|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
2-517 |
5.31e-109 |
|
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: 335.21 E-value: 5.31e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:COG0028 61 ARATGKPGVCLVTSGPGATNLVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVPAKPRKGLVGRVvswylenylanlfagawepQPEgplpldiPQA 161
Cdd:COG0028 141 LRRAFRIATSGRPGPVVLDIPKD-------VQAAEAEEEPAPPELRGY-------------------RPR-------PAP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLtPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:COG0028 188 DPEAIEEAAELLAAAKRPVILAGGGARR-AGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWA-PDWV 312
Cdd:COG0028 267 AEADLVLAVGARFDDRVTGNwDEFAPDAKIIHIDIDPAEI----GKNYPVDLPIVGDAKAVLAALLEALEPRADDrAAWL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREADRQKEQTFREKAAmpvaqHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:COG0028 343 ARIAAWRAEYLAAYAADDG-----PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNV-ACSLAYTEYHKA 471
Cdd:COG0028 418 LPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYsGTDLPNPDFAKL 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622891768 472 AMGLGARGLLLsrENEDQVVKVLHDAQQQcrdGHPVVVNILIGRTD 517
Cdd:COG0028 498 AEAFGAKGERV--ETPEELEAALEEALAS---DGPALIDVRVDPEE 538
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
2-512 |
1.31e-93 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 295.48 E-value: 1.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK05858 62 AKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkEMVPAKPRkglvgrvvswylenylanlfagawePQPEGPLPLDiPQA 161
Cdd:PRK05858 142 VDQALQAAVTPHRGPVFVDFPMDHAF-------SMADDDGR-------------------------PGALTELPAG-PTP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAALKKADVIV 241
Cdd:PRK05858 189 DPDALARAAGLLAEAQRPVIMAGTDVWWG-HAEAALLRLAEELGIPVLMNGMGRGVVPADHPLAFSRARGKALGEADVVL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 242 LAGTVCDFRLSYGRVLSHSSKIIIVnrnreDMLLNSDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREAD-- 319
Cdd:PRK05858 268 VVGVPMDFRLGFGVFGGTAQLVHVD-----DAPPQRAHHRPVAAGLYGDLSAILSALAGAGGDRTDHQGWIEELRTAEta 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 320 -RQKEQTFREKAAMPvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALG 398
Cdd:PRK05858 343 aRARDAAELADDRDP----IHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 399 AKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWtqiSREQVPS---LGSNVACSLA-YTEYHKAAMG 474
Cdd:PRK05858 419 ARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAADLRpGTRYDEVVRA 495
|
490 500 510
....*....|....*....|....*....|....*....
gi 1622891768 475 LGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNIL 512
Cdd:PRK05858 496 LGGHGELVTVPAE------LGPALERAFAsGVPYLVNVL 528
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
340-513 |
3.71e-70 |
|
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: 222.02 E-value: 3.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 340 PVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPS--LGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSygLGLPVTTLLPDTRYDLVAEAFGGKGELV--TTPEELKPALKRA 158
|
170
....*....|....*.
gi 1622891768 498 QQQcrdGHPVVVNILI 513
Cdd:cd02004 159 LAS---GKPALINVII 171
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
4-513 |
1.24e-48 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 176.71 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 4 LSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTL---LQnRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK09259 69 LTQKPGVCLTVSAPGFLNGLTALANATTNCFPMIMISGSSEREivdLQ-QGDYEELDQLNAAKPFCKAAFRVNRAEDIGI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDVLypyfmvQKEMVPAKPRKGLVgRVVSwylenylanlfagawepqpegPLPLDIPq 160
Cdd:PRK09259 148 GVARAIRTAVSGRPGGVYLDLPAKVL------AQTMDADEALTSLV-KVVD---------------------PAPAQLP- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 aSPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAALKKADVI 240
Cdd:PRK09259 199 -APEAVDRALDLLKKAKRPLIILGKGAAYA-QADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAAARSLALANADVV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 241 VLAGTVCDFRLSYGR--VLSHSSKIIIVNRNREDMllNSDVfwkPQEA-VQGDVGSFVLKLVEGLQGQTWAP--DWVEEL 315
Cdd:PRK09259 277 LLVGARLNWLLSHGKgkTWGADKKFIQIDIEPQEI--DSNR---PIAApVVGDIGSVMQALLAGLKQNTFKApaEWLDAL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 316 READRQKEQTFREK--AAMPVAQHLNPVRVLQLVEETLPDnSILVVDGGDFVGTAAHLV---QPRGPlcwLDPGAFGTLG 390
Cdd:PRK09259 352 AERKEKNAAKMAEKlsTDTQPMNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIdmyKPRHR---LDCGTWGVMG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 391 VGAGFALGAKLC--RPdaeVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGwtqISR--EQVPSLGSNVACS--LA 464
Cdd:PRK09259 428 IGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGDPSPTvlVH 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1622891768 465 YTEYHKAAMGLGARGLLLSreNEDQVVKVLHDAQQQcrdGHPVVVNILI 513
Cdd:PRK09259 502 HARYDKMMEAFGGVGYNVT--TPDELRHALTEAIAS---GKPTLINVVI 545
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
2-449 |
1.77e-45 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 167.46 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGG--AASTLLQNRGALQAI-DQLSLFRPLCKFCASVRRVRDI 78
Cdd:PRK07524 59 ARVSGKPGVCFIITGPGMTNIATAMGQAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 79 VPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmvqkemvpAKPrkglvgrvvswylenylanlFAGAWEPQPEGPLPldi 158
Cdd:PRK07524 139 PEVLARAFAVFDSARPRPVHIEIPLDVL------------AAP--------------------ADHLLPAPPTRPAR--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRS-----AA 233
Cdd:PRK07524 184 PGPAPAALAQAAERLAAARRPLILAGGGAL---AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGASQSlpavrAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTV---CDFRLSY-GRVLSHSSKIII------VNRNREdmllnsdvfwkPQEAVQGDVGSFVLKLVEGLQ 303
Cdd:PRK07524 261 IAEADVVLAVGTElgeTDYDVYFdGGFPLPGELIRIdidpdqLARNYP-----------PALALVGDARAALEALLARLP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 304 GQTWAPDWVEELREADRQKEqtfREKAAMPVAQHlnpVRVLQLVEETLPDNsILVVDGGDFVGTAAHLVQPRGPLCWLD- 382
Cdd:PRK07524 330 GQAAAADWGAARVAALRQAL---RAEWDPLTAAQ---VALLDTILAALPDA-IFVGDSTQPVYAGNLYFDADAPRRWFNa 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISR 449
Cdd:PRK07524 403 STGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR 469
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
2-515 |
1.11e-42 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 160.55 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07525 63 TRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTpGPVFVELPIDvlYPYFMVQKEMvpakprkglvgrvvswylenylanlfagawePQPegpLPLDIPQA 161
Cdd:PRK07525 143 LNRVFDKAKRES-GPAQINIPRD--YFYGVIDVEI-------------------------------PQP---VRLERGAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVP---------CFLGG--MARGLLGRNHSlhirenr 230
Cdd:PRK07525 186 GEQSLAEAAELLSEAKFPVILSGAGVVLS-DAIEECKALAERLDAPvacgylhndAFPGShpLWVGPLGYNGS------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 SAALK---KADVIVLAGTvcdfRLSYGRVLSH--------SSKIIIVNRNREDMLLNsdvfwKPQE-AVQGDVGSFVLKL 298
Cdd:PRK07525 258 KAAMEliaKADVVLALGT----RLNPFGTLPQygidywpkDAKIIQVDINPDRIGLT-----KKVSvGICGDAKAVAREL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 299 VEGLQGQTWAP---------------DWVEELREADRQKEQ---TFREKAAMPVAQHLNPVRVLQLVEETLPDNSILVVD 360
Cdd:PRK07525 329 LARLAERLAGDagreerkaliaaeksAWEQELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPEDAIVSTD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 361 GGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGN 440
Cdd:PRK07525 409 IGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFR 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 441 DAGWTQISREQVPSLGSN-VACSL-AYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 515
Cdd:PRK07525 489 NYQWGAEKKNQVDFYNNRfVGTELdNNVSYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIEIMCNQ 563
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
2-513 |
3.33e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 159.15 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06276 58 ARASGKVGVCVATSGPGATNLVTGIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEMVPAKPRkglvgrvvswyLENYLANLFagawepqpegplpldipqA 161
Cdd:PRK06276 138 FRAAFEIAKTGRPGPVHIDLPKDVQEGELDLEKYPIPAKID-----------LPGYKPTTF------------------G 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADkLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:PRK06276 189 HPLQIKKAAELIAEAERPVILAGGGVIISGASEE-LIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGtvCDF--RLSyGRVLSHS--SKIIIVNRNREDMLLNSDVfwkpQEAVQGDVGSFVLKLVEGLQGQTWAPD 310
Cdd:PRK06276 268 TESDVLIAIG--CRFsdRTT-GDISSFApnAKIIHIDIDPAEIGKNVRV----DVPIVGDAKNVLRDLLAELMKKEIKNK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 --WVEELREadrqkeqtfREKAAMPVA----QHLNPVRVLQLVEETLPD-----NSILVVDGGDFVGTAAHLVQPRGPLC 379
Cdd:PRK06276 341 seWLERVKK---------LKKESIPRMdfddKPIKPQRVIKELMEVLREidpskNTIITTDVGQNQMWMAHFFKTSAPRS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV------GNDAGWTQI---SRE 450
Cdd:PRK06276 412 FISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIfdnrtlGMVYQWQNLyygKRQ 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622891768 451 QVPSLGSNvacslayTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAqqqCRDGHPVVVNILI 513
Cdd:PRK06276 492 SEVHLGET-------PDFVKLAESYGVKADRV--EKPDEIKEALKEA---IKSGEPYLLDIII 542
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
2-441 |
5.18e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 158.34 E-value: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK08527 61 ARASGKVGVAIVTSGPGFTNAVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDV-------LYPyfmVQKEMVPAKPrkglvgrvvswyleNYLANlfagawepqpegpl 154
Cdd:PRK08527 141 LKEAFYIARSGRPGPVHIDIPKDVtatlgefEYP---KEISLKTYKP--------------TYKGN-------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 155 pldipqasPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIR 227
Cdd:PRK08527 190 --------SRQIKKAAEAIKEAKKPLFYLGGGAILS-NASEEIRELVKKTGIPAVETLMARGVLRSDDPLllgmlgmHGS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 228 ENRSAALKKADVIVLAGTVCDFRLSyGRV--LSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLQ 303
Cdd:PRK08527 261 YAANMAMSECDLLISLGARFDDRVT-GKLseFAKHAKIIHVDIDPSSIskIVNADY------PIVGDLKNVLKEMLEELK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 304 G---QTWAPdWVEELREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCW 380
Cdd:PRK08527 334 EenpTTYKE-WREILKRYNELHPLSYEDSDEV-----LKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPFNYPRQL 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622891768 381 LDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK08527 408 ATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNN 468
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-446 |
4.04e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 155.37 E-value: 4.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MA----RLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVr 76
Cdd:PRK08322 53 MAatygRLTGKAGVCLSTLGPGATNLVTGVAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSP- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 77 DIVPTL-RAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenylanlfagAWEPQPEGPLP 155
Cdd:PRK08322 132 DNIPEVvREAFRLAEEERPGAVHLELPEDI---------------------------------------AAEETDGKPLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 156 LD---IPQASPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHS-------LH 225
Cdd:PRK08322 173 RSysrRPYASPKAIERAAEAIQAAKNPLILIGAGA-NRKTASKALTEFVDKTGIPFFTTQMGKGVIPETHPlslgtagLS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 226 IRENRSAALKKADVIVLAG-TVCDFrlSYGRVLSHSSKIII-VNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGL- 302
Cdd:PRK08322 252 QGDYVHCAIEHADLIINVGhDVIEK--PPFFMNPNGDKKVIhINFLPAEV----DPVYFPQVEVVGDIANSLWQLKERLa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 303 QGQTWAPDWVEELREADRQKEQTFREKAAMPVAqhlnPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPL-CWL 381
Cdd:PRK08322 326 DQPHWDFPRFLKIREAIEAHLEEGADDDRFPMK----PQRIVADLRKVMPDDDIVILDNGAYKIWFARNYRAYEPNtCLL 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 382 DpGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG-----WTQ 446
Cdd:PRK08322 402 D-NALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAygmirWKQ 470
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
2-479 |
4.66e-39 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 149.39 E-value: 4.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGG--AASTLLQNRGALQAI-DQLSLFRPLCKFCASVRRVRDI 78
Cdd:PRK08266 63 ARSTGRPGVCSVVPGPGVLNAGAALLTAYGCNSPVLCLTGqiPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 79 VPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmvqkemvpakprkGLVGRVvswylenylanlfagawEPQPEGPlPLDI 158
Cdd:PRK08266 143 PALVAEAFQQMLSGRPRPVALEMPWDVF-----------------GQRAPV-----------------AAAPPLR-PAPP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIreNRSAA---LK 235
Cdd:PRK08266 188 PAPDPDAIAAAAALIAAAKNPMIFVGGGAA---GAGEEIRELAEMLQAPVVAFRSGRGIVSDRHPLGL--NFAAAyelWP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 236 KADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREDMllnsdVFWKPQEAVQGDVGSFVLKLVEGLQGQ-TWAPDWVEE 314
Cdd:PRK08266 263 QTDVVIGIGSRLELPTFRWPWRPDGLKVIRIDIDPTEM-----RRLKPDVAIVADAKAGTAALLDALSKAgSKRPSRRAE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 315 LREADRQKEQTFreKAAMPVAQHLNPVRvlqlveETLPDNSIlVVDGGDFVGTAAHLVQP-RGPLCWLDPGAFGTLGVGA 393
Cdd:PRK08266 338 LRELKAAARQRI--QAVQPQASYLRAIR------EALPDDGI-FVDELSQVGFASWFAFPvYAPRTFVTCGYQGTLGYGF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 394 GFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSL-GSNVACSLAYTEYHKAA 472
Cdd:PRK08266 409 PTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFgGRVVASDLVNPDFVKLA 488
|
....*..
gi 1622891768 473 MGLGARG 479
Cdd:PRK08266 489 ESFGVAA 495
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-441 |
2.16e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 148.19 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06725 72 ARASGKVGVVFATSGPGATNLVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEmvpakprkglvgRVVSWYLEnylaNLFAGAWEPQpegplpldiPQA 161
Cdd:PRK06725 152 VQEAFYIAESGRPGPVLIDIPKD-------VQNE------------KVTSFYNE----VVEIPGYKPE---------PRP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:PRK06725 200 DSMKLREVAKAISKAKRPLLYIGG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAANMAV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRV--LSHSSKIIIVNRNREDMLLNSDVfwkpQEAVQGDVGSfVLKLVEGLQGQTWAPDWV 312
Cdd:PRK06725 279 TECDLLLALGVRFDDRVT-GKLelFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKK-ALHMLLHMSIHTQTDEWL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:PRK06725 353 QKVKTWKEEYPLSYKQKESE-----LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFG 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06725 428 FPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINN 476
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-515 |
5.42e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 146.84 E-value: 5.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06048 65 ARATGKVGVCVATSGPGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVlypyfmVQKEMVPAKPRKglvgrvVSwyLENYlanlfagawEPQPEGplpldipqa 161
Cdd:PRK06048 145 IKEAFHIASTGRPGPVLIDLPKDV------TTAEIDFDYPDK------VE--LRGY---------KPTYKG--------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAvETLGVPCFLGGMARGLLGRNHSLHI-------RENRSAAL 234
Cdd:PRK06048 193 NPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELA-ETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPdWVEE 314
Cdd:PRK06048 272 QESDLIIAVGARFDDRVT-GKLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQYCDRKE-WLDK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 315 LREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDnSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAG 394
Cdd:PRK06048 348 INQWKKEYPLKYKEREDV-----IKPQYVIEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 395 FALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA------GWTQISREQVPSlgsnVACSLAYTEY 468
Cdd:PRK06048 422 AAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDKRYS----HTCIKGSVDF 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622891768 469 HKAAMGLGARGLLLSRENEdqvvkvLHDAQQQCRD-GHPVVVNILIGR 515
Cdd:PRK06048 498 VKLAEAYGALGLRVEKPSE------VRPAIEEAVAsDRPVVIDFIVEC 539
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
1-515 |
1.08e-36 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 143.03 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSG--TVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAAstllqNRGaLQAID----QLSLFRPLCKFCASVRR 74
Cdd:PRK06154 73 YARATSgeRVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGY-----PRG-STDVApnfeSLRNYRHITKWCEQVTL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 75 VRDIVPTLRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkEMVPAKPrkglvgrvvswylENYlanlfagawepqpeGPL 154
Cdd:PRK06154 147 PDEVPELMRRAFTRLRNGRPGPVVLELPVDVLA-------EELDELP-------------LDH--------------RPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 155 PLDIPQASPQQVQRCVEILSRAKRPLMVLGsQALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENRSAA- 233
Cdd:PRK06154 193 RRSRPGADPVEVVEAAALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 ------LKKADVIVLAGtvCDF-RLSYGRVLSHSSKIIIVNRNREDmlLNSDVFWKpqEAVQGDVGSFVLKLVEGLQG-- 304
Cdd:PRK06154 272 atvahfLREADVLFGIG--CSLtRSYYGLPMPEGKTIIHSTLDDAD--LNKDYPID--HGLVGDAALVLKQMIEELRRrv 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 305 ------------------QTWAPDWVEELREADRQkeqtfrekaampvaqhLNPVRVLQLVEETL-PDNSILVVDGGDFV 365
Cdd:PRK06154 346 gpdrgraqqvaaeieavrAAWLAKWMPKLTSDSTP----------------INPYRVVWELQHAVdIKTVIITHDAGSPR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 366 GTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWT 445
Cdd:PRK06154 410 DQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN-FSM 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 446 QISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRDGHPVVVNILIGR 515
Cdd:PRK06154 489 GGYDKVMPVSTTKYRATDISGDYAAIARALGGYGERV--EDPEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
2-444 |
3.65e-35 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 138.58 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAAST--LLQNRGAL-QAIDQLSLFRPLCKFCASVRRVRDI 78
Cdd:PRK07064 61 ARVSGGLGVALTSTGTGAGNAAGALVEALTAGTPLLHITGQIETpyLDQDLGYIhEAPDQLTMLRAVSKAAFRVRSAETA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 79 VPTLRAAMAAAQSGTPGPVFVELPIDVLYpyfmvqkemvpakprkglvgRVVSWylenylanlfagawePQPEGPLPLDI 158
Cdd:PRK07064 141 LATIREAVRVALTAPTGPVSVEIPIDIQA--------------------AEIEL---------------PDDLAPVHVAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVEtLGVPCFLGGMARGLLGRNHSLHIRE-NRSAA---- 233
Cdd:PRK07064 186 PEPDAAAVAELAERLAAARRPLLWLGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLGAfNNSAAveal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTvcdfRLSYGRVLSHSSKI------IIVNRNREDMLLNSDVFwkpqeaVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK07064 262 YKTCDLLLVVGS----RLRGNETLKYSLALprplirVDADAAADGRGYPNDLF------VHGDAARVLARLADRLEGRLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 308 A-PDWVEELREADRQKEQTFRekaampvaQHLNPVRVL-QLVEETLPDNSILVVDGGDFVGTAAH-LVQPRGPLCWLDPG 384
Cdd:PRK07064 332 VdPAFAADLRAAREAAVADLR--------KGLGPYAKLvDALRAALPRDGNWVRDVTISNSTWGNrLLPIFEPRANVHAL 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 385 AfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGW 444
Cdd:PRK07064 404 G-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-434 |
3.68e-35 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 139.17 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06965 79 ARATGKVGVALVTSGPGVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLY---PYFMVQK-EMVPAKP-RKGLVGrvvswylenylanlfagawepqpegplpl 156
Cdd:PRK06965 159 VKKAFYIARTGRPGPVVVDIPKDVSKtpcEYEYPKSvEMRSYNPvTKGHSG----------------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 157 dipqaspqQVQRCVEILSRAKRPLMVLGSQALLTPKSADkLRAAVETLGVPCF-----LGGMAR------GLLGrnhsLH 225
Cdd:PRK06965 210 --------QIRKAVSLLLSAKRPYIYTGGGVILANASRE-LRQLADLLGYPVTntlmgLGAYPAsdkkflGMLG----MH 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 226 IRENRSAALKKADVIVLAGTVCDFRL--SYGRVLSHSSKII--------IVNRNREDMllnsdvfwkpqeAVQGDVGSFV 295
Cdd:PRK06965 277 GTYEANMAMQHCDVLIAIGARFDDRVigNPAHFASRPRKIIhididpssISKRVKVDI------------PIVGDVKEVL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 296 LKLVEGLQGQTWAPD------W---VEELREADRQKEQTFREKaampvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVG 366
Cdd:PRK06965 345 KELIEQLQTAEHGPDadalaqWwkqIEGWRSRDCLKYDRESEI--------IKPQYVVEKLWELTDGDAFVCSDVGQHQM 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622891768 367 TAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK06965 417 WAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPV 484
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-520 |
6.45e-35 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 137.68 E-value: 6.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK08617 61 IGRLTGKPGVVLVTSGPGVSNLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDVLypyfmvqKEMVPAKPRKGLvgrvvswylenylanlfagawEPQPEGPlpldipq 160
Cdd:PRK08617 141 VLANAFRAAESGRPGAAFVSLPQDVV-------DAPVTSKAIAPL---------------------SKPKLGP------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 ASPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHslhirENRsaalkkadvi 240
Cdd:PRK08617 186 ASPEDINYLAELIKNAKLPVLLLGMRA-SSPEVTAAIRRLLERTNLPVVETFQAAGVISREL-----EDH---------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 241 vLAGTVCDFRLSYG-RVLSHSSKIIIV------------NRNREDMLLNSDV-------FWKPQEAVQGDVGSFVLKLVE 300
Cdd:PRK08617 250 -FFGRVGLFRNQPGdELLKKADLVITIgydpieyeprnwNSEGDATIIHIDVlpaeidnYYQPERELIGDIAATLDLLAE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 301 GLQGQTWAPDWVEELreADRQKEQTFREKAAMPVAQHL-NPVRVLQLVEETLPDNSILVVDGGDF-VGTAAHL--VQPRG 376
Cdd:PRK08617 329 KLDGLSLSPQSLEIL--EELRAQLEELAERPARLEEGAvHPLRIIRALQDIVTDDTTVTVDVGSHyIWMARYFrsYEPRH 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 377 PLcwldpgaFG----TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQV 452
Cdd:PRK08617 407 LL-------FSngmqTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEE 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622891768 453 PSLGSNVACSLAYTEYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrDGhPVVVNILIgrtDFRD 520
Cdd:PRK08617 480 MKYGRSSGVDFGPVDFVKYAESFGAKG--LRVTSPDELEPVLREALAT--DG-PVVIDIPV---DYSD 539
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
2-103 |
6.70e-35 |
|
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: 128.42 E-value: 6.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:cd07035 54 ARATGKPGVVLVTSGPGLTNAVTGLANAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEA 133
|
90 100
....*....|....*....|..
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPI 103
Cdd:cd07035 134 LRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-447 |
3.16e-33 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 133.08 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIvPT 81
Cdd:PRK08199 66 GKLTGRPGICFVTRGPGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARI-PE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRA-AMAAAQSGTPGPVFVELPIDVLYpyfmvQKEMVPAKPRkglvGRVVswylenylanlfagawEPQPegplpldipq 160
Cdd:PRK08199 145 LVSrAFHVATSGRPGPVVLALPEDVLS-----ETAEVPDAPP----YRRV----------------AAAP---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 aSPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVP----------------CFLG----GMARGLLGR 220
Cdd:PRK08199 190 -GAADLARLAELLARAERPLVILGG-SGWTEAAVADLRAFAERWGLPvacafrrqdlfdnrhpNYAGdlglGINPALAAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 221 nhslhIREnrsaalkkADVIVLAGTvcdfRLsyGRVLSHSSKIIIVNRNREDML--------LNSdVFwKPQEAVQGDVG 292
Cdd:PRK08199 268 -----IRE--------ADLVLAVGT----RL--GEVTTQGYTLLDIPVPRQTLVhvhpdaeeLGR-VY-RPDLAIVADPA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 293 SFVLKL--VEGLQGQTWApDWVEELREADRQkeqtfrEKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAH 370
Cdd:PRK08199 327 AFAAALaaLEPPASPAWA-EWTAAAHADYLA------WSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATWLHR 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 371 LVQPRGPLCWLDPGAfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQI 447
Cdd:PRK08199 400 FFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
2-441 |
5.95e-33 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 132.58 E-value: 5.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFcasVRRVRD---I 78
Cdd:PRK06112 69 ARVSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKW---VRRVTVaerI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 79 VPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmVQKEMVPAKPRKglvgrvvswylenylANLfaGAWepqpegplPLDI 158
Cdd:PRK06112 146 DDYVDQAFTAATSGRPGPVVLLLPADLL-----TAAAAAPAAPRS---------------NSL--GHF--------PLDR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------------- 224
Cdd:PRK06112 196 TVPAPQRLAEAASLLAQAQRPVVVAGGGVHIS-GASAALAALQSLAGLPVATTNMGKGAVDETHPLslgvvgslmgprsp 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 225 --HIREnrsaALKKADVIVLAGTvcdfRLSYG-----RVLSHSSKIII-------VNRNREDMLLNSDVfwkpQEAVQGd 290
Cdd:PRK06112 275 grHLRD----LVREADVVLLVGT----RTNQNgtdswSLYPEQAQYIHidvdgeeVGRNYEALRLVGDA----RLTLAA- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 291 vgsfvLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPV---AQHLNPVRVLQLVEETLPDNSILVVDGG-DFVG 366
Cdd:PRK06112 342 -----LTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPVAlsdASPIRPERIMAELQAVLTGDTIVVADASySSIW 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622891768 367 TAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06112 417 VANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNN 491
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-442 |
3.34e-32 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 130.21 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK08155 70 MARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenYLANLFAGAWePQPEGPLPldIPQ 160
Cdd:PRK08155 150 VISDAFRIAQSGRPGPVWIDIPKDV-------------------------------QTAVIELEAL-PAPAEKDA--APA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 ASPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAA 233
Cdd:PRK08155 196 FDEESIRDAAAMINAAKRPVLYLGG-GVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLslgmlgmHGARSTNYI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTVCDFRlSYGRVLSH--SSKIIIVNRNREDMllnsDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWApDW 311
Cdd:PRK08155 275 LQEADLLIVLGARFDDR-AIGKTEQFcpNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLPLVEAQPRA-EW 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 312 VEelREADRQKEQTFrekaAMPVAQH-LNPVRVLQLVEETLPDNSILVVDGGD---FVGTAAHLVQPRGplcWLDPGAFG 387
Cdd:PRK08155 349 HQ--LVADLQREFPC----PIPKADDpLSHYGLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRPRQ---WLTSGGLG 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622891768 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGNDA 442
Cdd:PRK08155 420 TMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
2-106 |
8.72e-32 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 120.03 E-value: 8.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQA-IDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:pfam02776 57 ARATGKPGVVLVTSGPGATNALTGLANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPE 136
|
90 100
....*....|....*....|....*.
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDVL 106
Cdd:pfam02776 137 VLRRAFRAALSGRPGPVYLEIPLDVL 162
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
2-515 |
1.21e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 129.01 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07418 80 ARATGKVGVCFGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFmvqkEMVPAKPrkglvGRVVswyLENYlanlfagawEPQPEGplpldipqa 161
Cdd:PRK07418 160 VAEAFHIASSGRPGPVLIDIPKDVGQEEF----DYVPVEP-----GSVK---PPGY---------RPTVKG--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAAL 234
Cdd:PRK07418 210 NPRQINAALKLIEEAERPLLYVGGGA-ISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRVLSHSS--KII---I----VNRNRedmllnsdvfwKPQEAVQGDVGSFVLKLVEGLQGQ 305
Cdd:PRK07418 289 TECDLLIAVGARFDDRVT-GKLDEFASraKVIhidIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 306 TWAP---DWVEELreadrqkeQTFREKAAMPVAQH---LNPVRVLQLVEETLPDnSILVVDGGDFVGTAAHLVQpRGPLC 379
Cdd:PRK07418 357 TTPPrtqAWLERI--------NRWKQDYPLVVPPYegeIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAQFLR-NGPRR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQISREQVPSL---- 455
Cdd:PRK07418 427 WISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQWQESFyger 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622891768 456 --GSNVACSLAytEYHKAAMGLGARGLLLSRENEdqvvkvLHDAQQQC--RDGhPVVVNILIGR 515
Cdd:PRK07418 506 ysASNMEPGMP--DFVKLAEAFGVKGMVISERDQ------LKDAIAEAlaHDG-PVLIDVHVRR 560
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
2-440 |
1.48e-31 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 128.56 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07789 89 AQATGRVGVCMATSGPGATNLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLypyfmvQKEMVpakprkglvgrvvswylenylanlFAgaWEPQPEGPLPLDIPQA 161
Cdd:PRK07789 169 IAEAFHIASTGRPGPVLVDIPKDAL------QAQTT------------------------FS--WPPRMDLPGYRPVTKP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADkLRAAVETLGVPCFLGGMARGLLGRNHSLHI-------RENRSAAL 234
Cdd:PRK07789 217 HGKQIREAAKLIAAARRPVLYVGGGVIRAEASAE-LRELAELTGIPVVTTLMARGAFPDSHPQHLgmpgmhgTVAAVAAL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRLSyGRVLSHS--SKIIIVN-------RNREdmllnSDVFwkpqeaVQGDVGSFVLKLVEGLQGQ 305
Cdd:PRK07789 296 QRSDLLIALGARFDDRVT-GKLDSFApdAKVIHADidpaeigKNRH-----ADVP------IVGDVKEVIAELIAALRAE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 306 TWA---PD---WVEELREADRQKEQTFREkaamPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLC 379
Cdd:PRK07789 364 HAAggkPDltaWWAYLDGWRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRT 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV-MALVGN 440
Cdd:PRK07789 440 WLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVALINN 501
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-441 |
5.11e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 126.86 E-value: 5.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK07282 68 AKSTGKLGVAVVTSGPGATNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglVGRVVSWYLEnylanlfagawepqPEGPLPLDIPQA 161
Cdd:PRK07282 148 ITEAVHIATTGRPGPVVIDLPKDV--------------------SALETDFIYD--------------PEVNLPSYQPTL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQ--QVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSA 232
Cdd:PRK07282 194 EPNdmQIKKILKQLSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflgmggmHGSYAANI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 233 ALKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWV 312
Cdd:PRK07282 273 AMTEADFMINIGSRFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLAEPTVHNNTEKWI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 313 EELREaDRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVG 392
Cdd:PRK07282 350 EKVTK-DKNRVRSYDKKERV-----VQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFG 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622891768 393 AGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK07282 424 IPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNN 472
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
2-438 |
7.54e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 126.11 E-value: 7.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06456 63 ARASGVPGVCTATSGPGTTNLVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYPyfMVQKEMVPAKPrkglvgrvvswYLENYlanlfagawepqpeGPLPLDIpqa 161
Cdd:PRK06456 143 IKNAFYIATTGRPGPVVIDIPRDIFYE--KMEEIKWPEKP-----------LVKGY--------------RDFPTRI--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAvETLGVPCFLGGMARGLLGRNHSLHI-------RENRSAAL 234
Cdd:PRK06456 193 DRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPLYFgpmgyygRAEASMAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRL--SYGRVLSHSSKIIIVNRNREDmllnSDVFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPD-- 310
Cdd:PRK06456 272 LESDAMLVVGARFSDRTftSYDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIILRELIKAITELGQKRDrs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 -WVEELREADRQKEQTFREKAAmpvaQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTL 389
Cdd:PRK06456 348 aWLKRVKEYKEYYSQFYYTEEN----GKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTM 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622891768 390 GVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV 438
Cdd:PRK06456 424 GFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI 472
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
2-442 |
1.32e-29 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 122.55 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06466 62 ARATGKTGVVLVTSGPGATNAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYPyfmVQKemvpakprkglvgrvvswYLENYLANLFAGAWEPQPEGplpldipqa 161
Cdd:PRK06466 142 IKKAFYIAQSGRPGPVVVDIPKDMTNP---AEK------------------FEYEYPKKVKLRSYSPAVRG--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLM------VLGSQALLTPKSADKLRAAVET--LGVPCFLGGMAR--GLLGrnhsLHIRENRS 231
Cdd:PRK06466 192 HSGQIRKAVEMLLAAKRPVIysgggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEAN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 232 AALKKADVIVLAGTVCDFRLSYG-RVLSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLQGQTWA 308
Cdd:PRK06466 268 MAMHHADVILAVGARFDDRVTNGpAKFCPNAKIIHIDIDPASIskTIKADI------PIVGPVESVLTEMLAILKEIGEK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 309 PD------WVEELREAdRQKEQTFREKAAMPVAqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLD 382
Cdd:PRK06466 342 PDkealaaWWKQIDEW-RGRHGLFPYDKGDGGI--IKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWIN 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDA 442
Cdd:PRK06466 419 SGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-437 |
5.29e-29 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 120.73 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK07979 61 LARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDVLYPyfmvQKEMVPAKPRKglvgrvVSwyLENYlanlfagawEPQPEGplpldipq 160
Cdd:PRK07979 141 VLKKAFWLAASGRPGPVVVDLPKDILNP----ANKLPYVWPES------VS--MRSY---------NPTTQG-------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 aSPQQVQRCVEILSRAKRPLMVLGSQAlLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHS-------LHIRENRSAA 233
Cdd:PRK07979 192 -HKGQIKRALQTLVAAKKPVVYVGGGA-INAACHQQLKELVEKLNLPVVSSLMGLGAFPATHRqslgmlgMHGTYEANMT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTVCDFRLSYGRVLSHSSKIII---VNRNREDMLLNSDVfwkpqeAVQGDvGSFVLKLVEGLQGQTWAPD 310
Cdd:PRK07979 270 MHNADVIFAVGVRFDDRTTNNLAKYCPNATVLhidIDPTSISKTVTADI------PIVGD-ARQVLEQMLELLSQESAHQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 WVEELREADRQKEQtFREKAAM---PVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFG 387
Cdd:PRK07979 343 PLDEIRDWWQQIEQ-WRARQCLkydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLG 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622891768 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMAL 437
Cdd:PRK07979 422 TMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
1-434 |
8.71e-29 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 119.99 E-value: 8.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK08978 57 YARATGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVPAKPrkglvgrvvswylenylaNLFAgawepqpegplPLDIPQ 160
Cdd:PRK08978 137 IMAEAFEIASSGRPGPVLVDIPKD-------IQLAEGELEP------------------HLTT-----------VENEPA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 161 ASPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVP--CFLGGMarGLLGRNHS-----LHIRENRSA- 232
Cdd:PRK08978 181 FPAAELEQARALLAQAKKPVLYVGGGVGMA-GAVPALREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAn 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 233 -ALKKADVIVLAGTVCDFRLSyGRVLSHSS--KIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLQGQTW 307
Cdd:PRK08978 258 lAVQECDLLIAVGARFDDRVT-GKLNTFAPhaKVIHLDIDPAEInkLRQAHV------ALQGDLNALLPALQQPLNIDAW 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 308 ApDWVEELREadrqkEQTFREKAAmpvAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFG 387
Cdd:PRK08978 331 R-QHCAQLRA-----EHAWRYDHP---GEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLG 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1622891768 388 TLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK08978 402 TMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPV 448
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
360-511 |
2.13e-28 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 110.37 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 360 DGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVG 439
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622891768 440 NDAGWTQISREQVPSLGSNVAC----SLAYTEYHKAAMGLGARGllLSRENEDQVVKVLHDAQQQcrdGHPVVVNI 511
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGpsgkILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEALEH---DGPALIDV 151
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-441 |
2.45e-28 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 118.86 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06882 62 ARSTGKVGCVLVTSGPGATNAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPST 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEMvpakPRKglvgrvVSwyLENYLANLfagawepqpegplpldipQA 161
Cdd:PRK06882 142 IKKAFYIASTGRPGPVVIDIPKDMVNPANKFTYEY----PEE------VS--LRSYNPTV------------------QG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCF-----LGGMAR------GLLGrnhsLHIRENR 230
Cdd:PRK06882 192 HKGQIKKALKALLVAKKPVLFVGG-GVITAECSEQLTQFAQKLNLPVTsslmgLGAYPStdkqflGMLG----MHGTYEA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 SAALKKADVIVLAGTVCDFRLS--YGRVLSHsSKIIIVNRNREDMLLNSDVFWKPQEAVQGDVGSFVLKLVEG--LQGQT 306
Cdd:PRK06882 267 NNAMHESDLILGIGVRFDDRTTnnLAKYCPN-AKVIHIDIDPTSISKNVPAYIPIVGSAKNVLEEFLSLLEEEnlAKSQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 307 WAPDWVEELREADRQKEQTFREKAAMpvaqhLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAF 386
Cdd:PRK06882 346 DLTAWWQQINEWKAKKCLEFDRTSDV-----IKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFDKPRRWINSGGA 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622891768 387 GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PRK06882 421 GTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
2-434 |
6.63e-28 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 117.61 E-value: 6.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK08979 62 ARATGKVGVVLVTSGPGATNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYPYFMVQKEmvpakprkglvgrvvswylenYLANLFAGAWEPQPEGplpldipqa 161
Cdd:PRK08979 142 IKKAFYIASTGRPGPVVIDLPKDCLNPAILHPYE---------------------YPESIKMRSYNPTTSG--------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLTpkSADK-LRAAVETLGVPCFLGGMARGLLGRNHS-------LHIRENRSAA 233
Cdd:PRK08979 192 HKGQIKRGLQALLAAKKPVLYVGGGAIIS--GADKqILQLAEKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVGSFVLKLVEGLQGQTWAPD--- 310
Cdd:PRK08979 270 MHNADLIFGIGVRFDDRTT-NNLEKYCPNATILHIDIDPSSISKTV--RVDIPIVGSADKVLDSMLALLDESGETNDeaa 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 311 ---WVEELreadrqkeQTFREKAAMpvAQHLNPVRVL-QLVEETL----PDNSILVVDGGDFVGTAAHLVQPRGPLCWLD 382
Cdd:PRK08979 347 iasWWNEI--------EVWRSRNCL--AYDKSSERIKpQQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWIN 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK08979 417 SGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
2-441 |
3.98e-27 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 115.22 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PLN02470 71 AKASGKVGVCIATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVlypyfmvQKEM-VP--AKPRKglvgrvvswyLENYLANLfagawePQPegplpldi 158
Cdd:PLN02470 151 IREAFFLASSGRPGPVLVDIPKDI-------QQQLaVPnwNQPMK----------LPGYLSRL------PKP-------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASpqQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRE-------NRS 231
Cdd:PLN02470 200 PEKS--QLEQIVRLISESKRPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYAN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 232 AALKKADVIVLAGTVCDFRLSyGRVLSHSSKIIIVNRNREDMLLNSDVfwKPQEAVQGDVgSFVLKLVEGL--QGQTWAP 309
Cdd:PLN02470 275 YAVDSADLLLAFGVRFDDRVT-GKLEAFASRASIVHIDIDPAEIGKNK--QPHVSVCADV-KLALQGLNKLleERKAKRP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 310 DWVEELREADRQKEQ---TFREKAAMPVAQHlnpvrVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAF 386
Cdd:PLN02470 351 DFSAWRAELDEQKEKfplSYPTFGDAIPPQY-----AIQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGL 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622891768 387 GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGND 441
Cdd:PLN02470 426 GAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
2-444 |
6.52e-26 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 111.25 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLlqNRGAL-----------QAIDQLSLFRPLCKFCA 70
Cdd:PRK08327 70 ALVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYT--EEGELgsrntrihwtqEMRDQGGLVREYVKWDY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 71 SVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPIDVLypyfmVQKemvpakprkglVGRVvswylenylanlfagawEPQP 150
Cdd:PRK08327 148 EIRRGDQIGEVVARAIQIAMSEPKGPVYLTLPREVL-----AEE-----------VPEV-----------------KADA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 151 EGPLPLDIPQASPQQVQRCVEILSRAKRPLmVLGSQALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIRENR 230
Cdd:PRK08327 195 GRQMAPAPPAPDPEDIARAAEMLAAAERPV-IITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 SAALKKADVIVLAGTVCDFRLSYGRvLSHSSKIIIVNrnrEDMLLNSDVFWK-PQE-AVQGDVGSFVLKLVEGLQGQTWA 308
Cdd:PRK08327 274 RADLAEADLVLVVDSDVPWIPKKIR-PDADARVIQID---VDPLKSRIPLWGfPCDlCIQADTSTALDQLEERLKSLASA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 309 PDWVEELREADRQKEQTFREKAAMPVAQHL------NPVRVLQLVEETLPDNSILVVDGGdFVGTAAHLvqpRGPLCWLD 382
Cdd:PRK08327 350 ERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL---NKPGSYFG 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622891768 383 PGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFV--RHKIPVMALVGNDAGW 444
Cdd:PRK08327 426 DGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
2-434 |
7.43e-26 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 111.34 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK09107 69 ARSTGKPGVVLVTSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDVLYpyfmVQKEMVPakPRKGLVGRvvswylenylanlfagAWEPQPEGplpldipqa 161
Cdd:PRK09107 149 IHEAFHVATSGRPGPVVVDIPKDVQF----ATGTYTP--PQKAPVHV----------------SYQPKVKG--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQALLT-PKSADKLRAAVETLGVP--CFLGGMAR---------GLLGrnhsLHIREN 229
Cdd:PRK09107 198 DAEAITEAVELLANAKRPVIYSGGGVINSgPEASRLLRELVELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 230 RSAALKKADVIVLAGTVCDFRLSyGRVLS---HSSKIII------VNRNredmlLNSDVfwkpqeAVQGDVGSFVLKLVE 300
Cdd:PRK09107 274 ANMAMHDCDVMLCVGARFDDRIT-GRLDAfspNSKKIHIdidpssINKN-----VRVDV------PIIGDVGHVLEDMLR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 301 GLQGQTWAPD------WVEELREADRQKEQTFREKAAMPVAQHlnpvRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQP 374
Cdd:PRK09107 342 LWKARGKKPDkealadWWGQIARWRARNSLAYTPSDDVIMPQY----AIQRLYELTKGRDTYITTEVGQHQMWAAQFFGF 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 375 RGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPV 434
Cdd:PRK09107 418 EEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPV 477
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
338-516 |
3.01e-24 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 100.28 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 418 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSN-VACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHD 496
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPALQK 161
|
170 180
....*....|....*....|
gi 1622891768 497 AQQQCRDGHPVVVNILIGRT 516
Cdd:cd02013 162 AIAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
342-513 |
1.09e-23 |
|
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: 97.71 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 342 RVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 422 IEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKA-AMGLGARGLLLsrENEDQVVKVLHDAQQq 500
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAAlAEAYGAKGVRV--EDPEDLEAALAEALA- 157
|
170
....*....|...
gi 1622891768 501 cRDGhPVVVNILI 513
Cdd:cd00568 158 -AGG-PALIEVKT 168
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
2-450 |
2.84e-23 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 103.63 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:CHL00099 71 ARSTGKVGVCFATSGPGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSGTPGPVFVELPIDV---LYPYFMVqkemVPAKPRKGLVGrvvswylenylanlfagaWEPqpegplpldI 158
Cdd:CHL00099 151 VAEAFYIAKHGRPGPVLIDIPKDVgleKFDYYPP----EPGNTIIKILG------------------CRP---------I 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 159 PQASPQQVQRCVEILSRAKRPLMVLGSQALLTpKSADKLRAAVETLGVPCFLGGMARGLLGRNHSLHIrenrsaalkkaD 238
Cdd:CHL00099 200 YKPTIKRIEQAAKLILQSSQPLLYVGGGAIIS-DAHQEITELAELYKIPVTTTLMGKGIFDEDHPLCL-----------G 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 239 VIVLAGTV--------CDFRLSYG-----RVL-------SHSSKIII------VNRNRedmllnsdvfwKPQEAVQGDVG 292
Cdd:CHL00099 268 MLGMHGTAyanfavseCDLLIALGarfddRVTgkldefaCNAQVIHIdidpaeIGKNR-----------IPQVAIVGDVK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 293 SFVLKLVEGLQGQTWAPDwvEELREADRQKEQTFREKAAMPVAQH---LNPVRVLQLVEETLPDnSILVVDGGDFVGTAA 369
Cdd:CHL00099 337 KVLQELLELLKNSPNLLE--SEQTQAWRERINRWRKEYPLLIPKPstsLSPQEVINEISQLAPD-AYFTTDVGQHQMWAA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 370 HL--VQPRGplcWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDaGWTQI 447
Cdd:CHL00099 414 QFlkCKPRK---WLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINN-KWQGM 489
|
...
gi 1622891768 448 SRE 450
Cdd:CHL00099 490 VRQ 492
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
6-515 |
9.42e-23 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 101.98 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 6 GTVGVAAVTAGPGLTNTVTAVKNAqMAQS-PVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPTLRA 84
Cdd:PRK11269 67 GNIGVCIGTSGPAGTDMITGLYSA-SADSiPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 85 AMAAAQSGTPGPVFVELPIDvlypyfmVQKEMVpakprkglvgrvvswylenylanlfagAWEPQPEGPLPLDIPQASPQ 164
Cdd:PRK11269 146 AFHLMRSGRPGPVLIDLPFD-------VQVAEI---------------------------EFDPDTYEPLPVYKPAATRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 165 QVQRCVEILSRAKRPLMVLGSqALLTPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL----------HIRENrsAAL 234
Cdd:PRK11269 192 QIEKALEMLNAAERPLIVAGG-GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLmagmvglqtsHRYGN--ATL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 235 KKADVIVLAGTVCDFRlsygrvlsHSSKIIIVNRNREdmLLNSD--------VFwKPQEAVQGDVGSFVLKLVEGLQGQT 306
Cdd:PRK11269 269 LASDFVLGIGNRWANR--------HTGSVEVYTKGRK--FVHVDieptqigrVF-GPDLGIVSDAKAALELLVEVAREWK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 307 WA------PDWVEELREadrqkeqtfrEKAAMPVAQH-----LNPVRVLQLVEETLPDNSILV-------VDGGDFVgta 368
Cdd:PRK11269 338 AAgrlpdrSAWVADCQE----------RKRTLLRKTHfdnvpIKPQRVYEEMNKAFGRDTCYVstiglsqIAAAQFL--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 369 aHLVQPRGplcWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQIS 448
Cdd:PRK11269 405 -HVYKPRH---WINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYLGLIR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 449 REQVPsLGSNVACSLAY------------TEYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 515
Cdd:PRK11269 481 QAQRA-FDMDYCVQLAFeninspelngygVDHVKVAEGLGCKAIRVFKPED--IAPALEQAKALMAEFRvPVVVEVILER 557
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
338-513 |
8.69e-22 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 92.59 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 418 GYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDA 497
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRV--EDPDELEAALDEA 159
|
170
....*....|....*.
gi 1622891768 498 QQQcrDGhPVVVNILI 513
Cdd:cd02014 160 LAA--DG-PVVIDVVT 172
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
2-513 |
1.16e-20 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 95.45 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK08611 63 AKLTGKIGVCLSIGGPGAIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSgTPGPVFVELPIDVLypyfmvqKEMVPAKPRKGlvgrvvswylenylANLFAgawepqpegplpLDIPQA 161
Cdd:PRK08611 143 VNQAIRTAYE-KKGVAVLTIPDDLP-------AQKIKDTTNKT--------------VDTFR------------PTVPSP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQQVQRCVEILSRAKRPLMVLGSQAlltpKSA-DKLRAAVETLGVPCFLGGMARGLLGRNH--SL----HIRENRS-AA 233
Cdd:PRK08611 189 KPKDIKKAAKLINKAKKPVILAGLGA----KHAkEELLAFAEKAKIPIIHTLPAKGIIPDDHpySLgnlgKIGTKPAyEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 234 LKKADVIVLAGTvcDFrlSYGRVLSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFVLKLVEGLqgqtwapDW 311
Cdd:PRK08611 265 MQEADLLIMVGT--NY--PYVDYLPKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALHQLTENI-------KH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 312 VEELR--EADRQKEQTFREKAAMPVAQHLNPVR---VLQLVEETLPDNSILVVD-GGDFVGTAAHL-VQPRGPL---CWL 381
Cdd:PRK08611 328 VEDRRflEACQENMAKWWKWMEEDENNASTPIKperVMAAIQKIADDDAVLSVDvGTVTVWSARYLnLGTNQKFiisSWL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 382 dpgafGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVAC 461
Cdd:PRK08611 408 -----GTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAAGELEYAI 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 462 SLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQQCRdghPVVVNILI 513
Cdd:PRK08611 483 DLSDMDYAKFAEACGGKGYRV--EKAEELDPAFEEALAQDK---PVIIDVYV 529
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
2-487 |
1.48e-18 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 88.73 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPT 81
Cdd:PRK06457 59 AKITGKPSACMGTSGPGSIHLLNGLYDAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 82 LRAAMAAAQSgTPGPVFVELPIDVLypyfmvqkemvpakpRKGLvgrvvswylenylanlfagawEPQPEGPLPLDIPQA 161
Cdd:PRK06457 139 IRRAIREAIS-KRGVAHINLPVDIL---------------RKSS---------------------EYKGSKNTEVGKVKY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 162 SPQqVQRCVEILSRAKRPLMVLGSQALLTPKSADKLraaVETLGVPCF----------------LGGMarGLLGRNHSLh 225
Cdd:PRK06457 182 SID-FSRAKELIKESEKPVLLIGGGTRGLGKEINRF---AEKIGAPIIytlngkgilpdldpkvMGGI--GLLGTKPSI- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 226 irenrsAALKKADVIVLAGTVcdfrLSYGRVLSHSSKIIIVNRNREDM--LLNSDVfwkpqeAVQGDVGSFV-LKLVEgl 302
Cdd:PRK06457 255 ------EAMDKADLLIMLGTS----FPYVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYPIPVAEFLnIDIEE-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 303 qgqtwAPDWVEElrEADRQKEQTFR--EKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCW 380
Cdd:PRK06457 317 -----KSDKFYE--ELKGKKEDWLDsiSKQENSLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 381 LDPGAFGTLGVGAGFALGAKLCR-PDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQ----VPSL 455
Cdd:PRK06457 390 IFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQevmgYPEW 469
|
490 500 510
....*....|....*....|....*....|..
gi 1622891768 456 GSNvacsLAYTEYHKAAMGLGARGLLLSRENE 487
Cdd:PRK06457 470 GVD----LYNPDFTKIAESIGFKGFRLEEPKE 497
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
166-298 |
1.21e-17 |
|
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: 79.53 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 166 VQRCVEILSRAKRPLMVLGSQALLtPKSADKLRAAVETLGVPCFLGGMARGLLGRNHSL-------HIRENRSAALKKAD 238
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRR-SGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622891768 239 VIVLAGTVCDFRLSYGRVLSHSS--KIIIVNRNREDMLLNSdvfwKPQEAVQGDVGSFVLKL 298
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLPEFAPdaKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
2-517 |
1.81e-16 |
|
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: 82.13 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGAL--------QAIDQLSLFRPLCkfCASVR 73
Cdd:COG3961 63 ARVNG-LGALVTTYGVGELSAINGIAGAYAERVPVVHIVGAPGTRAQRRGPLlhhtlgdgDFDHFLRMFEEVT--VAQAV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 74 -----------RVrdivptLRAAMAAAQsgtpgPVFVELPIDVlypyfmVQKEMVPakprkglvgrvvswylenylanlf 142
Cdd:COG3961 140 ltpenaaaeidRV------LAAALREKR-----PVYIELPRDV------ADAPIEP------------------------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 143 agawepqPEGPLPLDIPQASPQQVQRCV----EILSRAKRPLMVLGSQAL---LTpksaDKLRAAVETLGVPCFLGGMAR 215
Cdd:COG3961 179 -------PEAPLPLPPPASDPAALAAAVaaaaERLAKAKRPVILAGVEVHrfgLQ----EELLALAEKTGIPVATTLLGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 216 GLLGRNHSLHI--------RENRSAALKKADVIVLAGTV-CDFRLSYgrvlsHSSKIiivnrNREDMLlnsdvfwkpqea 286
Cdd:COG3961 248 SVLDESHPQFIgtyagaasSPEVREYVENADCVLCLGVVfTDTNTGG-----FTAQL-----DPERTI------------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 287 vqgDVGSFVLKLveglqGQTWAP-----DWVEELREADRQKEQTFREKAAMPVA------QHLNPVRVLQLVEETLPDNS 355
Cdd:COG3961 306 ---DIQPDSVRV-----GGHIYPgvslaDFLEALAELLKKRSAPLPAPAPPPPPppaapdAPLTQDRLWQRLQAFLDPGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 356 ILVVDGGD--FVGTAAHLvqPRG------PLcWldpgafGTLG--VGAgfALGAKLCRPDAEVWCLFGDGAFGYSLIEFD 425
Cdd:COG3961 378 IVVADTGTslFGAADLRL--PEGatfiaqPL-W------GSIGytLPA--ALGAALAAPDRRVILLVGDGAFQLTAQELS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 426 TFVRHKIPVMALVGNDAGWTqISREQVPSLGS-NVacsLAYTEYHKAAMGLGARGLLLSR-ENEDQVVKVLHDAQQQCRd 503
Cdd:COG3961 447 TMLRYGLKPIIFVLNNDGYT-IERAIHGPDGPyND---IANWDYAKLPEAFGGGNALGFRvTTEGELEEALAAAEANTD- 521
|
570
....*....|....
gi 1622891768 504 gHPVVVNILIGRTD 517
Cdd:COG3961 522 -RLTLIEVVLDKMD 534
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
338-440 |
4.09e-14 |
|
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: 70.60 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDggdfVGT----AAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFG 413
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTD----VGQhqmwAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDG 76
|
90 100
....*....|....*....|....*..
gi 1622891768 414 DGAFGYSLIEFDTFVRHKIPVMALVGN 440
Cdd:cd02015 77 DGSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
340-520 |
4.71e-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: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 340 PVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGY 419
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 420 SLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAYTEYHKAAMGLGARGLLLsrENEDQVVKVLHDAQQ 499
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRI--ESADDLLPVLERALA 158
|
170 180
....*....|....*....|.
gi 1622891768 500 QcrDGhPVVVNILIgrtDFRD 520
Cdd:cd02010 159 A--DG-VHVIDCPV---DYSE 173
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
2-417 |
5.03e-13 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 71.48 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAastllQNRGAL-----QAIDQLSLFR----PLCKFCASV 72
Cdd:PRK08273 62 AKFTGEVGVCLATSGPGAIHLLNGLYDAKLDHVPVVAIVGQ-----QARAALgghyqQEVDLQSLFKdvagAFVQMVTVP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 73 RRVRDIVP-TLRAAMAaaqsgTPGPVFVELPIDVlypyfmvQKEMVPAKPRK-GLVGRVVSWylenylanlfagawePQP 150
Cdd:PRK08273 137 EQLRHLVDrAVRTALA-----ERTVTAVILPNDV-------QELEYEPPPHAhGTVHSGVGY---------------TRP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 151 EgPLPldipqaSPQQVQRCVEILSRAKRPLMVLGSQALltpKSADKLRAAVETLGvpcflGGMARGLLGRnhslhirenr 230
Cdd:PRK08273 190 R-VVP------YDEDLRRAAEVLNAGRKVAILVGAGAL---GATDEVIAVAERLG-----AGVAKALLGK---------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 231 sAALKK-----ADVIVLAGTvcdfRLSYgRVLSHSSKIIIVNRNredmllnsdvF----WKPQE----AVQGDVGSFVLK 297
Cdd:PRK08273 245 -AALPDdlpwvTGSIGLLGT----KPSY-ELMRECDTLLMVGSS----------FpyseFLPKEgqarGVQIDIDGRMLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 298 L---VE-GLQGQTWA------------PD--WVEELREADRQKEQTFREKAAMPvAQHLNPVRVLQLVEETLPDNSILVV 359
Cdd:PRK08273 309 LrypMEvNLVGDAAEtlrallpllerkKDrsWRERIEKWVARWWETLEARAMVP-ADPVNPQRVFWELSPRLPDNAILTA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622891768 360 DGGDFVG-TAAHLVQPRGPLCWLDpGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:PRK08273 388 DSGSCANwYARDLRMRRGMMASLS-GTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAM 445
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
338-513 |
1.28e-12 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 66.08 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 338 LNPVRVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAfGTLGVGAGFALGAKLCRPDAEVWCLFGDGAF 417
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 418 GYSLIEFDTFVRHKIPVMALVGNDAGWtQISREQVPSLGSNVACSLAY---------TEYHKAAMGLGARGLLLSRENEd 488
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVETPEE- 157
|
170 180
....*....|....*....|....*.
gi 1622891768 489 qvvkvLHDAQQQC-RDGHPVVVNILI 513
Cdd:cd02002 158 -----LDEALREAlAEGGPALIEVVV 178
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
11-444 |
2.13e-12 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 69.21 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 11 AAVTAGPGLTNTVTAVKNaqmaQSP-VLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVPTLRAAMAAA 89
Cdd:PRK07092 81 SAAGVGNAMGNLFTAFKN----HTPlVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 90 QSGTPGPVFVELPIDvlypyfmvqKEMVPAKPrkgLVGRVVSwylenylanlFAGAwepqpegplpldipqASPQQVQRC 169
Cdd:PRK07092 157 MQPPRGPVFVSIPYD---------DWDQPAEP---LPARTVS----------SAVR---------------PDPAALARL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 170 VEILSRAKRPLMVLG-----SQAL-LTPKSADKLRAAV------------ETLgvPCFlggmaRGLLGRnhslhIRENRS 231
Cdd:PRK07092 200 GDALDAARRPALVVGpavdrAGAWdDAVRLAERHRAPVwvapmsgrcsfpEDH--PLF-----AGFLPA-----SREKIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 232 AALKKADVIVLAGTVCdFRL---SYGRVLSHSSKIIIVNrnrEDMLLNSdvfWKPQ-EAVQGDVGSFVLKLVEGL-QGQT 306
Cdd:PRK07092 268 ALLDGHDLVLVIGAPV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVGDIRLALRDLLALLpPSAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 307 WAPDWVEELREADRQKEqtfrekaAMPVAQhlnpvrVLQLVEETLPDNSILVVDGGDFVGTaahlVQPRGPlcWLDPGAF 386
Cdd:PRK07092 341 PAPPARPMPPPAPAPGE-------PLSVAF------VLQTLAALRPADAIVVEEAPSTRPA----MQEHLP--MRRQGSF 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622891768 387 -----GTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGW 444
Cdd:PRK07092 402 ytmasGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
2-105 |
8.90e-12 |
|
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: 63.34 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRR---VRDI 78
Cdd:cd07039 58 AKLTGKLGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSpeqLPEL 137
|
90 100
....*....|....*....|....*...
gi 1622891768 79 VPT-LRAAMAaaqsgTPGPVFVELPIDV 105
Cdd:cd07039 138 LDRaIRTAIA-----KRGVAVLILPGDV 160
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
342-517 |
1.34e-11 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 63.32 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 342 RVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGpLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 422 IEFDTFVRHKIPVMALVGNDAGWT---QISREQVPslgsnvacslaYTE-----YHKAAMGLGARGLLLSR--ENEDQVV 491
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFrvKTEGELD 153
|
170 180
....*....|....*....|....*.
gi 1622891768 492 KVLHDAQQQCrdGHPVVVNILIGRTD 517
Cdd:cd02005 154 EALKDALFNR--DKLSLIEVILPKDD 177
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
2-476 |
8.65e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 61.04 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVL-LLGGAASTLLQNRGALQAiDQLSLFRPLCKFcasVRRVRD--- 77
Cdd:PRK12474 63 GRIAGKPAVTLLHLGPGLANGLANLHNARRAASPIVnIVGDHAVEHLQYDAPLTS-DIDGFARPVSRW---VHRSASaga 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 78 IVPTLRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenylanlfagAWEPQPEGPLPL- 156
Cdd:PRK12474 139 VDSDVARAVQAAQSAPGGIATLIMPADV---------------------------------------AWNEAAYAAQPLr 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 157 DIPQA--SPQQVQRCVEILSRAKRPLMVLGSQALLTP--KSADKLRAAVetlGVPCFLGGMA-RGLLGRNHSLHIR---- 227
Cdd:PRK12474 180 GIGPApvAAETVERIAALLRNGKKSALLLRGSALRGAplEAAGRIQAKT---GVRLYCDTFApRIERGAGRVPIERipyf 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 228 -ENRSAALKKADVIVLAGT---VCDFrlSY----GRVLSHSSKIIIVNRNREDmllnsdvfwkpqeavqgdvgsfvlkLV 299
Cdd:PRK12474 257 hEQITAFLKDVEQLVLVGAkppVSFF--AYpgkpSWGAPPGCEIVYLAQPDED-------------------------LA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 300 EGLQgqtwapDWVEELREADRQKEQTFREKAAMPVAQhLNPVRVLQLVEETLPDNSIlVVDGGDFVGTAAHLVQPRGPLC 379
Cdd:PRK12474 310 QALQ------DLADAVDAPAEPAARTPLALPALPKGA-LNSLGVAQLIAHRTPDQAI-YADEALTSGLFFDMSYDRARPH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 380 WLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAG----WTQISREQVPSL 455
Cdd:PRK12474 382 THLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSyailNGELQRVGAQGA 461
|
490 500
....*....|....*....|....*
gi 1622891768 456 GSNVACSLAY----TEYHKAAMGLG 476
Cdd:PRK12474 462 GRNALSMLDLhnpeLNWMKIAEGLG 486
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
1-102 |
9.80e-09 |
|
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: 54.27 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSGtVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:cd06586 54 YARAGG-PPVVIVTSGTGLLNAINGLADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPA 132
|
90 100
....*....|....*....|...
gi 1622891768 81 T-LRAAMAAAQSgtPGPVFVELP 102
Cdd:cd06586 133 GiDHAIRTAYAS--QGPVVVRLP 153
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
2-438 |
3.18e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 49.84 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVL-LLGGAASTLLQNRGALQAiDQLSLFRPLCKFCASVRRVRDIVP 80
Cdd:PRK07586 59 ARMAGKPAATLLHLGPGLANGLANLHNARRARTPIVnIVGDHATYHRKYDAPLTS-DIEALARPVSGWVRRSESAADVAA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 81 TLRAAMAAAQSGTPGPVFVELPIDVlypyfmvqkemvpakprkglvgrvvswylenylanlfagAWEP--QPEGPLPL-D 157
Cdd:PRK07586 138 DAAAAVAAARGAPGQVATLILPADV---------------------------------------AWSEggPPAPPPPApA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 158 IPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAVET---LGVPCFLGGMARGLlGRnhsLHIR------E 228
Cdd:PRK07586 179 PAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATgarLLAETFPARMERGA-GR---PAVErlpyfaE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 229 NRSAALKKADVIVLAGTvcdfrlsygrvlshsskiiivnrnredmllNSDVFW-----KPQEAVQGDVGsfVLKLVEGLQ 303
Cdd:PRK07586 255 QALAQLAGVRHLVLVGA------------------------------KAPVAFfaypgKPSRLVPEGCE--VHTLAGPGE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 304 GQTWAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVRVLQLVEETLPDNSILVVDGGDF-VGTAAHLVQPRgPLCWLD 382
Cdd:PRK07586 303 DAAAALEALADALGAKPAAPPLAAPARPPLPTGALTPEAIAQVIAALLPENAIVVDESITSgRGFFPATAGAA-PHDWLT 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891768 383 -PGafGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALV 438
Cdd:PRK07586 382 lTG--GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVI 436
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
370-515 |
1.82e-05 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 45.73 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 370 HLVQPRGplcWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAgWTQISR 449
Cdd:cd02006 43 HVYKPRH---WINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIR 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622891768 450 EQVPSLGSNVACSLAY------------TEYHKAAMGLGARGLLLSRENEdqVVKVLHDAQQQCRDGH-PVVVNILIGR 515
Cdd:cd02006 119 QAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTKPEE--LAAAFEQAKKLMAEHRvPVVVEAILER 195
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
160-221 |
6.74e-05 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 43.40 E-value: 6.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622891768 160 QASPQQVQRCVEILSRAKRPLMVLGSQALLTPKSADKLRAAVETLGVP-CFLGGMARGLLGRN 221
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
1-103 |
3.01e-04 |
|
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: 41.33 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 1 MARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVR------R 74
Cdd:cd07037 54 LAKASGRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPppedddD 133
|
90 100
....*....|....*....|....*....
gi 1622891768 75 VRDIVPTLRAAMAAAQSGTPGPVFVELPI 103
Cdd:cd07037 134 LWYLLRLANRAVLEALSAPPGPVHLNLPF 162
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
342-511 |
1.42e-03 |
|
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: 39.98 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 342 RVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLCWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSL 421
Cdd:cd02003 3 EVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 422 IEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACSLAY--------------TEYHKAAMGLGARglLLSRENE 487
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDrdqesgqldgallpVDFAANARSLGAR--VEKVKTI 160
|
170 180
....*....|....*....|....
gi 1622891768 488 DQVVKVLHDAQQQCRdghPVVVNI 511
Cdd:cd02003 161 EELKAALAKAKASDR---TTVIVI 181
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
2-102 |
3.26e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 40.61 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891768 2 ARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPVLLLGGAASTLLQNRGALQAIDQLSLFRPLCKFCASVRRVRDIVP- 80
Cdd:PLN02980 359 ARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPa 438
|
90 100
....*....|....*....|....*..
gi 1622891768 81 -----TLRAAMAAAQSGTPGPVFVELP 102
Cdd:PLN02980 439 rmvltTLDSAVHWATSSPCGPVHINCP 465
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
389-415 |
4.92e-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: 39.02 E-value: 4.92e-03
10 20
....*....|....*....|....*..
gi 1622891768 389 LGVGAGFALGAKLCRPDAEVWCLFGDG 415
Cdd:cd02012 111 LSVAVGMALAEKLLGFDYRVYVLLGDG 137
|
|
|