|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
52-624 |
4.36e-132 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 398.38 E-value: 4.36e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 52 RHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTV 130
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 131 TAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 211 DvlypyfmVQKEMVPAKPPKGLVGRVvswylenylanlfagawepQPEgplpldiPQASPQQVQRCVEILSRAKRPLMVL 290
Cdd:COG0028 163 D-------VQAAEAEEEPAPPELRGY-------------------RPR-------PAPDPEAIEEAAELLAAAKRPVILA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 291 GSQALLtPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGTVCDFRLSYG-R 362
Cdd:COG0028 210 GGGARR-AGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALAEADLVLAVGARFDDRVTGNwD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 363 VLSHSSKIIIVNRNREEMLLNsdifWKPQEAVQGDVGSFVLKLVEGLQGQTWA-PDWVEELREADRQKEQTFREKAAmpv 441
Cdd:COG0028 289 EFAPDAKIIHIDIDPAEIGKN----YPVDLPIVGDAKAVLAALLEALEPRADDrAAWLARIAAWRAEYLAAYAADDG--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 442 aqHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGD 521
Cdd:COG0028 362 --PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 522 GAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKV 600
Cdd:COG0028 440 GGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKLAEAFGAKGERV--ETPEELEAA 517
|
570 580
....*....|....*....|....
gi 21361361 601 LHDAQQQcrdGHPVVVNILIGRTD 624
Cdd:COG0028 518 LEEALAS---DGPALIDVRVDPEE 538
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
53-619 |
1.00e-115 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 356.34 E-value: 1.00e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 53 HGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK05858 6 HAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 LYPyfMVQKEMVPAKPPkglvgrvvswylenylanlfagawePQPEGPLPldipqaSPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:PRK05858 166 AFS--MADDDGRPGALT-------------------------ELPAGPTP------DPDALARAAGLLAEAQRPVIMAGT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 QALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSYGRVLSHSSKIII 372
Cdd:PRK05858 213 DVWWG-HAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFGVFGGTAQLVHV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 373 VnrnREEMLLNSDIfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREAD---RQKEQTFREKAAMPvaqhLNPVQ 449
Cdd:PRK05858 292 D---DAPPQRAHHR--PVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAEtaaRARDAAELADDRDP----IHPMR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 450 VLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLI 529
Cdd:PRK05858 363 VYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 530 EFDTFVRHKIPVMALVGNDAGWtqiSREQVPS---LGSNVACGLA-YTDYHKAAMGLGARGLLLSRENEdqvvkvLHDAQ 605
Cdd:PRK05858 443 DVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRALGGHGELVTVPAE------LGPAL 513
|
570
....*....|....*
gi 21361361 606 QQCRD-GHPVVVNIL 619
Cdd:PRK05858 514 ERAFAsGVPYLVNVL 528
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
447-620 |
8.71e-69 |
|
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: 221.25 E-value: 8.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 447 PVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 526
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 527 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPS--LGSNVACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDA 604
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSygLGLPVTTLLPDTRYDLVAEAFGGKGELV--TTPEELKPALKRA 158
|
170
....*....|....*.
gi 21361361 605 QQQcrdGHPVVVNILI 620
Cdd:cd02004 159 LAS---GKPALINVII 171
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
58-568 |
1.05e-59 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 209.46 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 58 VAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQ 137
Cdd:PRK09259 16 VIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTALANAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 138 MAQSPILLLGGAASTL---LQnRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLy 214
Cdd:PRK09259 96 TNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 215 pyfmvQKEMVPAKPPKGLVgRVVSwylenylanlfagawepqpegPLPLDIPqaSPQQVQRCVEILSRAKRPLMVLGSQA 294
Cdd:PRK09259 174 -----AQTMDADEALTSLV-KVVD---------------------PAPAQLP--APEAVDRALDLLKKAKRPLIILGKGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 295 LLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSYGR--VLSHSSKIII 372
Cdd:PRK09259 225 AYAQADEQ-IREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgkTWGADKKFIQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 373 VNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQTWAP--DWVEELREADRQKEQTFREK--AAMPVAQHLNPV 448
Cdd:PRK09259 304 IDIEPQEIDSNRPI----AAPVVGDIGSVMQALLAGLKQNTFKApaEWLDALAERKEKNAAKMAEKlsTDTQPMNFYNAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 449 QVLQLVEETLPDnSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC--RPdaeVWCLFGDGAFGY 526
Cdd:PRK09259 380 GAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGDSAFGF 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21361361 527 SLIEFDTFVRHKIPVMALVGNDAGwtqISR--EQVPSLGSNVAC 568
Cdd:PRK09259 456 SGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSP 496
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
54-620 |
8.58e-59 |
|
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: 206.50 E-value: 8.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 LYPYFMvqkemvpakppkglvgrvvswylENYLANLFAGAWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:TIGR00118 163 TTAEIE-----------------------YPYPEKVNLPGYRPTVKG---------HPLQIKKAAELINLAKKPVILVGG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 QALLTPTSAdKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGTVCDFRLSyGRV-- 363
Cdd:TIGR00118 211 GVIIAGASE-ELKELAERIQIPVTTTLMGLGSFPEDHPLslgmlgmHGTKTANLAVHECDLIIAVGARFDDRVT-GNLak 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 364 LSHSSKIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKLVEGL--QGQTWAPDWVEELREadrqkeqtFREKAAMPV 441
Cdd:TIGR00118 289 FAPNAKIIHIDIDPAEIGKNV----RVDIPIVGDARNVLEELLKKLfeLKERKESAWLEQINK--------WKKEYPLKM 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 442 AQH---LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCL 518
Cdd:TIGR00118 357 DYTeegIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 519 FGDGAFGYSLIEFDTFVRHKIPVMALVGNDA------GWTQISREQVPSlGSNVACGlayTDYHKAAMGLGARGLLLSRE 592
Cdd:TIGR00118 437 TGDGSFQMNLQELSTAVQYDIPVKILILNNRylgmvrQWQELFYEERYS-HTHMGSL---PDFVKLAEAYGIKGIRIEKP 512
|
570 580
....*....|....*....|....*....
gi 21361361 593 NEdqvvkvLHDA-QQQCRDGHPVVVNILI 620
Cdd:TIGR00118 513 EE------LDEKlKEALSSNEPVLLDVVV 535
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
58-210 |
2.28e-56 |
|
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: 187.74 E-value: 2.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 58 VAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQ 137
Cdd:cd07035 3 LVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLANAY 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361361 138 MAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:cd07035 83 LDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
56-622 |
9.01e-56 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 199.07 E-value: 9.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 56 ENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:PRK07525 10 EAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 136 AQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTpGPVFVELPVDvlYP 215
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 216 YFMVQKEMvpakppkglvgrvvswylenylanlfagawePQPegpLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQAL 295
Cdd:PRK07525 167 YGVIDVEI-------------------------------PQP---VRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 296 LTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLH---IRENRSAA----LKKADVIVLAGTvcdfRLSYGRVLSH-- 366
Cdd:PRK07525 213 LS-DAIEECKALAERLDAPVACGYLHNDAFPGSHPLWvgpLGYNGSKAamelIAKADVVLALGT----RLNPFGTLPQyg 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 367 ------SSKIIIVNRNREEMLLNsdifwKPQE-AVQGDVGSFVLKLVEGLQGQTWAP---------------DWVEELRE 424
Cdd:PRK07525 288 idywpkDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVARELLARLAERLAGDagreerkaliaaeksAWEQELSS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 425 ADRQKEQ---TFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAG 501
Cdd:PRK07525 363 WDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 502 FALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSN-VACGL-AYTDYHKAA 579
Cdd:PRK07525 443 AIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNVSYAGIA 522
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 21361361 580 MGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 622
Cdd:PRK07525 523 EAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
55-584 |
9.56e-56 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 197.89 E-value: 9.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 55 GENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVK 134
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 135 NAQMAQSPILLLGG--AASTLLQNRGALQAV-DQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVD 211
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 212 VlypyfMVQKEMVPAKPPKGLVGRvvswylenylanlfagawepqpegplpldiPQASPQQVQRCVEILSRAKRPLMVLG 291
Cdd:PRK07524 165 V-----LAAPADHLLPAPPTRPAR------------------------------PGPAPAALAQAAERLAAARRPLILAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 292 SQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRS-----AALKKADVIVLAGTV---CDFRLSY-GR 362
Cdd:PRK07524 210 GGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrALIAEADVVLAVGTElgeTDYDVYFdGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 363 VLSHSSKIII------VNRNREemllnsdifwkPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEqtfREK 436
Cdd:PRK07524 287 FPLPGELIRIdidpdqLARNYP-----------PALALVGDARAALEALLARLPGQAAAADWGAARVAALRQAL---RAE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 437 AAMPVAQHlnpVQVLQLVEETLPDNsILVVDGGDFVGTAAHLVQPRGPLRWLD-PGAFGTLGVGAGFALGAKLCRPDAEV 515
Cdd:PRK07524 353 WDPLTAAQ---VALLDTILAALPDA-IFVGDSTQPVYAGNLYFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPERPV 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361361 516 WCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGA 584
Cdd:PRK07524 429 VCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGC 497
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
54-620 |
1.53e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 198.44 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 134 KNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVL 213
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 214 YPYFMVQKEMVPAKPPkglvgrvvswyLENYLANLFagawepqpegplpldipqASPQQVQRCVEILSRAKRPLMVLGSQ 293
Cdd:PRK06276 163 EGELDLEKYPIPAKID-----------LPGYKPTTF------------------GHPLQIKKAAELIAEAERPVILAGGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 294 ALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGtvCDF--RLSyGRVL 364
Cdd:PRK06276 214 VIISGASEE-LIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSVTESDVLIAIG--CRFsdRTT-GDIS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 SHS--SKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQTWAPD--WVEELREadrqkeqtfREKAAMP 440
Cdd:PRK06276 290 SFApnAKIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNKseWLERVKK---------LKKESIP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 441 VA----QHLNPVQVLQLVEETLPD-----NSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRP 511
Cdd:PRK06276 357 RMdfddKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 512 DAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV------GNDAGWTQI---SREQVPSLGSNvacglayTDYHKAAMGL 582
Cdd:PRK06276 437 DANVIAITGDGGFLMNSQELATIAEYDIPVVICIfdnrtlGMVYQWQNLyygKRQSEVHLGET-------PDFVKLAESY 509
|
570 580 590
....*....|....*....|....*....|....*...
gi 21361361 583 GARGLLLsrENEDQVVKVLHDAqqqCRDGHPVVVNILI 620
Cdd:PRK06276 510 GVKADRV--EKPDEIKEALKEA---IKSGEPYLLDIII 542
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
54-627 |
2.76e-55 |
|
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: 196.51 E-value: 2.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAV 133
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 134 KNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVL 213
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 214 YPyfMVQKEMVPAKP-PKglvgrvvswylenylanlfAGAwepqpegplpldipqASPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:TIGR02418 161 DS--PVSVKAIPASYaPK-------------------LGA---------------APDDAIDEVAEAIQNAKLPVLLLGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 QAlLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHplhirENRsaalkkadvivLAGTVCDFRLSYGRVLSHSSKIII 372
Cdd:TIGR02418 205 RA-SSPETTEAVRRLLKKTQLPVVETFQGAGAVSREL-----EDH-----------FFGRVGLFRNQPGDRLLKQADLVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 373 V-------------NRNREEMLLNSDI-------FWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQT 432
Cdd:TIGR02418 268 TigydpieyeprnwNSENDATIVHIDVepaqidnNYQPDLELVGDIASTLDLLAERIPGYELPPDALAILEDLKQQREAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 433 FREKAAmPVAQHLNPVQVLQLVEETLPDNSILVVDGGDF-VGTAAHLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLCRP 511
Cdd:TIGR02418 348 DRVPAT-LKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHyIWMARYFRSYR-ARHLLISNGMQTLGVALPWAIGAALVRP 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 512 DAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLsr 591
Cdd:TIGR02418 426 NTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSSGVDFGPIDFVKYAESFGAKGLRV-- 503
|
570 580 590
....*....|....*....|....*....|....*.
gi 21361361 592 ENEDQVVKVLHDAQQQcrDGhPVVVNILIgrtDFRD 627
Cdd:TIGR02418 504 ESPDQLEPTLRQAMEV--EG-PVVVDIPV---DYSD 533
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
54-213 |
1.79e-53 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 180.51 E-value: 1.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQA-VDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVD 211
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 21361361 212 VL 213
Cdd:pfam02776 161 VL 162
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
54-587 |
1.29e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 187.10 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 134 KNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDvl 213
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 214 ypyfmVQKEmvpakppkglvgRVVSWYLEnylaNLFAGAWEPQpegplpldiPQASPQQVQRCVEILSRAKRPLMVLGSq 293
Cdd:PRK06725 175 -----VQNE------------KVTSFYNE----VVEIPGYKPE---------PRPDSMKLREVAKAISKAKRPLLYIGG- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 294 ALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGTVCDFRLSyGRV--L 364
Cdd:PRK06725 224 GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAVTECDLLLALGVRFDDRVT-GKLelF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 SHSSKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSfVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMpvaqh 444
Cdd:PRK06725 303 SPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKK-ALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESE----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 524
Cdd:PRK06725 373 LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASF 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361361 525 GYSLIEFDTFVRHKIPVMALVGNDA------GWTQI---SREQVPSLGSnvacglayTDYHKAAMGLGARGL 587
Cdd:PRK06725 453 QMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS--------PDFVKVAEAYGVKGL 516
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
62-586 |
9.59e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 184.26 E-value: 9.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQS 141
Cdd:PRK08322 11 LENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 142 PILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVrDIVPTL-RAAMAAAQSGTPGPVFVELPVDVlypyfmvq 220
Cdd:PRK08322 91 PMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP-DNIPEVvREAFRLAEEERPGAVHLELPEDI-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 221 kemvpakppkglvgrvvswylenylanlfagAWEPQPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLMVLGSQAlLT 297
Cdd:PRK08322 162 -------------------------------AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGA-NR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 298 PTSADKLRAAVETLGVPCFLGGMARGLLGRNHP-------LHIRENRSAALKKADVIVLAG-TVCDFrlSYGRVLSHSSK 369
Cdd:PRK08322 210 KTASKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLSQGDYVHCAIEHADLIINVGhDVIEK--PPFFMNPNGDK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 370 III-VNRNREEMllnsDIFWKPQEAVQGDVGSFVLKLVEGL-QGQTWAPDWVEELREADRQKEQTFREKAAMPVAqhlnP 447
Cdd:PRK08322 288 KVIhINFLPAEV----DPVYFPQVEVVGDIANSLWQLKERLaDQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK----P 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 448 VQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYS 527
Cdd:PRK08322 360 QRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMN 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361361 528 LIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNvaCGLAYT--DYHKAAMGLGARG 586
Cdd:PRK08322 440 SQELETAVRLGLPLVVLILNDNAYGMIRWKQENMGFED--FGLDFGnpDFVKYAESYGAKG 498
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
54-622 |
9.70e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 184.59 E-value: 9.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 134 KNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVl 213
Cdd:PRK06048 90 ATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDV- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 214 ypyfmVQKEMVPAKPPKglvgrvVSwyLENYlanlfagawEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVLGSQ 293
Cdd:PRK06048 169 -----TTAEIDFDYPDK------VE--LRGY---------KPTYKG---------NPQQIKRAAELIMKAERPIIYAGGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 294 ALLTPTSADKLRAAvETLGVPCFLGGMARGLLGRNHPLHI-------RENRSAALKKADVIVLAGTVCDFRLSyGRVLSH 366
Cdd:PRK06048 218 VISSNASEELVELA-ETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARFDDRVT-GKLASF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 367 S--SKIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKLVEGLQGQTWAPdWVEELREADRQKEQTFREKAAMpvaqh 444
Cdd:PRK06048 296 ApnAKIIHIDIDPAEISKNV----KVDVPIVGDAKQVLKSLIKYVQYCDRKE-WLDKINQWKKEYPLKYKEREDV----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 524
Cdd:PRK06048 366 IKPQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 525 GYSLIEFDTFVRHKIPVMALVGNDA------GWTQISREQVPSlgsnVACGLAYTDYHKAAMGLGARGLLLSRENEdqvv 598
Cdd:PRK06048 445 QMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDKRYS----HTCIKGSVDFVKLAEAYGALGLRVEKPSE---- 516
|
570 580
....*....|....*....|....*
gi 21361361 599 kvLHDAQQQCRD-GHPVVVNILIGR 622
Cdd:PRK06048 517 --VRPAIEEAVAsDRPVVIDFIVEC 539
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
54-548 |
4.14e-50 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 182.99 E-value: 4.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHIspLLVACE---KLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTV 130
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAI--LNIYDEiykQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 131 TAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 211 DV-------LYPyfmVQKEMVPAKPpkglvgrvvswyleNYLANlfagawepqpegplpldipqasPQQVQRCVEILSRA 283
Cdd:PRK08527 163 DVtatlgefEYP---KEISLKTYKP--------------TYKGN----------------------SRQIKKAAEAIKEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 284 KRPLMVLGSQALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGTVCDF 356
Cdd:PRK08527 204 KKPLFYLGGGAILS-NASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 357 RLSyGRV--LSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQG---QTWAPdWVEELREADRQK 429
Cdd:PRK08527 283 RVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELKEenpTTYKE-WREILKRYNELH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 430 EQTFREKAAMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 509
Cdd:PRK08527 355 PLSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLA 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 21361361 510 RPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 548
Cdd:PRK08527 430 VPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
54-586 |
6.77e-50 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 181.75 E-value: 6.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVT 131
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 132 AVKNAQMAQSPILLLGG--AASTLLQNRGALQAV-DQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVEL 208
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 209 PVDVLypyfmvqkemvpakppkGLVGRVvswylenylanlfagawEPQPEGPlPLDIPQASPQQVQRCVEILSRAKRPLM 288
Cdd:PRK08266 166 PWDVF-----------------GQRAPV-----------------AAAPPLR-PAPPPAPDPDAIAAAAALIAAAKNPMI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 289 VLGSQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIreNRSAA---LKKADVIVLAGTVCDFRLSYGRVLS 365
Cdd:PRK08266 211 FVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLGL--NFAAAyelWPQTDVVIGIGSRLELPTFRWPWRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 366 HSSKIIIVNRNREEMllnsdIFWKPQEAVQGDVGSFVLKLVEGLQGQ-TWAPDWVEELREAdrqkeqtfreKAAmpVAQH 444
Cdd:PRK08266 286 DGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAgSKRPSRRAELREL----------KAA--ARQR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQ----VLQLVEETLPDNSIlVVDGGDFVGTAAHLVQP-RGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLF 519
Cdd:PRK08266 349 IQAVQpqasYLRAIREALPDDGI-FVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSIT 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361361 520 GDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSL-GSNVACGLAYTDYHKAAMGLGARG 586
Cdd:PRK08266 428 GDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLAESFGVAA 495
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
44-622 |
4.35e-49 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 180.01 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 44 HKVDKASVRHGGENVAAVLRAHGVRFIFtlvGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSG--TVGVAAVT 121
Cdd:PRK06154 12 HLPAEAKTMKVAEAVAEILKEEGVELLF---GFPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 122 AGPGLTNTVTAVKNAQMAQSPILLLGGAAstllqNRGaLQAVD----QLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQ 197
Cdd:PRK06154 89 YGPGAENAFGGVAQAYGDSVPVLFLPTGY-----PRG-STDVApnfeSLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 198 SGTPGPVFVELPVDVLYpyfmvqkEMVPAKPpkglvgrvvswylENYlanlfagawepqpeGPLPLDIPQASPQQVQRCV 277
Cdd:PRK06154 163 NGRPGPVVLELPVDVLA-------EELDELP-------------LDH--------------RPSRRSRPGADPVEVVEAA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 278 EILSRAKRPLMVLGsQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAA-------LKKADVIVLA 350
Cdd:PRK06154 209 ALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARpatvahfLREADVLFGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 351 GtvCDF-RLSYGRVLSHSSKIIIVNRNREEmlLNSDIFWKpqEAVQGDVGSFVLKLVEGLQGQTW-----APDWVEELRE 424
Cdd:PRK06154 288 G--CSLtRSYYGLPMPEGKTIIHSTLDDAD--LNKDYPID--HGLVGDAALVLKQMIEELRRRVGpdrgrAQQVAAEIEA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 425 ADRQKEQTFREK---AAMPvaqhLNPVQVLQLVEETL-PDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGA 500
Cdd:PRK06154 362 VRAAWLAKWMPKltsDSTP----INPYRVVWELQHAVdIKTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 501 GFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND---AGWTQISREQVPSLGSNVACGlaytDYHK 577
Cdd:PRK06154 438 GLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNfsmGGYDKVMPVSTTKYRATDISG----DYAA 513
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 21361361 578 AAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 622
Cdd:PRK06154 514 IARALGGYGERV--EDPEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
54-551 |
3.73e-47 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 174.41 E-value: 3.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGkIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAAST--LLQNRGAL-QAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELP 209
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 210 VDVLYpyfmvqkemvpakppkglvgRVVSWylenylanlfagawePQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMV 289
Cdd:PRK07064 165 IDIQA--------------------AEIEL---------------PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 290 LGSQALltpTSADKLRAAVEtLGVPCFLGGMARGLLGRNHPLHIRE-NRSAA----LKKADVIVLAGTvcdfRLSYGRVL 364
Cdd:PRK07064 210 LGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAvealYKTCDLLLVVGS----RLRGNETL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 SHSSKI------IIVNRNREEMLLNSDIFwkpqeaVQGDVGSFVLKLVEGLQGQTWA-PDWVEELREADRQKEQTFReka 437
Cdd:PRK07064 282 KYSLALprplirVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLSVdPAFAADLRAAREAAVADLR--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 438 ampvaQHLNPVQVL-QLVEETLPDNSILVVDGGDFVGTAAH-LVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCRPDAEV 515
Cdd:PRK07064 353 -----KGLGPYAKLvDALRAALPRDGNWVRDVTISNSTWGNrLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKT 426
|
490 500 510
....*....|....*....|....*....|....*.
gi 21361361 516 WCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGW 551
Cdd:PRK07064 427 VGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
52-627 |
8.35e-47 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 173.50 E-value: 8.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 52 RHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVT 131
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 132 AVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVD 211
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 212 VLypyfmvqKEMVPAKPPKGLvgrvvswylenylanlfagawEPQPEGPlpldipqASPQQVQRCVEILSRAKRPLMVLG 291
Cdd:PRK08617 165 VV-------DAPVTSKAIAPL---------------------SKPKLGP-------ASPEDINYLAELIKNAKLPVLLLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 292 SQAlLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHplhirENRSAA-------------LKKADVIVLAGtvcdfrl 358
Cdd:PRK08617 210 MRA-SSPEVTAAIRRLLERTNLPVVETFQAAGVISREL-----EDHFFGrvglfrnqpgdelLKKADLVITIG------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 359 sYGRV--------LSHSSKIIIVNRNREEMllnsDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELreADRQKE 430
Cdd:PRK08617 277 -YDPIeyeprnwnSEGDATIIHIDVLPAEI----DNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLEIL--EELRAQ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 431 QTFREKAAMPVAQHL-NPVQVLQLVEETLPDNSILVVDGGDF-VGTAAHL--VQPRGPLrwldpgaFG----TLGVGAGF 502
Cdd:PRK08617 350 LEELAERPARLEEGAvHPLRIIRALQDIVTDDTTVTVDVGSHyIWMARYFrsYEPRHLL-------FSngmqTLGVALPW 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 503 ALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGL 582
Cdd:PRK08617 423 AIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAESF 502
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 21361361 583 GARGllLSRENEDQVVKVLHDAQQQcrDGhPVVVNILIgrtDFRD 627
Cdd:PRK08617 503 GAKG--LRVTSPDELEPVLREALAT--DG-PVVIDIPV---DYSD 539
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
54-541 |
2.48e-45 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 169.98 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTV 130
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGavlYIYDELYKQDK--IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 131 TAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 211 DvlypyfmVQKEMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVL 290
Cdd:PRK06965 181 D-------VSKTPCEYEYPKSVEMR----------------SYNPVTKG---------HSGQIRKAVSLLLSAKRPYIYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 291 GSQALLTPTSADkLRAAVETLGVPCF-----LGGMAR------GLLGrnhpLHIRENRSAALKKADVIVLAGTVCDFRL- 358
Cdd:PRK06965 229 GGGVILANASRE-LRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFDDRVi 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 359 -SYGRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTWAPD------W---VEELREAD 426
Cdd:PRK06965 304 gNPAHFASRPRKIIHIDIDPSSIskRVKVDI------PIVGDVKEVLKELIEQLQTAEHGPDadalaqWwkqIEGWRSRD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 427 RQKEQTFREKaampvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGA 506
Cdd:PRK06965 378 CLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGI 449
|
490 500 510
....*....|....*....|....*....|....*
gi 21361361 507 KLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 541
Cdd:PRK06965 450 KMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPV 484
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
54-604 |
3.14e-45 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 169.56 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFtlvGGHI-SPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK06112 16 VAHAIARALKRHGVEQIF---GQSLpSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFcvsVRRVRD---IVPTLRAAMAAAQSGTPGPVFVELP 209
Cdd:PRK06112 93 LAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 210 VDVLypyfmvqkeMVPAKPPkglvgrvvswylenylanlfaGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMV 289
Cdd:PRK06112 170 ADLL---------TAAAAAP---------------------AAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 290 LGSQALLTpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL----------------HIREnrsaALKKADVIVLAGTv 353
Cdd:PRK06112 220 AGGGVHIS-GASAALAALQSLAGLPVATTNMGKGAVDETHPLslgvvgslmgprspgrHLRD----LVREADVVLLVGT- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 354 cdfRLSYG-----RVLSHSSKIII-------VNRNREEMLLNSDifwkPQEAVQGdvgsfvLKLVEGLQGQTWAPDWVEE 421
Cdd:PRK06112 294 ---RTNQNgtdswSLYPEQAQYIHidvdgeeVGRNYEALRLVGD----ARLTLAA------LTDALRGRDLAARAGRRAA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 422 LREADRQKEQTFREKAAMPV---AQHLNPVQVLQLVEETLPDNSILVVDGG-DFVGTAAHLVQPRGPLRWLDPGAFGTLG 497
Cdd:PRK06112 361 LEPAIAAGREAHREDSAPVAlsdASPIRPERIMAELQAVLTGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLAGLG 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 498 VGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA--GWtQISREQVPSLGSNVACGLAYTDY 575
Cdd:PRK06112 441 WGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF-QKHAETVKFGTHTDACHFAAVDH 519
|
570 580
....*....|....*....|....*....
gi 21361361 576 HKAAMGLGARGllLSRENEDQVVKVLHDA 604
Cdd:PRK06112 520 AAIARACGCDG--VRVEDPAELAQALAAA 546
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
62-622 |
3.66e-45 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 169.85 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQ 137
Cdd:PRK07418 29 LKRHGVKHIFGYPGGAILPIydeLYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNLVTGIATAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 138 MAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYF 217
Cdd:PRK07418 109 MDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPKDVGQEEF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 218 mvqkEMVPAKP----PKGlvgrvvswylenylanlfagaWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVLGSQ 293
Cdd:PRK07418 189 ----DYVPVEPgsvkPPG---------------------YRPTVKG---------NPRQINAALKLIEEAERPLLYVGGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 294 AlLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGTVCDFRLSyGRVLSH 366
Cdd:PRK07418 235 A-ISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAVTECDLLIAVGARFDDRVT-GKLDEF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 367 SS--KII---I----VNRNReemllnsdifwKPQEAVQGDVGSFVLKLVEGLQGQTWAP---DWVEELreadrqkeQTFR 434
Cdd:PRK07418 313 ASraKVIhidIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEPTTPPrtqAWLERI--------NRWK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 435 EKAAMPVAQH---LNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHLVQpRGPLRWLDPGAFGTLGVGAGFALGAKLCRP 511
Cdd:PRK07418 374 QDYPLVVPPYegeIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 512 DAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQISREQVPSL------GSNVACGLAytDYHKAAMGLGAR 585
Cdd:PRK07418 452 DEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQWQESFygerysASNMEPGMP--DFVKLAEAFGVK 528
|
570 580 590
....*....|....*....|....*....|....*....
gi 21361361 586 GLLLSRENEdqvvkvLHDAQQQC--RDGhPVVVNILIGR 622
Cdd:PRK07418 529 GMVISERDQ------LKDAIAEAlaHDG-PVLIDVHVRR 560
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
52-554 |
1.73e-44 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 166.97 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 52 RHGGENVAAVLRAHGVRFIFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTV 130
Cdd:PRK08199 8 RTGGQILVDALRANGVERVFCVPGESYLAVLDALhDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 131 TAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:PRK08199 88 IGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 211 DVLYpyfmvQKEMVPAKPPkglvGRVVswylenylanlfagawEPQPegplpldipqaSPQQVQRCVEILSRAKRPLMVL 290
Cdd:PRK08199 168 DVLS-----ETAEVPDAPP----YRRV----------------AAAP-----------GAADLARLAELLARAERPLVIL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 291 GSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRE-----NRS--AALKKADVIVLAGTvcdfRLsyGRV 363
Cdd:PRK08199 212 GG-SGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGDlglgiNPAlaARIREADLVLAVGT----RL--GEV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 364 LSHSSKIIIVNRNReEMLLNSDI-------FWKPQEAVQGDVGSFVLKL--VEGLQGQTWApDWVEELREADRQkeqtfr 434
Cdd:PRK08199 285 TTQGYTLLDIPVPR-QTLVHVHPdaeelgrVYRPDLAIVADPAAFAAALaaLEPPASPAWA-EWTAAAHADYLA------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 435 EKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCRPDAE 514
Cdd:PRK08199 357 WSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATWLHRFFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERT 435
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 21361361 515 VWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQI 554
Cdd:PRK08199 436 VVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
54-549 |
4.12e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 160.26 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 lypyfmvqkemvpakppkglvgrvvswylenYLANLFAGAWePQPEGPLPldIPQASPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:PRK08155 175 -------------------------------QTAVIELEAL-PAPAEKDA--APAFDEESIRDAAAMINAAKRPVLYLGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 qALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGTVCDFRlSYGRVLS 365
Cdd:PRK08155 221 -GVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYILQEADLLIVLGARFDDR-AIGKTEQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 366 H--SSKIIIVNRNREEMllnsDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWApDWVEelREADRQKEQTFrekaAMPVAQ 443
Cdd:PRK08155 299 FcpNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQPRA-EWHQ--LVADLQREFPC----PIPKAD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 444 H-LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDG 522
Cdd:PRK08155 368 DpLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDG 447
|
490 500
....*....|....*....|....*...
gi 21361361 523 AFGYSLIEFDTFVRHKIPV-MALVGNDA 549
Cdd:PRK08155 448 SLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
43-548 |
4.89e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 160.37 E-value: 4.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 43 LHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGTVGVAAVT 121
Cdd:PRK07282 1 MEKISLESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFeGIRHILARHEQGALHEAEGYAKSTGKLGVAVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 122 AGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTP 201
Cdd:PRK07282 81 SGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 202 GPVFVELPVDVlypyfmvqkemvpakppkglVGRVVSWYLEnylanlfagawepqPEGPLPLDIPQASPQ--QVQRCVEI 279
Cdd:PRK07282 161 GPVVIDLPKDV--------------------SALETDFIYD--------------PEVNLPSYQPTLEPNdmQIKKILKQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 280 LSRAKRPLMVLGSqALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKADVIVLAGT 352
Cdd:PRK07282 207 LSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANIAMTEADFMINIGS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 353 VCDFRL-SYGRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREaDRQK 429
Cdd:PRK07282 286 RFDDRLtGNPKTFAKNAKVAHIDIDPAEIgkIIKTDI------PVVGDAKKALQMLLAEPTVHNNTEKWIEKVTK-DKNR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 430 EQTFREKAAMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC 509
Cdd:PRK07282 359 VRSYDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIA 433
|
490 500 510
....*....|....*....|....*....|....*....
gi 21361361 510 RPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 548
Cdd:PRK07282 434 NPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNN 472
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
54-541 |
1.21e-41 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 158.89 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAV 133
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 134 KNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDvl 213
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 214 ypyfmVQKEMVPAKPPkglvgrvvswylenylanlfagawePQPegplPLDIPQASPQQVQRCVEILSRAKRPLMVLG-- 291
Cdd:PRK08978 161 -----IQLAEGELEPH-------------------------LTT----VENEPAFPAAELEQARALLAQAKKPVLYVGgg 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 292 ---SQALltptsaDKLRAAVETLGVP--CFLGGMarGLLGRNHP-----LHIRENRSA--ALKKADVIVLAGTVCDFRLS 359
Cdd:PRK08978 207 vgmAGAV------PALREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDRVT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 360 yGRVLSHSS--KIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTWApDWVEELREadrqkEQTFRE 435
Cdd:PRK08978 279 -GKLNTFAPhaKVIHLDIDPAEInkLRQAHV------ALQGDLNALLPALQQPLNIDAWR-QHCAQLRA-----EHAWRY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 436 KAAmpvAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEV 515
Cdd:PRK08978 346 DHP---GEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTV 422
|
490 500
....*....|....*....|....*.
gi 21361361 516 WCLFGDGAFGYSLIEFDTFVRHKIPV 541
Cdd:PRK08978 423 ICVSGDGSFMMNVQELGTIKRKQLPV 448
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
54-620 |
2.32e-41 |
|
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: 158.46 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLL--VACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVT 131
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMdaLSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 132 AVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTpGPVFVELPVD 211
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 212 vlYPYFMVQKEmvpakppkglvgrvvSWYlenylanlFAGAWEPQPEGPLPLDipqaspQQVQRCVEILSRAKRPLMVLG 291
Cdd:TIGR02720 160 --FGWQEIPDN---------------DYY--------ASSVSYQTPLLPAPDV------EAVTRAVQTLKAAERPVIYYG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 292 SQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLagtVCDFRLSYGRVLSHSskII 371
Cdd:TIGR02720 209 IGAR---KAGEELEALSEKLKIPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEALF---QADLVLFVGNNYPFA--EV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 372 IVNRNREEMLLNSDI----FWKPQE---AVQGDVGSF---VLKLVEGLQGQTW-------APDWveelreadRQKEQTFR 434
Cdd:TIGR02720 281 SKAFKNTKYFIQIDIdpakLGKRHHtdiAVLADAKKAlaaILAQVEPRESTPWwqanvanVKNW--------RAYLASLE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 435 EKAAMPvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAE 514
Cdd:TIGR02720 353 DKTEGP----LQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQ 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 515 VWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLSRenE 594
Cdd:TIGR02720 429 VFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVNK--I 506
|
570 580
....*....|....*....|....*.
gi 21361361 595 DQVVKVLHDAQQQcRDGHPVVVNILI 620
Cdd:TIGR02720 507 EQLPAVFEQAKAI-KQGKPVLIDAKI 531
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
54-548 |
3.96e-40 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 154.69 E-value: 3.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLgGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 LYPYFMVQKEMvpakpPKGLvgrvvswYLENYLANLfagawepqpegplpldipQASPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:PRK06882 166 VNPANKFTYEY-----PEEV-------SLRSYNPTV------------------QGHKGQIKKALKALLVAKKPVLFVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 qALLTPTSADKLRAAVETLGVPCF-----LGGMAR------GLLGrnhpLHIRENRSAALKKADVIVLAGTVCDFRLS-- 359
Cdd:PRK06882 216 -GVITAECSEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEANNAMHESDLILGIGVRFDDRTTnn 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 360 YGRVLSHsSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEG--LQGQTWAPDWVEELREADRQKEQTFREKA 437
Cdd:PRK06882 291 LAKYCPN-AKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEEnlAKSQTDLTAWWQQINEWKAKKCLEFDRTS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 438 AMpvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWC 517
Cdd:PRK06882 370 DV-----IKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVC 444
|
490 500 510
....*....|....*....|....*....|.
gi 21361361 518 LFGDGAFGYSLIEFDTFVRHKIPVMALVGND 548
Cdd:PRK06882 445 VTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
54-549 |
9.15e-40 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 153.75 E-value: 9.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGG---HISPLLVACEKlgIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTV 130
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGavlHIYDALFKQDK--VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 131 TAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 211 DVLYPyfmvqKEMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVL 290
Cdd:PRK06466 164 DMTNP-----AEKFEYEYPKKVKLR----------------SYSPAVRG---------HSGQIRKAVEMLLAAKRPVIYS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 291 GSQALLTPTSAdKLRAAVETLGVPCF-----LGGMAR------GLLGrnhpLHIRENRSAALKKADVIVLAGTVCDFRLS 359
Cdd:PRK06466 214 GGGVVLGNASA-LLTELAHLLNLPVTntlmgLGGFPGtdrqflGMLG----MHGTYEANMAMHHADVILAVGARFDDRVT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 360 YG-RVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTWAPD------WVEELREAdRQKE 430
Cdd:PRK06466 289 NGpAKFCPNAKIIHIDIDPASIskTIKADI------PIVGPVESVLTEMLAILKEIGEKPDkealaaWWKQIDEW-RGRH 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 431 QTFREKAAMPVAqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCR 510
Cdd:PRK06466 362 GLFPYDKGDGGI--IKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAF 439
|
490 500 510
....*....|....*....|....*....|....*....
gi 21361361 511 PDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 549
Cdd:PRK06466 440 PDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
54-541 |
3.53e-39 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 151.90 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 LYPYFmvqkeMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:PRK08979 166 LNPAI-----LHPYEYPESIKMR----------------SYNPTTSG---------HKGQIKRGLQALLAAKKPVLYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 QALLtpTSADK-LRAAVETLGVPCFLGGMARGLLGRNHP-------LHIRENRSAALKKADVIVLAGTVCDFRLSygrvl 364
Cdd:PRK08979 216 GAII--SGADKqILQLAEKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNADLIFGIGVRFDDRTT----- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 shsskiiivnRNREEMLLNSDIFW---KP---QEAVQGD---VGSF------VLKLVEGLQGQ-------TWAPDwVEEL 422
Cdd:PRK08979 289 ----------NNLEKYCPNATILHidiDPssiSKTVRVDipiVGSAdkvldsMLALLDESGETndeaaiaSWWNE-IEVW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 423 READRQKEQTFREKaampvaqhLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGF 502
Cdd:PRK08979 358 RSRNCLAYDKSSER--------IKPQQVIETLYKLTNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPA 429
|
490 500 510
....*....|....*....|....*....|....*....
gi 21361361 503 ALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 541
Cdd:PRK08979 430 AMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
54-586 |
4.74e-39 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 151.53 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVA----CEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNT 129
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 130 VTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELP 209
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 210 VDVLYPyfMVQKEMVPAKPpkglvgrvvswYLENYlanlfagawepqpeGPLPLDIpqaSPQQVQRCVEILSRAKRPLMV 289
Cdd:PRK06456 164 RDIFYE--KMEEIKWPEKP-----------LVKGY--------------RDFPTRI---DRLALKKAAEILINAERPIIL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 290 LGSQALLTPTSADKLRAAvETLGVPCFLGGMARGLLGRNHPLHI-------RENRSAALKKADVIVLAGTVCDFR--LSY 360
Cdd:PRK06456 214 VGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAALESDAMLVVGARFSDRtfTSY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 361 GRVLSHSSKIIIVNRNREEmllnSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPD---WVEELREADRQKEQTFREKA 437
Cdd:PRK06456 293 DEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIILRELIKAITELGQKRDrsaWLKRVKEYKEYYSQFYYTEE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 438 ampvAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWC 517
Cdd:PRK06456 369 ----NGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVD 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361361 518 LFGDGAFGYSLIEFDTFVRHKIPVMALVgNDAGWTQISREQVPSLGSNVACGLAY---TDYHKAAMGLGARG 586
Cdd:PRK06456 445 LDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVRQVQDLFFGKRIVGVDYgpsPDFVKLAEAFGALG 515
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
54-622 |
2.99e-38 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 149.75 E-value: 2.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPL---LVACEKLgiRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTV 130
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTKV--RHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 131 TAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPV 210
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 211 DVLypyfmvQKEMVpakppkglvgrvvswylenylanlFagAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVL 290
Cdd:PRK07789 191 DAL------QAQTT------------------------F--SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 291 GSQALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHPLHI-------RENRSAALKKADVIVLAGTVCDFRLSyGRV 363
Cdd:PRK07789 239 GGGVIRAEASAE-LRELAELTGIPVVTTLMARGAFPDSHPQHLgmpgmhgTVAAVAALQRSDLLIALGARFDDRVT-GKL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 364 LSHS--SKIIIVN-------RNREemllnSDIFwkpqeaVQGDVGSFVLKLVEGLQGQTWA---PD---WVEELREADRQ 428
Cdd:PRK07789 317 DSFApdAKVIHADidpaeigKNRH-----ADVP------IVGDVKEVIAELIAALRAEHAAggkPDltaWWAYLDGWRET 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 429 KEQTFREkaamPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKL 508
Cdd:PRK07789 386 YPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 509 CRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGNDA-----GWTQISREQVPSlGSNVACGLAYT-DYHKAAMG 581
Cdd:PRK07789 462 GRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINNGNlgmvrQWQTLFYEERYS-NTDLHTHSHRIpDFVKLAEA 540
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 21361361 582 LGARGLllsR-ENEDQVVKVLHDAQQQcrDGHPVVVNILIGR 622
Cdd:PRK07789 541 YGCVGL---RcEREEDVDAVIEKARAI--NDRPVVIDFVVGK 577
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
54-544 |
1.12e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 147.69 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGgIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 LYPYFmvqkeMVPAKPPKGLVGRvvswylenylanlfagAWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLMVLGS 292
Cdd:PRK07979 166 LNPAN-----KLPYVWPESVSMR----------------SYNPTTQG---------HKGQIKRALQTLVAAKKPVVYVGG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 293 QALLTPTSADkLRAAVETLGVPCFLGGMARGLLGRNHP-------LHIRENRSAALKKADVIVLAGTVCDFRLSYGRVLS 365
Cdd:PRK07979 216 GAINAACHQQ-LKELVEKLNLPVVSSLMGLGAFPATHRqslgmlgMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 366 HSSKIII---VNRNREEMLLNSDIfwkpqeAVQGDvGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQtFREKAAM--- 439
Cdd:PRK07979 295 CPNATVLhidIDPTSISKTVTADI------PIVGD-ARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQ-WRARQCLkyd 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 440 PVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLF 519
Cdd:PRK07979 367 THSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVT 446
|
490 500
....*....|....*....|....*
gi 21361361 520 GDGAFGYSLIEFDTFVRHKIPVMAL 544
Cdd:PRK07979 447 GDGSIQMNIQELSTALQYELPVLVL 471
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
65-620 |
8.93e-37 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 145.23 E-value: 8.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 65 HGVRFIFTLVGGHISPL---LVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQ 140
Cdd:CHL00099 23 HGVKHIFGYPGGAILPIydeLYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 141 SPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV---LYPYF 217
Cdd:CHL00099 103 VPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVgleKFDYY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 218 MVqkemVPAKPPKGLVGrvvswylenylanlfagaWEPqpegplpldIPQASPQQVQRCVEILSRAKRPLMVLGSQALLT 297
Cdd:CHL00099 183 PP----EPGNTIIKILG------------------CRP---------IYKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 298 pTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIrenrsaalkkaDVIVLAGTV--------CDFRLSYG-----RV- 363
Cdd:CHL00099 232 -DAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCL-----------GMLGMHGTAyanfavseCDLLIALGarfddRVt 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 364 -----LSHSSKIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKLVEGLQGQTWAPDwvEELREADRQKEQTFREKAA 438
Cdd:CHL00099 300 gkldeFACNAQVIHIDIDPAEIGKNR----IPQVAIVGDVKKVLQELLELLKNSPNLLE--SEQTQAWRERINRWRKEYP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 439 MPVAQH---LNPVQVLQLVEETLPDnSILVVDGGDFVGTAAHL--VQPRgplRWLDPGAFGTLGVGAGFALGAKLCRPDA 513
Cdd:CHL00099 374 LLIPKPstsLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlkCKPR---KWLSSAGLGTMGYGLPAAIGAQIAHPNE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 514 EVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQISRE-QVPSLG-----SNVACGLAytDYHKAAMGLGARGL 587
Cdd:CHL00099 450 LVICISGDASFQMNLQELGTIAQYNLPIKIIIINN-KWQGMVRQwQQAFYGeryshSNMEEGAP--DFVKLAEAYGIKGL 526
|
570 580 590
....*....|....*....|....*....|...
gi 21361361 588 LLsrENEDQVVKVLHDAQQQcrDGhPVVVNILI 620
Cdd:CHL00099 527 RI--KSRKDLKSSLKEALDY--DG-PVLIDCQV 554
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
62-594 |
3.09e-36 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 143.36 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQS 141
Cdd:PRK07710 26 LEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLADAMIDSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 142 PILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDvlypyfMVQK 221
Cdd:PRK07710 106 PLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD------MVVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 222 EmvpakppkglvgrvvswylenylanlfaGAWEPQPEGPLPLDIPQASPQ--QVQRCVEILSRAKRPLMVLGSQALLTPT 299
Cdd:PRK07710 180 E----------------------------GEFCYDVQMDLPGYQPNYEPNllQIRKLVQAVSVAKKPVILAGAGVLHAKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 300 SaDKLRAAVETLGVPcflggMARGLLG-----RNHPL-------HIRENRSAALKKADVIVLAGTVCDFRLSyGRVLSHS 367
Cdd:PRK07710 232 S-KELTSYAEQQEIP-----VVHTLLGlggfpADHPLflgmagmHGTYTANMALYECDLLINIGARFDDRVT-GNLAYFA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 368 SKIIIVNRNREEMLLNSDIfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKaampvAQHLNP 447
Cdd:PRK07710 305 KEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQEGKKENHHEWLSLLKNWKEKYPLSYKRN-----SESIKP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 448 VQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYS 527
Cdd:PRK07710 378 QKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMT 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361361 528 LIEFDTFVRHKIPVMALVGNDAG------WTQISREQVPSlGSNVACglaYTDYHKAAMGLGARGLLLSRENE 594
Cdd:PRK07710 458 LQELSVIKELSLPVKVVILNNEAlgmvrqWQEEFYNQRYS-HSLLSC---QPDFVKLAEAYGIKGVRIDDELE 526
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
52-548 |
1.67e-35 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 141.41 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 52 RHGGENVAAVLRAHGVRFIFTLVGG-----HISPLLVACeklgIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGL 126
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGasmeiHQALTRSNC----IRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 127 TNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFV 206
Cdd:PLN02470 89 TNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 207 ELPVDvlypyfmVQKEM-VPA-KPPKGLVGrvvswylenYLANLfagawePQPegplpldiPQASpqQVQRCVEILSRAK 284
Cdd:PLN02470 169 DIPKD-------IQQQLaVPNwNQPMKLPG---------YLSRL------PKP--------PEKS--QLEQIVRLISESK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 285 RPLMVLGSQALltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRE-------NRSAALKKADVIVLAGTVCDFR 357
Cdd:PLN02470 217 RPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANYAVDSADLLLAFGVRFDDR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 358 LSyGRVLSHSS--KIIIVNRNREEMLLNSdifwKPQEAVQGDVgSFVLKLVEGL--QGQTWAPDWVEELREADRQKEQ-- 431
Cdd:PLN02470 294 VT-GKLEAFASraSIVHIDIDPAEIGKNK----QPHVSVCADV-KLALQGLNKLleERKAKRPDFSAWRAELDEQKEKfp 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 432 -TFREKAAMPVAQHlnpvqVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCR 510
Cdd:PLN02470 368 lSYPTFGDAIPPQY-----AIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAAN 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 21361361 511 PDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 548
Cdd:PLN02470 443 PDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
54-541 |
3.43e-34 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 137.53 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVAC-EKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 LYpyfmvqkemvpAK----PPKGLVGRVvswylenylanlfagAWEPQPEGplpldipqaSPQQVQRCVEILSRAKRPLM 288
Cdd:PRK09107 173 QF-----------ATgtytPPQKAPVHV---------------SYQPKVKG---------DAEAITEAVELLANAKRPVI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 289 VLGSQALLT-PTSADKLRAAVETLGVP--CFLGGMAR---------GLLGrnhpLHIRENRSAALKKADVIVLAGTVCDF 356
Cdd:PRK09107 218 YSGGGVINSgPEASRLLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYEANMAMHDCDVMLCVGARFDD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 357 RLSyGRVLS---HSSKIII------VNRNreemlLNSDIfwkpqeAVQGDVGSFVLKLVEGLQGQTWAPD------WVEE 421
Cdd:PRK09107 294 RIT-GRLDAfspNSKKIHIdidpssINKN-----VRVDV------PIIGDVGHVLEDMLRLWKARGKKPDkealadWWGQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 422 LREADRQKEQTFREKAAMPVAQHlnpvQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAG 501
Cdd:PRK09107 362 IARWRARNSLAYTPSDDVIMPQY----AIQRLYELTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 21361361 502 FALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 541
Cdd:PRK09107 438 AALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
58-622 |
3.39e-32 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 131.64 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 58 VAAVLRAHGVRFIFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAMARLS-GTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:PRK11269 10 AVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGLYS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 136 AqMAQS-PILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDvly 214
Cdd:PRK11269 90 A-SADSiPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFD--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 215 pyfmVQKEMVpakppkglvgrvvswylenylanlfagAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSqA 294
Cdd:PRK11269 166 ----VQVAEI---------------------------EFDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG-G 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 295 LLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL----------HIRENrsAALKKADVIVLAGTVCDFRlsygrvl 364
Cdd:PRK11269 214 VINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATLLASDFVLGIGNRWANR------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 sHSSKIIIVNRNREemLLNSDI-------FWKPQEAVQGDVGSFVLKLVEGLQGQTWA------PDWVEELREadrqkeq 431
Cdd:PRK11269 285 -HTGSVEVYTKGRK--FVHVDIeptqigrVFGPDLGIVSDAKAALELLVEVAREWKAAgrlpdrSAWVADCQE------- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 432 tfrEKAAMPVAQH-----LNPVQVLQLVEETLPDNSILV-------VDGGDFVgtaaHLVQPRgplRWLDPGAFGTLGVG 499
Cdd:PRK11269 355 ---RKRTLLRKTHfdnvpIKPQRVYEEMNKAFGRDTCYVstiglsqIAAAQFL----HVYKPR---HWINCGQAGPLGWT 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 500 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPsLGSNVACGLAY------- 572
Cdd:PRK11269 425 IPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIRQAQRA-FDMDYCVQLAFeninspe 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 21361361 573 -----TDYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 622
Cdd:PRK11269 504 lngygVDHVKVAEGLGCKAIRVFKPED--IAPALEQAKALMAEFRvPVVVEVILER 557
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
62-551 |
5.71e-31 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 127.81 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLLVACEK---LGIRVVDT---RHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKN 135
Cdd:PRK08327 17 LKELGVDYIFINSGTDYPPIIEAKARaraAGRPLPEFvicPHEIVAISMAHGYALVTGKPQAVMVHVDVGTANALGGVHN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 136 AQMAQSPILLLGGAASTLlqNRGAL-----------QAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPV 204
Cdd:PRK08327 97 AARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMSEPKGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 205 FVELPVDVLypyfmVQKemvpakppkglVGRVvswylenylanlfagawEPQPEGPLPLDIPQASPQQVQRCVEILSRAK 284
Cdd:PRK08327 175 YLTLPREVL-----AEE-----------VPEV-----------------KADAGRQMAPAPPAPDPEDIARAAEMLAAAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 285 RPLmVLGSQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSYGRvL 364
Cdd:PRK08327 222 RPV-IITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDPRADLAEADLVLVVDSDVPWIPKKIR-P 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 SHSSKIIIVNrnreEMLLNSDI-FWK-PQE-AVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPV 441
Cdd:PRK08327 300 DADARVIQID----VDPLKSRIpLWGfPCDlCIQADTSTALDQLEERLKSLASAERRRARRRRAAVRELRIRQEAAKRAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 442 AQHL------NPVQVLQLVEETLPDNSILVVDGGdFVGTAAHLvqpRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEV 515
Cdd:PRK08327 376 IERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPGSYFGDGSAGGLGWALGAALGAKLATPDRLV 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 21361361 516 WCLFGDGAFGYSLIEFDTFV--RHKIPVMALVGNDAGW 551
Cdd:PRK08327 452 IATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
467-618 |
5.52e-30 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 115.38 E-value: 5.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 467 DGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVG 546
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361361 547 NDAGWTQISREQVPSLGSNVAC----GLAYTDYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrdGHPVVVNI 618
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGpsgkILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
54-620 |
3.69e-27 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 116.25 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVAC--EKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVT 131
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 132 AVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKF---CVSVRRVRDIVPT-LRAAMAAAqsgtpGPVFVE 207
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYnhqIMSAENLPEIVNQaIRTAYEKK-----GVAVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 208 LPVDVLypyfmvqKEMVPAKPpkglvgrvvswyleNYLANLFAgawepqpegplpLDIPQASPQQVQRCVEILSRAKRPL 287
Cdd:PRK08611 161 IPDDLP-------AQKIKDTT--------------NKTVDTFR------------PTVPSPKPKDIKKAAKLINKAKKPV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 288 MVLGsqaLLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL------HIRENRS-AALKKADVIVLAGTvcDFrlSY 360
Cdd:PRK08611 208 ILAG---LGAKHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYslgnlgKIGTKPAyEAMQEADLLIMVGT--NY--PY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 361 GRVLSHSSKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFVLKLVEGLqgqtwapDWVEELR--EADRQKEQTFREK 436
Cdd:PRK08611 281 VDYLPKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALHQLTENI-------KHVEDRRflEACQENMAKWWKW 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 437 AAMPVAQHLNPV---QVLQLVEETLPDNSILVVD-GGDFVGTAAHL-VQPRGPL---RWLdpgafGTLGVGAGFALGAKL 508
Cdd:PRK08611 348 MEEDENNASTPIkpeRVMAAIQKIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL-----GTMGCGLPGAIAAKI 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 509 CRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLL 588
Cdd:PRK08611 423 AFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYR 502
|
570 580 590
....*....|....*....|....*....|..
gi 21361361 589 LsrENEDQVVKVLHDAQQQCRdghPVVVNILI 620
Cdd:PRK08611 503 V--EKAEELDPAFEEALAQDK---PVIIDVYV 529
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
61-594 |
6.12e-26 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 112.23 E-value: 6.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 61 VLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQ 140
Cdd:PRK06457 11 VLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYDAKMDH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 141 SPILLLGGAASTLLQNRGALQAVDQLSLFRPlckfcVSVRRVRDIVP-----TLRAAMAAAQSgTPGPVFVELPVDVLyp 215
Cdd:PRK06457 91 APVIALTGQVESDMIGHDYFQEVNLTKLFDD-----VAVFNQILINPenaeyIIRRAIREAIS-KRGVAHINLPVDIL-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 216 yfmvqkemvpakppkglvgRVVSWYLENYlanlfagaWEPQPEGPLPLDIPQASpqqvqrcvEILSRAKRPLMVLGSQAL 295
Cdd:PRK06457 163 -------------------RKSSEYKGSK--------NTEVGKVKYSIDFSRAK--------ELIKESEKPVLLIGGGTR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 296 ltpTSADKLRAAVETLGVPCFLGGMARGLLGRNHP--------LHIRENRSAaLKKADVIVLAGTVcdfrLSYGRVLSHS 367
Cdd:PRK06457 208 ---GLGKEINRFAEKIGAPIIYTLNGKGILPDLDPkvmggiglLGTKPSIEA-MDKADLLIMLGTS----FPYVNFLNKS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 368 SKIIIVNRNREEM--LLNSDIfwkpqeAVQGDVGSFV-LKLVEglqgqtwAPDWVEElrEADRQKEQTFR--EKAAMPVA 442
Cdd:PRK06457 280 AKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLnIDIEE-------KSDKFYE--ELKGKKEDWLDsiSKQENSLD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 443 QHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCR-PDAEVWCLFGD 521
Cdd:PRK06457 345 KPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGD 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361361 522 GAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQ----VPSLGSNvacgLAYTDYHKAAMGLGARGLLLSRENE 594
Cdd:PRK06457 425 GGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEWGVD----LYNPDFTKIAESIGFKGFRLEEPKE 497
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
449-620 |
4.13e-25 |
|
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: 101.95 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 449 QVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 528
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 529 IEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQq 607
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVsGTDLSNPDFAALAEAYGAKGVRV--EDPEDLEAALAEALA- 157
|
170
....*....|...
gi 21361361 608 cRDGhPVVVNILI 620
Cdd:cd00568 158 -AGG-PALIEVKT 168
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
445-623 |
4.56e-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: 99.89 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 524
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 525 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSN-VACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHD 603
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
|
170 180
....*....|....*....|
gi 21361361 604 AQQQCRDGHPVVVNILIGRT 623
Cdd:cd02013 162 AIAMMAEGKTTVIEIVCDQE 181
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
62-624 |
6.29e-24 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 106.01 E-value: 6.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAMARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQ 140
Cdd:COG3961 15 LAELGIRHIFGVPGDYNLPFLdAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGIAGAYAER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 141 SPILLLGGAASTLLQNRGALqaV----------DQLSLFRPLCkfCVSVR-----------RVrdivptLRAAMAAAQsg 199
Cdd:COG3961 94 VPVVHIVGAPGTRAQRRGPL--LhhtlgdgdfdHFLRMFEEVT--VAQAVltpenaaaeidRV------LAAALREKR-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 200 tpgPVFVELPVDVlypyfmVQKEMVPakppkglvgrvvswylenylanlfagawepqPEGPLPLDIPQASPQQVQRCV-- 277
Cdd:COG3961 162 ---PVYIELPRDV------ADAPIEP-------------------------------PEAPLPLPPPASDPAALAAAVaa 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 278 --EILSRAKRPLMVLGSQAL---LTptsaDKLRAAVETLGVPCFLGGMARGLLGRNHPLHI--------RENRSAALKKA 344
Cdd:COG3961 202 aaERLAKAKRPVILAGVEVHrfgLQ----EELLALAEKTGIPVATTLLGKSVLDESHPQFIgtyagaasSPEVREYVENA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 345 DVIVLAGTV-CDFrlsygrvlshsskiiivnrnreemllNSDIF--WKPQEAVQgDVGSFVLKLveglqGQTWAP----- 416
Cdd:COG3961 278 DCVLCLGVVfTDT--------------------------NTGGFtaQLDPERTI-DIQPDSVRV-----GGHIYPgvsla 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 417 DWVEELREADRQKEQTFREKAAMPVAQHLNPVQVL------QLVEETLPDNSILVVDGGD--FVGTAAHLvqPRGpLRWL 488
Cdd:COG3961 326 DFLEALAELLKKRSAPLPAPAPPPPPPPAAPDAPLtqdrlwQRLQAFLDPGDIVVADTGTslFGAADLRL--PEG-ATFI 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 489 DPGAFGTLG--VGAgfALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTqISReqvpslgsnV 566
Cdd:COG3961 403 AQPLWGSIGytLPA--ALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYT-IER---------A 470
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361361 567 ACGL--AYTD-----YHKAAMGLGARGLLLSR-ENEDQVVKVLHDAQQQCRdgHPVVVNILIGRTD 624
Cdd:COG3961 471 IHGPdgPYNDianwdYAKLPEAFGGGNALGFRvTTEGELEEALAAAEANTD--RLTLIEVVLDKMD 534
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
55-212 |
1.23e-23 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 97.62 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 55 GENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAV 133
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 134 KNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRR---VRDIVPT-LRAAMAaaqsgTPGPVFVELP 209
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPELLDRaIRTAIA-----KRGVAVLILP 157
|
...
gi 21361361 210 VDV 212
Cdd:cd07039 158 GDV 160
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
445-620 |
8.65e-23 |
|
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: 95.68 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 524
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 525 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDA 604
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
|
170
....*....|....*.
gi 21361361 605 QQQcrDGhPVVVNILI 620
Cdd:cd02014 160 LAA--DG-PVVIDVVT 172
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
273-405 |
1.88e-18 |
|
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: 81.84 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 273 VQRCVEILSRAKRPLMVLGSQALLtPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPL-------HIRENRSAALKKAD 345
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRR-SGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361361 346 VIVLAGTVCDFRLSYGRVLSHSS--KIIIVNRNREEMLLNSdifwKPQEAVQGDVGSFVLKL 405
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPdaKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
62-524 |
4.81e-18 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 88.04 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLLVACEKLG--IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMA 139
Cdd:PRK08273 13 LREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYDAKLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 140 QSPILLLGGAastllQNRGAL-----QAVDQLSLFR----PLCKFCVSVRRVRDIVP-TLRAAMAaaqsgTPGPVFVELP 209
Cdd:PRK08273 93 HVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVPEQLRHLVDrAVRTALA-----ERTVTAVILP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 210 VDvlypyfmVQKEmvPAKPPKGLVGRVVSwylenylanlfaGAWEPQPEgPLPldipqaSPQQVQRCVEILSRAKRPLMV 289
Cdd:PRK08273 163 ND-------VQEL--EYEPPPHAHGTVHS------------GVGYTRPR-VVP------YDEDLRRAAEVLNAGRKVAIL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 290 LGSQALltpTSADKLRAAVETLGvpcflGGMARGLLGRnhplhirenrsAALKK-----ADVIVLAGTvcdfRLSYgRVL 364
Cdd:PRK08273 215 VGAGAL---GATDEVIAVAERLG-----AGVAKALLGK-----------AALPDdlpwvTGSIGLLGT----KPSY-ELM 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 365 SHSSKIIIVNRNreemllnsdiF----WKPQE----AVQGDVGSFVLKL---VE-GLQGQTWA------------PD--W 418
Cdd:PRK08273 271 RECDTLLMVGSS----------FpyseFLPKEgqarGVQIDIDGRMLGLrypMEvNLVGDAAEtlrallpllerkKDrsW 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 419 VEELREADRQKEQTFREKAAMPvAQHLNPVQVLQLVEETLPDNSILVVDGGDFVG-TAAHLVQPRGPLRWLDpGAFGTLG 497
Cdd:PRK08273 341 RERIEKWVARWWETLEARAMVP-ADPVNPQRVFWELSPRLPDNAILTADSGSCANwYARDLRMRRGMMASLS-GTLATMG 418
|
490 500
....*....|....*....|....*..
gi 21361361 498 VGAGFALGAKLCRPDAEVWCLFGDGAF 524
Cdd:PRK08273 419 PAVPYAIAAKFAHPDRPVIALVGDGAM 445
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
58-210 |
1.03e-17 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 80.47 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 58 VAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGtVGVAAVTAGPGLTNTVTAVKNA 136
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361361 137 QMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPT-LRAAMAAAQSgtPGPVFVELPV 210
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGiDHAIRTAYAS--QGPVVVRLPR 154
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
49-591 |
1.13e-15 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 80.00 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 49 ASVRHGgenVAAVLRAHGVRFIFTLVGGHISPLLVACEKlGIRVVDTRHEVTAVFAADAMARLSGTVGV----AAVTAGP 124
Cdd:PRK07092 12 TTVRDA---TIDLLRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFvnlhSAAGVGN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 125 GLTNTVTAVKNaqmaQSPILLLGGA-ASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGP 203
Cdd:PRK07092 88 AMGNLFTAFKN----HTPLVITAGQqARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 204 VFVELPVDvlypyfmvqKEMVPAKPpkgLVGRVVSwylenylanlFAGAwepqpegplpldipqASPQQVQRCVEILSRA 283
Cdd:PRK07092 164 VFVSIPYD---------DWDQPAEP---LPARTVS----------SAVR---------------PDPAALARLGDALDAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 284 KRPLMVLGSQALLTPTSADKLRAAvETLGVPCFLGGMA-RGLLGRNHPLH------IRENRSAALKKADVIVLAGTVCdF 356
Cdd:PRK07092 207 RRPALVVGPAVDRAGAWDDAVRLA-ERHRAPVWVAPMSgRCSFPEDHPLFagflpaSREKISALLDGHDLVLVIGAPV-F 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 357 RL---SYGRVLSHSSKIIIVNRNREEMLlnsdifWKPQ-EAVQGDVGSFVLKLVEGL-QGQTWAPDWVEELREADRQKEq 431
Cdd:PRK07092 285 TYhveGPGPHLPEGAELVQLTDDPGEAA------WAPMgDAIVGDIRLALRDLLALLpPSARPAPPARPMPPPAPAPGE- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 432 tfrekaAMPVAQhlnpvqVLQLVEETLPDNSILVVDGGDFVGTaahlVQPRgpLRWLDPGAF-----GTLGVGAGFALGA 506
Cdd:PRK07092 358 ------PLSVAF------VLQTLAALRPADAIVVEEAPSTRPA----MQEH--LPMRRQGSFytmasGGLGYGLPAAVGV 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 507 KLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQIsREQVPSLGSNVACGLAY--TDYHKAAMGLGA 584
Cdd:PRK07092 420 ALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGAL-RWFAPVFGVRDVPGLDLpgLDFVALARGYGC 498
|
....*..
gi 21361361 585 RGLLLSR 591
Cdd:PRK07092 499 EAVRVSD 505
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
445-547 |
9.51e-15 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 72.92 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQVLQLVEETLPDNSILVVDggdfVGT----AAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFG 520
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTD----VGQhqmwAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDG 76
|
90 100
....*....|....*....|....*..
gi 21361361 521 DGAFGYSLIEFDTFVRHKIPVMALVGN 547
Cdd:cd02015 77 DGSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
447-627 |
5.65e-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: 70.39 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 447 PVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 526
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 527 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQ 606
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRI--ESADDLLPVLERALA 158
|
170 180
....*....|....*....|.
gi 21361361 607 QcrDGhPVVVNILIgrtDFRD 627
Cdd:cd02010 159 A--DG-VHVIDCPV---DYSE 173
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
445-620 |
2.94e-13 |
|
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: 68.39 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 445 LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 524
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 525 GYSLIEFDTFVRHKIPVMALVGNDAGWtQISREQVPSLGSNVACGLAY---------TDYHKAAMGLGARGLLLSRENEd 595
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVETPEE- 157
|
170 180
....*....|....*....|....*.
gi 21361361 596 qvvkvLHDAQQQC-RDGHPVVVNILI 620
Cdd:cd02002 158 -----LDEALREAlAEGGPALIEVVV 178
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
56-549 |
3.03e-13 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 72.71 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 56 ENVAAVLRAHGVRFIFTLVGGHISPLLVACEK-LGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVK 134
Cdd:PRK06546 7 EQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRtGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 135 NAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGtPGPVFVELPVDVly 214
Cdd:PRK06546 87 DAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGDI-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 215 pyfmvqkemvpakppkglvgrvvswylenylanlfagAWEPQPEGPLPLDIPQA------SPQQVQRCVEILSRAKRPLM 288
Cdd:PRK06546 164 -------------------------------------ADEPAPEGFAPSVISPRrptvvpDPAEVRALADAINEAKKVTL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 289 VLGSQallTPTSADKLRAAVETLGVPC---------------FLGGMArGLLGRNHPlhirenrSAALKKADVIVLAGTv 353
Cdd:PRK06546 207 FAGAG---VRGAHAEVLALAEKIKAPVghslrgkewiqydnpFDVGMS-GLLGYGAA-------HEAMHEADLLILLGT- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 354 cDFrlSYGRVLShSSKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTF 433
Cdd:PRK06546 275 -DF--PYDQFLP-DVRTAQVDIDPEHLGRRTRV----DLAVHGDVAETIRALLPLVKEKTDRRFLDRMLKKHARKLEKVV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 434 rEKAAMPVAQH--LNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLdpGAF--GTLGVGAGFALGAKLC 509
Cdd:PRK06546 347 -GAYTRKVEKHtpIHPEYVASILDELAADDAVFTVDTGMCNVWAARYITPNGRRRVI--GSFrhGSMANALPHAIGAQLA 423
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 21361361 510 RPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 549
Cdd:PRK06546 424 DPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNS 463
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
54-583 |
3.78e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 72.21 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVpRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPIL-LLGGAASTLLQNRGALQAvDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVD 211
Cdd:PRK12474 87 LHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 212 VlypyfmvqkemvpakppkglvgrvvswylenylanlfagAWEPQPEGPLPL-DIPQA--SPQQVQRCVEILSRAKRPLM 288
Cdd:PRK12474 166 V---------------------------------------AWNEAAYAAQPLrGIGPApvAAETVERIAALLRNGKKSAL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 289 VLGSQALLTP--TSADKLRAAVetlGVPCFLGGMA-RGLLGRNH-PL----HIRENRSAALKKADVIVLAGT---VCDFr 357
Cdd:PRK12474 207 LLRGSALRGAplEAAGRIQAKT---GVRLYCDTFApRIERGAGRvPIeripYFHEQITAFLKDVEQLVLVGAkppVSFF- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 358 lSY----GRVLSHSSKIIIVNRNREEmllnsdifwkpqeavqgdvgsfvlkLVEGLQgqtwapDWVEELREADRQKEQTF 433
Cdd:PRK12474 283 -AYpgkpSWGAPPGCEIVYLAQPDED-------------------------LAQALQ------DLADAVDAPAEPAARTP 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 434 REKAAMPVAQhLNPVQVLQLVEETLPDNSIlVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDA 513
Cdd:PRK12474 331 LALPALPKGA-LNSLGVAQLIAHRTPDQAI-YADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDR 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361361 514 EVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG----WTQISREQVPSLGSNVACGLAY----TDYHKAAMGLG 583
Cdd:PRK12474 409 KVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSyailNGELQRVGAQGAGRNALSMLDLhnpeLNWMKIAEGLG 486
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
58-549 |
1.49e-12 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 70.40 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 58 VAAVLRAHGVRFIFTLVGGHISPLLVACEKLG-IRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNA 136
Cdd:PRK09124 9 IAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 137 QMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAqSGTPGPVFVELPVDVLYpy 216
Cdd:PRK09124 89 HRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDVAL-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 217 fmvqkEMVPAKPPkglvgrvVSWYlenylanlfagawepqpEGPLPLDIPQASpqQVQRCVEILSRAKRPLMVLGSQall 296
Cdd:PRK09124 166 -----KPAPERAT-------PHWY-----------------HAPQPVVTPAEE--ELRKLAALLNGSSNITLLCGSG--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 297 TPTSADKLRAAVETLGVPC---------------FLGGMArGLLGRNHPLHirenrsaALKKADVIVLAGTvcDFrlSYG 361
Cdd:PRK09124 212 CAGAHDELVALAETLKAPIvhalrgkehveydnpYDVGMT-GLIGFSSGYH-------AMMNCDTLLMLGT--DF--PYR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 362 RVLSHSSKIIIVNRNREEMLLNSDIfwkpQEAVQGDVGSFVLKLVEGLQGQTwAPDWVEELREADRQKEQTFREKA-AMP 440
Cdd:PRK09124 280 QFYPTDAKIIQIDINPGSLGRRSPV----DLGLVGDVKATLAALLPLLEEKT-DRKFLDKALEHYRKARKGLDDLAvPSD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 441 VAQHLNPVQVLQLVEETLPDNSILVVDggdfVGT----AAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVW 516
Cdd:PRK09124 355 GGKPIHPQYLARQISEFAADDAIFTCD----VGTptvwAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVV 430
|
490 500 510
....*....|....*....|....*....|...
gi 21361361 517 CLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 549
Cdd:PRK09124 431 ALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNS 463
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
452-624 |
2.01e-12 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 66.02 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 452 QLVEETLPDNSILVVDGGDFVGTAAHLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEF 531
Cdd:cd02005 9 QQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 532 DTFVRHKIPVMALVGNDAGWT---QISREQVPslgsnvacglaYTD-----YHKAAMGLGARGLLLSR--ENEDQVVKVL 601
Cdd:cd02005 88 STMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFrvKTEGELDEAL 156
|
170 180
....*....|....*....|...
gi 21361361 602 HDAQQQCrdGHPVVVNILIGRTD 624
Cdd:cd02005 157 KDALFNR--DKLSLIEVILPKDD 177
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
62-160 |
9.34e-11 |
|
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: 60.59 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLL-VACEKLGIRVVDTRHEVTAVFAADAMARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQ 140
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLdAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100
....*....|....*....|
gi 21361361 141 SPILLLGGAASTLLQNRGAL 160
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGLL 105
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
54-545 |
5.96e-10 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 62.17 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 54 GGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKL-GIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTA 132
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 133 VKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDV 212
Cdd:PRK07586 83 LHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQVATLILPADV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 213 lypyfmvqkemvpakppkglvgrvvswylenylanlfagAWEP--QPEGPLPL-DIPQASPQQVQRCVEILSRAKRPLMV 289
Cdd:PRK07586 163 ---------------------------------------AWSEggPPAPPPPApAPAAVDPAAVEAAAAALRSGEPTVLL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 290 LGSQALLTPTSADKLRAAVET---LGVPCFLGGMARgllGRNHPLHIR-----ENRSAALKKADVIVLAGT---VCDFrl 358
Cdd:PRK07586 204 LGGRALRERGLAAAARIAAATgarLLAETFPARMER---GAGRPAVERlpyfaEQALAQLAGVRHLVLVGAkapVAFF-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 359 SYgrvlshsskiiivnRNREEMLlnsdifwKPQEAVqgdvgsfVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAA 438
Cdd:PRK07586 279 AY--------------PGKPSRL-------VPEGCE-------VHTLAGPGEDAAAALEALADALGAKPAAPPLAAPARP 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 439 MPVAQHLNPVQVLQLVEETLPDNSILVVDGGDF-VGTAAHLVQPRgPLRWLD-PGafGTLGVGAGFALGAKLCRPDAEVW 516
Cdd:PRK07586 331 PLPTGALTPEAIAQVIAALLPENAIVVDESITSgRGFFPATAGAA-PHDWLTlTG--GAIGQGLPLATGAAVACPDRKVL 407
|
490 500
....*....|....*....|....*....
gi 21361361 517 CLFGDGAFGYSLIEFDTFVRHKIPVMALV 545
Cdd:PRK07586 408 ALQGDGSAMYTIQALWTQARENLDVTTVI 436
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
477-622 |
9.56e-06 |
|
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: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 477 HLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAgWTQISR 556
Cdd:cd02006 43 HVYKPR---HWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIR 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361361 557 EQVPSLGSNVACGLAY------------TDYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 622
Cdd:cd02006 119 QAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPEE--LAAAFEQAKKLMAEHRvPVVVEAILER 195
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
62-209 |
1.02e-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: 45.95 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 62 LRAHGVRFIFTLVGGHISPLLVACEKLG-IRV---VDTRhevTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQ 137
Cdd:cd07037 7 LKRLGVRDVVISPGSRSAPLALAAAEHPeFRLhvrVDER---SAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEAY 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361361 138 MAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVR------RVRDIVPTLRAAMAAAQSGTPGPVFVELP 209
Cdd:cd07037 84 YSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
449-618 |
2.62e-04 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 42.68 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 449 QVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 528
Cdd:cd02003 3 EVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 529 IEFDTFVRHKIPVMALVGNDAGWTQISREQVpSLGS---------------NVACGLAYTDYHKAAMGLGARglLLSREN 593
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQE-STGSgsfgtefrdrdqesgQLDGALLPVDFAANARSLGAR--VEKVKT 159
|
170 180
....*....|....*....|....*
gi 21361361 594 EDQVVKVLHDAQQQCRdghPVVVNI 618
Cdd:cd02003 160 IEELKAALAKAKASDR---TTVIVI 181
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
267-328 |
3.76e-04 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 41.47 E-value: 3.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361361 267 QASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVP-CFLGGMARGLLGRN 328
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
98-209 |
1.35e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 42.15 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361361 98 EVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCV 177
Cdd:PLN02980 348 ERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFF 427
|
90 100 110
....*....|....*....|....*....|....*...
gi 21361361 178 SVRRVRDIVP------TLRAAMAAAQSGTPGPVFVELP 209
Cdd:PLN02980 428 NLPPPTDLIParmvltTLDSAVHWATSSPCGPVHINCP 465
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| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
496-522 |
7.30e-03 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 38.64 E-value: 7.30e-03
10 20
....*....|....*....|....*..
gi 21361361 496 LGVGAGFALGAKLCRPDAEVWCLFGDG 522
Cdd:cd02012 111 LSVAVGMALAEKLLGFDYRVYVLLGDG 137
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