|
Name |
Accession |
Description |
Interval |
E-value |
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
230-403 |
1.02e-66 |
|
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: 209.70 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 230 PVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 309
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 310 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVP--RLGSDVACSLAYTDYHKAAMGLGAQGLILSRdnEDQVVKVLRDG 387
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLsyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTT--PEELKPALKRA 158
|
170
....*....|....*.
gi 1958790128 388 QklcQEGHAVVVNILI 403
Cdd:cd02004 159 L---ASGKPALINVII 171
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
38-369 |
2.53e-66 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 220.36 E-value: 2.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 38 PRPEGPLPLDiPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIR 117
Cdd:PRK05858 176 PGALTELPAG-PTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEA-ALLRLAEELGIPVLMNGMGRGVVPADHPLAFS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 118 QNRSAALKKADVVVLAGAVCDFRLSYGrVLNRKSSIIIVnrnrDDMLLNSDIFWKPQEAVQGDVGSFMIKLVEGLQGQTW 197
Cdd:PRK05858 254 RARGKALGEADVVLVVGVPMDFRLGFG-VFGGTAQLVHV----DDAPPQRAHHRPVAAGLYGDLSAILSALAGAGGDRTD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 198 SSDWVEELRKADQQKEQtyRDKALLP---VPQHlnPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPG 274
Cdd:PRK05858 329 HQGWIEELRTAETAARA--RDAAELAddrDPIH--PMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 275 AFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWtqiSREQVPR---LGSDVAC 351
Cdd:PRK05858 405 PFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW---GLEKHPMealYGYDVAA 481
|
330
....*....|....*....
gi 1958790128 352 SLA-YTDYHKAAMGLGAQG 369
Cdd:PRK05858 482 DLRpGTRYDEVVRALGGHG 500
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
30-407 |
9.45e-63 |
|
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: 211.17 E-value: 9.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 30 NLFAGAWEPRPEGPLPLDI---PQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRG 106
Cdd:COG0028 163 DVQAAEAEEEPAPPELRGYrprPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGA-AEELRALAERLGAPVVTTLMGKG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 107 LLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSYG-RVLNRKSSIIIVNRNRDDMLLNsdifWKPQEAVQ 178
Cdd:COG0028 242 AFPEDHPLylgmlgmHGTPAANEALAEADLVLAVGARFDDRVTGNwDEFAPDAKIIHIDIDPAEIGKN----YPVDLPIV 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 179 GDVGSFMIKLVEGLQGQTWS-SDWVEELRKADQQKEQTYRDKAllpvpQHLNPVRLLQQVEETLPDNALLVVDGGDFVAT 257
Cdd:COG0028 318 GDAKAVLAALLEALEPRADDrAAWLARIAAWRAEYLAAYAADD-----GPIKPQRVIAALREALPDDAIVVTDVGQHQMW 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 258 AAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQI 337
Cdd:COG0028 393 AARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMV 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790128 338 SREQVPRLGSDV-ACSLAYTDYHKAAMGLGAQGLilsR-DNEDQVVKVLRDGQklcQEGHAVVVNILIGRTD 407
Cdd:COG0028 473 RQWQELFYGGRYsGTDLPNPDFAKLAEAFGAKGE---RvETPEELEAALEEAL---ASDGPALIDVRVDPEE 538
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
39-351 |
1.22e-33 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 132.03 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 39 RPEGPLPLDIPqaSPQQVQRCVEILSRAKRPLLVLGSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ 118
Cdd:PRK09259 188 KVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGAAYAQADE-QIREFVEKTGIPFLPMSMAKGLLPDTHPQSAAA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 119 NRSAALKKADVVVLAGAVCDFRLSYGR--VLNRKSSIIIVNRNRDDMLLNSDIfwkpQEAVQGDVGSFMIKLVEGL--QG 194
Cdd:PRK09259 265 ARSLALANADVVLLVGARLNWLLSHGKgkTWGADKKFIQIDIEPQEIDSNRPI----AAPVVGDIGSVMQALLAGLkqNT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 195 QTWSSDWVEELRKADQQKEQTYRDK-ALLPVP-QHLNPVRLLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLD 272
Cdd:PRK09259 341 FKAPAEWLDALAERKEKNAAKMAEKlSTDTQPmNFYNALGAIRDVLKENPD-IYLVNEGANTLDLARNIIDMYKPRHRLD 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 273 PGAFGTLGVGAGFALGAKLC--QPeaeVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGwtqISR--EQVPRLGSD 348
Cdd:PRK09259 420 CGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGG---IYRgdDVNLSGAGD 493
|
...
gi 1958790128 349 VAC 351
Cdd:PRK09259 494 PSP 496
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
33-367 |
7.14e-33 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 129.71 E-value: 7.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 33 AGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNH 112
Cdd:PRK07524 168 APADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGAL---AAAAALRALAERLDAPVALTINAKGLLPAGH 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 113 PLHIRQNRS-----AALKKADVVVLAG---AVCDFRLSYGRVLNRKSSIIIVnrNRDDMLLNSdiFWKPQEAVQGDVGSF 184
Cdd:PRK07524 245 PLLLGASQSlpavrALIAEADVVLAVGtelGETDYDVYFDGGFPLPGELIRI--DIDPDQLAR--NYPPALALVGDARAA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 185 MIKLVEGLQGQTWSSDW----VEELRKAdQQKEQTyrdkallpvPQHLNPVRLLQQVEETLPDnALLVVDGGDFVATAAY 260
Cdd:PRK07524 321 LEALLARLPGQAAAADWgaarVAALRQA-LRAEWD---------PLTAAQVALLDTILAALPD-AIFVGDSTQPVYAGNL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 261 LVQPRGPLRWLD-PGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISR 339
Cdd:PRK07524 390 YFDADAPRRWFNaSTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR 469
|
330 340
....*....|....*....|....*...
gi 1958790128 340 EQVPRLGSDVACSLAYTDYHKAAMGLGA 367
Cdd:PRK07524 470 YMVARDIEPVGVDPYTPDFIALARAFGC 497
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
250-401 |
3.25e-29 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 111.14 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 250 DGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVG 329
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790128 330 NDAGWTQISREQVP----RLGSDVACSLAYTDYHKAAMGLGAQGliLSRDNEDQVVKVLRDGQKlcqEGHAVVVNI 401
Cdd:pfam02775 81 NNGGYGMTRGQQTPfgggRYSGPSGKILPPVDFAKLAEAYGAKG--ARVESPEELEEALKEALE---HDGPALIDV 151
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
43-405 |
1.42e-27 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 114.71 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 43 PLPLDIPQASPQQVQRCVEILSRAKRPLLVLG-----SQALlpptpaNKLRAAVETLGVPCFLGGMSRGLLGRNHPLH-- 115
Cdd:PRK07525 177 PVRLERGAGGEQSLAEAAELLSEAKFPVILSGagvvlSDAI------EECKALAERLDAPVACGYLHNDAFPGSHPLWvg 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 116 -IRQNRSAA----LKKADVVVLAGAvcdfRLSYGRVLN--------RKSSIIIVNRNRDDMLLNsdifwKPQE-AVQGDV 181
Cdd:PRK07525 251 pLGYNGSKAamelIAKADVVLALGT----RLNPFGTLPqygidywpKDAKIIQVDINPDRIGLT-----KKVSvGICGDA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 182 GSFMIKLVEGLQGQTWS---------------SDWVEELRKADQQKEQ---TYRDKALLPVPQHLNPVRLLQQVEETLPD 243
Cdd:PRK07525 322 KAVARELLARLAERLAGdagreerkaliaaekSAWEQELSSWDHEDDDpgtDWNEEARARKPDYMHPRQALREIQKALPE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 244 NALLVVDGGDFVATA-AYLvQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKV 322
Cdd:PRK07525 402 DAIVSTDIGNNCSIAnSYL-RFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNW 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 323 PVIALVGNDAGWTQISREQVPRLGSD-VACSL-AYTDYHKAAMGLGAQGLILsrDNEDQVVKVLRDGQKLCQEGHAVVVN 400
Cdd:PRK07525 481 PVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNVSYAGIAEAMGAEGVVV--DTQEELGPALKRAIDAQNEGKTTVIE 558
|
....*
gi 1958790128 401 ILIGR 405
Cdd:PRK07525 559 IMCNQ 563
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
232-377 |
3.03e-26 |
|
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: 103.49 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 232 RLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 311
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958790128 312 IEFDTFVRHKVPVIALVGNDAGWTQISREQVPRL-GSDVACSLAYTDYHKAAMGLGAQGLILSRDNE 377
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDPED 147
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
225-406 |
1.50e-25 |
|
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: 102.59 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 225 PQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 304
Cdd:cd02013 1 GNPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 305 GAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSD-VACSLAYTDYHKAAMGLGAQGLILsrDNEDQVVKV 383
Cdd:cd02013 81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITV--DKPEDVGPA 158
|
170 180
....*....|....*....|...
gi 1958790128 384 LRDGQKLCQEGHAVVVNILIGRT 406
Cdd:cd02013 159 LQKAIAMMAEGKTTVIEIVCDQE 181
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
228-369 |
1.47e-22 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 93.75 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 228 LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 307
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790128 308 GYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQG 369
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKG 143
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
39-331 |
2.53e-22 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 99.02 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 39 RPeGPLPLDIPQ-------------------------ASPQQVQRCVEILSRAKRPLLVLGSQALLPpTPANKLRAAVET 93
Cdd:PRK08527 152 RP-GPVHIDIPKdvtatlgefeypkeislktykptykGNSRQIKKAAEAIKEAKKPLFYLGGGAILS-NASEEIRELVKK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 94 LGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRLSyGRV--LNRKSSIIIVNRNRDDM- 163
Cdd:PRK08527 230 TGIPAVETLMARGVLRSDDPLllgmlgmHGSYAANMAMSECDLLISLGARFDDRVT-GKLseFAKHAKIIHVDIDPSSIs 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 164 -LLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQTWS--SDWVEELRKADQQKEQTYRDKALLPVPQHLnpvrlLQQVEET 240
Cdd:PRK08527 309 kIVNADY------PIVGDLKNVLKEMLEELKEENPTtyKEWREILKRYNELHPLSYEDSDEVLKPQWV-----IERVGEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 241 LPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRH 320
Cdd:PRK08527 378 LGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEY 457
|
330
....*....|.
gi 1958790128 321 KVPVIALVGND 331
Cdd:PRK08527 458 KIPVINIILNN 468
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
35-369 |
6.08e-22 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 97.98 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 35 AWEPRPEGPLPLD---IPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRN 111
Cdd:PRK08322 162 AAEETDGKPLPRSysrRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTA-SKALTEFVDKTGIPFFTTQMGKGVIPET 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 112 HP-------LHIRQNRSAALKKADVVVLAGavcdfrlsYGRV------LNRKSSIIIVNRNRDDMLLNSDIFwkPQEAVQ 178
Cdd:PRK08322 241 HPlslgtagLSQGDYVHCAIEHADLIINVG--------HDVIekppffMNPNGDKKVIHINFLPAEVDPVYF--PQVEVV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 179 GDVGSFMIKLVEGL-QGQTWSSDWVEELRKA-DQQKEQTYRDKALLPVPQhlnpvRLLQQVEETLPDNALLVVDGGDFVA 256
Cdd:PRK08322 311 GDIANSLWQLKERLaDQPHWDFPRFLKIREAiEAHLEEGADDDRFPMKPQ-----RIVADLRKVMPDDDIVILDNGAYKI 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 257 TAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQ 336
Cdd:PRK08322 386 WFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGM 465
|
330 340 350
....*....|....*....|....*....|...
gi 1958790128 337 ISREQVPRLGSDVACSLAYTDYHKAAMGLGAQG 369
Cdd:PRK08322 466 IRWKQENMGFEDFGLDFGNPDFVKYAESYGAKG 498
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
38-389 |
8.39e-21 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 94.44 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 38 PRPE--GPLPLDIPQASPQQVQRCVEILSRAKRPLLVLG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGR 110
Cdd:PRK06112 183 PRSNslGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGggvhiSGA------SAALAALQSLAGLPVATTNMGKGAVDE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 111 NHPLHI------------RQNRSAALKKADVVVLAGAVCDFRLSYGRVLNRKSSIII--------VNRNRDDMLLNSDif 170
Cdd:PRK06112 257 THPLSLgvvgslmgprspGRHLRDLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIhidvdgeeVGRNYEALRLVGD-- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 171 wkPQEAVQGdvgsfmikLVEGLQGQTWS---------SDWVEELRKADQQKEQTYRDKALLPVpqhlNPVRLLQQVEETL 241
Cdd:PRK06112 335 --ARLTLAA--------LTDALRGRDLAaragrraalEPAIAAGREAHREDSAPVALSDASPI----RPERIMAELQAVL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 242 PDNALLVVDGG-DFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRH 320
Cdd:PRK06112 401 TGDTIVVADASySSIWVANFLTARRAGMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRM 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790128 321 KVPVIALVGNDA--GWtQISREQVpRLGSDV-ACSLAYTDYHKAAMGLGAQGLILSRdnEDQVVKVLRDGQK 389
Cdd:PRK06112 481 GVPVTIVVLNNGilGF-QKHAETV-KFGTHTdACHFAAVDHAAIARACGCDGVRVED--PAELAQALAAAMA 548
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
30-369 |
2.07e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 93.15 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 30 NLFAGAWEPRPEGPL-PLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALlppTPANKLRAAVETLGVPC--FLGGmsRG 106
Cdd:PRK08266 168 DVFGQRAPVAAAPPLrPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAA---GAGEEIRELAEMLQAPVvaFRSG--RG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 107 LLGRNHPLHirQNRSAA---LKKADVVVLAGAVCDFRLSYGRVLNRKSSIIIVNRNRDDMllnsdIFWKPQEAVQGDVGS 183
Cdd:PRK08266 243 IVSDRHPLG--LNFAAAyelWPQTDVVIGIGSRLELPTFRWPWRPDGLKVIRIDIDPTEM-----RRLKPDVAIVADAKA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 184 FMIKLVEGLQGQ-TWSSDWVEELRKADQQKEQtyRDKALLPVPQHLNPVRllqqveETLPDNALlVVDGGDFVATAAYLV 262
Cdd:PRK08266 316 GTAALLDALSKAgSKRPSRRAELRELKAAARQ--RIQAVQPQASYLRAIR------EALPDDGI-FVDELSQVGFASWFA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 263 QP-RGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREQ 341
Cdd:PRK08266 387 FPvYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQ 466
|
330 340
....*....|....*....|....*....
gi 1958790128 342 VPRL-GSDVACSLAYTDYHKAAMGLGAQG 369
Cdd:PRK08266 467 KRRFgGRVVASDLVNPDFVKLAESFGVAA 495
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
40-332 |
3.61e-20 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 92.46 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 40 PEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL----- 114
Cdd:PRK08155 185 PAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELA-EKAQLPTTMTLMALGMLPKAHPLslgml 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 115 --HIRQNRSAALKKADVVVLAGAVCDFRlSYGRV--LNRKSSIIIVNRNRDDMllnsDIFWKPQEAVQGDVGSFMIKLVE 190
Cdd:PRK08155 264 gmHGARSTNYILQEADLLIVLGARFDDR-AIGKTeqFCPNAKIIHVDIDRAEL----GKIKQPHVAIQADVDDVLAQLLP 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 191 GLQGQTwSSDWVEelRKADQQKEQTyrdkalLPVPQHLNPVR---LLQQVEETLPDNALLVVDGGD---FVATAAYLVQP 264
Cdd:PRK08155 339 LVEAQP-RAEWHQ--LVADLQREFP------CPIPKADDPLShygLINAVAACVDDNAIITTDVGQhqmWTAQAYPLNRP 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790128 265 RgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGNDA 332
Cdd:PRK08155 410 R---QWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVkIILMNNEA 475
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
37-405 |
3.90e-20 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 92.57 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 37 EPRPEGPL-----PLDIPQASPQQVQRCVEILSRAKRPLLVLGsQALLPPTPANKLRAAVETLGVPCF--LGGMSRglLG 109
Cdd:PRK06154 180 EELDELPLdhrpsRRSRPGADPVEVVEAAALLLAAERPVIYAG-QGVLYAQATPELKELAELLEIPVMttLNGKSA--FP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 110 RNHPLHIRQNRSAA-------LKKADVVVLAGavCDF-RLSYGRVLNRKSSIIIVNRnrDDMLLNSDIFWKpqEAVQGDV 181
Cdd:PRK06154 257 EDHPLALGSGGRARpatvahfLREADVLFGIG--CSLtRSYYGLPMPEGKTIIHSTL--DDADLNKDYPID--HGLVGDA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 182 GSFMIKLVEGLQGQTW-----SSDWVEELRKADQQKEQTYRDKaLLPVPQHLNPVRLLQQVEETL-PDNALLVVDGG--- 252
Cdd:PRK06154 331 ALVLKQMIEELRRRVGpdrgrAQQVAAEIEAVRAAWLAKWMPK-LTSDSTPINPYRVVWELQHAVdIKTVIITHDAGspr 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 253 DFVATAAYLVQPRGPLRWldpGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDa 332
Cdd:PRK06154 410 DQLSPFYVASRPGSYLGW---GKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNN- 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958790128 333 GWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSRdnEDQVVKVLRDGQKLCQEGHAVVVNILIGR 405
Cdd:PRK06154 486 FSMGGYDKVMPVSTTKYRATDISGDYAAIARALGGYGERVED--PEMLVPALLRALRKVKEGTPALLEVITSE 556
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
53-377 |
2.73e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 86.75 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 53 PQQVQRCVEILSRAKRPLL-----VLGSQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHI-------RQNR 120
Cdd:PRK06048 194 PQQIKRAAELIMKAERPIIyagggVISSNA------SEELVELAETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 121 SAALKKADVVVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQTWSsD 200
Cdd:PRK06048 268 NYAIQESDLIIAVGARFDDRVT-GKLASFAPNAKIIHIDIDPAEISKNV--KVDVPIVGDAKQVLKSLIKYVQYCDRK-E 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 201 WVEELRKADQQKEQTYRDKALLPVPQHLnpvrlLQQVEETLPDnALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLG 280
Cdd:PRK06048 344 WLDKINQWKKEYPLKYKEREDVIKPQYV-----IEQIYELCPD-AIIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMG 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 281 VGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQISREQvpRLGSdvACSLA 354
Cdd:PRK06048 418 YGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGylgmvrQWQELFYDK--RYSH--TCIKG 493
|
330 340
....*....|....*....|...
gi 1958790128 355 YTDYHKAAMGLGAQGLILSRDNE 377
Cdd:PRK06048 494 SVDFVKLAEAYGALGLRVEKPSE 516
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
38-334 |
4.03e-17 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 83.12 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 38 PRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALlppTPANKLRAAVEtLGVPCFLGGMSRGLLGRNHPLHIR 117
Cdd:PRK07064 175 PDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGAR---HAGAEVKRLVD-LGFGVVTSTQGRGVVPEDHPASLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 118 Q-NRSAA----LKKADVVVLAGAvcDFR----LSYGRVLNRKSSIIIVNRNRDDMLLNSDIFwkpqeaVQGDVGSFMIKL 188
Cdd:PRK07064 251 AfNNSAAvealYKTCDLLLVVGS--RLRgnetLKYSLALPRPLIRVDADAAADGRGYPNDLF------VHGDAARVLARL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 189 VEGLQGQTW-SSDWVEELRKADQQKEQTYRDKallpvpqhLNPVRLL-QQVEETLPDNALLVVDggdfvATAA------Y 260
Cdd:PRK07064 323 ADRLEGRLSvDPAFAADLRAAREAAVADLRKG--------LGPYAKLvDALRAALPRDGNWVRD-----VTISnstwgnR 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958790128 261 LVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 334
Cdd:PRK07064 390 LLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
56-188 |
4.80e-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: 77.22 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 56 VQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKAD 128
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGA-SEELRELAEKLGIPVVTTLMGKGAFPEDHPLylgmlgmHGTPAANEALEEAD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790128 129 VVVLAGAVCDFRLSYGRV--LNRKSSIIIVNRNRDDMLLNSdifwKPQEAVQGDVGSFMIKL 188
Cdd:pfam00205 80 LVLAVGARFDDIRTTGKLpeFAPDAKIIHIDIDPAEIGKNY----PVDVPIVGDAKETLEAL 137
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
49-398 |
5.97e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 82.71 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 49 PQASPQQVQRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRS 121
Cdd:PRK06725 197 PRPDSMKLREVAKAISKAKRPLLYIGG-GVIHSGGSEELIEFARENRIPVVSTLMGLGAYPPGDPLflgmlgmHGTYAAN 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 122 AALKKADVVVLAGAVCDFRLSyGRV--LNRKSSIIIVNRNRDDMLLNSDIfwkpQEAVQGDVGSFMIKLVEgLQGQTWSS 199
Cdd:PRK06725 276 MAVTECDLLLALGVRFDDRVT-GKLelFSPHSKKVHIDIDPSEFHKNVAV----EYPVVGDVKKALHMLLH-MSIHTQTD 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 200 DWVEELRKADQQKEQTYRDKallpvPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTL 279
Cdd:PRK06725 350 EWLQKVKTWKEEYPLSYKQK-----ESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTM 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 280 GVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDA------GWTQI---SREQVPRLGSdva 350
Cdd:PRK06725 425 GFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKflgmvrQWQEMfyeNRLSESKIGS--- 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958790128 351 cslayTDYHKAAMGLGAQGliLSRDNEDQVVKVLRDGqkLCQEGHAVV 398
Cdd:PRK06725 502 -----PDFVKVAEAYGVKG--LRATNSTEAKQVMLEA--FAHEGPVVV 540
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
36-369 |
8.99e-17 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 82.19 E-value: 8.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 36 WEPRPEGPLPLDIPQ-ASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHPL 114
Cdd:PRK06456 176 WPEKPLVKGYRDFPTrIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELA-ELLHIPIVSTFPGKTAIPHDHPL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 115 HI-------RQNRSAALKKADVVVLAGAVCDFRL--SYGRVLNRKSSIIIVNRNRDDmllnSDIFWKPQEAVQGDVGSF- 184
Cdd:PRK06456 255 YFgpmgyygRAEASMAALESDAMLVVGARFSDRTftSYDEMVETRKKFIMVNIDPTD----GEKAIKVDVGIYGNAKIIl 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 185 --MIKLVEGLQGQTWSSDWVEELRKADQQKEQTYRDKAllpvPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLV 262
Cdd:PRK06456 331 reLIKAITELGQKRDRSAWLKRVKEYKEYYSQFYYTEE----NGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFW 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 263 QPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVgNDAGWTQISReQV 342
Cdd:PRK06456 407 EVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVI-FDNRTLGLVR-QV 484
|
330 340 350
....*....|....*....|....*....|....
gi 1958790128 343 PRL-------GSDVACSlayTDYHKAAMGLGAQG 369
Cdd:PRK06456 485 QDLffgkrivGVDYGPS---PDFVKLAEAFGALG 515
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
16-340 |
2.05e-16 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 81.25 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 16 MGRVVvwylqnclANLFAGAWEPRPeGPLPLDIP---------------------------QASPQQVQRCVEILSRAKR 68
Cdd:PRK07418 156 MARIV--------AEAFHIASSGRP-GPVLIDIPkdvgqeefdyvpvepgsvkppgyrptvKGNPRQINAALKLIEEAER 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 69 PLLVLGSQALLPPTPANkLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKADVVVLAGAVCDFRL 141
Cdd:PRK07418 227 PLLYVGGGAISAGAHAE-LKELAERFQIPVTTTLMGKGAFDEHHPLsvgmlgmHGTAYANFAVTECDLLIAVGARFDDRV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 142 --------SYGRVLNrkssIII----VNRNRddmllnsdifwKPQEAVQGDVGSFMIKLVEGLQGQTWS---SDWVEELr 206
Cdd:PRK07418 306 tgkldefaSRAKVIH----IDIdpaeVGKNR-----------RPDVPIVGDVRKVLVKLLERSLEPTTPprtQAWLERI- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 207 kadqqkeQTYRDKALLPVPQH---LNPVRLLQQVEETLPDnALLVVDGGDFVATAA-YLvqPRGPLRWLDPGAFGTLGVG 282
Cdd:PRK07418 370 -------NRWKQDYPLVVPPYegeIYPQEVLLAVRDLAPD-AYYTTDVGQHQMWAAqFL--RNGPRRWISSAGLGTMGFG 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958790128 283 AGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDaGWTQISRE 340
Cdd:PRK07418 440 MPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINN-GWQGMVRQ 496
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
45-410 |
2.12e-16 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 81.05 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 45 PLDIPQ---ASPQQVQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCF-----LGGMSRGL--------- 107
Cdd:PRK08617 177 PLSKPKlgpASPEDINYLAELIKNAKLPVLLLGMRASSPEV-TAAIRRLLERTNLPVVetfqaAGVISRELedhffgrvg 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 108 LGRNHP---LhirqnrsaaLKKADVVVLAGavcdfrlsYG------RVLNRKSSIIIVNRnrDDMLLNSDIFWKPQEAVQ 178
Cdd:PRK08617 256 LFRNQPgdeL---------LKKADLVITIG--------YDpieyepRNWNSEGDATIIHI--DVLPAEIDNYYQPERELI 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 179 GDVGSFMIKLVEGLQGQTWSSDWVEELRKADQQKEQtyRDKALLPVPQHL-NPVRLLQQVEETLPDNALLVVDGGDF--- 254
Cdd:PRK08617 317 GDIAATLDLLAEKLDGLSLSPQSLEILEELRAQLEE--LAERPARLEEGAvHPLRIIRALQDIVTDDTTVTVDVGSHyiw 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 255 VATAAYLVQPRGPLrwldpgaFG----TLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGN 330
Cdd:PRK08617 395 MARYFRSYEPRHLL-------FSngmqTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWN 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 331 DAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGliLSRDNEDQVVKVLRDGqkLCQEGhAVVVNILIgrtDFRD 410
Cdd:PRK08617 468 DGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKG--LRVTSPDELEPVLREA--LATDG-PVVIDIPV---DYSD 539
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
53-328 |
1.11e-15 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 79.03 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 53 PQQVQRCVEILSRAKRPLLVLGSQALLppTPANK-LRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAAL 124
Cdd:PRK06276 190 PLQIKKAAELIAEAERPVILAGGGVII--SGASEeLIELSELVKIPVCTTLMGKGAFPEDHPLalgmvgmHGTKAANYSV 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 125 KKADVVVLAGavCDFRlsyGRVLNRKSSIIivnrnRDDMLLNSDIfwKPQE---------AVQGDVGSFMIKLVEGLQGQ 195
Cdd:PRK06276 268 TESDVLIAIG--CRFS---DRTTGDISSFA-----PNAKIIHIDI--DPAEigknvrvdvPIVGDAKNVLRDLLAELMKK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 196 TWSSD--WVEELR--KADQQKEQTYRDKALlpVPQHLnpVRLLQQV--EETLPDNALLVVDGGDFVATAAYLVQPRGPLR 269
Cdd:PRK06276 336 EIKNKseWLERVKklKKESIPRMDFDDKPI--KPQRV--IKELMEVlrEIDPSKNTIITTDVGQNQMWMAHFFKTSAPRS 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958790128 270 WLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALV 328
Cdd:PRK06276 412 FISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
45-337 |
1.22e-15 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 78.76 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 45 PLDIPQASP--QQVQRCVEILSRAKRPLLVLG-----SQAllpptpANKLRAAVETLGVPCFLGGMSRGLLGRNHPLH-- 115
Cdd:PRK08199 181 PYRRVAAAPgaADLARLAELLARAERPLVILGgsgwtEAA------VADLRAFAERWGLPVACAFRRQDLFDNRHPNYag 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 116 ---IRQNRS--AALKKADVVVLAGAvcdfRLsyGRVLNRKSSIIIVNRNRDdMLLNSDI-------FWKPQEAVQGDVGS 183
Cdd:PRK08199 255 dlgLGINPAlaARIREADLVLAVGT----RL--GEVTTQGYTLLDIPVPRQ-TLVHVHPdaeelgrVYRPDLAIVADPAA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 184 F--MIKLVEGLQGQTWSsDWVEELRkadqqkeQTYRD-KALLPVPQHLNPVRLLQQVEETLPDNALLVVDGGDFvatAAY 260
Cdd:PRK08199 328 FaaALAALEPPASPAWA-EWTAAAH-------ADYLAwSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNY---ATW 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 261 L---VQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQI 337
Cdd:PRK08199 397 LhrfFRFRRYRTQLAPTS-GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTI 475
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
230-399 |
1.34e-15 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 74.25 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 230 PVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGY 309
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 310 SLIEFDTFVRHKVPVIALVGNDAGWTQISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILSrdNEDQVVKVLRDGqk 389
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIE--SADDLLPVLERA-- 156
|
170
....*....|
gi 1958790128 390 LCQEGHAVVV 399
Cdd:cd02010 157 LAADGVHVID 166
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
37-377 |
3.32e-15 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 77.18 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 37 EPRPEGPLPLDIPQASPQqVQRCVEILSRAKRPLLVLGSQALLPPTPANKLraaVETLGVPCF----------------L 100
Cdd:PRK06457 167 EYKGSKNTEVGKVKYSID-FSRAKELIKESEKPVLLIGGGTRGLGKEINRF---AEKIGAPIIytlngkgilpdldpkvM 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 101 GGMsrGLLGRNHPLhirqnrsAALKKADVVVLAGAVcdfrLSYGRVLNRKSSIIIVNRNRDDM--LLNSDIfwkpqeAVQ 178
Cdd:PRK06457 243 GGI--GLLGTKPSI-------EAMDKADLLIMLGTS----FPYVNFLNKSAKVIQVDIDNSNIgkRLDVDL------SYP 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 179 GDVGSFMI--------KLVEGLQGQtwSSDWVEELRKADQQkeqtyRDKALlpvpqhlNPVRLLQQVEETLPDNALLVVD 250
Cdd:PRK06457 304 IPVAEFLNidieeksdKFYEELKGK--KEDWLDSISKQENS-----LDKPM-------KPQRVAYIVSQKCKKDAVIVTD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 251 GGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLC-QPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVG 329
Cdd:PRK06457 370 TGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIY 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958790128 330 NDAGWTQISREQ----VPRLGSDvacsLAYTDYHKAAMGLGAQGLILSRDNE 377
Cdd:PRK06457 450 NNSKLGMIKFEQevmgYPEWGVD----LYNPDFTKIAESIGFKGFRLEEPKE 497
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
39-390 |
3.96e-15 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 77.15 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 39 RPeGPLPLDIPQ---------ASPQ----------------QVQRCVEILSRAKRPLLVLGSQALLPpTPANKLRAAVET 93
Cdd:PRK06965 170 RP-GPVVVDIPKdvsktpceyEYPKsvemrsynpvtkghsgQIRKAVSLLLSAKRPYIYTGGGVILA-NASRELRQLADL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 94 LGVPCF-----LGGMSR------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRL----SYGRVLNRKSSIIIVNR 158
Cdd:PRK06965 248 LGYPVTntlmgLGAYPAsdkkflGMLG----MHGTYEANMAMQHCDVLIAIGARFDDRVignpAHFASRPRKIIHIDIDP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 159 NRDDMLLNSDIfwkpqeAVQGDVGSFMIKLVEGLQ-----------GQTWSSdwVEELRKADQQKeqtYRDKALLPVPQH 227
Cdd:PRK06965 324 SSISKRVKVDI------PIVGDVKEVLKELIEQLQtaehgpdadalAQWWKQ--IEGWRSRDCLK---YDRESEIIKPQY 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 228 lnpvrllqqVEETLPD----NALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFG 303
Cdd:PRK06965 393 ---------VVEKLWEltdgDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITG 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 304 DGAFGYSLIEFDTFVRHKVPV--IAL----VGNDAGWTQIsrEQVPRLGSDVACSLAytDYHKAAMGLGAQGLILSRDNE 377
Cdd:PRK06965 464 EGSIQMCIQELSTCLQYDTPVkiISLnnryLGMVRQWQEI--EYSKRYSHSYMDALP--DFVKLAEAYGHVGMRIEKTSD 539
|
410
....*....|...
gi 1958790128 378 dqVVKVLRDGQKL 390
Cdd:PRK06965 540 --VEPALREALRL 550
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
38-335 |
1.13e-14 |
|
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: 75.58 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 38 PRPEGPLPLDIPQASPQQVQRCV----EILSRAKRPLLVLGSQAL---LpptpANKLRAAVETLGVPCFLGGMSRGLLGR 110
Cdd:COG3961 177 EPPEAPLPLPPPASDPAALAAAVaaaaERLAKAKRPVILAGVEVHrfgL----QEELLALAEKTGIPVATTLLGKSVLDE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 111 NHPLHI--------RQNRSAALKKADVVVLAGAV-CDFRL-SYGRVLNRKSSIIIvnrNRDDMLLNSDIFwkpqEAVQgd 180
Cdd:COG3961 253 SHPQFIgtyagaasSPEVREYVENADCVLCLGVVfTDTNTgGFTAQLDPERTIDI---QPDSVRVGGHIY----PGVS-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 181 vgsfMIKLVEGLqgqtwssdwVEELRKADQQKEQTYRDKALLPVP--QHLNPVRLLQQVEETLPDNALLVVDGGD--FVA 256
Cdd:COG3961 324 ----LADFLEAL---------AELLKKRSAPLPAPAPPPPPPPAApdAPLTQDRLWQRLQAFLDPGDIVVADTGTslFGA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 257 TAAYLvqPRGpLRWLDPGAFGTLG--VGAgfALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGW 334
Cdd:COG3961 391 ADLRL--PEG-ATFIAQPLWGSIGytLPA--ALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGY 465
|
.
gi 1958790128 335 T 335
Cdd:COG3961 466 T 466
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
37-334 |
5.25e-14 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 73.50 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 37 EPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLV---LGSQALLPPTpankLRAAVETLGVPCFLGGMSRGLLGRNHP 113
Cdd:PRK08327 191 KADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIItwrAGRTAEGFAS----LRRLAEELAIPVVEYAGEVVNYPSDHP 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 114 LHIRQNRSAALKKADVVVLAGAVCDFRLSYGRvLNRKSSIIIVnrnrDDMLLNSDI-FWK-PQE-AVQGDVGSFMIKLVE 190
Cdd:PRK08327 267 LHLGPDPRADLAEADLVLVVDSDVPWIPKKIR-PDADARVIQI----DVDPLKSRIpLWGfPCDlCIQADTSTALDQLEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 191 GLQGQTWSSDWVEELRKADQQKEQTYRDKALLPVPQHL------NPVRLLQQVEETLPDNALLVVDGGdFVATAAYLvqp 264
Cdd:PRK08327 342 RLKSLASAERRRARRRRAAVRELRIRQEAAKRAEIERLkdrgpiTPAYLSYCLGEVADEYDAIVTEYP-FVPRQARL--- 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958790128 265 RGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFV--RHKVPVIALVGNDAGW 334
Cdd:PRK08327 418 NKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEAAHWVaeRYGLPVLVVVFNNGGW 489
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
45-331 |
7.98e-14 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 73.26 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 45 PLDIPQASPQ------QVQRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL---- 114
Cdd:PRK07710 188 QMDLPGYQPNyepnllQIRKLVQAVSVAKKPVILAGA-GVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADHPLflgm 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 115 ---HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEG 191
Cdd:PRK07710 267 agmHGTYTANMALYECDLLINIGARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNV--PTEIPIVADAKQALQVLLQQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 192 LQGQTWSSDWVEELRKADQQKEQTYRDKAllpvpQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWL 271
Cdd:PRK07710 344 EGKKENHHEWLSLLKNWKEKYPLSYKRNS-----ESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFKTPDKWV 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 272 DPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 331
Cdd:PRK07710 419 TSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
40-330 |
1.06e-13 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 72.55 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 40 PEGPLPLDIPQASPQ--QVQRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL--- 114
Cdd:PRK07282 182 PEVNLPSYQPTLEPNdmQIKKILKQLSKAKKPVILAGG-GINYAEAATELNAFAERYQIPVVTTLLGQGTIATSHPLflg 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 115 ----HIRQNRSAALKKADVVVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVE 190
Cdd:PRK07282 261 mggmHGSYAANIAMTEADFMINIGSRFDDRLT-GNPKTFAKNAKVAHIDIDPAEIGKII--KTDIPVVGDAKKALQMLLA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 191 GLQGQTWSSDWVEELRKaDQQKEQTYRDKALLPVPQHLnpvrlLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRW 270
Cdd:PRK07282 338 EPTVHNNTEKWIEKVTK-DKNRVRSYDKKERVVQPQAV-----IERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNERQL 411
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958790128 271 LDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 330
Cdd:PRK07282 412 VTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIkVVMLNN 472
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
228-403 |
1.88e-13 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 68.01 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 228 LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAfGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 307
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 308 GYSLIEFDTFVRHKVPVIALVGNDAGWtQISREQVPRLGSDVACSLAY---------TDYHKAAMGLGAQGLILSRDNEd 378
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGY-GALRSFLKRVGPEGPGENAPdgldlldpgIDFAAIAKAFGVEAERVETPEE- 157
|
170 180
....*....|....*....|....*
gi 1958790128 379 qVVKVLRDGQklcQEGHAVVVNILI 403
Cdd:cd02002 158 -LDEALREAL---AEGGPALIEVVV 178
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
35-330 |
2.32e-13 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 71.55 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 35 AWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPAnKLRAAVETLGVPCFLGGMSRGLLGRNHPL 114
Cdd:PRK07789 200 SWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASA-ELRELAELTGIPVVTTLMARGAFPDSHPQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 115 HIRQ-------NRSAALKKADVVVLAGAVCDfrlsyGRVLNRKSSI-----II--------VNRNRddmllNSDIFwkpq 174
Cdd:PRK07789 279 HLGMpgmhgtvAAVAALQRSDLLIALGARFD-----DRVTGKLDSFapdakVIhadidpaeIGKNR-----HADVP---- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 175 eaVQGDVGSFMIKLVEGLQ------GQTWSSDWVEELRKADQQKEQTYRDkallPVPQHLNPVRLLQQVEETLPDNALLV 248
Cdd:PRK07789 345 --IVGDVKEVIAELIAALRaehaagGKPDLTAWWAYLDGWRETYPLGYDE----PSDGSLAPQYVIERLGEIAGPDAIYV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 249 VDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IAL 327
Cdd:PRK07789 419 AGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIkVAL 498
|
...
gi 1958790128 328 VGN 330
Cdd:PRK07789 499 INN 501
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
36-405 |
7.40e-13 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 70.01 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 36 WEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSqALLPPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPL- 114
Cdd:PRK11269 173 FDPDTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGG-GVINADASDLLVEFAELTGVPVIPTLMGWGAIPDDHPLm 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 115 ---------HIRQNrsAALKKADVVVLAGAvcdfrlsygRVLNRKSSIIIVNRnRDDMLLNSDI-------FWKPQEAVQ 178
Cdd:PRK11269 252 agmvglqtsHRYGN--ATLLASDFVLGIGN---------RWANRHTGSVEVYT-KGRKFVHVDIeptqigrVFGPDLGIV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 179 GDVGSFMIKLVEGLQGQTWS------SDWVEEL--RKADQQKEQTYRDkallpVPqhLNPVRLLQQVEETLPDNALLVVD 250
Cdd:PRK11269 320 SDAKAALELLVEVAREWKAAgrlpdrSAWVADCqeRKRTLLRKTHFDN-----VP--IKPQRVYEEMNKAFGRDTCYVST 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 251 GGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGN 330
Cdd:PRK11269 393 IGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVN 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 331 DAGWTQISREQVPrLGSDVACSLAY------------TDYHKAAMGLGAQGLILSRDNEdqVVKVLRDGQKLCQEGHA-V 397
Cdd:PRK11269 473 NAYLGLIRQAQRA-FDMDYCVQLAFeninspelngygVDHVKVAEGLGCKAIRVFKPED--IAPALEQAKALMAEFRVpV 549
|
....*...
gi 1958790128 398 VVNILIGR 405
Cdd:PRK11269 550 VVEVILER 557
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
232-407 |
1.47e-12 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 65.63 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 232 RLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGpLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSL 311
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKG-TRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 312 IEFDTFVRHKVPVIALVGNDAGWT---QISREQVPrlgsdvacslaYTD-----YHKAAMGLGAQGLILSRD--NEDQVV 381
Cdd:cd02005 85 QELSTMIRYGLNPIIFLINNDGYTierAIHGPEAS-----------YNDianwnYTKLPEVFGGGGGGLSFRvkTEGELD 153
|
170 180
....*....|....*....|....*.
gi 1958790128 382 KVLRDGQKLCqeGHAVVVNILIGRTD 407
Cdd:cd02005 154 EALKDALFNR--DKLSLIEVILPKDD 177
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
228-330 |
5.29e-12 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 64.06 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 228 LNPVRLLQQVEETLPDNALLVVDGGD---FVATAAYLVQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 304
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQhqmWAAQYYRFKKPR---SWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGD 77
|
90 100
....*....|....*....|....*.
gi 1958790128 305 GAFGYSLIEFDTFVRHKVPVIALVGN 330
Cdd:cd02015 78 GSFQMNIQELATAAQYNLPVKIVILN 103
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
45-378 |
1.29e-11 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 66.18 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 45 PLDIPQASPQQVQRCVEILSRAKRPLLVLGSQAllpPTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-----N 119
Cdd:PRK08611 182 RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGA---KHAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNlgkigT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 120 RSA--ALKKADVVVLAGAvcDFrlSYGRVLNRKSSIIIVNRNRDDM--LLNSDIfwkpqeAVQGDVGSFM------IKLV 189
Cdd:PRK08611 259 KPAyeAMQEADLLIMVGT--NY--PYVDYLPKKAKAIQIDTDPANIgkRYPVNV------GLVGDAKKALhqltenIKHV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 190 EG---LQG-----QTWSSdWVEElrkaDQQKEQTyrdkallpvPqhLNPVRLLQQVEETLPDNALLVVD-GGDFVATAAY 260
Cdd:PRK08611 329 EDrrfLEAcqenmAKWWK-WMEE----DENNAST---------P--IKPERVMAAIQKIADDDAVLSVDvGTVTVWSARY 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 261 L-VQPRGPL---RWLdpgafGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQ 336
Cdd:PRK08611 393 LnLGTNQKFiisSWL-----GTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAF 467
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958790128 337 ISREQVPRLGSDVACSLAYTDYHKAAMGLGAQGLILsRDNED 378
Cdd:PRK08611 468 IKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYRV-EKAEE 508
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
28-330 |
1.72e-11 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 65.67 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 28 LANLFAGAWEPRPeGPLPLDIP---------------------QASPQQVQRCVEILSRAKRPLLVLG-----SQAllpp 81
Cdd:PRK08978 138 MAEAFEIASSGRP-GPVLVDIPkdiqlaegelephlttvenepAFPAAELEQARALLAQAKKPVLYVGggvgmAGA---- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 82 TPAnkLRAAVETLGVP--CFLGGMsrGLLGRNHP-----LHIRQNRSA--ALKKADVVVLAGAVCDFRLSyGRvLNR--- 149
Cdd:PRK08978 213 VPA--LREFLAATGMPavATLKGL--GAVEADHPyylgmLGMHGTKAAnlAVQECDLLIAVGARFDDRVT-GK-LNTfap 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 150 KSSIIIVNRNRDDM--LLNSDIfwkpqeAVQGDvgsfMIKLVEGLQGQTWSSDWVEELRKADQQKEQTYRDKAllpvpQH 227
Cdd:PRK08978 287 HAKVIHLDIDPAEInkLRQAHV------ALQGD----LNALLPALQQPLNIDAWRQHCAQLRAEHAWRYDHPG-----EA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 228 LNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAF 307
Cdd:PRK08978 352 IYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSF 431
|
330 340
....*....|....*....|....
gi 1958790128 308 GYSLIEFDTFVRHKVPV-IALVGN 330
Cdd:PRK08978 432 MMNVQELGTIKRKQLPVkIVLLDN 455
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
36-334 |
8.01e-11 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 63.82 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 36 WEpRPEGPLPL-DIPQA---SPQQVQRCVEILSRAKRPLLVLGsqALLPPTPANKLRAAV-ETLGVPCFLGGMS-RGLLG 109
Cdd:PRK07092 173 WD-QPAEPLPArTVSSAvrpDPAALARLGDALDAARRPALVVG--PAVDRAGAWDDAVRLaERHRAPVWVAPMSgRCSFP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 110 RNHPLH------IRQNRSAALKKADVVVLAGAVCdFRL---SYGRVLNRKSSIIIVNrnrDDMLLNSdifWKPQ-EAVQG 179
Cdd:PRK07092 250 EDHPLFagflpaSREKISALLDGHDLVLVIGAPV-FTYhveGPGPHLPEGAELVQLT---DDPGEAA---WAPMgDAIVG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 180 DVGSFMIKLVEGLqgqtwssdwVEELRKADQQKEqtyRDKALLPVPQHLNPVRLLQQVEETLPDNALLVVDggdfvATAA 259
Cdd:PRK07092 323 DIRLALRDLLALL---------PPSARPAPPARP---MPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEE-----APST 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 260 YLV-QPRgpLRWLDPGAF-----GTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAG 333
Cdd:PRK07092 386 RPAmQEH--LPMRRQGSFytmasGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGR 463
|
.
gi 1958790128 334 W 334
Cdd:PRK07092 464 Y 464
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
55-324 |
2.37e-10 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 62.45 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 55 QVQRCVEILSRAKRPLL------VLGSQALLPPTPANKLRAAVET--LGVPCFLGGMSR--GLLGrnhpLHIRQNRSAAL 124
Cdd:PRK06466 195 QIRKAVEMLLAAKRPVIysgggvVLGNASALLTELAHLLNLPVTNtlMGLGGFPGTDRQflGMLG----MHGTYEANMAM 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 125 KKADVVVLAGAVCDfrlsyGRVLNRKSSII----IVNRNRDDMLLNSDIFWK-----PQEAVQGDVGSFMIKLVEGLQGQ 195
Cdd:PRK06466 271 HHADVILAVGARFD-----DRVTNGPAKFCpnakIIHIDIDPASISKTIKADipivgPVESVLTEMLAILKEIGEKPDKE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 196 TWSSDW--VEELRKA-DQQKEQTYRDKALLPvpqhlnpvrllQQVEETLPD----NALLVVDGGDFVATAAYLVQPRGPL 268
Cdd:PRK06466 346 ALAAWWkqIDEWRGRhGLFPYDKGDGGIIKP-----------QQVVETLYEvtngDAYVTSDVGQHQMFAAQYYKFNKPN 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790128 269 RWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 324
Cdd:PRK06466 415 RWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
55-324 |
3.03e-10 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 61.76 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 55 QVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAvETLGVPCFLGGMSRGLLGRNHP-------LHIRQNRSAALKKA 127
Cdd:PRK08979 195 QIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLA-EKLNLPVVSTLMGLGAFPGTHKnslgmlgMHGRYEANMAMHNA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 128 DVVVLAGAVCDFRLSyGRVLNRKSSIIIVNRNRDDMLLNSDIfwKPQEAVQGDVGSFMIKLVEGLQGQTWSSD------W 201
Cdd:PRK08979 274 DLIFGIGVRFDDRTT-NNLEKYCPNATILHIDIDPSSISKTV--RVDIPIVGSADKVLDSMLALLDESGETNDeaaiasW 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 202 VEELRKADQQKEQTYrDKAllpvPQHLNPvrllQQVEETL----PDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFG 277
Cdd:PRK08979 351 WNEIEVWRSRNCLAY-DKS----SERIKP----QQVIETLykltNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLG 421
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958790128 278 TLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV 324
Cdd:PRK08979 422 TMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV 468
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
52-331 |
6.48e-10 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 60.91 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 52 SPQQVQRCVEILSRAKRPLLVLGSQALlppTPANKLRAAVETLGVPCFLGGMSRGLLGRNHPLHIRQ-------NRSAAL 124
Cdd:PLN02470 201 EKSQLEQIVRLISESKRPVVYVGGGCL---NSSEELREFVELTGIPVASTLMGLGAFPASDELSLQMlgmhgtvYANYAV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 125 KKADVVVLAGAVCDFRLSyGRV--LNRKSSIIIVNRNRDDMLLNSdifwKPQEAVQGDVG---SFMIKLVEGLQGQTWS- 198
Cdd:PLN02470 278 DSADLLLAFGVRFDDRVT-GKLeaFASRASIVHIDIDPAEIGKNK----QPHVSVCADVKlalQGLNKLLEERKAKRPDf 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 199 SDWVEELrkaDQQKEQ---TYRDKALLPVPQHLnpvrlLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGA 275
Cdd:PLN02470 353 SAWRAEL---DEQKEKfplSYPTFGDAIPPQYA-----IQVLDELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGG 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790128 276 FGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 331
Cdd:PLN02470 425 LGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNN 480
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
55-327 |
7.12e-10 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 60.63 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 55 QVQRCVEILSRAKRPLLVLGSQALLPPTPAnKLRAAVETLGVPCF-----LGGM------SRGLLGrnhpLHIRQNRSAA 123
Cdd:PRK07979 195 QIKRALQTLVAAKKPVVYVGGGAINAACHQ-QLKELVEKLNLPVVsslmgLGAFpathrqSLGMLG----MHGTYEANMT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 124 LKKADVVVLAGAVCDFRLSYGRVLNRKSSIII---VNRNRDDMLLNSDIfwkpqeAVQGDVGSFMIKLVEgLQGQTWSSD 200
Cdd:PRK07979 270 MHNADVIFAVGVRFDDRTTNNLAKYCPNATVLhidIDPTSISKTVTADI------PIVGDARQVLEQMLE-LLSQESAHQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 201 WVEELRKADQQKEQtYRDKALL---PVPQHLNPVRLLQQVEETLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFG 277
Cdd:PRK07979 343 PLDEIRDWWQQIEQ-WRARQCLkydTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLG 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958790128 278 TLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIAL 327
Cdd:PRK07979 422 TMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVL 471
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
192-331 |
5.58e-08 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 54.92 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 192 LQGQTWSSDWVEELR--KADQQKEQTYRDKALLPvpqhlnpvrllQQVEETL----PDNALLVVDGGDFVATAAYLVQPR 265
Cdd:PRK06882 341 AKSQTDLTAWWQQINewKAKKCLEFDRTSDVIKP-----------QQVVEAIyrltNGDAYVASDVGQHQMFAALHYPFD 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958790128 266 GPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGND 331
Cdd:PRK06882 410 KPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN 475
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
55-330 |
1.01e-07 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 53.93 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 55 QVQRCVEILSRAKRPLLVLGSQALLPPTpANKLRAAVETLGVPCFLGGMSRGLLGRNHPL-------HIRQNRSAALKKA 127
Cdd:CHL00099 206 RIEQAAKLILQSSQPLLYVGGGAIISDA-HQEITELAELYKIPVTTTLMGKGIFDEDHPLclgmlgmHGTAYANFAVSEC 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 128 DVVVLAGAVCDFRLSyGRVLNRKSSIIIV-----------NRNrddmllnsdifwkPQEAVQGDVGSFMIKLVEGL---- 192
Cdd:CHL00099 285 DLLIALGARFDDRVT-GKLDEFACNAQVIhididpaeigkNRI-------------PQVAIVGDVKKVLQELLELLknsp 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 193 ------QGQTWssdwveelrkadQQKEQTYRDKALLPVPQH---LNPVRLLQQVEETLPDnALLVVDGGDFVATAAYL-- 261
Cdd:CHL00099 351 nlleseQTQAW------------RERINRWRKEYPLLIPKPstsLSPQEVINEISQLAPD-AYFTTDVGQHQMWAAQFlk 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 262 VQPRgplRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPV-IALVGN 330
Cdd:CHL00099 418 CKPR---KWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIkIIIINN 484
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
228-405 |
2.53e-07 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 50.74 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 228 LNPVRLLQQVEETL-PDNALLVVDGGDFVATAAYLVQPRgPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGA 306
Cdd:cd02006 8 IKPQRVYEEMNKAFgRDVRYVTTIGLSQIAGAQMLHVYK-PRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 307 FGYSLIEFDTFVRHKVPVIALVGNDAgWTQISREQVPRLGSDVACSLAY------------TDYHKAAMGLGAQGLILSR 374
Cdd:cd02006 87 FQFMIEELAVGAQHRIPYIHVLVNNA-YLGLIRQAQRAFDMDYQVNLAFeninsselggygVDHVKVAEGLGCKAIRVTK 165
|
170 180 190
....*....|....*....|....*....|..
gi 1958790128 375 DNEdqVVKVLRDGQKLCQEGHA-VVVNILIGR 405
Cdd:cd02006 166 PEE--LAAAFEQAKKLMAEHRVpVVVEAILER 195
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
39-324 |
3.62e-07 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 52.40 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 39 RPeGPLPLDIP--------------------------QASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANK-LRAAV 91
Cdd:PRK09107 160 RP-GPVVVDIPkdvqfatgtytppqkapvhvsyqpkvKGDAEAITEAVELLANAKRPVIYSGGGVINSGPEASRlLRELV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 92 ETLGVP--CFLGGMSR---------GLLGrnhpLHIRQNRSAALKKADVVVLAGAVCDFRLSyGRV-----LNRKSSIII 155
Cdd:PRK09107 239 ELTGFPitSTLMGLGAypasgknwlGMLG----MHGTYEANMAMHDCDVMLCVGARFDDRIT-GRLdafspNSKKIHIDI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 156 ----VNRNrddmlLNSDIfwkpqeAVQGDVGSFMIKLVEGLQGQTWSSD------WVEELRKADQQKEQTYRDKALLPVP 225
Cdd:PRK09107 314 dpssINKN-----VRVDV------PIIGDVGHVLEDMLRLWKARGKKPDkealadWWGQIARWRARNSLAYTPSDDVIMP 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 226 QHLnpvrlLQQVEE-TLPDNALLVVDGGDFVATAAYLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGD 304
Cdd:PRK09107 383 QYA-----IQRLYElTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGD 457
|
330 340
....*....|....*....|
gi 1958790128 305 GAFGYSLIEFDTFVRHKVPV 324
Cdd:PRK09107 458 ASIQMCIQEMSTAVQYNLPV 477
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
201-380 |
3.38e-05 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 46.06 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 201 WVEELRKADQQKEQTYRDKALLPvPQHLNPVRLLQQVEETLPDNALLVVDGGDfVAT--AAYLVQPRGPLRWLDpGAFGT 278
Cdd:PRK08273 340 WRERIEKWVARWWETLEARAMVP-ADPVNPQRVFWELSPRLPDNAILTADSGS-CANwyARDLRMRRGMMASLS-GTLAT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 279 LGVGAGFALGAKLCQPEAEVWCLFGDGAFGYS-LIEFDTFVRH-----KVPVIALVGNDAGWTQISREQVPRLGS---DV 349
Cdd:PRK08273 417 MGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwsDPRLIVLVLNNRDLNQVTWEQRVMEGDpkfEA 496
|
170 180 190
....*....|....*....|....*....|.
gi 1958790128 350 ACSLAYTDYHKAAMGLGAQGLILsrDNEDQV 380
Cdd:PRK08273 497 SQDLPDVPYARFAELLGLKGIRV--DDPEQL 525
|
|
| CdhB |
COG1880 |
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion]; |
50-111 |
7.45e-04 |
|
CO dehydrogenase/acetyl-CoA synthase epsilon subunit [Energy production and conversion];
Pssm-ID: 441484 Cd Length: 168 Bit Score: 39.93 E-value: 7.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958790128 50 QASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAVETLGVP-CFLGGMSRGLLGRN 111
Cdd:COG1880 13 TAKAVKPEVAAKMIKKAKRPLLIVGPEALDDEELLERAIEIAKKAGIPiAATGHSIKGFVERG 75
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
190-368 |
3.42e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 39.47 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 190 EGLQGQTWSSDWVeelrkaDQQKEQTYRDKALLPVPQH--LNPVRLLQQVEETLPDNALlVVDGGDFVATAAYLVQPRGP 267
Cdd:PRK12474 307 DLAQALQDLADAV------DAPAEPAARTPLALPALPKgaLNSLGVAQLIAHRTPDQAI-YADEALTSGLFFDMSYDRAR 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790128 268 LRWLDPGAFGTLGVGAGFALGAKLCQPEAEVWCLFGDGAFGYSLIEFDTFVRHKVPVIALVGNDAGWTQISREqVPRLGS 347
Cdd:PRK12474 380 PHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNGE-LQRVGA 458
|
170 180 190
....*....|....*....|....*....|
gi 1958790128 348 DVACSLAYT---------DYHKAAMGLGAQ 368
Cdd:PRK12474 459 QGAGRNALSmldlhnpelNWMKIAEGLGVE 488
|
|
| |
