
Cdd:PRK07710 206 RKLVQAVSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLflgmagmHGTYTANMALYECDL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 357 VVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDLLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKAD 436
Cdd:PRK07710 285 LINIGARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 437 QQKEQTYRDKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGA 516
Cdd:PRK07710 362 EKYPLSYKRNS-----ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGA 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1318663320 517 KLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PRK07710 437 QLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
64-557 |
6.76e-35 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 140.12 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPL---LVACEKLgiRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTV 140
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 141 TAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLypyfmvEKEMiptklpnslmgrvvvwylqnclanLFvgAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVL 300
Cdd:PRK07789 191 DAL------QAQT------------------------TF--SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDfrlsyGRV 373
Cdd:PRK07789 239 GGGVIRAEASA-ELRELAELTGIPVVTTLMARGAFPDSHPQHLGMpgmhgtvAAVAALQRSDLLIALGARFD-----DRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSI-----II--------VNRNRddlllNSDIFwkpqeaVQGDVGSFMIKLVEGLQ------GQMWSSDWAEELRK 434
Cdd:PRK07789 313 TGKLDSFapdakVIhadidpaeIGKNR-----HADVP------IVGDVKEVIAELIAALRaehaagGKPDLTAWWAYLDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 435 ADQQKEQTYRDkalmPVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFAL 514
Cdd:PRK07789 382 WRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAM 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1318663320 515 GAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:PRK07789 458 GAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINN 501
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
75-557 |
2.54e-34 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 137.91 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 75 HGVRFVFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 150
Cdd:CHL00099 23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 151 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV---LYPYF 227
Cdd:CHL00099 103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 228 MVEKEMIPTKLPnslmgrvvvwylqnclanlfvgAWEPrpegplpldIPQASPQQVQRCVEILSRAKRPLLVLGSQALLP 307
Cdd:CHL00099 183 PPEPGNTIIKIL----------------------GCRP---------IYKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 308 PTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLNRKSSI 380
Cdd:CHL00099 232 DA-HQEITELAELYKIPVTTTLMGKGIFDEDHPLclgmlgmHGTAYANFAVSECDLLIALGARFDDRVT-GKLDEFACNA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIV-----------NRNrddlllnsdifwkPQEAVQGDVGSFMIKLVEglqgqmwSSDWAEELRKADQQ---KEQTYRDK 446
Cdd:CHL00099 310 QVIhididpaeigkNRI-------------PQVAIVGDVKKVLQELLE-------LLKNSPNLLESEQTqawRERINRWR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 447 ALMPVL-----QHLNPVWVLQQVEETLPDnALLVVDGGDFVATAAYL--VQPRgplRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:CHL00099 370 KEYPLLipkpsTSLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlkCKPR---KWLSSAGLGTMGYGLPAAIGAQIA 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 1318663320 520 QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 557
Cdd:CHL00099 446 HPNELVICISGDASFQMNLQELGTIAQYNLPIkIIIINN 484
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
72-561 |
1.23e-33 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 135.90 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 72 LRAHGVRFVFTLVGGHISPLLVACEK---LGIRVVDT---RHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:PRK08327 17 LKELGVDYIFINSGTDYPPIIEAKARaraAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANALGGVHN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 146 AQVAQSPVLLLGGAASTLlqKRGAL-----------QAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPV 214
Cdd:PRK08327 97 AARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 215 FVELPLDVLypyfmVEKemiptklpnslmgrvvvwylqnclanlfVGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAK 294
Cdd:PRK08327 175 YLTLPREVL-----AEE----------------------------VPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 295 RPLLV---LGSQALLPPTpankLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQNRSAALKKADVVvlagavcdfrlsyg 371
Cdd:PRK08327 222 RPVIItwrAGRTAEGFAS----LRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLV-------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 372 rvlnrkssiiivnrnrddLLLNSDIFWKPQE------------------------------AVQGDVGSFMIKLVEGLQG 421
Cdd:PRK08327 284 ------------------LVVDSDVPWIPKKirpdadarviqidvdplksriplwgfpcdlCIQADTSTALDQLEERLKS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 422 QMWSSDWAEELRKADQQKEQTYRDKALMPVLQHL------NPVWVLQQVEETLPDNALLVVDGGdFVATAAYLvqpRGPL 495
Cdd:PRK08327 346 LASAERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPG 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1318663320 496 RWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFV--RHKVPVIALVGNDAGW 561
Cdd:PRK08327 422 SYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
64-551 |
2.29e-33 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 135.22 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 lypYFMVEKEMIPTKLPnslmgrvvvwylqnclanlFVGAWEPRPEGplpldipqaSPQQVQRCVEILSRAKRPLLVLGS 302
Cdd:PRK09107 173 ---QFATGTYTPPQKAP-------------------VHVSYQPKVKG---------DAEAITEAVELLANAKRPVIYSGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 303 QALLPPTPANK-LRAAVETLGVP--CFLGGMSR---------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSy 370
Cdd:PRK09107 222 GVINSGPEASRlLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYEANMAMHDCDVMLCVGARFDDRIT- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 371 GRV-----LNRKSSIII----VNRN-RDDLllnsdifwkpqeAVQGDVGSFMIKLVEGLQGQMWSSD------WAEELRK 434
Cdd:PRK09107 297 GRLdafspNSKKIHIDIdpssINKNvRVDV------------PIIGDVGHVLEDMLRLWKARGKKPDkealadWWGQIAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 435 ADQQKEQTYR--DKALMPvlQHlnpvwVLQQVEE-TLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAG 511
Cdd:PRK09107 365 WRARNSLAYTpsDDVIMP--QY-----AIQRLYElTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 551
Cdd:PRK09107 438 AALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
66-632 |
3.08e-31 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 128.94 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 143
Cdd:PRK11269 8 DAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:PRK11269 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ypyfMVEKEmiptklpnslmgrvvvwylqnclanlfvgaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 303
Cdd:PRK11269 168 ----VAEIE------------------------------FDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL----------HIRQNrsAALKKADVVVLAGAvcdfrlsygRV 373
Cdd:PRK11269 213 GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATLLASDFVLGIGN---------RW 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 374 LNRKSSIIIVNRnRDDLLLNSDI-------FWKPQEAVQGDVGSFMIKLVEGLQGQMWS------SDWAEEL--RKADQQ 438
Cdd:PRK11269 282 ANRHTGSVEVYT-KGRKFVHVDIeptqigrVFGPDLGIVSDAKAALELLVEVAREWKAAgrlpdrSAWVADCqeRKRTLL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQTYRDkalMPVlqhlNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 518
Cdd:PRK11269 361 RKTHFDN---VPI----KPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 519 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPrLGSDVACSLAY------------TDYH 586
Cdd:PRK11269 434 ADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRA-FDMDYCVQLAFeninspelngygVDHV 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1318663320 587 KAAMGLGAQGLILSRdnKDQVVKVLREGQQLCQDGHA-VVVNILIGR 632
Cdd:PRK11269 513 KVAEGLGCKAIRVFK--PEDIAPALEQAKALMAEFRVpVVVEVILER 557
|
|
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
66-632 |
3.42e-30 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 226469 [Multi-domain] Cd Length: 592 Bit Score: 125.77 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLT-GTVGVAAVTAGPGLTNTVTAV 143
Cdd:COG3960 8 DAAVYVLEKEGITTAFGVPGAAINPFYSALRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVL 223
Cdd:COG3960 88 YSASADSIPILCITGQAPRARLHKEDFQAVDIEAIAKPVSKWAVTVREPALVPRVLQQAFHLMRSGRPGPVLIDLPFDVQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 224 ypyfMVEKEmiptklpnslmgrvvvwylqnclanlfvgaWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSq 303
Cdd:COG3960 168 ----VAEIE------------------------------FDPDMYEPLPVYKPAATRVQAEKALAMLIQAERPLIVAGG- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 ALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-NRSAALKKADVVVLAGavcDFRLSYG-RVLNRKS-SI 380
Cdd:COG3960 213 GVINADAAALLQEFAELTGVPVIPTLMGWGCIPDDHPLMAGMvGLQTSHRYGNATLLAS---DMVFGIGnRWANRHTgSV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 381 IIVNRNRDdlLLNSDI-------FWKPQEAVQGDVGSFMIKLVEglQGQMWSS-----DWAEELRKADQQKEQTYRDKAL 448
Cdd:COG3960 290 EVYTEGRK--FIHVDIeptqigrVFCPDLGIVSDAKAALTLLLD--VAQEWKKagklpCRKAWVADCQQRKRTLLRKTHF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 MPVlqHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCL 528
Cdd:COG3960 366 DNV--PVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAAQFLHVFKPRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 529 FGDGAFGYSLIEFDTFVRHKVPVIALVGNDAgWTQISREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQG 596
Cdd:COG3960 444 SGDYDFQFLIEELAVGAQFKIPYIHVLVNNA-YLGLIRQAQRAFDMDYCVQLAFeninssevngygVDHVKVAEGLGCKA 522
|
570 580 590
....*....|....*....|....*....|....*..
gi 1318663320 597 LILSRDNkdQVVKVLREGQQLCQDGHA-VVVNILIGR 632
Cdd:COG3960 523 IRVFKPE--DIAPAFEQAKALMAQHRVpVVVEVILER 557
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
62-558 |
7.51e-29 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 121.38 E-value: 7.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 62 RHGGESVAAVLRAHGVRFVFTLVGG-----HISPLLVACeklgIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGL 136
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGasmeiHQALTRSNC----IRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 137 TNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFV 216
Cdd:PLN02470 89 TNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 217 ELPLDVlypyfmvEKEM-IPT-KLPNSLMGrvvvwYLQNClanlfvgawePRPegplpldiPQASpqQVQRCVEILSRAK 294
Cdd:PLN02470 169 DIPKDI-------QQQLaVPNwNQPMKLPG-----YLSRL----------PKP--------PEKS--QLEQIVRLISESK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 295 RPLLVLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAALKKADVVVLAGAVCDFR 367
Cdd:PLN02470 217 RPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANYAVDSADLLLAFGVRFDDR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 368 LSyGRV--LNRKSSIIIVNRNRDDLLLNSdifwKPQEAVQGDVG---SFMIKLVEGLQGQMWS-SDWAEELrkaDQQKEQ 441
Cdd:PLN02470 294 VT-GKLeaFASRASIVHIDIDPAEIGKNK----QPHVSVCADVKlalQGLNKLLEERKAKRPDfSAWRAEL---DEQKEK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 442 ---TYRDKAlmpvlQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 518
Cdd:PLN02470 366 fplSYPTFG-----DAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAA 440
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1318663320 519 CQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 558
Cdd:PLN02470 441 ANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
477-626 |
1.89e-28 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 426974 [Multi-domain] Cd Length: 151 Bit Score: 111.14 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 477 DGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVG 556
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663320 557 NDAGWTQISREQVP----RLGSDVACSLAYTDYHKAAMGLGAQGliLSRDNKDQVVKVLREGqqLCQDGHAVVV 626
Cdd:pfam02775 81 NNGGYGMTRGQQTPfgggRYSGPSGKILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEA--LEHDGPALID 150
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
66-604 |
2.80e-26 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 113.39 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKN 145
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 146 AQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLDVLYp 225
Cdd:PRK06457 86 AKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAIS-KRGVAHINLPVDILR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 226 yfmvekemiptklpnslMGRvvvwylqnclanlfvgawEPRPEGPLPLDIPQASPQqVQRCVEILSRAKRPLLVLGSQAL 305
Cdd:PRK06457 164 -----------------KSS------------------EYKGSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 306 LPPTPANKLraaVETLGVPCF----------------LGGMsrGLLGRNHPLhirqnrsAALKKADVVVLAGAVcdfrLS 369
Cdd:PRK06457 208 GLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI-------EAMDKADLLIMLGTS----FP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 370 YGRVLNRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFMI--------KLVEGLQGQMwsSDWAEELRKADQQk 439
Cdd:PRK06457 272 YVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLNidieeksdKFYEELKGKK--EDWLDSISKQENS- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 440 eqtyRDKALmpvlqhlNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 519
Cdd:PRK06457 343 ----LDKPM-------KPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 520 -QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGA 594
Cdd:PRK06457 412 vENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEWGVD----LYNPDFTKIAESIGF 487
|
570
....*....|
gi 1318663320 595 QGLILSRDNK 604
Cdd:PRK06457 488 KGFRLEEPKE 497
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
460-626 |
2.51e-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: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 460 VLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLI 539
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 540 EFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQGLILSRDnkDQVVKVLREGQQlc 618
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDP--EDLEAALAEALA-- 157
|
....*...
gi 1318663320 619 QDGHAVVV 626
Cdd:cd00568 158 AGGPALIE 165
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
455-633 |
2.66e-24 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 100.66 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLRE 613
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
|
170 180
....*....|....*....|
gi 1318663320 614 GQQLCQDGHAVVVNILIGRT 633
Cdd:cd02013 162 AIAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
65-222 |
5.68e-24 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 98.78 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 65 GESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAV 143
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 144 KNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRR---VRDIVPT-LRTAIAaaqsgTPGPVFVELP 219
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPELLDRaIRTAIA-----KRGVAVLILP 157
|
...
gi 1318663320 220 LDV 222
Cdd:cd07039 158 GDV 160
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
455-630 |
1.59e-22 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 94.90 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILsrDNKDQVVKVLREG 614
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
|
170
....*....|....*.
gi 1318663320 615 QQlcQDGhAVVVNILI 630
Cdd:cd02014 160 LA--ADG-PVVIDVVT 172
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
64-596 |
5.08e-22 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 100.46 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVAC--EKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVT 141
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 142 AVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSgTPGPVFVELPLD 221
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VLypyfmVEKEMIPTKLPNSLMgrvvvwylqnclanlfvgaweprpegplPLDIPQASPQQVQRCVEILSRAKRPLLVLG 301
Cdd:PRK08611 165 LP-----AQKIKDTTNKTVDTF----------------------------RPTVPSPKPKDIKKAAKLINKAKKPVILAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 302 SQAllpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----NRSA--ALKKADVVVLAGAvcDFrlSYGRVL 374
Cdd:PRK08611 212 LGA---KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNlgkigTKPAyeAMQEADLLIMVGT--NY--PYVDYL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 375 NRKSSIIIVNRNRDDL--LLNSDIfwkpqeAVQGDVGSFM------IKLVE------GLQGQMwsSDWAEELRKADQQKE 440
Cdd:PRK08611 285 PKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALhqltenIKHVEdrrfleACQENM--AKWWKWMEEDENNAS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 441 QTYRDKALMPVLQhlnpvwvlqqveETLPDNALLVVD-GGDFVATAAYL-VQPRGPL---RWLdpgafGTLGVGAGFALG 515
Cdd:PRK08611 357 TPIKPERVMAAIQ------------KIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL-----GTMGCGLPGAIA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 516 AKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQ 595
Cdd:PRK08611 420 AKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGK 499
|
.
gi 1318663320 596 G 596
Cdd:PRK08611 500 G 500
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
106-594 |
1.28e-21 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 226471 [Multi-domain] Cd Length: 617 Bit Score: 99.39 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 106 RHEVTAVFAADAVARLTGTVGVAAVTA--GPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMS------ 177
Cdd:COG3962 63 HNEQGMAHAAIAYAKQHRRRRIYAVTSsiGPGAANMVTAAALAHVNRLPVLLLPGDVFATRQPDPVLQQLEQFGdgtitt 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 178 --LFRPLCKFCASVRRVRDIVPTLRTAIAA-AQSGTPGPVFVELPLDVL-----YP-YFMVEKemiptklpnslmgrvvV 248
Cdd:COG3962 143 ndCFRPVSRYFDRITRPEQLMSALPRAMRVmTDPADCGPVTLALCQDVQaeaydYPeSFFEKR----------------V 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 249 WYlqnclanlfvgaweprpegplpLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPAnKLRAAVETLGVPCFLG 328
Cdd:COG3962 207 WR----------------------IRRPPPDERELADAAALIKSAKKPLIVAGGGVLYSGARE-ALRAFAETHGIPVVET 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 329 GMSRGLLGRNHPLHI---------RQNRSAAlkKADVVVLAGA-VCDFRLSyGRVLNRKSSIIIVNRNRDDLllnsDIFW 398
Cdd:COG3962 264 QAGKSALAWDHPLNLggvgvtgtlAANRAAE--EADLVIGIGTrLQDFTTG-SKALFKNPGVKFLNLNVQPF----DAYK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 399 KPQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKAdqqkEQTYRDKALMPVLQHLNP------VWVLQQVEETLPDNA 472
Cdd:COG3962 337 HDALPLVADARAGLEALSEALGGYRTAAGWTDERERL----KAAWDAEADAPTAKNHFLntlptqTQVIGAVQRTISDDS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 473 LLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVI 552
Cdd:COG3962 413 VVVCAAGSLPGDLHKLWRAGVPGTYHLEYGFSCMGYEIAGGLGAKAAEPDREVYVMVGDGSYMMLNSELATSVMLGKKII 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1318663320 553 ALVGNDAGWTQISREQVPRLGSDVACSLAYT---------DYHKAAMGLGA 594
Cdd:COG3962 493 VVLLDNRGYGCINRLQMATGGASFNNLLRDTdheeeilqvDFAAHAESYGA 543
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
68-219 |
4.56e-18 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 81.62 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 68 VAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNA 146
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1318663320 147 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELP 219
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLP 153
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
283-415 |
2.22e-16 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 76.06 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 283 VQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKAD 355
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGA-SEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1318663320 356 VVVLAGAVCDFRLSYGRV--LNRKSSIIIVNRNRDDLLLNSdifwKPQEAVQGDVGSFMIKL 415
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLpeFAPDAKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
59-561 |
1.98e-15 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 79.23 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 59 TSIRHggeSVAAVLRAHGVRFVFTLVGGHISPLLVACEKlGIRVVDTRHEVTAVFAADAVARLTGTVGV----AAVTAGP 134
Cdd:PRK07092 12 TTVRD---ATIDLLRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFvnlhSAAGVGN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 135 GLTNTVTAVKNaqvaQSP-VLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGP 213
Cdd:PRK07092 88 AMGNLFTAFKN----HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 214 VFVELPLDvlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEpRPEGPLPL-DIPQA---SPQQVQRCVEI 289
Cdd:PRK07092 164 VFVSIPYD----------------------------------------DWD-QPAEPLPArTVSSAvrpDPAALARLGDA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 290 LSRAKRPLLVLGsqALLPPTPANKLRAAV-ETLGVPCFLGGMS-RGLLGRNHPLH------IRQNRSAALKKADVVVLAG 361
Cdd:PRK07092 203 LDAARRPALVVG--PAVDRAGAWDDAVRLaERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLVIG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 362 AVCdFRL---SYGRVLNRKSSIIIVNrnrDDLLLNSdifWKPQ-EAVQGDVGSFMIKLVEGLqgqmwssdwAEELRKADQ 437
Cdd:PRK07092 281 APV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVGDIRLALRDLLALL---------PPSARPAPP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 438 QKEQTYRDKALMPVlqhLNPVWVLQQVEETLPDNALLVVDggdfvATAAYLV-QPRgpLRWLDPGAF-----GTLGVGAG 511
Cdd:PRK07092 345 ARPMPPPAPAPGEP---LSVAFVLQTLAALRPADAIVVEE-----APSTRPAmQEH--LPMRRQGSFytmasGGLGYGLP 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 561
Cdd:PRK07092 415 AAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
66-625 |
6.62e-15 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 77.72 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 66 ESVAAVLRAHGVRFVFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVK 144
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 145 NAQVAQSPVLLLggaASTLLQKR---GALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGtPGPVFVELPLD 221
Cdd:PRK06546 87 DAHRSGAPVLAI---ASHIPSAQigsGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 222 VlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPLDIPQA------SPQQVQRCVEILSRAKR 295
Cdd:PRK06546 163 I---------------------------------------ADEPAPEGFAPSVISPRrptvvpDPAEVRALADAINEAKK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 296 PLLVLGS---------QALlpptpANKLRAAV-ETLGVPCFLG-------GMSrGLLGRNHPlhirqnrSAALKKADVVV 358
Cdd:PRK06546 204 VTLFAGAgvrgahaevLAL-----AEKIKAPVgHSLRGKEWIQydnpfdvGMS-GLLGYGAA-------HEAMHEADLLI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 359 LAGAvcDFrlSYGRVLNRKsSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQGQMWSSDWAEELRKADQQ 438
Cdd:PRK06546 271 LLGT--DF--PYDQFLPDV-RTAQVDIDPEHLGRRTRV----DLAVHGDVAETIRALLPLVKEKTDRRFLDRMLKKHARK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 439 KEQ---TYRDKalmpVLQH--LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLdpGAF--GTLGVGAG 511
Cdd:PRK06546 342 LEKvvgAYTRK----VEKHtpIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVI--GSFrhGSMANALP 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 512 FALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ----VPRLGSDVacslAYTDYHK 587
Cdd:PRK06546 416 HAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMlvdgLPDFGTDH----PPVDYAA 491
|
570 580 590
....*....|....*....|....*....|....*...
gi 1318663320 588 AAMGLGAQGLILSrDNKDqVVKVLREGqqLCQDGHAVV 625
Cdd:PRK06546 492 IAAALGIHAVRVE-DPKD-VRGALREA--FAHPGPALV 525
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
457-626 |
1.57e-14 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 71.94 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 457 PVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 536
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 537 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSrdNKDQVVKVLREGqq 616
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIE--SADDLLPVLERA-- 156
|
170
....*....|
gi 1318663320 617 LCQDGHAVVV 626
Cdd:cd02010 157 LAADGVHVID 166
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
72-534 |
6.86e-14 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 74.56 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 72 LRAHGVRFVFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVA 149
Cdd:PRK08273 13 LREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 150 QSPVLLLGGAastllQKRGAL-----QAIDQMSLFR----PLCKFCASVRRVRDIVP-TLRTAIAaaqsgTPGPVFVELP 219
Cdd:PRK08273 93 HVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVDrAVRTALA-----ERTVTAVILP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 220 LDVL---YPYFMVEKEMIPTKLPNSlMGRVVvwylqnclanlfvgawePRPEgplpldipqaspqQVQRCVEILSRAKRP 296
Cdd:PRK08273 163 NDVQeleYEPPPHAHGTVHSGVGYT-RPRVV-----------------PYDE-------------DLRRAAEVLNAGRKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LLVLGSQALlppTPANKLRAAVETLGvpcflGGMSRGLLGRnhplhirqnrsAALKKaDVVVLAGAVcdfrlsyGrVLNR 376
Cdd:PRK08273 212 AILVGAGAL---GATDEVIAVAERLG-----AGVAKALLGK-----------AALPD-DLPWVTGSI-------G-LLGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 377 KSSIIIVnRNRDDLLLNSDIF----WKPQE----AVQGDVGSFMIKL---VE-GLQG--------------QMWSSDWAE 430
Cdd:PRK08273 264 KPSYELM-RECDTLLMVGSSFpyseFLPKEgqarGVQIDIDGRMLGLrypMEvNLVGdaaetlrallplleRKKDRSWRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 431 ELRKADQQKEQTYRDKALMPVlQHLNPVWVLQQVEETLPDNALLVVDGGDfVAT--AAYLVQPRGPLRWLDpGAFGTLGV 508
Cdd:PRK08273 343 RIEKWVARWWETLEARAMVPA-DPVNPQRVFWELSPRLPDNAILTADSGS-CANwyARDLRMRRGMMASLS-GTLATMGP 419
|
490 500
....*....|....*....|....*.
gi 1318663320 509 GAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:PRK08273 420 AVPYAIAAKFAHPDRPVIALVGDGAM 445
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
455-630 |
7.87e-14 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 69.93 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 534
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 535 GYSLIEFDTFVRHKVPVIALVGNDAGWtQISREQVPRLGSDVACSLAY---------TDYHKAAMGLGAQGLILSRdnKD 605
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVET--PE 156
|
170 180
....*....|....*....|....*
gi 1318663320 606 QVVKVLREGQqlcQDGHAVVVNILI 630
Cdd:cd02002 157 ELDEALREAL---AEGGPALIEVVV 178
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
76-567 |
1.45e-13 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 226470 [Multi-domain] Cd Length: 557 Bit Score: 73.52 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 76 GVRFVFTLVGGHISPLLVA-CEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQSPVL 154
Cdd:COG3961 18 GIKSIFGVPGDYNLSLLDKiYSVPGLRWVGNANELNAAYAADGYARLNG-ISALVTTFGVGELSALNGIAGSYAEHVPVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 155 LLGGAASTLLQKRGAL--------QAIDQMSLFRPLCkfCASV------RRVRDIVPTLRTAIAAAQsgtpgPVFVELPL 220
Cdd:COG3961 97 HIVGVPTTSAQASGLLlhhtlgdgDFKVFHRMSKEIT--CAQAmltdinTAPREIDRVIRTALKQRR-----PVYIGLPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 221 DVLYpyfmvekemiptklpnslmgrvvvwylQNClanlfvgawePRPEGPLPLDIPQASPQQ----VQRCVEILSRAKRP 296
Cdd:COG3961 170 DVAD---------------------------LPI----------EAPLTPLDLQLKTSDPEAlsevIDTIAELINKAKKP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 297 LLVLGsqallPPTPANKLRAAVETL----GVPCFLGGMSRGLLGRNHPLHIRQ-NRSAALKKADVVVlagAVCDFRLSYG 371
Cdd:COG3961 213 VILAD-----ALVSRFGLEKELKKLinatGFPVATLPMGKGVIDESHPNYLGVyNGKLSEPEVREAV---ESADLILTIG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 372 RVLNRKSSIIIVNR-NRDDLLlnsdifwkpqeavqgDVGSFMIKLVEGLQGQMWSSDWAEELRKAdqqkeQTYRDKALMP 450
Cdd:COG3961 285 VLLTDFNTGGFTYQyKPANII---------------EIHPDSVKIKDAVFTNLSMKDALQELAKK-----IDKRNLSAPP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 451 VLQH--------------LNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGA 516
Cdd:COG3961 345 VAYPartpptpyppanepLTQEWLWNTVQNFLKPGDVIIAETGTSFFGALDIRLPKG-ATFISQPLWGSIGYTLPAALGA 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1318663320 517 KLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTqISRE 567
Cdd:COG3961 424 ALAAPDRRVILFIGDGSLQLTVQEISTMIRWGLKPIIFVLNNDGYT-IERA 473
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
455-557 |
4.15e-13 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 67.91 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 455 LNPVWVLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 531
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQhqmWAAQYYRFKKPR---SWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
|
90 100
....*....|....*....|....*.
gi 1318663320 532 GAFGYSLIEFDTFVRHKVPVIALVGN 557
Cdd:cd02015 78 GSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
72-219 |
2.93e-12 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 64.82 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 72 LRAHGVRFVFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAVARLTGtVGVAAVTAGPGLTNTVTAVKNAQVAQ 150
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLdAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 151 SPVLLLGGAASTLLQKRGA-----LQAID---QMSLFRPLCkfCASVRRVRDIVPT------LRTAIAAAQsgtpgPVFV 216
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGLllhhtLGDGDfdvFLKMFEEIT--CAAARLTDPENAAeeidrvLRTALRESR-----PVYI 158
|
...
gi 1318663320 217 ELP 219
Cdd:cd07038 159 EIP 161
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
459-634 |
1.09e-11 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 63.71 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 459 WVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 538
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 539 IEFDTFVRHKVPVIALVGNDAGWT---QISREQVPrlgsdvacslaYTD-----YHKAAMGLGAQGLILSRD--NKDQVV 608
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFRvkTEGELD 153
|
170 180
....*....|....*....|....*.
gi 1318663320 609 KVLREGQQLCqdGHAVVVNILIGRTD 634
Cdd:cd02005 154 EALKDALFNR--DKLSLIEVILPKDD 177
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
64-595 |
2.66e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 66.43 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVL-LLGGAASTLLQKRGALQAiDQMSLFRPLCKFcasVRRVRD---IVPTLRTAIAAAQSGTPGPVFVEL 218
Cdd:PRK12474 87 LHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASagaVDSDVARAVQAAQSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 219 PLDVlypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEPRPEGPLPL-DIPQA--SPQQVQRCVEILSRAKR 295
Cdd:PRK12474 163 PADV---------------------------------------AWNEAAYAAQPLrGIGPApvAAETVERIAALLRNGKK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 296 PLLVLGSQALL--PPTPANKLRAAVetlGVPCFLGGMS-RGLLGRNH-PL----HIRQNRSAALKKADVVVLAGAvcDFR 367
Cdd:PRK12474 204 SALLLRGSALRgaPLEAAGRIQAKT---GVRLYCDTFApRIERGAGRvPIeripYFHEQITAFLKDVEQLVLVGA--KPP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 368 LSYGRVLNRKSSIIIVNRNRDDLLlnsdifwKPQEavqgdvgsfmiKLVEGLQgqmwssDWAEELrkaDQQKEQTYRDKA 447
Cdd:PRK12474 279 VSFFAYPGKPSWGAPPGCEIVYLA-------QPDE-----------DLAQALQ------DLADAV---DAPAEPAARTPL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 448 LMPVLQH--LNPVWVLQQVEETLPDNAlLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEV 525
Cdd:PRK12474 332 ALPALPKgaLNSLGVAQLIAHRTPDQA-IYADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKV 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1318663320 526 WCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREqVPRLGSDVACSLAYT---------DYHKAAMGLGAQ 595
Cdd:PRK12474 411 VCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGE-LQRVGAQGAGRNALSmldlhnpelNWMKIAEGLGVE 488
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
64-362 |
9.25e-11 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 64.48 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 64 GGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTA 142
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 143 VKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDV 222
Cdd:PRK07586 83 LHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 lypyfmvekemiptklpnslmgrvvvwylqnclanlfvgAWEP--RPEGPLPL-DIPQASPQQVQRCVEILSRAKRPLLV 299
Cdd:PRK07586 163 ---------------------------------------AWSEggPPAPPPPApAPAAVDPAAVEAAAAALRSGEPTVLL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 300 LGSQALLPPTPANKLRAAVET---LGVPCFLGGMSRGlLGRNH----PLHIRQNRsAALKKADVVVLAGA 362
Cdd:PRK07586 204 LGGRALRERGLAAAARIAAATgarLLAETFPARMERG-AGRPAverlPYFAEQAL-AQLAGVRHLVLVGA 271
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
68-559 |
5.24e-10 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 62.31 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 68 VAAVLRAHGVRFVFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNA 146
Cdd:PRK09124 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 147 QVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAqSGTPGPVFVELPLDVLYpy 226
Cdd:PRK09124 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDVAL-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 227 fmvekEMIPTKLPnslmgrvVVWYlqnclanlfvgaweprpEGPLPLDIPQASpqQVQRCVEILSRAKRPLLVLGS---Q 303
Cdd:PRK09124 166 -----KPAPERAT-------PHWY-----------------HAPQPVVTPAEE--ELRKLAALLNGSSNITLLCGSgcaG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 304 AllpptpANKLRAAVETLGVPC---------------FLGGMSrGLLGRNHPLHirqnrsaALKKADVVVLAGavCDFrl 368
Cdd:PRK09124 215 A------HDELVALAETLKAPIvhalrgkehveydnpYDVGMT-GLIGFSSGYH-------AMMNCDTLLMLG--TDF-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 369 SYGRVLNRKSSIIIVNRNRDDLLLNSDIfwkpQEAVQGDVGSFMIKLVEGLQgqmwssdwaeelRKADqqkeQTYRDKAL 448
Cdd:PRK09124 277 PYRQFYPTDAKIIQIDINPGSLGRRSPV----DLGLVGDVKATLAALLPLLE------------EKTD----RKFLDKAL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 449 M----------------PVLQHLNPVWVLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGF 512
Cdd:PRK09124 337 EhyrkarkglddlavpsDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQ 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1318663320 513 ALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA 559
Cdd:PRK09124 417 ALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
|
|
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
72-560 |
6.61e-07 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism];
Pssm-ID: 224087 [Multi-domain] Cd Length: 566 Bit Score: 52.33 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 72 LRAHGVRFVFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQ 150
Cdd:COG1165 18 LARLGVRDVVICPGSRSTPLALAAAAHdAITVHVHIDERSAGFFALGLAKASKRPVAVICTSGTAVANLYPAVIEANLSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 151 SPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLR----TAIAAAQSGT---PGPVFVELPLDV- 222
Cdd:COG1165 98 VPLIVLTADRPPELRGCGANQAIDQTGLFGSYVRASIDLPLPEDDIEALWylrtIASAAAQQARtphAGPVHINVPFREp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 223 LYPyfmvekEMIPTKLPNSLMgrvvvwylqnclanlfvgawepRPEGPLPLDIPQASPQQVQRCVEI--LSRAKRPLLVL 300
Cdd:COG1165 178 LVP------DLEPEGAGTPWG----------------------RPLGHWWFYTGPWTVDQGPDLLSEwfFWRQKRGVIVA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 301 GSqalLPPTPANKLRAAVETLGVPCFLGGMSrGLlgRNHPLH----IRQNRSAALKKADVVVLAGAvcdfRLSYGRVLNR 376
Cdd:COG1165 230 GR---MSAQEGKGILALANTLGWPILADPLS-PL--RNYIPCydlwLANPKAAEKLRPDIVIQFGS----PPTSKRLLQW 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 377 KSS-----IIIVNRNRDdlllNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQmwsSDWAEELRKADQQKEQTYRDKALMPV 451
Cdd:COG1165 300 LADtepieYWVVDPGGG----WLDPSHHATTRLSADVATWARSIHPAGRIR---KPWLDEWLALNEKARQAVRDQLAAEA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 452 LQHLNPVWVLQqveETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDP-GAFGTLGVGAGfALGAKLCQpEAEVWCLFG 530
Cdd:COG1165 373 LTEAHLAAALA---DLLPPQDQLFVGNSMPVRDVDALGQLPAGYRVYSNrGASGIDGTVST-ALGIARAT-QKPTVALIG 447
|
490 500 510
....*....|....*....|....*....|.
gi 1318663320 531 DGAFGYSLIEFDTFVRHKVP-VIALVGNDAG 560
Cdd:COG1165 448 DLSFLHDLNGLLLLKKVPQPlTIVVVNNNGG 478
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|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
485-632 |
1.05e-05 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 46.89 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 485 AAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAgWTQI 564
Cdd:cd02006 38 GAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 565 SREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQGLILSRDNkdQVVKVLREGQQLCQDGHA-VVVNILIG 631
Cdd:cd02006 117 IRQAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPE--ELAAAFEQAKKLMAEHRVpVVVEAILE 194
|
.
gi 1318663320 632 R 632
Cdd:cd02006 195 R 195
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
72-220 |
1.67e-05 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 45.57 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663320 72 LRAHGVRFVFTLVGGHISPLLVACEKLG-IRV---VDTRhevTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQ 147
Cdd:cd07037 7 LKRLGVRDVVISPGSRSAPLALAAAEHPeFRLhvrVDER---SAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1318663320 148 VAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVR------RVRDIVPTLRTAIAAAQSGTPGPVFVELPL 220
Cdd:cd07037 84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
|