|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-323 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 656.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPPFFMVR-GGTEVIHINFRSAEVDAVY 79
Cdd:PRK08322 224 GIPFFTTQMGKGVIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVGHDVIEKPPFFMNPnGDKKVIHINFLPAEVDPVY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 80 FPQVEVIGDIANAVWQISEALNDTSHWDFTRLMAIREANEAQIAEGADDNRFPVYPQRMVADIRRVLPSEGIVALDNGIY 159
Cdd:PRK08322 304 FPQVEVVGDIANSLWQLKERLADQPHWDFPRFLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAY 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 160 KIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGY 239
Cdd:PRK08322 384 KIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAY 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 240 GMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSENDRILNSELRER 319
Cdd:PRK08322 464 GMIRWKQENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSENDRVLNQELGEL 543
|
....
gi 2174414276 320 ALAV 323
Cdd:PRK08322 544 SCQL 547
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
135-311 |
5.84e-112 |
|
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: 321.93 E-value: 5.84e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 135 PQRMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMM 214
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 215 NSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTP 294
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|....*..
gi 2174414276 295 GVHVIDCPVDYSENDRI 311
Cdd:cd02010 161 GVHVIDCPVDYSENIRL 177
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-308 |
2.92e-110 |
|
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: 330.97 E-value: 2.92e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPPFFM--VRGGTEVIHINFRSAEVDAV 78
Cdd:COG0028 230 GAPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWdeFAPDAKIIHIDIDPAEIGKN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 79 YFPQVEVIGDIANAVWQISEALNDTSHWDFTRLMAIREANEAQIAEGADDnRFPVYPQRMVADIRRVLPSEGIVALDNGI 158
Cdd:COG0028 310 YPVDLPIVGDAKAVLAALLEALEPRADDRAAWLARIAAWRAEYLAAYAAD-DGPIKPQRVIAALREALPDDAIVVTDVGQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 159 YKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDG 238
Cdd:COG0028 389 HQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGG 468
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2174414276 239 YGMIRWKQANM-GFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSEN 308
Cdd:COG0028 469 LGMVRQWQELFyGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-308 |
2.11e-76 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 243.61 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERH-PRFLGNAAL---SSGDfvhRAVEAADLIVNIGHDVIEKPPFFMVRGGT-EVIHINFRSAEV 75
Cdd:PRK08617 229 NLPVVETFQAAGVISRELeDHFFGRVGLfrnQPGD---ELLKKADLVITIGYDPIEYEPRNWNSEGDaTIIHIDVLPAEI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 76 DAVYFPQVEVIGDIANAVWQISEALNDTSHWDFTR--LMAIREANEAQIAEGADDNRFPVYPQRMVADIRRVLPSEGIVA 153
Cdd:PRK08617 306 DNYYQPERELIGDIAATLDLLAEKLDGLSLSPQSLeiLEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 154 LDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVI 233
Cdd:PRK08617 386 VDVGSHYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHII 465
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2174414276 234 LRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSEN 308
Cdd:PRK08617 466 WNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDN 540
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-307 |
1.88e-55 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 189.44 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDViekpPF--FMVRGgTEVIHINFRSAEVDAV 78
Cdd:PRK08611 229 KIPIIHTLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNY----PYvdYLPKK-AKAIQIDTDPANIGKR 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 79 YFPQVEVIGDIANAVWQISEALNDTSHWDFtrLMAIREANEA---QIAEGADDNRFPVYPQRMVADIRRVLPSEGIVALD 155
Cdd:PRK08611 304 YPVNVGLVGDAKKALHQLTENIKHVEDRRF--LEACQENMAKwwkWMEEDENNASTPIKPERVMAAIQKIADDDAVLSVD 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 156 NGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILR 235
Cdd:PRK08611 382 VGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLN 461
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2174414276 236 DDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSE 307
Cdd:PRK08611 462 NQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNA 533
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
132-304 |
2.59e-52 |
|
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: 170.02 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 132 PVYPQRMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGG 211
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 212 FMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCI 291
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEAL 160
|
170
....*....|...
gi 2174414276 292 KTPGVHVIDCPVD 304
Cdd:cd02014 161 AADGPVVIDVVTD 173
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
155-301 |
6.01e-52 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 168.15 E-value: 6.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 155 DNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVIL 234
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2174414276 235 RDDGYGMIRWKQANMG----FTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDC 301
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGggrySGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
137-303 |
2.31e-48 |
|
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: 159.73 E-value: 2.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 137 RMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNS 216
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 217 QELETAVRLGMHITVVILRDDGYGMIRWKQ-ANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPG 295
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQeAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 2174414276 296 VHVIDCPV 303
Cdd:cd00568 161 PALIEVKT 168
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
133-308 |
4.26e-46 |
|
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: 154.58 E-value: 4.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 133 VYPQRMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGF 212
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 213 MMNSQELETAVRLGMHITVVILRDDGYGMIR-WKQANMG----FTDFGldyGNPDFVKYAEAYGANGHRVESAEGLLPLL 287
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRqWQELFYEgrysHTTLD---SNPDFVKLAEAYGIKGLRVEKPEELEAAL 157
|
170 180
....*....|....*....|.
gi 2174414276 288 EHCIKTPGVHVIDCPVDYSEN 308
Cdd:cd02015 158 KEALASDGPVLLDVLVDPEEN 178
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
1-307 |
8.26e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 163.77 E-value: 8.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMVRggTEVIHINFRSAEVD 76
Cdd:PRK06276 231 KIPVCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGcrfsDRTTGDISSFAPN--AKIIHIDIDPAEIG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALNDTSHWDFTRLM-AIREANEAQIAEGADDNRfPVYPQRMVADIRRVL-----PSEG 150
Cdd:PRK06276 309 KNVRVDVPIVGDAKNVLRDLLAELMKKEIKNKSEWLeRVKKLKKESIPRMDFDDK-PIKPQRVIKELMEVLreidpSKNT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 151 IVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHIT 230
Cdd:PRK06276 388 IITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 231 VVILRDDGYGMI-RWKQ----ANMGFTDFGldyGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDY 305
Cdd:PRK06276 468 ICIFDNRTLGMVyQWQNlyygKRQSEVHLG---ETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDP 544
|
..
gi 2174414276 306 SE 307
Cdd:PRK06276 545 AE 546
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
2-308 |
6.25e-45 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 161.02 E-value: 6.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMVrgGTEVIHINFRSAEVDA 77
Cdd:CHL00099 246 IPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGarfdDRVTGKLDEFAC--NAQVIHIDIDPAEIGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 78 VYFPQVEVIGDIANAVWQISEAL-NDTSHWDFTRLMAIREaneaQIAEGADDnrFP---------VYPQRMVADIRRVLP 147
Cdd:CHL00099 324 NRIPQVAIVGDVKKVLQELLELLkNSPNLLESEQTQAWRE----RINRWRKE--YPllipkpstsLSPQEVINEISQLAP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 148 sEGIVALDNGIYKIWFARNYKAhKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGM 227
Cdd:CHL00099 398 -DAYFTTDVGQHQMWAAQFLKC-KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 228 HITVVILRDDGYGMIR-WKQANMG--FTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVD 304
Cdd:CHL00099 476 PIKIIIINNKWQGMVRqWQQAFYGerYSHSNMEEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVI 555
|
....
gi 2174414276 305 YSEN 308
Cdd:CHL00099 556 EDEN 559
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
3-303 |
1.66e-41 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 151.32 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 3 PFITTQMGKGVVDERHPRFLGNAAlssgdfVHRAVEAADLIVNIG---HDVIEKPPFfmVRGGTEVIHINFRSAEVDAvY 79
Cdd:PRK08266 233 PVVAFRSGRGIVSDRHPLGLNFAA------AYELWPQTDVVIGIGsrlELPTFRWPW--RPDGLKVIRIDIDPTEMRR-L 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 80 FPQVEVIGDIANAVWQISEALNDTSHWDFTRLMAIREANEAqiaegADDNRFPVYPQRMVAD-IRRVLPSEGIVAldNGI 158
Cdd:PRK08266 304 KPDVAIVADAKAGTAALLDALSKAGSKRPSRRAELRELKAA-----ARQRIQAVQPQASYLRaIREALPDDGIFV--DEL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 159 YKIWFARNY--KAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRD 236
Cdd:PRK08266 377 SQVGFASWFafPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNN 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2174414276 237 DGYGMIRWKQANM-GFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPV 303
Cdd:PRK08266 457 NAYGNVRRDQKRRfGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
2-308 |
7.56e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 150.20 E-value: 7.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMVRGgtEVIHINFRSAEVDA 77
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGarfdDRVTGKLDEFASRA--KVIHIDIDPAEVGK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 78 VYFPQVEVIGDIANAVWQISEALND------TSHWdFTRLMAIREANEAQIAEGADdnrfPVYPQRMVADIRRVLPsEGI 151
Cdd:PRK07418 331 NRRPDVPIVGDVRKVLVKLLERSLEpttpprTQAW-LERINRWKQDYPLVVPPYEG----EIYPQEVLLAVRDLAP-DAY 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 152 VALDNGIYKIWFARnYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITV 231
Cdd:PRK07418 405 YTTDVGQHQMWAAQ-FLRNGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKT 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 232 VILRDDGYGMIR-WKQANMG--FTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSEN 308
Cdd:PRK07418 484 VIINNGWQGMVRqWQESFYGerYSASNMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDEN 563
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
13-322 |
3.81e-40 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 147.71 E-value: 3.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 13 VVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----------HDVIEKPpffmvRGGTEVIHINFRSAEVDAVYFPQ 82
Cdd:PRK08199 244 LFDNRHPNYAGDLGLGINPALAARIREADLVLAVGtrlgevttqgYTLLDIP-----VPRQTLVHVHPDAEELGRVYRPD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 83 VEVIGDIANAVWQISE-ALNDTSHWDfTRLMAIREANEA----QIAEGADDNrfpvypQRMVADIRRVLPSEGIVALDNG 157
Cdd:PRK08199 319 LAIVADPAAFAAALAAlEPPASPAWA-EWTAAAHADYLAwsapLPGPGAVQL------GEVMAWLRERLPADAIITNGAG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 158 IYKIWFARNYKAHKPNTvlldnALA----TMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHItVVI 233
Cdd:PRK08199 392 NYATWLHRFFRFRRYRT-----QLAptsgSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPI-IVI 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 234 LRDDG-YGMIRWKQANmgftDF-----GLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDyse 307
Cdd:PRK08199 466 VVNNGmYGTIRMHQER----EYpgrvsGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID--- 538
|
330
....*....|....*....
gi 2174414276 308 NDRILN----SELRERALA 322
Cdd:PRK08199 539 PEAITPtatlSQIREQALA 557
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-304 |
8.65e-38 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 141.44 E-value: 8.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAAL-----SSGDFVHRAVEAADLIVNIGHDVIEK--------PPffmvrgGTEVIH 67
Cdd:PRK06112 241 GLPVATTNMGKGAVDETHPLSLGVVGSlmgprSPGRHLRDLVREADVVLLVGTRTNQNgtdswslyPE------QAQYIH 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 68 INFRSAEVDAVYfPQVEVIGDIANAVWQISEALNDTshwDFTRLMAIREANEAQIAEG-----------ADDNRFPVYPQ 136
Cdd:PRK06112 315 IDVDGEEVGRNY-EALRLVGDARLTLAALTDALRGR---DLAARAGRRAALEPAIAAGreahredsapvALSDASPIRPE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 137 RMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNT-VLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMN 215
Cdd:PRK06112 391 RIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHV 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 216 SQELETAVRLGMHITVVILRDDGYGMirwkQANMGFTDFG-----LDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHC 290
Cdd:PRK06112 471 WAELETARRMGVPVTIVVLNNGILGF----QKHAETVKFGthtdaCHFAAVDHAAIARACGCDGVRVEDPAELAQALAAA 546
|
330
....*....|....
gi 2174414276 291 IKTPGVHVIDCPVD 304
Cdd:PRK06112 547 MAAPGPTLIEVITD 560
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
3-308 |
3.59e-37 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 139.52 E-value: 3.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 3 PFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKppffmVRGGTE-------VIHINFRSAEV 75
Cdd:PRK06048 237 PVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDR-----VTGKLAsfapnakIIHIDIDPAEI 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 76 DAVYFPQVEVIGDIANAVWQISEALN--DTSHWdFTRLMAIREANEAQIAEGADdnrfPVYPQRMVADIRRVLPsEGIVA 153
Cdd:PRK06048 312 SKNVKVDVPIVGDAKQVLKSLIKYVQycDRKEW-LDKINQWKKEYPLKYKERED----VIKPQYVIEQIYELCP-DAIIV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 154 LDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVI 233
Cdd:PRK06048 386 TEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAI 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 234 LRDDGYGMIR-WKQAnmgFTDFGLDY----GNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSEN 308
Cdd:PRK06048 466 LNNGYLGMVRqWQEL---FYDKRYSHtcikGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEEN 542
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-308 |
4.71e-37 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 139.46 E-value: 4.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMvrGGTEVIHINFRSAEVD 76
Cdd:PRK08527 231 GIPAVETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGarfdDRVTGKLSEFA--KHAKIIHVDIDPSSIS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALNDTSHWDFTRLMAI-REANEAQIAEGADDNRFpVYPQRMVADIRRVLPSEGIVALD 155
Cdd:PRK08527 309 KIVNADYPIVGDLKNVLKEMLEELKEENPTTYKEWREIlKRYNELHPLSYEDSDEV-LKPQWVIERVGELLGDDAIISTD 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 156 NGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILR 235
Cdd:PRK08527 388 VGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILN 467
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2174414276 236 DDGYGMIRWKQA-----NMGFTDFGLdygNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSEN 308
Cdd:PRK08527 468 NNFLGMVRQWQTffyeeRYSETDLST---QPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFEN 542
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
1-307 |
4.69e-36 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 136.50 E-value: 4.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGhdviekppffmvrggTEVIHINFRSAEVDAVyf 80
Cdd:PRK06457 221 GAPIIYTLNGKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLG---------------TSFPYVNFLNKSAKVI-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 81 pQVEV----IGDIANA----VWQISEALN----DTSHWDFTRLMAIREANEAQIAEGADDNRFPVYPQRMVADIRRVLPS 148
Cdd:PRK06457 284 -QVDIdnsnIGKRLDVdlsyPIPVAEFLNidieEKSDKFYEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKK 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 149 EGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLV-HPDRPVISVCGDGGFMMNSQELETAVRLGM 227
Cdd:PRK06457 363 DAVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 228 HITVVILRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSE 307
Cdd:PRK06457 443 PVKIIIYNNSKLGMIKFEQEVMGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNE 522
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
2-308 |
7.02e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 133.35 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG---HDVIEKPPFFMVRGGTeVIHINFRSAEVDAV 78
Cdd:PRK07710 244 IPVVHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGarfDDRVTGNLAYFAKEAT-VAHIDIDPAEIGKN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 79 YFPQVEVIGDIANAVWQI---SEALNDTSHWdftrlmaireanEAQIAEGADdnRFPVY---------PQRMVADIRRVL 146
Cdd:PRK07710 323 VPTEIPIVADAKQALQVLlqqEGKKENHHEW------------LSLLKNWKE--KYPLSykrnsesikPQKAIEMLYEIT 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 147 PSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLG 226
Cdd:PRK07710 389 KGEAIVTTDVGQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELS 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 227 MHITVVILRDDGYGMIR-WKQAnmgFTD----FGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDC 301
Cdd:PRK07710 469 LPVKVVILNNEALGMVRqWQEE---FYNqrysHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDC 545
|
....*..
gi 2174414276 302 PVDYSEN 308
Cdd:PRK07710 546 RVLQSEK 552
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
1-308 |
4.07e-34 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 131.24 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKppffmVRGGTEV-------IHINFRSA 73
Cdd:PRK06725 242 RIPVVSTLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDR-----VTGKLELfsphskkVHIDIDPS 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 74 EVD---AVYFPqveVIGDIANAVW---------QISEALNDTSHWDftrlmaireaNEAQIAEGADDNRFPvyPQRMVAD 141
Cdd:PRK06725 317 EFHknvAVEYP---VVGDVKKALHmllhmsihtQTDEWLQKVKTWK----------EEYPLSYKQKESELK--PQHVINL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 142 IRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELET 221
Cdd:PRK06725 382 VSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQT 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 222 AVRLGMHITVVILRDDGYGMIR-WKQAnmgFTDFGLD---YGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVH 297
Cdd:PRK06725 462 IAENNIPVKVFIINNKFLGMVRqWQEM---FYENRLSeskIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPV 538
|
330
....*....|.
gi 2174414276 298 VIDCPVDYSEN 308
Cdd:PRK06725 539 VVDFCVEEGEN 549
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
1-300 |
3.12e-32 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 125.76 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG---HD-VIEKPPFFMvrGGTEVIHINFRSAEVD 76
Cdd:PRK08978 224 GMPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGarfDDrVTGKLNTFA--PHAKVIHLDIDPAEIN 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALnDTSHWdftrlmaireanEAQIAEGADDNRF-------PVYPQRMVADIRRVLPSE 149
Cdd:PRK08978 302 KLRQAHVALQGDLNALLPALQQPL-NIDAW------------RQHCAQLRAEHAWrydhpgeAIYAPALLKQLSDRKPAD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 150 GIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHI 229
Cdd:PRK08978 369 TVVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 230 TVVILRDDGYGMIR-WKQ----ANMGFTDfgLDyGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPG---VHV-ID 300
Cdd:PRK08978 449 KIVLLDNQRLGMVRqWQQlffdERYSETD--LS-DNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGpylLHVsID 525
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
2-300 |
7.98e-32 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 124.95 E-value: 7.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPPFFMVRGGTEVIHINFRSAEVDAVYFP 81
Cdd:TIGR02720 227 IPLISTGLAKGIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYPFAEVSKAFKNTKYFIQIDIDPAKLGKRHHT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 82 QVEVIGDIANAVWQI---SEALNDTSHWDFTrlMAIREANEAQIAEGADDNRFPVYPQRMVADIRRVLPSEGIVALDNGI 158
Cdd:TIGR02720 307 DIAVLADAKKALAAIlaqVEPRESTPWWQAN--VANVKNWRAYLASLEDKTEGPLQAYQVYRAINKIAEDDAIYSIDVGD 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 159 YKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDG 238
Cdd:TIGR02720 385 ININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCT 464
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2174414276 239 YGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHC--IKTPGVHVID 300
Cdd:TIGR02720 465 YGFIKDEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLID 528
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-308 |
8.96e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 121.74 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMVRGGteVIHINFRSAEVD 76
Cdd:PRK08155 239 QLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGarfdDRAIGKTEQFCPNAK--IIHVDIDRAELG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALNDTSHWDFTRLMAIREANEAQIAEGADDnrfPVYPQRMVADIRRVLPSEGIVALDN 156
Cdd:PRK08155 317 KIKQPHVAIQADVDDVLAQLLPLVEAQPRAEWHQLVADLQREFPCPIPKADD---PLSHYGLINAVAACVDDNAIITTDV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 157 GIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRD 236
Cdd:PRK08155 394 GQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNN 473
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2174414276 237 DGYGMIRwKQANMGFTD--FGLDY-GNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSEN 308
Cdd:PRK08155 474 EALGLVH-QQQSLFYGQrvFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEK 547
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
1-307 |
4.95e-30 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 119.56 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPpfF-----MVRGGTEVIHINFRSAEV 75
Cdd:PRK06456 235 HIPIVSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRT--FtsydeMVETRKKFIMVNIDPTDG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 76 DAVYFPQVEVIGD-------IANAVWQISEAlNDTSHWdftrLMAIREANE--AQIAEGADDNRFPvyPQRMVADIRRVL 146
Cdd:PRK06456 313 EKAIKVDVGIYGNakiilreLIKAITELGQK-RDRSAW----LKRVKEYKEyySQFYYTEENGKLK--PWKIMKTIRQAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 147 PSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLG 226
Cdd:PRK06456 386 PRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEH 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 227 MHITVVILRDDGYGMIRWKQaNMGFTD--FGLDYGN-PDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPV 303
Cdd:PRK06456 466 IPVISVIFDNRTLGLVRQVQ-DLFFGKriVGVDYGPsPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPV 544
|
....
gi 2174414276 304 DYSE 307
Cdd:PRK06456 545 DKEE 548
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-288 |
5.77e-30 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 119.54 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG---HDVIEKPPFFMVRGGTeVIHINFRSAEVDAV 78
Cdd:PRK07282 239 IPVVTTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGsrfDDRLTGNPKTFAKNAK-VAHIDIDPAEIGKI 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 79 YFPQVEVIGDIANAVWQISEAlnDTSHWDFTRLMAIREANEAQIAEGADDNRFpVYPQRMVADIRRVLPSEGIVALDNGI 158
Cdd:PRK07282 318 IKTDIPVVGDAKKALQMLLAE--PTVHNNTEKWIEKVTKDKNRVRSYDKKERV-VQPQAVIERIGELTNGDAIVVTDVGQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 159 YKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDG 238
Cdd:PRK07282 395 HQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHS 474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2174414276 239 YGMIR-WKQANM-GFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLE 288
Cdd:PRK07282 475 LGMVRqWQESFYeGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLE 526
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
1-307 |
1.30e-29 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 118.69 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVV---DERHPRFLGnaaLSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMVRGgtEVIHINFRSA 73
Cdd:PLN02470 241 GIPVASTLMGLGAFpasDELSLQMLG---MHGTVYANYAVDSADLLLAFGvrfdDRVTGKLEAFASRA--SIVHIDIDPA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 74 EVDAVYFPQVEVIGDIANAVWQISEAL--NDTSHWDFTrlmAIREANEAQIAEgaddnrFP---------VYPQRMVADI 142
Cdd:PLN02470 316 EIGKNKQPHVSVCADVKLALQGLNKLLeeRKAKRPDFS---AWRAELDEQKEK------FPlsyptfgdaIPPQYAIQVL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 143 RRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETA 222
Cdd:PLN02470 387 DELTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATI 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 223 VRLGMHITVVILRDDGYGMI-----RWKQANMGFTDFGlDYGN-----PDFVKYAEAYGANGHRVESAEGLLPLLEHCIK 292
Cdd:PLN02470 467 HVENLPVKIMVLNNQHLGMVvqwedRFYKANRAHTYLG-DPDAeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLD 545
|
330
....*....|....*
gi 2174414276 293 TPGVHVIDCPVDYSE 307
Cdd:PLN02470 546 TPGPYLLDVIVPHQE 560
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-288 |
4.47e-29 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 117.00 E-value: 4.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGN-------AALSsgdfvhrAVEAADLIVNIG----HDVIEKPPFFMvrGGTEVIHIN 69
Cdd:PRK07789 259 GIPVVTTLMARGAFPDSHPQHLGMpgmhgtvAAVA-------ALQRSDLLIALGarfdDRVTGKLDSFA--PDAKVIHAD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 70 FRSAEVDAVYFPQVEVIGDIANAVWQISEALN---------DTSHWdFTRLMAIREANEAQIAEGADDNrfpVYPQRMVA 140
Cdd:PRK07789 330 IDPAEIGKNRHADVPIVGDVKEVIAELIAALRaehaaggkpDLTAW-WAYLDGWRETYPLGYDEPSDGS---LAPQYVIE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 141 DIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELE 220
Cdd:PRK07789 406 RLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELA 485
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2174414276 221 TAVRLGMHITVVILRDDGYGMIRWKQA---NMGFTDFGLDYGN---PDFVKYAEAYGANGHRVESAEGLLPLLE 288
Cdd:PRK07789 486 TCAIEGIPIKVALINNGNLGMVRQWQTlfyEERYSNTDLHTHShriPDFVKLAEAYGCVGLRCEREEDVDAVIE 559
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-307 |
1.49e-28 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 115.23 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMvrGGTEVIHINFRSAEVD 76
Cdd:PRK06466 234 NLPVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGarfdDRVTNGPAKFC--PNAKIIHIDIDPASIS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALNDTSHwdftrlMAIREANEA---QIAEGADDNRFPVY---------PQRMVADIRR 144
Cdd:PRK06466 312 KTIKADIPIVGPVESVLTEMLAILKEIGE------KPDKEALAAwwkQIDEWRGRHGLFPYdkgdggiikPQQVVETLYE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 145 VLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVR 224
Cdd:PRK06466 386 VTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 225 LGMHITVVILRDDGYGMIR-WKQANMGfTDFGLDYGN--PDFVKYAEAYGANGHRVESAEGLLPLLEHC--IKTPGVhVI 299
Cdd:PRK06466 466 YGLPVKIINLNNGALGMVRqWQDMQYE-GRHSHSYMEslPDFVKLAEAYGHVGIRITDLKDLKPKLEEAfaMKDRLV-FI 543
|
....*...
gi 2174414276 300 DCPVDYSE 307
Cdd:PRK06466 544 DIYVDRSE 551
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
135-304 |
1.19e-26 |
|
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: 103.38 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 135 PQRMVADIRRVLPSEGIVALDNGIYKIWfARNY-KAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFM 213
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDW-ARYIlRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 214 MNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMgfTDFGLDYG----NPDFVKYAEAYGANGHRVESAEGLLPLLEH 289
Cdd:cd02004 80 FSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLS--YGLGLPVTtllpDTRYDLVAEAFGGKGELVTTPEELKPALKR 157
|
170
....*....|....*
gi 2174414276 290 CIKTPGVHVIDCPVD 304
Cdd:cd02004 158 ALASGKPALINVIID 172
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
1-300 |
2.84e-26 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 108.54 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAAlssgdfVHRAVEA----ADLIVNIG---------HDVIEKPpffmvrggTEVIH 67
Cdd:PRK07064 228 GFGVVTSTQGRGVVPEDHPASLGAFN------NSAAVEAlyktCDLLLVVGsrlrgnetlKYSLALP--------RPLIR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 68 INFRSAEVDAVYFPQVEVIGDIANAVWQISEALNDTS----HWDFtRLMAIREANEAQIAEGADDNRfpvypqRMVADIR 143
Cdd:PRK07064 294 VDADAAADGRGYPNDLFVHGDAARVLARLADRLEGRLsvdpAFAA-DLRAAREAAVADLRKGLGPYA------KLVDALR 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 144 RVLPSEGIVALDNGIY-KIWFARNYKAHKPNTvlldNALATMGA---GLPSAMAAHLVHPDRPVISVCGDGGFMMNSQEL 219
Cdd:PRK07064 367 AALPRDGNWVRDVTISnSTWGNRLLPIFEPRA----NVHALGGGigqGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 220 ETAVRLGMHITVVILRDDGYGMIRWKQ-ANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHV 298
Cdd:PRK07064 443 ATAVQENANMVIVLMNDGGYGVIRNIQdAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVL 522
|
..
gi 2174414276 299 ID 300
Cdd:PRK07064 523 VE 524
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
3-300 |
1.43e-25 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 106.60 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 3 PFITTQMGKGVVDERHPRFLG-NAALSSGdfvhRAVEA-ADLIVNIGHDVIEKPPFFMVRGG----TEVIHINFRSAEVD 76
Cdd:PRK07524 229 PVALTINAKGLLPAGHPLLLGaSQSLPAV----RALIAeADVVLAVGTELGETDYDVYFDGGfplpGELIRIDIDPDQLA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALNDTS---HWDFTRLMAIREANEAQIAegaddnrfPVYP--QRMVADIRRVLPSEGI 151
Cdd:PRK07524 305 RNYPPALALVGDARAALEALLARLPGQAaaaDWGAARVAALRQALRAEWD--------PLTAaqVALLDTILAALPDAIF 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 152 VAlDNG--IYkiwfARNYKAHKPNTVLLDNA---LATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLG 226
Cdd:PRK07524 377 VG-DSTqpVY----AGNLYFDADAPRRWFNAstgYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEAD 451
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2174414276 227 MHITVVILRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVID 300
Cdd:PRK07524 452 LPLIVLLWNNDGYGEIRRYMVARDIEPVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIE 525
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
2-308 |
2.18e-25 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 106.15 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPPFFMVR--GGTEVIHINFRSAEVDAVY 79
Cdd:PRK06882 235 LPVTSSLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKycPNAKVIHIDIDPTSISKNV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 80 FPQVEVIGDIANAVWQISEALND----TSHWDFTRL-MAIREANEAQIAEgADDNRFPVYPQRMVADIRRVLPSEGIVAL 154
Cdd:PRK06882 315 PAYIPIVGSAKNVLEEFLSLLEEenlaKSQTDLTAWwQQINEWKAKKCLE-FDRTSDVIKPQQVVEAIYRLTNGDAYVAS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 155 DNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVIL 234
Cdd:PRK06882 394 DVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSL 473
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2174414276 235 RDDGYGMIRWKQANMGFTDFGLDYGN--PDFVKYAEAYGANGHRVESAEGLLPLLEHC--IKTPGVHViDCPVDYSEN 308
Cdd:PRK06882 474 NNRFLGMVKQWQDLIYSGRHSQVYMNslPDFAKLAEAYGHVGIQIDTPDELEEKLTQAfsIKDKLVFV-DVNVDETEH 550
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
157-308 |
3.89e-25 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 105.56 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 157 GIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRD 236
Cdd:PRK09107 405 GQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 237 DGYGMIR-WKQanmgftdfgLDYGN----------PDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDY 305
Cdd:PRK09107 485 QYMGMVRqWQQ---------LLHGNrlshsyteamPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVAN 555
|
...
gi 2174414276 306 SEN 308
Cdd:PRK09107 556 LEN 558
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
184-303 |
6.84e-25 |
|
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: 98.82 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 184 MGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGF------TDFGLD 257
Cdd:cd02002 51 LGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPegpgenAPDGLD 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2174414276 258 YGNP--DFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPV 303
Cdd:cd02002 131 LLDPgiDFAAIAKAFGVEAERVETPEELDEALREALAEGGPALIEVVV 178
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
1-308 |
1.86e-24 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 103.73 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG----HDVIEKPPFFMVRGgTEVIHINFRSAEVD 76
Cdd:PRK06965 249 GYPVTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGarfdDRVIGNPAHFASRP-RKIIHIDIDPSSIS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 77 AVYFPQVEVIGDIANAVWQISEALNDTSHW-DFTRLMAIREANEAQIAEGA---DDNRFPVYPQRMVADIRRVLPSEGIV 152
Cdd:PRK06965 328 KRVKVDIPIVGDVKEVLKELIEQLQTAEHGpDADALAQWWKQIEGWRSRDClkyDRESEIIKPQYVVEKLWELTDGDAFV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 153 ALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVV 232
Cdd:PRK06965 408 CSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKII 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 233 ILRDDGYGMIR-WKQanmgftdfgLDYGN----------PDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHV-ID 300
Cdd:PRK06965 488 SLNNRYLGMVRqWQE---------IEYSKryshsymdalPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRTVfLD 558
|
....*...
gi 2174414276 301 CPVDYSEN 308
Cdd:PRK06965 559 FQTDPTEN 566
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-289 |
3.55e-24 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 102.54 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLG--NAALSSGDfVHRAVEAADLIVNIGhdviekpPFF--MVRGG-------TEVIHIN 69
Cdd:COG3961 237 GIPVATTLLGKSVLDESHPQFIGtyAGAASSPE-VREYVENADCVLCLG-------VVFtdTNTGGftaqldpERTIDIQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 70 FRSAEVDAVYFPQVEvIGDIANAVwqISEALNDTSHWDFTRLMAireaneAQIAEGADDnrfPVYPQRMVADIRRVLPSE 149
Cdd:COG3961 309 PDSVRVGGHIYPGVS-LADFLEAL--AELLKKRSAPLPAPAPPP------PPPPAAPDA---PLTQDRLWQRLQAFLDPG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 150 GIVALDNGIYkiWF-ARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMH 228
Cdd:COG3961 377 DIVVADTGTS--LFgAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLK 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2174414276 229 ITVVILRDDGYG---MIRWKQA--NmgftdfglDYGNPDFVKYAEAYGAN---GHRVESAEGLLPLLEH 289
Cdd:COG3961 455 PIIFVLNNDGYTierAIHGPDGpyN--------DIANWDYAKLPEAFGGGnalGFRVTTEGELEEALAA 515
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
2-292 |
1.87e-23 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 100.66 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPPFFMVRGGTEVIHINFRSAEVDAVYFP 81
Cdd:PRK06154 243 IPVMTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGLPMPEGKTIIHSTLDDADLNKDYPI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 82 QVEVIGDIANAVWQISEALNDTSHWDFTR-------LMAIREANEAQIAEGADDNRFPVYPQRMVADIRRVL-PSEGIVA 153
Cdd:PRK06154 323 DHGLVGDAALVLKQMIEELRRRVGPDRGRaqqvaaeIEAVRAAWLAKWMPKLTSDSTPINPYRVVWELQHAVdIKTVIIT 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 154 LDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVI 233
Cdd:PRK06154 403 HDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTIL 482
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2174414276 234 LRDDGYGmIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIK 292
Cdd:PRK06154 483 LNNFSMG-GYDKVMPVSTTKYRATDISGDYAAIARALGGYGERVEDPEMLVPALLRALR 540
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
132-291 |
1.41e-21 |
|
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: 90.26 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 132 PVYPQRMVADIRRVLPSEGIVALDNG-IYKIwfARNYKAH-KPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGD 209
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGnICSV--ANSYLRFeKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 210 GGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQanmgfTDF------GLDYGNPDFVKYAEAYGANGHRVESAEGL 283
Cdd:cd02013 81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQ-----VDFynnrfvGTELESESFAKIAEACGAKGITVDKPEDV 155
|
....*...
gi 2174414276 284 LPLLEHCI 291
Cdd:cd02013 156 GPALQKAI 163
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
184-304 |
1.98e-21 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 94.64 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 184 MGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDF-GLDYGNPD 262
Cdd:PRK07092 409 LGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPVFGVRDVpGLDLPGLD 488
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2174414276 263 FVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVD 304
Cdd:PRK07092 489 FVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
165-304 |
2.23e-21 |
|
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: 90.06 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 165 RNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRW 244
Cdd:cd02003 31 KLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINN 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2174414276 245 KQANMGFTDFGLDY-------GNP-------DFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVD 304
Cdd:cd02003 111 LQESTGSGSFGTEFrdrdqesGQLdgallpvDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
2-308 |
2.82e-21 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 94.15 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 2 IPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIGHDVIEKPPFFMVR--GGTEVIHINFRSAEVDAVY 79
Cdd:PRK07979 235 LPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKycPNATVLHIDIDPTSISKTV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 80 FPQVEVIGDIANAVWQISEALN-DTSHWDFTRL----MAIrEANEAQIAEGADDNRFPVYPQRMVADIRRVLPSEGIVAL 154
Cdd:PRK07979 315 TADIPIVGDARQVLEQMLELLSqESAHQPLDEIrdwwQQI-EQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 155 DNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVIL 234
Cdd:PRK07979 394 DVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 235 RDDGYGMIRWKQANMGFTDFGLDYGN--PDFVKYAEAYGANGHRVESAEGLLP----LLEHCIKTPGVHViDCPVDYSEN 308
Cdd:PRK07979 474 NNRYLGMVKQWQDMIYSGRHSQSYMQslPDFVRLAEAYGHVGIQISHPDELESklseALEQVRNNRLVFV-DVTVDGSEH 552
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-308 |
5.53e-21 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 93.35 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG-------HDVIEK--PpffmvrgGTEVIHINF- 70
Cdd:PRK08979 234 NLPVVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGvrfddrtTNNLEKycP-------NATILHIDId 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 71 -----RSAEVDAVYFPQVEVIGDIANAVWQISEALNDTSHWDF--TRLMAIREANeaqiAEGADDNRFPVYPQRMVADIR 143
Cdd:PRK08979 307 pssisKTVRVDIPIVGSADKVLDSMLALLDESGETNDEAAIASwwNEIEVWRSRN----CLAYDKSSERIKPQQVIETLY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 144 RVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAV 223
Cdd:PRK08979 383 KLTNGDAYVASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTAL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 224 RLGMHITVVILRDDGYGMIRWKQANMGFTDFGLDYGN--PDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHV-ID 300
Cdd:PRK08979 463 QYDIPVKIINLNNRFLGMVKQWQDMIYQGRHSHSYMDsvPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVD 542
|
....*...
gi 2174414276 301 CPVDYSEN 308
Cdd:PRK08979 543 INVDETEH 550
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
126-300 |
1.20e-20 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 92.36 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 126 ADDNRFPVYPQRMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVIS 205
Cdd:PRK09124 352 PSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 206 VCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLP 285
Cdd:PRK09124 432 LSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDG 511
|
170
....*....|....*
gi 2174414276 286 LLEHCIKTPGVHVID 300
Cdd:PRK09124 512 ALQRAFAHDGPALVD 526
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
115-283 |
8.69e-20 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 89.97 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 115 REANEAQIAEGADdnrfPVYPQRMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAA 194
Cdd:PRK08273 352 WETLEARAMVPAD----PVNPQRVFWELSPRLPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 195 HLVHPDRPVISVCGDGGFMMNSQ-ELETAVRLGMH-----ITVVILRDDGYGMIRWKQANMGftdfgldyGNP------- 261
Cdd:PRK08273 428 KFAHPDRPVIALVGDGAMQMNGMaELITVAKYWRQwsdprLIVLVLNNRDLNQVTWEQRVME--------GDPkfeasqd 499
|
170 180
....*....|....*....|....*.
gi 2174414276 262 ----DFVKYAEAYGANGHRVESAEGL 283
Cdd:PRK08273 500 lpdvPYARFAELLGLKGIRVDDPEQL 525
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
1-96 |
1.24e-19 |
|
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: 83.38 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGDFVHRAVEAADLIVNIG---HDVIEKPPFFMVRGGTEVIHINFRSAEVDA 77
Cdd:pfam00205 39 GIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADLVLAVGarfDDIRTTGKLPEFAPDAKIIHIDIDPAEIGK 118
|
90
....*....|....*....
gi 2174414276 78 VYFPQVEVIGDIANAVWQI 96
Cdd:pfam00205 119 NYPVDVPIVGDAKETLEAL 137
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
1-233 |
2.01e-18 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 85.54 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAAlssgdfvHRAVEAADLIVNIGHDVIEKPPFFMVRGGTEVIHINFRSAEVDAVYF 80
Cdd:PRK05858 231 GIPVLMNGMGRGVVPADHPLAFSRAR-------GKALGEADVVLVVGVPMDFRLGFGVFGGTAQLVHVDDAPPQRAHHRP 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 81 PQVEVIGDIANAVWQISEALNDTSHWD--FTRLMAIREANEAQIAEGADDNRFPVYPQRMVADIRRVLPSEGIVALDNGI 158
Cdd:PRK05858 304 VAAGLYGDLSAILSALAGAGGDRTDHQgwIEELRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGD 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2174414276 159 YKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVI 233
Cdd:PRK05858 384 FVSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVI 458
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
185-300 |
4.63e-18 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 84.51 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 185 GAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFG------LDY 258
Cdd:PRK07586 388 GQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGpraldmLDL 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2174414276 259 GNP--DFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVID 300
Cdd:PRK07586 468 DDPdlDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIE 511
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
18-291 |
6.69e-17 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 81.20 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 18 HPRFLGnaalssgdFVHRA-VEAADLIVNIGHDVIEKPPFFMVRGGTEVIHINfrsaeVDAVY-------FPQVEVI-GD 88
Cdd:PRK08327 265 HPLHLG--------PDPRAdLAEADLVLVVDSDVPWIPKKIRPDADARVIQID-----VDPLKsriplwgFPCDLCIqAD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 89 IANAVWQISEALndTSHWD------FTRLMAIREANEAQIAEGADD-----NRFPVYPQRMVADIRRVLPSEGIVALDNG 157
Cdd:PRK08327 332 TSTALDQLEERL--KSLASaerrraRRRRAAVRELRIRQEAAKRAEierlkDRGPITPAYLSYCLGEVADEYDAIVTEYP 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 158 IyKIWFARnykAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQE--LETAVRLGMHITVVILR 235
Cdd:PRK08327 410 F-VPRQAR---LNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFN 485
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2174414276 236 DDGYGMIRW-----------KQAN-MGFTDFGLDygnPDFVKYAEAYGANGHRVESAEGLLPLLEHCI 291
Cdd:PRK08327 486 NGGWLAVKEavlevypegyaARKGtFPGTDFDPR---PDFAKIAEAFGGYGERVEDPEELKGALRRAL 550
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
128-300 |
9.96e-17 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 80.80 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 128 DNRFPVYPQRMVADIRRVLPSEGIVALDNGIYKIWFARnYKAHKPNTVLLDNAL-ATMGAGLPSAMAAHLVHPDRPVISV 206
Cdd:PRK06546 354 EKHTPIHPEYVASILDELAADDAVFTVDTGMCNVWAAR-YITPNGRRRVIGSFRhGSMANALPHAIGAQLADPGRQVISM 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 207 CGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFGLDYGNPDFVKYAEAYGANGHRVESAEGLLPL 286
Cdd:PRK06546 433 SGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKLEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGA 512
|
170
....*....|....
gi 2174414276 287 LEHCIKTPGVHVID 300
Cdd:PRK06546 513 LREAFAHPGPALVD 526
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
1-313 |
8.01e-15 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 75.02 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGnAALSSgdfvhrAVEAADLIVNIG--------HDvieKPPFFmvRGGTEVIHINFRS 72
Cdd:PRK09259 241 GIPFLPMSMAKGLLPDTHPQSAA-AARSL------ALANADVVLLVGarlnwllsHG---KGKTW--GADKKFIQIDIEP 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 73 AEVDAVYFPQVEVIGDIANAVWQISEALNDT-----SHWdFTRLMAIREANEAQIAEGADDNRFPVYPQRMVADIRRV-- 145
Cdd:PRK09259 309 QEIDSNRPIAAPVVGDIGSVMQALLAGLKQNtfkapAEW-LDALAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVlk 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 146 ------LPSEGIVALDNgiykiwfARNY-KAHKPNTVLLDNALATMGAGLPSAMAAhLVHPDRPVISVCGDGGFMMNSQE 218
Cdd:PRK09259 388 enpdiyLVNEGANTLDL-------ARNIiDMYKPRHRLDCGTWGVMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGME 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 219 LETAVRLGMHITVVILRDDgyGMIRWKQANMGftdFGLDYGNPDFVKYA------EAYGANGHRVESAEGLLPLLEHCIK 292
Cdd:PRK09259 460 VETICRYNLPVTVVIFNNG--GIYRGDDVNLS---GAGDPSPTVLVHHArydkmmEAFGGVGYNVTTPDELRHALTEAIA 534
|
330 340
....*....|....*....|....
gi 2174414276 293 TPGVHVIDC---PVDYSENDRILN 313
Cdd:PRK09259 535 SGKPTLINVvidPAAGTESGHITN 558
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-288 |
4.49e-14 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 72.71 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 1 GIPFITTQMGKGVVDERHPRFLGNAALSSGdfvHR----AVEAADLIVNIG------H----DViekppffmVRGGTEVI 66
Cdd:PRK11269 231 GVPVIPTLMGWGAIPDDHPLMAGMVGLQTS---HRygnaTLLASDFVLGIGnrwanrHtgsvEV--------YTKGRKFV 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 67 HINFRSAEVDAVYFPQVEVIGDIANAV---------WQISEALNDTSHWdftrLMAIREANEAQIAEGADDNrFPVYPQR 137
Cdd:PRK11269 300 HVDIEPTQIGRVFGPDLGIVSDAKAALellvevareWKAAGRLPDRSAW----VADCQERKRTLLRKTHFDN-VPIKPQR 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 138 MVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQ 217
Cdd:PRK11269 375 VYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 218 ELETAVRLGMHITVVILRDDGYGMIRwkQANMGFT-DF--GLDYGNP----------DFVKYAEAYGANGHRVESAEGLL 284
Cdd:PRK11269 455 ELAVGAQFNLPYIHVLVNNAYLGLIR--QAQRAFDmDYcvQLAFENInspelngygvDHVKVAEGLGCKAIRVFKPEDIA 532
|
....
gi 2174414276 285 PLLE 288
Cdd:PRK11269 533 PALE 536
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
104-292 |
5.87e-14 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 72.34 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 104 SHWDFTRLMAIREANEAQIAEGADdnrfPVYPQRMVADIRRVLPSEGIVALDNGiykiwfarnykahkpNTVLLDNA--- 180
Cdd:PRK07525 361 SSWDHEDDDPGTDWNEEARARKPD----YMHPRQALREIQKALPEDAIVSTDIG---------------NNCSIANSylr 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 181 -------LATM-----GAGLPSAMAAHLVHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQA- 247
Cdd:PRK07525 422 fekgrkyLAPGsfgncGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVd 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2174414276 248 --NMGFTDFGLDyGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIK 292
Cdd:PRK07525 502 fyNNRFVGTELD-NNVSYAGIAEAMGAEGVVVDTQEELGPALKRAID 547
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
137-289 |
2.97e-10 |
|
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: 58.31 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 137 RMVADIRRVLPSEGIVALDNGIykIWFARNYKAHKPNTVLLDNAL-ATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMN 215
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGT--SWFGALDLKLPKGTRFISQPLwGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 216 SQELETAVRLGMHITVVILRDDGYGMIR----WKQA-NmgftdfglDYGNPDFVKYAEAYGANGH----RVESAEGLLPL 286
Cdd:cd02005 84 VQELSTMIRYGLNPIIFLINNDGYTIERaihgPEASyN--------DIANWNYTKLPEVFGGGGGglsfRVKTEGELDEA 155
|
...
gi 2174414276 287 LEH 289
Cdd:cd02005 156 LKD 158
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
137-281 |
1.01e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 56.42 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 137 RMVADIrrvLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNAlATMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMNS 216
Cdd:PRK12474 348 QLIAHR---TPDQAIYADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTM 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2174414276 217 QELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFG------LDYGNP--DFVKYAEAYGANGHRVESAE 281
Cdd:PRK12474 424 QALWTMARENLDVTVVIFANRSYAILNGELQRVGAQGAGrnalsmLDLHNPelNWMKIAEGLGVEASRATTAE 496
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
132-289 |
8.89e-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: 48.82 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 132 PVYPQRMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHLVHPDRPVISVCGDGG 211
Cdd:cd02006 7 PIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 212 FMMNSQELETAVRLGMHITVVILRDDGYGMIRwkQANMGFT-DFGLD-------------YGnPDFVKYAEAYGANGHRV 277
Cdd:cd02006 87 FQFMIEELAVGAQHRIPYIHVLVNNAYLGLIR--QAQRAFDmDYQVNlafeninsselggYG-VDHVKVAEGLGCKAIRV 163
|
170
....*....|..
gi 2174414276 278 ESAEGLLPLLEH 289
Cdd:cd02006 164 TKPEELAAAFEQ 175
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
178-304 |
1.26e-04 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 41.81 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 178 DNALAT-MGAGLPSamaahlvhpDRPVISVCGD-------GGFMMNSQEletavrlGMHITVVILRDDGYGMIRWKQANM 249
Cdd:cd02009 54 DGTLSTaLGIALAT---------DKPTVLLTGDlsflhdlNGLLLGKQE-------PLNLTIVVINNNGGGIFSLLPQAS 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2174414276 250 GFTDFGLDYGNP---DFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVD 304
Cdd:cd02009 118 FEDEFERLFGTPqglDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
183-241 |
1.87e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 41.49 E-value: 1.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 183 TMGAGLPSAMAAHLVHPDRPVISVCGDGGFMMN-SQELETAVRLGMHITVVILRDDGYGM 241
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSgILGLINAVYNKANITVVILDNRTTAM 111
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
185-239 |
3.05e-03 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 39.30 E-value: 3.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2174414276 185 GAGLPSAMAAhlvhPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGY 239
Cdd:PLN02573 435 GATLGYAQAA----PDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGY 485
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
129-238 |
7.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 37.12 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2174414276 129 NRFPVyPQRMVADIRRvlpSEGIVA-LDNGIYKIWFArnykAHKPNTVLLdnaLATMGAGLPSAMAAHLVHPDRPVISVC 207
Cdd:PRK06163 14 NRFDL-TCRLVAKLKD---EEAVIGgIGNTNFDLWAA----GQRPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALE 82
|
90 100 110
....*....|....*....|....*....|.
gi 2174414276 208 GDGGFMMNSQELETAVRLGMHITVVILRDDG 238
Cdd:PRK06163 83 GDGSLLMQLGALGTIAALAPKNLTIIVMDNG 113
|
|
| |
