|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-552 |
0e+00 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 957.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 1 MSDSLPQRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRG 80
Cdd:PRK08199 1 MTSTPRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 81 PGATHAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGP 160
Cdd:PRK08199 81 PGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 161 VVVALPEEILFGSAQVADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFR 240
Cdd:PRK08199 161 VVLALPEDVLSETAEVPDAPPYRRVAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 RQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSLVRSPAPAQTLIHVHPDSAELNRVYLARLP 320
Cdd:PRK08199 241 RQDLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGYTLLDIPVPRQTLVHVHPDAEELGRVYRPDLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IQATPCAFAEALADLAPLPSSTWQDWREAAHADYLAYSTPaasDPAVQGVDLASVVAYLSENLPDDAVIANGAGNYAVWV 400
Cdd:PRK08199 321 IVADPAAFAAALAALEPPASPAWAEWTAAAHADYLAWSAP---LPGPGAVQLGEVMAWLRERLPADAIITNGAGNYATWL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 401 HRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGTIRM 480
Cdd:PRK08199 398 HRFFRFRRYRTQLAPTSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRM 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597231 481 HQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPRQITPQARLA 552
Cdd:PRK08199 478 HQEREYPGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPEAITPTATLS 549
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
6-552 |
0e+00 |
|
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: 627.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 6 PQRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATH 85
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 86 AANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVAL 165
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 166 PEEILFgsAQVADAPEPRVLPG-----RPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFR 240
Cdd:COG0028 161 PKDVQA--AEAEEEPAPPELRGyrprpAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 RQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSlvrSPAPAQTLIHVHPDSAELNRVYLARLP 320
Cdd:COG0028 239 GKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWD---EFAPDAKIIHIDIDPAEIGKNYPVDLP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IQATPCAFAEALADL---APLPSSTWQDWREAAHADYLAySTPAASDPavqgVDLASVVAYLSENLPDDAVIANGAGNYA 397
Cdd:COG0028 316 IVGDAKAVLAALLEAlepRADDRAAWLARIAAWRAEYLA-AYAADDGP----IKPQRVIAALREALPDDAIVVTDVGQHQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 398 VWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLG 476
Cdd:COG0028 391 MWAARYLRFRRPRRFLTSGGlGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLG 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597231 477 TIRMHQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPRQITPQARLA 552
Cdd:COG0028 471 MVRQWQELFYGGRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATLD 546
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
10-541 |
5.30e-120 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 365.20 E-value: 5.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEEI 169
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 170 LFGSAQVaDAPEPRVLPG-RPGATA----MAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDL 244
Cdd:TIGR00118 163 TTAEIEY-PYPEKVNLPGyRPTVKGhplqIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 245 FDNRDPHYAGQLGF-GAAPALLErLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARLPI-- 321
Cdd:TIGR00118 242 FPEDHPLSLGMLGMhGTKTANLA-VHECDLIIAVGARFDDRVTGN---LAKFAPNAKIIHIDIDPAEIGKNVRVDIPIvg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 322 QATPC--AFAEALADLAPLPSSTW----QDWReaahADYlaystPAASDPAVQGVDLASVVAYLSENLPDDAVIANGAGN 395
Cdd:TIGR00118 318 DARNVleELLKKLFELKERKESAWleqiNKWK----KEY-----PLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 396 YAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGaTPVVIVV-NNG 473
Cdd:TIGR00118 389 HQMWAAQFYPFRKPRRFITSGGlGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYD-IPVKILIlNNR 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597231 474 MLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:TIGR00118 468 YLGMVRQWQELFYEERYSHTHMGSlPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVD 536
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
8-543 |
1.19e-105 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 327.61 E-value: 1.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 8 RNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDtDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAA 87
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 88 NGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPE 167
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 168 EILFGSAQVADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDLFDN 247
Cdd:PRK08978 160 DIQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 248 RDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSlvrSPAPAQTLIHVHPDSAELNRVYLARLPIQATPCA 327
Cdd:PRK08978 240 DHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLN---TFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 328 FAEALAdlAPLPSSTWQDWREAAHADY-LAYSTPaasDPAVQGVDLasvVAYLSENLPDDAVIANGAGNYAVWVHRFYRY 406
Cdd:PRK08978 317 LLPALQ--QPLNIDAWRQHCAQLRAEHaWRYDHP---GEAIYAPAL---LKQLSDRKPADTVVTTDVGQHQMWVAQHMRF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 407 RQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQfGATPVVIVV-NNGMLGTIRMHQER 484
Cdd:PRK08978 389 TRPENFITSSGlGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKR-KQLPVKIVLlDNQRLGMVRQWQQL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 485 EYPGRVSATRL-DNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPR 543
Cdd:PRK08978 468 FFDERYSETDLsDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDEL 527
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
9-541 |
2.04e-104 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 324.47 E-value: 2.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDgIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQV--ESAFKGReaFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP 166
Cdd:PRK08322 81 GVAYAQLGGMPMVAITGQKpiKRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 167 EEIlfGSAQVADAPEPRVLPGRPGA--TAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDL 244
Cdd:PRK08322 159 EDI--AAEETDGKPLPRSYSRRPYAspKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 245 FDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGEtpsagYSLVR-SPAPAQTLIHVHPDSAELNRVYLARLP--- 320
Cdd:PRK08322 237 IPETHPLSLGTAGLSQGDYVHCAIEHADLIINVGHDVIE-----KPPFFmNPNGDKKVIHINFLPAEVDPVYFPQVEvvg 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 -IQATPCAFAEALADLAPLPSSTWQDWREAAHADYLAYSTPAASDPAVQgvdlaSVVAYLSENLPDDAVIA--NGAgnYA 397
Cdd:PRK08322 312 dIANSLWQLKERLADQPHWDFPRFLKIREAIEAHLEEGADDDRFPMKPQ-----RIVADLRKVMPDDDIVIldNGA--YK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 398 VWVHRFYRYRQARTQLApTNG--AMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGML 475
Cdd:PRK08322 385 IWFARNYRAYEPNTCLL-DNAlaTMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAY 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597231 476 GTIRMHQEREYpGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:PRK08322 464 GMIRWKQENMG-FEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVD 528
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
9-547 |
2.12e-101 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 317.85 E-value: 2.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDgIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSD-LIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGSAQVADAPEPRVLP---------GRPGATAMAelRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSF 239
Cdd:PRK06276 161 VQEGELDLEKYPIPAKIDlpgykpttfGHPLQIKKA--AELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 240 RRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARL 319
Cdd:PRK06276 239 MGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGD---ISSFAPNAKIIHIDIDPAEIGKNVRVDV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 320 PIQATPCA-FAEALADLAPLPSSTWQDWREAAHadYLAYSTPAASDPAVQGVDLASVVAYLSENLPD-----DAVIANGA 393
Cdd:PRK06276 316 PIVGDAKNvLRDLLAELMKKEIKNKSEWLERVK--KLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 394 GNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGaTPVVIVV-N 471
Cdd:PRK06276 394 GQNQMWMAHFFKTSAPRSFISSGGlGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYD-IPVVICIfD 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597231 472 NGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPRQITP 547
Cdd:PRK06276 473 NRTLGMVYQWQNLYYGKRQSEVHLGEtPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEALP 549
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-541 |
1.98e-99 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 312.09 E-value: 1.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 1 MSDSLPQRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDgIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRG 80
Cdd:PRK06048 1 MTGSTEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSD-LRHILVRHEQAAAHAADGYARATGKVGVCVATSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 81 PGATHAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGP 160
Cdd:PRK06048 80 PGATNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 161 VVVALPEEILFGSAQVaDAPEPRVLPG-RP----GATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPV 235
Cdd:PRK06048 160 VLIDLPKDVTTAEIDF-DYPDKVELRGyKPtykgNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 236 ATSFRRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVY 315
Cdd:PRK06048 239 TTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGK---LASFAPNAKIIHIDIDPAEISKNV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 316 LARLPIQA-TPCAFAEALADLAPLPSSTWQDWREAAHADYlaystPAASDPAVQGVDLASVVAYLSENLPdDAVIANGAG 394
Cdd:PRK06048 316 KVDVPIVGdAKQVLKSLIKYVQYCDRKEWLDKINQWKKEY-----PLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 395 NYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNG 473
Cdd:PRK06048 390 QHQMWAAQYFKYKYPRTFITSGGlGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNG 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597231 474 MLGTIRMHQEREYPGRVSATRL-DNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:PRK06048 470 YLGMVRQWQELFYDKRYSHTCIkGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVE 538
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
7-541 |
1.68e-94 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 299.32 E-value: 1.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 7 QRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHA 86
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 87 ANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP 166
Cdd:PRK08527 82 VTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 167 EEIlfgSAQVAD--APEPRVLPG-RP----GATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSF 239
Cdd:PRK08527 162 KDV---TATLGEfeYPKEISLKTyKPtykgNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 240 RRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSLVRSPApaqTLIHVHPDSAELNRVYLARL 319
Cdd:PRK08527 239 MARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHA---KIIHVDIDPSSISKIVNADY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 320 PIQATpcaFAEALADLAPL----PSSTWQDWREAAhADY-----LAYSTpaaSDPAVQGvdlASVVAYLSENLPDDAVIA 390
Cdd:PRK08527 316 PIVGD---LKNVLKEMLEElkeeNPTTYKEWREIL-KRYnelhpLSYED---SDEVLKP---QWVIERVGELLGDDAIIS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 391 NGAGNYAVWVHRFYRYRQARtQLAPTN--GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGaTPVV- 467
Cdd:PRK08527 386 TDVGQHQMWVAQFYPFNYPR-QLATSGglGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYK-IPVIn 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597231 468 IVVNNGMLGTIRMHQEREYPGRVSATRLD-NPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:PRK08527 464 IILNNNFLGMVRQWQTFFYEERYSETDLStQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKID 538
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
7-544 |
1.02e-93 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 297.39 E-value: 1.02e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 7 QRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHA 86
Cdd:PRK08155 12 RFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 87 ANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP 166
Cdd:PRK08155 92 VTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 167 EEILFGSAQVADAPEPrVLPGRPGATAMAELRE---LLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQD 243
Cdd:PRK08155 172 KDVQTAVIELEALPAP-AEKDAAPAFDEESIRDaaaMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 244 LFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARLPIQA 323
Cdd:PRK08155 251 MLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGK---TEQFCPNAKIIHVDIDRAELGKIKQPHVAIQA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 324 TpcaFAEALADLAPL----PSSTWQDWREAAHADYlAYSTPAASDPaVQGVDLASVVAylsENLPDDAVIANGAGNYAVW 399
Cdd:PRK08155 328 D---VDDVLAQLLPLveaqPRAEWHQLVADLQREF-PCPIPKADDP-LSHYGLINAVA---ACVDDNAIITTDVGQHQMW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 400 VHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGTI 478
Cdd:PRK08155 400 TAQAYPLNRPRQWLTSGGlGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597231 479 RMHQEREYPGRVSATRLD-NPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPRQ 544
Cdd:PRK08155 480 HQQQSLFYGQRVFAATYPgKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEE 546
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
10-527 |
3.09e-93 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 296.11 E-value: 3.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTdGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYES-GLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEEI 169
Cdd:PRK06725 96 LADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 170 LFGSAqVADAPEPRVLPG-----RPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDL 244
Cdd:PRK06725 176 QNEKV-TSFYNEVVEIPGykpepRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 245 FDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSLVrspAPAQTLIHVHPDSAELNRVYLARLPIQAT 324
Cdd:PRK06725 255 YPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELF---SPHSKKVHIDIDPSEFHKNVAVEYPVVGD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 325 pcaFAEALADLAPLPSSTWQD-WREAAHADYLAYSTPAASDPAVqgVDLASVVAYLSENLPDDAVIANGAGNYAVWVHRF 403
Cdd:PRK06725 332 ---VKKALHMLLHMSIHTQTDeWLQKVKTWKEEYPLSYKQKESE--LKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 404 YRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGTIRMHQ 482
Cdd:PRK06725 407 YKAKNPRTFLTSGGlGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQ 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15597231 483 EREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRA 527
Cdd:PRK06725 487 EMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEA 531
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
8-508 |
4.34e-90 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 287.87 E-value: 4.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 8 RNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAA 87
Cdd:PRK07282 10 KSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 88 NGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPE 167
Cdd:PRK07282 90 TGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 168 EIlfGSAQVADAPEPRV-LPG-----RPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRR 241
Cdd:PRK07282 170 DV--SALETDFIYDPEVnLPSyqptlEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 242 QDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGEtpsagySLVRSP---APAQTLIHVHPDSAELNRVYLAR 318
Cdd:PRK07282 248 QGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDD------RLTGNPktfAKNAKVAHIDIDPAEIGKIIKTD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 319 LPIQATPCAFAEALADLaPLPSSTWQDWREAAHADylaYSTPAASDPAVQGVDLASVVAYLSENLPDDAVIANGAGNYAV 398
Cdd:PRK07282 322 IPVVGDAKKALQMLLAE-PTVHNNTEKWIEKVTKD---KNRVRSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 399 WVHRFYRYRQARtQLAPTN--GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLG 476
Cdd:PRK07282 398 WAAQYYPYQNER-QLVTSGglGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLG 476
|
490 500 510
....*....|....*....|....*....|...
gi 15597231 477 TIRMHQEREYPGRVSATRLDN-PDFVALARAFG 508
Cdd:PRK07282 477 MVRQWQESFYEGRTSESVFDTlPDFQLMAQAYG 509
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
6-529 |
5.93e-90 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 288.80 E-value: 5.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 6 PQR-NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGAT 84
Cdd:PRK07789 28 PERmTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 85 HAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVA 164
Cdd:PRK07789 108 NLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 165 LPEEILFGSAQVADAPEPRvLPG-RPGATAMA-ELRE---LLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSF 239
Cdd:PRK07789 188 IPKDALQAQTTFSWPPRMD-LPGyRPVTKPHGkQIREaakLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 240 RRQDLFDNRDPHYAGQLGF-GAAPALLErLRQADLLLVVGARL-----GETPSAgyslvrspAPAQTLIHVHPDSAELNR 313
Cdd:PRK07789 267 MARGAFPDSHPQHLGMPGMhGTVAAVAA-LQRSDLLIALGARFddrvtGKLDSF--------APDAKVIHADIDPAEIGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 314 VYLARLPI----QATPCAFAEAL-ADLAPLPSSTWQDWREAAH---ADY-LAYSTPAASDPAVQgvdlaSVVAYLSENLP 384
Cdd:PRK07789 338 NRHADVPIvgdvKEVIAELIAALrAEHAAGGKPDLTAWWAYLDgwrETYpLGYDEPSDGSLAPQ-----YVIERLGEIAG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 385 DDAVIANGAGNYAVWVHRFYRYRQARTQLaptN----GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQ 460
Cdd:PRK07789 413 PDAIYVAGVGQHQMWAAQFIDYEKPRTWL---NsgglGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAI 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597231 461 FGATPVVIVVNNGMLGTIRMHQEREYPGRVSATRLDN-----PDFVALARAFGAHAERVECSADFPAAFRRARE 529
Cdd:PRK07789 490 EGIPIKVALINNGNLGMVRQWQTLFYEERYSNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARA 563
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
10-537 |
7.98e-87 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 278.43 E-value: 7.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDT-DGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAgDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAF--KGREAFQEV-DYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVAL 165
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGQIPSALigKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 166 PEEILFGSAQVADAPEPRVLPGRPG-ATAMAELRELLANARRPLLVLGGSGWDSAARKRlgAFVEANGLPVaTSFRR-QD 243
Cdd:PRK08266 166 PWDVFGQRAPVAAAPPLRPAPPPAPdPDAIAAAAALIAAAKNPMIFVGGGAAGAGEEIR--ELAEMLQAPV-VAFRSgRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 244 LFDNRDPHYagqLGFGAApalLERLRQADLLLVVGARLgETPsagYSLVRSPAPAQTLIHVHPDSAELNRvYLARLPIQA 323
Cdd:PRK08266 243 IVSDRHPLG---LNFAAA---YELWPQTDVVIGIGSRL-ELP---TFRWPWRPDGLKVIRIDIDPTEMRR-LKPDVAIVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 324 TPCAFAEALADLAPLPSSTWQDwREAAHADylaysTPAASDPAVQGVD-LASVVAYLSENLPDDAVIANG------AGNY 396
Cdd:PRK08266 312 DAKAGTAALLDALSKAGSKRPS-RRAELRE-----LKAAARQRIQAVQpQASYLRAIREALPDDGIFVDElsqvgfASWF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 397 AVWVHrfyryrQARTQLAPT-NGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGML 475
Cdd:PRK08266 386 AFPVY------APRTFVTCGyQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAY 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597231 476 GTIRMHQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:PRK08266 460 GNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIE 521
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
7-537 |
2.42e-85 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 276.93 E-value: 2.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 7 QRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALY--DTDG-IRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGA 83
Cdd:PRK07418 18 RATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 84 THAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVV 163
Cdd:PRK07418 98 TNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 164 ALPEEI---LFGSAQVadAPEPRVLPG-----RPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPV 235
Cdd:PRK07418 178 DIPKDVgqeEFDYVPV--EPGSVKPPGyrptvKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 236 ATSFRRQDLFDNRDPHYAGQLGF-GAAPALLErLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRV 314
Cdd:PRK07418 256 TTTLMGKGAFDEHHPLSVGMLGMhGTAYANFA-VTECDLLIAVGARFDDRVTGK---LDEFASRAKVIHIDIDPAEVGKN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 315 YLARLPIQATpcaFAEALADL--------APLPSSTW----QDWREaahaDYLAYSTPAASDPAVQGVDLAsvvayLSEN 382
Cdd:PRK07418 332 RRPDVPIVGD---VRKVLVKLlersleptTPPRTQAWleriNRWKQ----DYPLVVPPYEGEIYPQEVLLA-----VRDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 383 LPdDAVIANGAGNYAVWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFG 462
Cdd:PRK07418 400 AP-DAYYTTDVGQHQMWAAQFLRNGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYG 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597231 463 ATPVVIVVNNGMLGTIRMHQEREYPGRVSATRLDN--PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:PRK07418 479 INVKTVIINNGWQGMVRQWQESFYGERYSASNMEPgmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLID 555
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
10-541 |
4.99e-81 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 264.39 E-value: 4.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYD---TDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHA 86
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlaNGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 87 ANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP 166
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 167 EEILFGSAQVADAPEPRVLPG-RPGATAMAELR-----ELLANARRPLLVLG-GSGWDSAARKRLgAFVEANGLPVATSF 239
Cdd:PRK06456 164 RDIFYEKMEEIKWPEKPLVKGyRDFPTRIDRLAlkkaaEILINAERPIILVGtGVVWSNATPEVL-ELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 240 RRQDLFDNRDPHYAGQLG-FGAAPALLERLrQADLLLVVGARLGETPSAGYSLVRSPAPAQTLIHVHPDSAElnRVYLAR 318
Cdd:PRK06456 243 PGKTAIPHDHPLYFGPMGyYGRAEASMAAL-ESDAMLVVGARFSDRTFTSYDEMVETRKKFIMVNIDPTDGE--KAIKVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 319 LPIQATPCAFAEALADLAP-----LPSSTW----QDWREaAHADYLAYSTPAASDPavqgvdlASVVAYLSENLPDDAVI 389
Cdd:PRK06456 320 VGIYGNAKIILRELIKAITelgqkRDRSAWlkrvKEYKE-YYSQFYYTEENGKLKP-------WKIMKTIRQALPRDAIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 390 ANGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVI 468
Cdd:PRK06456 392 TTGVGQHQMWAEVFWEVLEPRTFLTSSGmGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597231 469 VVNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:PRK06456 472 IFDNRTLGLVRQVQDLFFGKRIVGVDYGPsPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVD 545
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
10-508 |
8.98e-81 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 263.53 E-value: 8.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEEI 169
Cdd:PRK06466 86 IATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 170 LFGSAQVA-DAPEPRVL-----PGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQD 243
Cdd:PRK06466 166 TNPAEKFEyEYPKKVKLrsyspAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 244 LFDNRDPHYAGQLGF-GAAPALLErLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARLPI- 321
Cdd:PRK06466 246 GFPGTDRQFLGMLGMhGTYEANMA-MHHADVILAVGARFDDRVTNG---PAKFCPNAKIIHIDIDPASISKTIKADIPIv 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 322 QATPCAFAEALADL--------APLPSSTWQ---DWReaAHADYLAYSTPAASDPAVQgvdlaSVVAYLSENLPDDAVIA 390
Cdd:PRK06466 322 GPVESVLTEMLAILkeigekpdKEALAAWWKqidEWR--GRHGLFPYDKGDGGIIKPQ-----QVVETLYEVTNGDAYVT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 391 NGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIV 469
Cdd:PRK06466 395 SDVGQHQMFAAQYYKFNKPNRWINSGGlGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIIN 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15597231 470 VNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFG 508
Cdd:PRK06466 475 LNNGALGMVRQWQDMQYEGRHSHSYMESlPDFVKLAEAYG 514
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
9-537 |
1.64e-80 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 262.77 E-value: 1.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTdGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK07710 17 TGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDC-GIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGSAQVaDAPEPRVLPG-----RPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQD 243
Cdd:PRK07710 176 MVVEEGEF-CYDVQMDLPGyqpnyEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 244 LFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARLPIQA 323
Cdd:PRK07710 255 GFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGN---LAYFAKEATVAHIDIDPAEIGKNVPTEIPIVA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 324 TPCAFAEALADlaplpsstwQDWREAAHADYLAY------STPAASDPAVQGVDLASVVAYLSENLPDDAVIANGAGNYA 397
Cdd:PRK07710 332 DAKQALQVLLQ---------QEGKKENHHEWLSLlknwkeKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 398 VWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLG 476
Cdd:PRK07710 403 MWAAQYYPFKTPDKWVTSGGlGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALG 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597231 477 TIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:PRK07710 483 MVRQWQEEFYNQRYSHSLLSCqPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVID 544
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
6-537 |
2.64e-80 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 261.71 E-value: 2.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 6 PQRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDtDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATH 85
Cdd:PRK08617 3 KKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALED-SGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 86 AANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVAL 165
Cdd:PRK08617 82 LATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 166 PEEILfgSAQVAD---APEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFR-- 240
Cdd:PRK08617 162 PQDVV--DAPVTSkaiAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQaa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 ---RQDLFDnrdpHYAGQLG-FGAAPA-LLerLRQADLLLVVGarlgetpsagYSLVR-SPA-----PAQTLIHVHPDSA 309
Cdd:PRK08617 240 gviSRELED----HFFGRVGlFRNQPGdEL--LKKADLVITIG----------YDPIEyEPRnwnseGDATIIHIDVLPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 310 ELNRVYLARLP----IQATPCAFAEALADLApLPSSTwQDWREAAHADYLAYSTPAASDPAvQGVDLASVVAYLSENLPD 385
Cdd:PRK08617 304 EIDNYYQPEREligdIAATLDLLAEKLDGLS-LSPQS-LEILEELRAQLEELAERPARLEE-GAVHPLRIIRALQDIVTD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 386 DAVIANGAGNYAVWVHRFYRYRQARtQLAPTNG--AMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGA 463
Cdd:PRK08617 381 DTTVTVDVGSHYIWMARYFRSYEPR-HLLFSNGmqTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKL 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597231 464 TPVVIVVNNGMLGTIRMHQEREYpGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:PRK08617 460 NIVHIIWNDGHYNMVEFQEEMKY-GRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVID 532
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
10-541 |
3.47e-79 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 258.53 E-value: 3.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDtDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALED-KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEEI 169
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 170 LFGSAQV-ADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFR-----RQD 243
Cdd:TIGR02418 160 VDSPVSVkAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQgagavSRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 244 LFDnrdpHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSLVRSpapaQTLIHVHPDSAELNRVYLARLP--- 320
Cdd:TIGR02418 240 LED----HFFGRVGLFRNQPGDRLLKQADLVITIGYDPIEYEPRNWNSEND----ATIVHIDVEPAQIDNNYQPDLElvg 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 -IQATPCAFAEALADLAPLPSStwQDWREAAHADYLAYSTPAAsDPAVQGVDLASVVAYLSENLPDDAVIANGAGNYAVW 399
Cdd:TIGR02418 312 dIASTLDLLAERIPGYELPPDA--LAILEDLKQQREALDRVPA-TLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 400 VHRFYRYRQARtQLAPTNG--AMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGT 477
Cdd:TIGR02418 389 MARYFRSYRAR-HLLISNGmqTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNM 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597231 478 IRMHQEREYpGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:TIGR02418 468 VEFQEEMKY-QRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVD 530
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
7-541 |
2.62e-78 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 257.71 E-value: 2.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 7 QRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHA 86
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 87 ANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP 166
Cdd:PRK09107 90 VTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 167 EEILFGS--------AQVADAPEPRVlpgRPGATAMAELRELLANARRPLLVLGG----SGwdSAARKRLGAFVEANGLP 234
Cdd:PRK09107 170 KDVQFATgtytppqkAPVHVSYQPKV---KGDAEAITEAVELLANAKRPVIYSGGgvinSG--PEASRLLRELVELTGFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 235 VATSFRRQDLFDNRDPHYAGQLGF-GAAPALLErLRQADLLLVVGARLGETPSAgysLVRSPAPAQTLIHVHPDSAELNR 313
Cdd:PRK09107 245 ITSTLMGLGAYPASGKNWLGMLGMhGTYEANMA-MHDCDVMLCVGARFDDRITG---RLDAFSPNSKKIHIDIDPSSINK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 314 VYLARLPIQATpcaFAEALADL-------APLPSST-----WQD---WREAAHADYLAYSTPAASDPAVQgvdlasvvaY 378
Cdd:PRK09107 321 NVRVDVPIIGD---VGHVLEDMlrlwkarGKKPDKEaladwWGQiarWRARNSLAYTPSDDVIMPQYAIQ---------R 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 379 LSENLPD-DAVIANGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELA 456
Cdd:PRK09107 389 LYELTKGrDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGlGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 457 TAAQFGAtPVVI-VVNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRARESGRPA 534
Cdd:PRK09107 469 TAVQYNL-PVKIfILNNQYMGMVRQWQQLLHGNRLSHSYTEAmPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPV 547
|
....*..
gi 15597231 535 LLELLTD 541
Cdd:PRK09107 548 IFDCRVA 554
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-542 |
2.79e-78 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 257.42 E-value: 2.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 2 SDSLPQRNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGP 81
Cdd:PRK06965 15 SPPAADSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 82 GATHAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPV 161
Cdd:PRK06965 95 GVTNAVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 162 VVALPEEILFGSAQVA--DAPEPRVL-PGRPG-ATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVAT 237
Cdd:PRK06965 175 VVDIPKDVSKTPCEYEypKSVEMRSYnPVTKGhSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 238 SFRRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGEtpsagySLVRSPA----PAQTLIHVHPDSAELNR 313
Cdd:PRK06965 255 TLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDD------RVIGNPAhfasRPRKIIHIDIDPSSISK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 314 VYLARLPI----------------QATPCAFAEALADLAplpsSTWQDWREaahADYLAYS-TPAASDPAVqgvdlasVV 376
Cdd:PRK06965 329 RVKVDIPIvgdvkevlkelieqlqTAEHGPDADALAQWW----KQIEGWRS---RDCLKYDrESEIIKPQY-------VV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 377 AYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQEL 455
Cdd:PRK06965 395 EKLWELTDGDAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGlGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQEL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 456 ATAAQFGaTPVVIV-VNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRARE-SGR 532
Cdd:PRK06965 475 STCLQYD-TPVKIIsLNNRYLGMVRQWQEIEYSKRYSHSYMDAlPDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDR 553
|
570
....*....|
gi 15597231 533 PALLELLTDP 542
Cdd:PRK06965 554 TVFLDFQTDP 563
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
9-508 |
6.13e-78 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 256.38 E-value: 6.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK06882 5 SGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:PRK06882 85 GIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGSAQVADAPEPRV--------LPGRPGATAMAeLRELLAnARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFR 240
Cdd:PRK06882 165 MVNPANKFTYEYPEEVslrsynptVQGHKGQIKKA-LKALLV-AKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 RQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARLP 320
Cdd:PRK06882 243 GLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNN---LAKYCPNAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IQATP----CAFAEALADLAPLPSST-----WQDWREAAHADYLAYSTpaaSDPAVQGVDLASVVAYLSENlpdDAVIAN 391
Cdd:PRK06882 320 IVGSAknvlEEFLSLLEEENLAKSQTdltawWQQINEWKAKKCLEFDR---TSDVIKPQQVVEAIYRLTNG---DAYVAS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 392 GAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGaTPVVIV- 469
Cdd:PRK06882 394 DVGQHQMFAALHYPFDKPRRWINSGGaGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYD-IPVVIVs 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15597231 470 VNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFG 508
Cdd:PRK06882 473 LNNRFLGMVKQWQDLIYSGRHSQVYMNSlPDFAKLAEAYG 512
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
11-538 |
9.34e-78 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 254.51 E-value: 9.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 11 GQILVEALRRNAVDTVYCIPGESYLPVLDALYDTdGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGV 90
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGS-GIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 91 HTAQQDSTPMILF--VGQVESAFKGREAFQEV-DYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPE 167
Cdd:PRK07524 84 GQAYADSIPMLVIssVNRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 168 EIL-FGSAQVADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRlgAFVEANGLPVATSFRRQDLFD 246
Cdd:PRK07524 164 DVLaAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAALR--ALAERLDAPVALTINAKGLLP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 247 NRDPhyagqLGFGAAPALL---ERLRQADLLLVVGARLGETPSAGYSLVRSPAPAqTLIHVHPDSAELNRVYLARLPIQA 323
Cdd:PRK07524 242 AGHP-----LLLGASQSLPavrALIAEADVVLAVGTELGETDYDVYFDGGFPLPG-ELIRIDIDPDQLARNYPPALALVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 324 TPCAFAEALadLAPLPSSTWQDWREAAHADYLAYSTPAASDPAVQGvdLASVVAYLSENLPDDAVIANG-----AGNYAV 398
Cdd:PRK07524 316 DARAALEAL--LARLPGQAAAADWGAARVAALRQALRAEWDPLTAA--QVALLDTILAALPDAIFVGDStqpvyAGNLYF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 399 WVHRFYRYRQARTQLaptnGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGTI 478
Cdd:PRK07524 392 DADAPRRWFNASTGY----GTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEI 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 479 RMHQEREYPGRVSATrLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLEL 538
Cdd:PRK07524 468 RRYMVARDIEPVGVD-PYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
8-544 |
1.79e-77 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 255.43 E-value: 1.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 8 RNGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAA 87
Cdd:PLN02470 13 RKGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 88 NGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPE 167
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 168 EILFGSAqVADAPEPRVLPGR-------PGATAMAELRELLANARRPLLVLGGSGWDSAarKRLGAFVEANGLPVATSFR 240
Cdd:PLN02470 173 DIQQQLA-VPNWNQPMKLPGYlsrlpkpPEKSQLEQIVRLISESKRPVVYVGGGCLNSS--EELREFVELTGIPVASTLM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 RQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGYSLVRSPApaqTLIHVHPDSAELNRVYLARLP 320
Cdd:PLN02470 250 GLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRA---SIVHIDIDPAEIGKNKQPHVS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IqatpCA-FAEALADL------APLPSSTWQDWREAAHADYLAYstPAASDPAVQGVDLASVVAYLSENLPDDAVIANGA 393
Cdd:PLN02470 327 V----CAdVKLALQGLnklleeRKAKRPDFSAWRAELDEQKEKF--PLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 394 GNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATaAQFGATPV-VIVVN 471
Cdd:PLN02470 401 GQHQMWAAQWYKYKEPRRWLTSGGlGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELAT-IHVENLPVkIMVLN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 472 NGMLGTIRMHQEREYPGRVSATRLDN--------PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTdPR 543
Cdd:PLN02470 480 NQHLGMVVQWEDRFYKANRAHTYLGDpdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIV-PH 558
|
.
gi 15597231 544 Q 544
Cdd:PLN02470 559 Q 559
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-547 |
2.05e-77 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 255.07 E-value: 2.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 1 MSDSLPQRNGGQILVEALRRNAVDTVYcipGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRG 80
Cdd:PRK06112 7 APGFTLNGTVAHAIARALKRHGVEQIF---GQSLPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 81 PGATHAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGP 160
Cdd:PRK06112 84 PAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 161 VVVALPEEILFGSAQVADAPEPRVLP------GRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLP 234
Cdd:PRK06112 164 VVLLLPADLLTAAAAAPAAPRSNSLGhfpldrTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 235 VATSFRRQDLFDNRDPHYAGQLGFGAAPALLER-----LRQADLLLVVGARLGETPSAGYSLVrsPAPAQtLIHVHPDSA 309
Cdd:PRK06112 244 VATTNMGKGAVDETHPLSLGVVGSLMGPRSPGRhlrdlVREADVVLLVGTRTNQNGTDSWSLY--PEQAQ-YIHIDVDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 310 ELNRVYLA-RLPIQA--TPCAFAEAL------------ADLAPLPSSTWQDWREAAHADYLAYSTPAASDpavqgvdlaS 374
Cdd:PRK06112 321 EVGRNYEAlRLVGDArlTLAALTDALrgrdlaaragrrAALEPAIAAGREAHREDSAPVALSDASPIRPE---------R 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 375 VVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAPTNG--AMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYP 452
Cdd:PRK06112 392 IMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGMRFLTPRGlaGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVW 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 453 QELATAAQFGATPVVIVVNNGMLGTIRMHQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGR 532
Cdd:PRK06112 472 AELETARRMGVPVTIVVLNNGILGFQKHAETVKFGTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPG 551
|
570
....*....|....*
gi 15597231 533 PALLELLTDPRQITP 547
Cdd:PRK06112 552 PTLIEVITDPSAFPP 566
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
9-527 |
5.50e-77 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 253.59 E-value: 5.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK08979 5 SGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:PRK08979 85 GIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILfGSAQVADAPEPRVLPGR---PGATAMA-----ELRELLAnARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFR 240
Cdd:PRK08979 165 CL-NPAILHPYEYPESIKMRsynPTTSGHKgqikrGLQALLA-AKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 RQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPSAGyslVRSPAPAQTLIHVHPDSAELNRVYLARLP 320
Cdd:PRK08979 243 GLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNN---LEKYCPNATILHIDIDPSSISKTVRVDIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IQATpcafAEALAD--LAPLPSST-----------WQD---WREaahADYLAYSTPAASDPAVQgvdlasVVAYLSENLP 384
Cdd:PRK08979 320 IVGS----ADKVLDsmLALLDESGetndeaaiaswWNEievWRS---RNCLAYDKSSERIKPQQ------VIETLYKLTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 385 DDAVIANGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGa 463
Cdd:PRK08979 387 GDAYVASDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYD- 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597231 464 TPVVIV-VNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFGAHAERVECSADFPAAFRRA 527
Cdd:PRK08979 466 IPVKIInLNNRFLGMVKQWQDMIYQGRHSHSYMDSvPDFAKIAEAYGHVGIRISDPDELESGLEKA 531
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
14-537 |
1.14e-75 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 250.39 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 14 LVEALRRNAVDTVYCIPGESYLPVLDALYDTDG---IRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGV 90
Cdd:CHL00099 16 LIDSLVRHGVKHIFGYPGGAILPIYDELYAWEKkglIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 91 HTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP---- 166
Cdd:CHL00099 96 ATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPkdvg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 167 -EEILFgsaQVADAPEPRV-LPG-----RPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSF 239
Cdd:CHL00099 176 lEKFDY---YPPEPGNTIIkILGcrpiyKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 240 RRQDLFDNRDPHYAGQLGF-GAAPALLErLRQADLLLVVGARLGETPSAgySLVRSPAPAQtLIHVHPDSAELNRvylAR 318
Cdd:CHL00099 253 MGKGIFDEDHPLCLGMLGMhGTAYANFA-VSECDLLIALGARFDDRVTG--KLDEFACNAQ-VIHIDIDPAEIGK---NR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 319 LP-------IQATPCAFAEAL--ADLAPLPSSTwQDWREAAHADYLAY--STPAASdpavQGVDLASVVAYLSENLPdDA 387
Cdd:CHL00099 326 IPqvaivgdVKKVLQELLELLknSPNLLESEQT-QAWRERINRWRKEYplLIPKPS----TSLSPQEVINEISQLAP-DA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 388 VIANGAGNYAVWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVV 467
Cdd:CHL00099 400 YFTTDVGQHQMWAAQFLKCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKI 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597231 468 IVVNNGMLGTIRMHQEREYPGRVSATRLDN--PDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:CHL00099 480 IIINNKWQGMVRQWQQAFYGERYSHSNMEEgaPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLID 551
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
5-542 |
1.21e-75 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 250.30 E-value: 1.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 5 LPQRNGGQILVEALRRNAVDTVYCIPGESYLPVLDAL-YDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGA 83
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 84 THAANGVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRpGPVVV 163
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 164 ALPEEILfgSAQVADAPE---PRVLPG--RPGATAMAELRELLANARRPLLvLGGSGWDSaARKRLGAFVEANGLPVATS 238
Cdd:PRK08611 160 TIPDDLP--AQKIKDTTNktvDTFRPTvpSPKPKDIKKAAKLINKAKKPVI-LAGLGAKH-AKEELLAFAEKAKIPIIHT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 239 FRRQDLFDNRDPHYAGQLG-FGAAPAlLERLRQADLLLVVGARLgetPSAGYslvrSPAPAQTlIHVHPDSAELNRVYLA 317
Cdd:PRK08611 236 LPAKGIIPDDHPYSLGNLGkIGTKPA-YEAMQEADLLIMVGTNY---PYVDY----LPKKAKA-IQIDTDPANIGKRYPV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 318 RLPIQA-TPCAFAEALADLAPLPSSTW--------QDWREAAHADYLAYSTPAASDpavqgvdlaSVVAYLSENLPDDAV 388
Cdd:PRK08611 307 NVGLVGdAKKALHQLTENIKHVEDRRFleacqenmAKWWKWMEEDENNASTPIKPE---------RVMAAIQKIADDDAV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 389 IANGAGNYAVWVHRFYRyrqartqLAPTN--------GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQ 460
Cdd:PRK08611 378 LSVDVGTVTVWSARYLN-------LGTNQkfiisswlGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 461 FGATPVVIVVNNGMLGTIRMHQ----EREYpgrvsATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALL 536
Cdd:PRK08611 451 YKLPIVVVVLNNQQLAFIKYEQqaagELEY-----AIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVII 525
|
....*.
gi 15597231 537 ELLTDP 542
Cdd:PRK08611 526 DVYVDP 531
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
9-538 |
1.11e-73 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 244.13 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK07064 4 TVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREA--FQEV-DYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVAL 165
Cdd:PRK07064 84 ALVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 166 PEEILFGSAQVAD--APEPRVLPgRPGATAMAELRELLANARRPLLVLGGSGwdSAARKRLGAFVEAnGLPVATSFRRQD 243
Cdd:PRK07064 164 PIDIQAAEIELPDdlAPVHVAVP-EPDAAAVAELAERLAAARRPLLWLGGGA--RHAGAEVKRLVDL-GFGVVTSTQGRG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 244 LFDNRDPHYAGqlGFGAAPALLERLRQADLLLVVGARLGETPSAGYSLvrsPAPaQTLIHVHPDSAELNRVYLARLPIQA 323
Cdd:PRK07064 240 VVPEDHPASLG--AFNNSAAVEALYKTCDLLLVVGSRLRGNETLKYSL---ALP-RPLIRVDADAAADGRGYPNDLFVHG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 324 TPCAFAEALADLapLPSSTWQDwreAAHADYLAYSTPAASDPAVQGV-DLASVVAYLSENLPDDAV------IANgagny 396
Cdd:PRK07064 314 DAARVLARLADR--LEGRLSVD---PAFAADLRAAREAAVADLRKGLgPYAKLVDALRAALPRDGNwvrdvtISN----- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 397 AVWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLG 476
Cdd:PRK07064 384 STWGNRLLPIFEPRANVHALGGGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597231 477 TIRMHQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLEL 538
Cdd:PRK07064 464 VIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
14-540 |
7.88e-71 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 237.59 E-value: 7.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 14 LVEALRRNAVDTVYCIPGESYLPVLDaLYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVHTA 93
Cdd:PRK07525 12 FVETLQAHGITHAFGIIGSAFMDASD-LFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 94 QQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRpGPVVVALPEEILFGS 173
Cdd:PRK07525 91 YWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYFYGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 174 AQVaDAPEP-RVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDLFDNRDPHY 252
Cdd:PRK07525 170 IDV-EIPQPvRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAFPGSHPLW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 253 AGQLGFGAAPALLERLRQADLLLVVGARL---GETPsaGYSLVRSPAPAQtLIHV-----------------HPDSAELN 312
Cdd:PRK07525 249 VGPLGYNGSKAAMELIAKADVVLALGTRLnpfGTLP--QYGIDYWPKDAK-IIQVdinpdrigltkkvsvgiCGDAKAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 313 RVYLARLP---------------IQATPCAFAEALADLAPLPSSTWQDWREAAHADYLAYSTPAASDPAVQGVdlasvva 377
Cdd:PRK07525 326 RELLARLAerlagdagreerkalIAAEKSAWEQELSSWDHEDDDPGTDWNEEARARKPDYMHPRQALREIQKA------- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 378 ylsenLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAP-TNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELA 456
Cdd:PRK07525 399 -----LPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPgSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 457 TAAQFGATPVVIVVNNGMLGTIRMHQEREYPGRVSATRLD-NPDFVALARAFGAHAERVECSADFPAAFRRA---RESGR 532
Cdd:PRK07525 474 TAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDnNVSYAGIAEAMGAEGVVVDTQEELGPALKRAidaQNEGK 553
|
....*...
gi 15597231 533 PALLELLT 540
Cdd:PRK07525 554 TTVIEIMC 561
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
9-508 |
2.06e-70 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 236.29 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK07979 5 SGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:PRK07979 85 GIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGSAQVadapePRVLP-------------GRPGATAMAeLRELLAnARRPLLVLGGSGWDSAARKRLGAFVEANGLPV 235
Cdd:PRK07979 165 ILNPANKL-----PYVWPesvsmrsynpttqGHKGQIKRA-LQTLVA-AKKPVVYVGGGAINAACHQQLKELVEKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 236 ATSFRRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETPS---AGYslvrspAPAQTLIHVHPDSAELN 312
Cdd:PRK07979 238 VSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTnnlAKY------CPNATVLHIDIDPTSIS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 313 RVYLARLPIQATPCAFAEALADLAPLPSST---------WQ---DWREAAHADYlaystpaasDPAVQGVDLASVVAYLS 380
Cdd:PRK07979 312 KTVTADIPIVGDARQVLEQMLELLSQESAHqpldeirdwWQqieQWRARQCLKY---------DTHSEKIKPQAVIETLW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 381 ENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAA 459
Cdd:PRK07979 383 RLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGlGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTAL 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15597231 460 QFGATPVVIVVNNGMLGTIRMHQEREYPGRVSATRLDN-PDFVALARAFG 508
Cdd:PRK07979 463 QYELPVLVLNLNNRYLGMVKQWQDMIYSGRHSQSYMQSlPDFVRLAEAYG 512
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
14-541 |
1.31e-67 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 228.98 E-value: 1.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 14 LVEALRRNAVDTVYCIPGESYLPVLDaLYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVHTA 93
Cdd:TIGR03457 8 FVEVLVANGVTHAFGIMGSAFMDAMD-LFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAIAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 94 QQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRpGPVVVALPEEILFGS 173
Cdd:TIGR03457 87 YWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYFYGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 174 AQVaDAPEP-RVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDLFDNRDPHY 252
Cdd:TIGR03457 166 IDV-EIPRPvRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFPASHPLW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 253 AGQLGFGAAPALLERLRQADLLLVVGARLGETPS-AGYSLVRSPAPAQtLIHVHPDSAELNRVYLARLPIQATPCAFAEA 331
Cdd:TIGR03457 245 VGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTlPQYGIDYWPKNAK-IIQVDANAKMIGLVKKVTVGICGDAKAAAAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 332 L-------------ADLAPLPSSTWQDW----REAAHADYLAYSTPAASDPAVQGVDLA--SVVAYLSENLPDDAVIANG 392
Cdd:TIGR03457 324 IlqrlagkagdanrAERKAKIQAERSAWeqelSEMTHERDPFSLDMIVEQRQEEGNWLHprQVLRELEKAMPEDAIVSTD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 393 AGNYAVWVHRFYRYRQARTQLAP-TNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVN 471
Cdd:TIGR03457 404 IGNINSVANSYLRFEKPRKFLAPmSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIPVTAVVFR 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597231 472 NGMLGTIRMHQEREYPGRVSATRLDNP-DFVALARAFGAHAERVECSADFPAAFRRA---RESGRPALLELLTD 541
Cdd:TIGR03457 484 NRQWGAEKKNQVDFYNNRFVGTELESElSFAGIADAMGAKGVVVDKPEDVGPALKKAiaaQAEGKTTVIEIVCT 557
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
375-540 |
2.22e-65 |
|
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: 210.19 E-value: 2.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 375 VVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQART-QLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQ 453
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRfLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 454 ELATAAQFGATPVVIVVNNGMLGTIRMHQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRP 533
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGP 161
|
....*..
gi 15597231 534 ALLELLT 540
Cdd:cd00568 162 ALIEVKT 168
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
10-546 |
3.68e-61 |
|
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: 211.62 E-value: 3.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALY-DTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSaERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSgRPGPVVVALPEE 168
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ilFGSAQVAD-------APEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDsaARKRLGAFVEANGLPVATSFRR 241
Cdd:TIGR02720 160 --FGWQEIPDndyyassVSYQTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIGARK--AGEELEALSEKLKIPLISTGLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 242 QDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLgetPSAGYSlvRSPAPAQTLIHVHPDSAELNRVYLARLPI 321
Cdd:TIGR02720 236 KGIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNY---PFAEVS--KAFKNTKYFIQIDIDPAKLGKRHHTDIAV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 322 QATPCAFAEA-LADLAPLPSSTW--------QDWReaahaDYLAYSTPAASDPavqgVDLASVVAYLSENLPDDAVIANG 392
Cdd:TIGR02720 311 LADAKKALAAiLAQVEPRESTPWwqanvanvKNWR-----AYLASLEDKTEGP----LQAYQVYRAINKIAEDDAIYSID 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 393 AGNYAVWVHRFYRYR-QARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVN 471
Cdd:TIGR02720 382 VGDININSNRHLKMTpKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFS 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597231 472 NGMLGTIRMHQErEYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRAR--ESGRPALLEL-LTDPRQIT 546
Cdd:TIGR02720 462 NCTYGFIKDEQE-DTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKaiKQGKPVLIDAkITGDRPLP 538
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
12-544 |
4.66e-61 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 210.84 E-value: 4.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 12 QILVEALRRNAVDTVYCIPGESYLPVLDALYDTDgIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVH 91
Cdd:PRK06457 6 EVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSK-VKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 92 TAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRpGPVVVALPEEILF 171
Cdd:PRK06457 85 DAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDILR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 172 GSAQVADAPEPRVlPGRPGATAMAELRELLANARRPLLVLGGSGWDsaARKRLGAFVEANGLPVATSFRRQDLFDNRDPH 251
Cdd:PRK06457 164 KSSEYKGSKNTEV-GKVKYSIDFSRAKELIKESEKPVLLIGGGTRG--LGKEINRFAEKIGAPIIYTLNGKGILPDLDPK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 252 YAGQLG-FGAAPAlLERLRQADLLLVVGarlgetpsAGYSLVRSPAPAQTLIHVHPDSAELNRVYLARLPIqatPCAFAE 330
Cdd:PRK06457 241 VMGGIGlLGTKPS-IEAMDKADLLIMLG--------TSFPYVNFLNKSAKVIQVDIDNSNIGKRLDVDLSY---PIPVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 331 ALADLAPLPSSTWQDWREAAHADYLAYSTPAASDpaVQGVDLASVVAY-LSENLPDDAVIANGAGNYAVWVHRFYRYRQA 409
Cdd:PRK06457 309 FLNIDIEEKSDKFYEELKGKKEDWLDSISKQENS--LDKPMKPQRVAYiVSQKCKKDAVIVTDTGNVTMWTARHFRASGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 410 RT-QLAPTNGAMGYGLPAAIAASL-RDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGTIRMHQE-REY 486
Cdd:PRK06457 387 QTfIFSAWLGSMGIGVPGSVGASFaVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEvMGY 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597231 487 PGRvsATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPRQ 544
Cdd:PRK06457 467 PEW--GVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNE 522
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
12-167 |
5.53e-61 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 198.14 E-value: 5.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 12 QILVEALRRNAVDTVYCIPGESYLPVLDALYDtDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVH 91
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597231 92 TAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPE 167
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
10-548 |
8.64e-59 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 204.57 E-value: 8.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDtDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGARE-EGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEEI 169
Cdd:PRK05858 86 MAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 170 LFGSAQVADAPEPRVLPGR---PGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSfrrqdlfd 246
Cdd:PRK05858 166 AFSMADDDGRPGALTELPAgptPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMN-------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 247 nrdphyaGQlGFGAAPA----LLER-----LRQADLLLVVGA----RLgetpsaGYSLVRSPAPAqtlihVHPDSAELNR 313
Cdd:PRK05858 238 -------GM-GRGVVPAdhplAFSRargkaLGEADVVLVVGVpmdfRL------GFGVFGGTAQL-----VHVDDAPPQR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 314 VYlaRLPIQATPC----AFAEALADlAPLPSSTWQDWREAAHAdylAYSTPAASDPAVQGVDL-----ASVVAYLSENLP 384
Cdd:PRK05858 299 AH--HRPVAAGLYgdlsAILSALAG-AGGDRTDHQGWIEELRT---AETAARARDAAELADDRdpihpMRVYGELAPLLD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 385 DDAVIANGAGNYAVWVHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGa 463
Cdd:PRK05858 373 RDAIVIGDGGDFVSYAGRYIDPYRPGCWLDPGPfGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHN- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 464 TPVVIVV-NNGMLGTIRMHQEREYPGRVSA-----TRLDNpdfvaLARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:PRK05858 452 LPVVSVIgNNGIWGLEKHPMEALYGYDVAAdlrpgTRYDE-----VVRALGGHGELVTVPAELGPALERAFASGVPYLVN 526
|
570
....*....|.
gi 15597231 538 LLTDPRQITPQ 548
Cdd:PRK05858 527 VLTDPSVAYPR 537
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
10-170 |
1.05e-58 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 192.83 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 10 GGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQ-EVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
..
gi 15597231 169 IL 170
Cdd:pfam02776 161 VL 162
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
8-543 |
8.99e-57 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 199.46 E-value: 8.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 8 RNGGQILVEALRRNAVDTVYCIPGESYLPVLDAL-----YDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPG 82
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKararaAGRPLPEFVICPHEIVAISMAHGYALVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 83 ATHAANGVHTAQQDSTPMILFVGQV----ESAFKGREAF----QEV-DYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVA 153
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFAGRSpyteEGELGSRNTRihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 154 TSGRPGPVVVALPEEIL---FGSAQVADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEA 230
Cdd:PRK08327 167 MSEPKGPVYLTLPREVLaeeVPEVKADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASLRRLAEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 231 NGLPVATSFRRQDLFDNRDPHYAGQLgfgaaPALLerLRQADLLLVVGARLGETPSAGyslvrSPAPAQTLIHVHPDSAE 310
Cdd:PRK08327 247 LAIPVVEYAGEVVNYPSDHPLHLGPD-----PRAD--LAEADLVLVVDSDVPWIPKKI-----RPDADARVIQIDVDPLK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 311 LN---RVYLARLPIQATPCAFAEALAD-LAPLPSSTWQD-------WREAAHADYLAYSTPAASDPAVQGVDLASVVAYL 379
Cdd:PRK08327 315 SRiplWGFPCDLCIQADTSTALDQLEErLKSLASAERRRarrrraaVRELRIRQEAAKRAEIERLKDRGPITPAYLSYCL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 380 SENLPDDAVIANgagNYAVwVHRFYRYRQARTQLA-PTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQE--LA 456
Cdd:PRK08327 395 GEVADEYDAIVT---EYPF-VPRQARLNKPGSYFGdGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaHW 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 457 TAAQFGATPVVIVVNNGMLGTIRMHQEREYP-------GRVSATRLD-NPDFVALARAFGAHAERVECSADFPAAFRRA- 527
Cdd:PRK08327 471 VAERYGLPVLVVVFNNGGWLAVKEAVLEVYPegyaarkGTFPGTDFDpRPDFAKIAEAFGGYGERVEDPEELKGALRRAl 550
|
570
....*....|....*....
gi 15597231 528 ---RESGRPALLELLTDPR 543
Cdd:PRK08327 551 aavRKGRRSAVLDVIVDRV 569
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
15-541 |
7.20e-56 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 197.51 E-value: 7.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 15 VEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLT-GRPGICFVTRGPGATHAANGVHTA 93
Cdd:PRK11269 11 VLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITGLYSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 94 QQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP-----EE 168
Cdd:PRK11269 91 SADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPfdvqvAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGSAqvADAPEPrvlPGRPGATAMAELR--ELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDLFD 246
Cdd:PRK11269 171 IEFDPD--TYEPLP---VYKPAATRAQIEKalEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMGWGAIP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 247 NRDPHYAGQLG------FGAApALLErlrqADLLLVVGARLGETPSAGYSLVRSpapAQTLIHVHPDSAELNRVYLARLP 320
Cdd:PRK11269 246 DDHPLMAGMVGlqtshrYGNA-TLLA----SDFVLGIGNRWANRHTGSVEVYTK---GRKFVHVDIEPTQIGRVFGPDLG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IQATPCAFAEALADLA-------PLPssTWQDWreAAHADYLAYSTPAASDPAVQGVDLASVVAYLSENLPDDAVIANGA 393
Cdd:PRK11269 318 IVSDAKAALELLVEVArewkaagRLP--DRSAW--VADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 394 GNYAVWVHRFYR-YRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNN 472
Cdd:PRK11269 394 GLSQIAAAQFLHvYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 473 GMLGTIRMHQ---EREYPGRVSATRLDNP-------DFVALARAFGAHAERVECSADFPAAFRRAR----ESGRPALLEL 538
Cdd:PRK11269 474 AYLGLIRQAQrafDMDYCVQLAFENINSPelngygvDHVKVAEGLGCKAIRVFKPEDIAPALEQAKalmaEFRVPVVVEV 553
|
...
gi 15597231 539 LTD 541
Cdd:PRK11269 554 ILE 556
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
15-541 |
4.20e-54 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 191.32 E-value: 4.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 15 VEALRRNAVDTVYCIPGESYLPVLDALydTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVHTAQ 94
Cdd:PRK07092 19 IDLLRRFGITTVFGNPGSTELPFLRDF--PDDFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 95 QDSTPMILFVGQVESAFKGREAF-QEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPeeilfgs 173
Cdd:PRK07092 97 KNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIP------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 174 AQVADAPEPRVLP------GRPGATAMAELRELLANARRPLLVLGGS-----GWDSAAR--KRLGAFVEanglpVATSFR 240
Cdd:PRK07092 170 YDDWDQPAEPLPArtvssaVRPDPAALARLGDALDAARRPALVVGPAvdragAWDDAVRlaERHRAPVW-----VAPMSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 241 RQDlFDNRDPHYAGQLGfgAAPA-LLERLRQADLLLVVGArlgetPSAGYSlVRSPAP----AQTLIHVHPDSAELnrvy 315
Cdd:PRK07092 245 RCS-FPEDHPLFAGFLP--ASREkISALLDGHDLVLVIGA-----PVFTYH-VEGPGPhlpeGAELVQLTDDPGEA---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 316 lARLPI-QATPCAFAEALADLAPLPSSTWqdwREAAHADYLAYSTPAASDPavqgVDLASVVAYLSENLPDDAVIANGAG 394
Cdd:PRK07092 312 -AWAPMgDAIVGDIRLALRDLLALLPPSA---RPAPPARPMPPPAPAPGEP----LSVAFVLQTLAALRPADAIVVEEAP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 395 NYAVWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGM 474
Cdd:PRK07092 384 STRPAMQEHLPMRRQGSFYTMASGGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597231 475 LGTIR----MHQEREYPGrvsaTRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:PRK07092 464 YGALRwfapVFGVRDVPG----LDLPGLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
2-540 |
1.59e-53 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 190.79 E-value: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 2 SDSLP----QRNGGQILVEALRRNAVDTVYCIPGESylpvldaLYDTD---GIRTVVTRHEGAASNMADAYGKLTG--RP 72
Cdd:PRK06154 10 NAHLPaeakTMKVAEAVAEILKEEGVELLFGFPVNE-------LFDAAaaaGIRPVIARTERVAVHMADGYARATSgeRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 73 GICFVTRGPGATHAANGVHTAQQDSTPMILFVG-------QVESAFKGREAFQEVdyvqmfsglAKWAVEIDRIERIPEI 145
Cdd:PRK06154 83 GVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTgyprgstDVAPNFESLRNYRHI---------TKWCEQVTLPDEVPEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 146 VGRAFSVATSGRPGPVVVALPEEIL---FGSAQVADAPEPRVLPGrPGATAMAELRELLANARRPLLVLGGSGWDSAARK 222
Cdd:PRK06154 154 MRRAFTRLRNGRPGPVVLELPVDVLaeeLDELPLDHRPSRRSRPG-ADPVEVVEAAALLLAAERPVIYAGQGVLYAQATP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 223 RLGAFVEANGLPVATSFRRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLLLVVGARLGETpsagYSLVRSPApAQTLI 302
Cdd:PRK06154 233 ELKELAELLEIPVMTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRS----YYGLPMPE-GKTII 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 303 HVHPDSAELNRVYL--------ARLPIQATpcaFAEALADLAPLPSSTWQDWRE--AAHADYLAYSTP---AASDPavqg 369
Cdd:PRK06154 308 HSTLDDADLNKDYPidhglvgdAALVLKQM---IEELRRRVGPDRGRAQQVAAEieAVRAAWLAKWMPkltSDSTP---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 370 VDLASVVAYLSENL-PDDAVIANGAGNYAVWVHRFYRYRQARTQLA-PTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGC 447
Cdd:PRK06154 381 INPYRVVWELQHAVdIKTVIITHDAGSPRDQLSPFYVASRPGSYLGwGKTTQLGYGLGLAMGAKLARPDALVINLWGDAA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 448 FMMYPQELATAAQFGATPVVIVVNNGMLGTIRMHQEREYPgRVSATRLDNpDFVALARAFGAHAERVECSADFPAAFRRA 527
Cdd:PRK06154 461 FGMTGMDFETAVRERIPILTILLNNFSMGGYDKVMPVSTT-KYRATDISG-DYAAIARALGGYGERVEDPEMLVPALLRA 538
|
570
....*....|....*.
gi 15597231 528 ---RESGRPALLELLT 540
Cdd:PRK06154 539 lrkVKEGTPALLEVIT 554
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
375-542 |
7.13e-52 |
|
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: 175.38 E-value: 7.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 375 VVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLapTN---GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMY 451
Cdd:cd02015 6 VIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWL--TSgglGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 452 PQELATAAQFGAtPVVIVV-NNGMLGTIRMHQEREYPGRVSATRLD-NPDFVALARAFGAHAERVECSADFPAAFRRARE 529
Cdd:cd02015 84 IQELATAAQYNL-PVKIVIlNNGSLGMVRQWQELFYEGRYSHTTLDsNPDFVKLAEAYGIKGLRVEKPEELEAALKEALA 162
|
170
....*....|...
gi 15597231 530 SGRPALLELLTDP 542
Cdd:cd02015 163 SDGPVLLDVLVDP 175
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
392-537 |
6.02e-51 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 171.61 E-value: 6.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 392 GAGNYAVWVHRFYRYRQARTQLAPT-NGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVV 470
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGgLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 471 NNGMLGTIRMHQEREYPGRVSATR---LDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLE 537
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSgkiLPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALID 150
|
|
| Gcl |
COG3960 |
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism]; |
15-529 |
3.32e-45 |
|
Glyoxylate carboligase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443160 [Multi-domain] Cd Length: 588 Bit Score: 167.92 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 15 VEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLT-GRPGICFVTRGPGATHAANGVHTA 93
Cdd:COG3960 10 VAVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHVLARHVEGASHMAEGYTRAKaGNIGVCIGTSGPAGTDMITGLYSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 94 QQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALP-----EE 168
Cdd:COG3960 90 SADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVLEPAQVPRVFQQAFHLMRSGRPGPVLIDLPidvqmAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGsaqvADAPEPrVLPGRPGAT-AMAE-LRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDLFD 246
Cdd:COG3960 170 IEFD----IDTYEP-LPVYKPAATrAQIEkALDMLNAAERPLIVAGGGIINADASDLLVEFAELTGVPVIPTLMGWGSIP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 247 NRDPHYAGQLG------FGAApALLErlrqADLLLVVGARLGETPSAGYSLVRSpapAQTLIHVHPDSAELNRVYLARLP 320
Cdd:COG3960 245 DDHPLMAGMVGlqtshrYGNA-TLLA----SDFVLGIGNRWANRHTGSLDVYTK---GRKFVHVDIEPTQIGRVFAPDLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 321 IQATPCAFAEALADLA-------PLPSstWQDWreAAHADYLAYSTPAASDPAVQGVDLASVVAYLSENLPDDAVIANGA 393
Cdd:COG3960 317 IVSDAKAALELFVEVArerkaagKLPD--RSAW--AAECQERKRTMLRKTHFDNVPIKPQRVYEEMNKAFGRDTRYVSTI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 394 GNYAVWVHRFYRYRQARTQL-APTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNN 472
Cdd:COG3960 393 GLSQIAAAQFLHVYKPRHWInCGQAGPLGWTIPAALGVVAADPDRPVVALSGDYDFQFMIEELAVGAQFKLPYIHVVVNN 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597231 473 GMLGTIRMHQ---EREYPGRVSATRLDNP-------DFVALARAFGAHAERVECSADFPAAFRRARE 529
Cdd:COG3960 473 SYLGLIRQAQrgfDMDYCVQLAFENINAPelggygvDHVKVAEGLGCKAIRVTDPEEIAPAFEEAKA 539
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
14-543 |
1.75e-44 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 165.93 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 14 LVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVHTA 93
Cdd:PRK06546 9 LVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLYDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 94 QQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATsGRPGPVVVALPEEIlfGS 173
Cdd:PRK06546 89 HRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAV-AGGGVSVVTLPGDI--AD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 174 AQVADAPEPRVLPGR-----PGATAMAELRELLANARRPLLvLGGSGwDSAARKRLGAFVEANGLPVATSFRRQDL--FD 246
Cdd:PRK06546 166 EPAPEGFAPSVISPRrptvvPDPAEVRALADAINEAKKVTL-FAGAG-VRGAHAEVLALAEKIKAPVGHSLRGKEWiqYD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 247 NR-DPHYAGQLGFGAApalLERLRQADLLLVVGArlgETPSAGYslvrspAPAQTLIHVHPDSAELNRVYLARLPIQATp 325
Cdd:PRK06546 244 NPfDVGMSGLLGYGAA---HEAMHEADLLILLGT---DFPYDQF------LPDVRTAQVDIDPEHLGRRTRVDLAVHGD- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 326 caFAEALADLAPL----PSSTWQDWREAAHADYL-----AYSTPAASDPAVQGVDLASVvayLSENLPDDAVIANGAGNY 396
Cdd:PRK06546 311 --VAETIRALLPLvkekTDRRFLDRMLKKHARKLekvvgAYTRKVEKHTPIHPEYVASI---LDELAADDAVFTVDTGMC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 397 AVWVHRFYRYRQARTQLAP-TNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGaTPVVIVV-NNGM 474
Cdd:PRK06546 386 NVWAARYITPNGRRRVIGSfRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYD-LPVKVVVfNNST 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 475 LGTIRMhqEREYPGRVS-ATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPR 543
Cdd:PRK06546 465 LGMVKL--EMLVDGLPDfGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPN 532
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
12-552 |
3.71e-42 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 159.38 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 12 QILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANGVH 91
Cdd:PRK09124 7 DYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 92 TAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRpGPVVVALPEEILF 171
Cdd:PRK09124 87 DCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNR-GVAVVVLPGDVAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 172 GSAQVADAPEPRVLPG---RPGATAMAELRELLANARRPLLvLGGSGWdSAARKRLGAFVEANGLPVATSFRRQDLFDNR 248
Cdd:PRK09124 166 KPAPERATPHWYHAPQpvvTPAEEELRKLAALLNGSSNITL-LCGSGC-AGAHDELVALAETLKAPIVHALRGKEHVEYD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 249 DPHYAGQLGFGAAPALLERLRQADLLLVVGARLgetP-SAGYslvrsPAPAqTLIHVHPDSAELNRVYLARLPIQATpca 327
Cdd:PRK09124 244 NPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDF---PyRQFY-----PTDA-KIIQIDINPGSLGRRSPVDLGLVGD--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 328 FAEALADLAP-LPSSTWQDWREAAHADYL-------AYSTPAASDPAVQGVDLASVVaylSENLPDDAVIANGAGNYAVW 399
Cdd:PRK09124 312 VKATLAALLPlLEEKTDRKFLDKALEHYRkarkgldDLAVPSDGGKPIHPQYLARQI---SEFAADDAIFTCDVGTPTVW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 400 VHRFYRYRQARTQLAPTN-GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFgATPVVIVV-NNGMLGT 477
Cdd:PRK09124 389 AARYLKMNGKRRLLGSFNhGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQL-KLPVKIVVfNNSVLGF 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597231 478 IRMhqEREYPGRVSA-TRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPRQ--ITPQARLA 552
Cdd:PRK09124 468 VAM--EMKAGGYLTDgTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQElaMPPQIKLE 543
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
1-542 |
4.16e-42 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 159.00 E-value: 4.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 1 MSDSLPQRNGGQILVEALRRNAVDTVYCIPGesyLPVLD--ALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVT 78
Cdd:PRK09259 3 MSDQLQLTDGFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 79 RGPGATHAANGVHTAQQDSTPMILFVGQVEsafkgREA--FQEVDYVQM-----FSGLAKWAVEIDRIERIPEIVGRAFS 151
Cdd:PRK09259 80 SAPGFLNGLTALANATTNCFPMIMISGSSE-----REIvdLQQGDYEELdqlnaAKPFCKAAFRVNRAEDIGIGVARAIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 152 VATSGRPGPVVVALPEEILfgsAQVADA------------PEPRVLPGRpgaTAMAELRELLANARRPLLVLGGSGWDSA 219
Cdd:PRK09259 155 TAVSGRPGGVYLDLPAKVL---AQTMDAdealtslvkvvdPAPAQLPAP---EAVDRALDLLKKAKRPLIILGKGAAYAQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 220 ARKRLGAFVEANGLPVATSFRRQDLFDNRDPHYAgqlgfGAAPALLerLRQADLLLVVGARL------GETPSAGyslvr 293
Cdd:PRK09259 229 ADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSA-----AAARSLA--LANADVVLLVGARLnwllshGKGKTWG----- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 294 spaPAQTLIHVHPDSAEL--NRVYLARLP--IQATPCAFAEALADLAPLPSSTWQDWREAAHADYLAYSTPA-ASDPAVQ 368
Cdd:PRK09259 297 ---ADKKFIQIDIEPQEIdsNRPIAAPVVgdIGSVMQALLAGLKQNTFKAPAEWLDALAERKEKNAAKMAEKlSTDTQPM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 369 GV--DLASVVAYLSENlPDDAVIANGAG--NYAVWVHRFYryrQARTQLAP-TNGAMGYGLPAAIAASLrDPQRSVVCFA 443
Cdd:PRK09259 374 NFynALGAIRDVLKEN-PDIYLVNEGANtlDLARNIIDMY---KPRHRLDCgTWGVMGIGMGYAIAAAV-ETGKPVVAIE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 444 GDGCFMMYPQELATAAQFGATPVVIVVNNGmlGTIR-MHQEREYPGRVSATRLD-NPDFVALARAFGAHAERVECSADFP 521
Cdd:PRK09259 449 GDSAFGFSGMEVETICRYNLPVTVVIFNNG--GIYRgDDVNLSGAGDPSPTVLVhHARYDKMMEAFGGVGYNVTTPDELR 526
|
570 580
....*....|....*....|.
gi 15597231 522 AAFRRARESGRPALLELLTDP 542
Cdd:PRK09259 527 HALTEAIASGKPTLINVVIDP 547
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
9-169 |
5.04e-41 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 145.39 E-value: 5.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRpGPVVVALPEE 168
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
.
gi 15597231 169 I 169
Cdd:cd07039 160 V 160
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
375-542 |
1.88e-40 |
|
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: 144.60 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 375 VVAYLSENLPDDAVIANGAGNYAVWVHRFYRYR-QARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQ 453
Cdd:cd02014 7 VAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNgKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 454 ELATAAQFGATPVVIVVNNGMLGTIRMHQERE-YPgrVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGR 532
Cdd:cd02014 87 DLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMgQP--EFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALAADG 164
|
170
....*....|
gi 15597231 533 PALLELLTDP 542
Cdd:cd02014 165 PVVIDVVTDP 174
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
9-539 |
3.98e-39 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 149.61 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK07586 2 NGAESLVRTLVDGGVDVCFANPGTSEMHFVAALDRVPGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDyvqmFSGLAK----WAVEIDRIERIPEIVGRAFSVATSGRPGPVVVA 164
Cdd:PRK07586 82 NLHNARRARTPIVNIVGDHATYHRKYDAPLTSD----IEALARpvsgWVRRSESAADVAADAAAAVAAARGAPGQVATLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 165 LPEEILFGSAQVADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATsfrrqDL 244
Cdd:PRK07586 158 LPADVAWSEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATGARLLA-----ET 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 245 FDNRDPHYAG-----QLGFGAAPAlLERLRQADLLLVVGARlgeTPSA--GY-----SLVRSPAPAQTLIHVHPDSAeln 312
Cdd:PRK07586 233 FPARMERGAGrpaveRLPYFAEQA-LAQLAGVRHLVLVGAK---APVAffAYpgkpsRLVPEGCEVHTLAGPGEDAA--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 313 rvylARLpiqatpcafaEALAD-LAPLPsstwqdwreaAHADYLAYSTPAASDPAVQGVDLASVVAYLsenLPDDAVIAN 391
Cdd:PRK07586 306 ----AAL----------EALADaLGAKP----------AAPPLAAPARPPLPTGALTPEAIAQVIAAL---LPENAIVVD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 392 GAGNYAVWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVN 471
Cdd:PRK07586 359 ESITSGRGFFPATAGAAPHDWLTLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597231 472 NGMLGTIRMHQER---EYPGRVSA--TRLDNP--DFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELL 539
Cdd:PRK07586 439 NRAYAILRGELARvgaGNPGPRALdmLDLDDPdlDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEAV 513
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
11-550 |
4.22e-39 |
|
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: 150.31 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 11 GQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICfVTRGPGATHAANGV 90
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALV-TTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 91 HTAQQDSTPMILFVGQVESAFKGREA-----FQEVDY---VQMFSGLAKWAVEIDrIERIPEIVGRAFSVATSGRPgPVV 162
Cdd:COG3961 87 AGAYAERVPVVHIVGAPGTRAQRRGPllhhtLGDGDFdhfLRMFEEVTVAQAVLT-PENAAAEIDRVLAAALREKR-PVY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 163 VALPEEIlfgSAQVADAPEPRVLPGRPG------ATAMAELRELLANARRPLLvLGGSGWDSA-ARKRLGAFVEANGLPV 235
Cdd:COG3961 165 IELPRDV---ADAPIEPPEAPLPLPPPAsdpaalAAAVAAAAERLAKAKRPVI-LAGVEVHRFgLQEELLALAEKTGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 236 ATSFRRQDLFDNRDPHYAGqLGFGAA--PALLERLRQADLLLVVGARLGETPSAGYSlvRSPAPAQTlIHVHPDSAELNR 313
Cdd:COG3961 241 ATTLLGKSVLDESHPQFIG-TYAGAAssPEVREYVENADCVLCLGVVFTDTNTGGFT--AQLDPERT-IDIQPDSVRVGG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 314 VYLARLPIQAtpcaFAEALADLAPLPSSTWQdwreaahadylAYSTPAASDPAV--QGVDLASVVAYLSENL-PDDAVIA 390
Cdd:COG3961 317 HIYPGVSLAD----FLEALAELLKKRSAPLP-----------APAPPPPPPPAApdAPLTQDRLWQRLQAFLdPGDIVVA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 391 -NGAGNYAVWVHRFYRyrQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIV 469
Cdd:COG3961 382 dTGTSLFGAADLRLPE--GATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 470 VNNGMLGTIRMHQEREYPGRVsatrLDNPDFVALARAFGAH---AERVECSADFPAAFRRARE-SGRPALLELLTDPRQI 545
Cdd:COG3961 460 LNNDGYTIERAIHGPDGPYND----IANWDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEAnTDRLTLIEVVLDKMDA 535
|
....*
gi 15597231 546 TPQAR 550
Cdd:COG3961 536 PPLLK 540
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
11-542 |
4.39e-39 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 150.83 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 11 GQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDG-IRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAANG 89
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 90 VHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLA-KWAVEIDRIERIPEIVGRAFSVATSGRpGPVVVALPEE 168
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVAgAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 IlfgsaQVADAPEP----------------RVLPGRPGATAMAElrelLANARRPLLVLGGSGWDSAARKrLGAFVEANG 232
Cdd:PRK08273 165 V-----QELEYEPPphahgtvhsgvgytrpRVVPYDEDLRRAAE----VLNAGRKVAILVGAGALGATDE-VIAVAERLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 233 LPVATSFRRQDLFDNRDPHYAGQLG-FGAAPAlLERLRQADLLLVVGArlgetpSAGYS--LvrsPAPAQ---TLIHVHP 306
Cdd:PRK08273 235 AGVAKALLGKAALPDDLPWVTGSIGlLGTKPS-YELMRECDTLLMVGS------SFPYSefL---PKEGQargVQIDIDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 307 DSAELnrvylaRLPIQATPCA-FAEALADLAPL----PSSTWQDWREAAHADYLAYSTPAASDPAvQGVDLASVVAYLSE 381
Cdd:PRK08273 305 RMLGL------RYPMEVNLVGdAAETLRALLPLlerkKDRSWRERIEKWVARWWETLEARAMVPA-DPVNPQRVFWELSP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 382 NLPDDAVIANGAGNYAVWVHRFYRYRQ-ARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQ-ELATAA 459
Cdd:PRK08273 378 RLPDNAILTADSGSCANWYARDLRMRRgMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGMaELITVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 460 QF-----GATPVVIVVNNGMLGTIRMHQeREYPGR---VSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESG 531
Cdd:PRK08273 458 KYwrqwsDPRLIVLVLNNRDLNQVTWEQ-RVMEGDpkfEASQDLPDVPYARFAELLGLKGIRVDDPEQLGAAWDEALAAD 536
|
570
....*....|.
gi 15597231 532 RPALLELLTDP 542
Cdd:PRK08273 537 RPVVLEVKTDP 547
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
40-547 |
4.48e-39 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 151.05 E-value: 4.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 40 ALY-DTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTR--GPGATHAANGVHTAQQDSTPMILFVG----------- 105
Cdd:COG3962 50 ALEqDPDELPTYQGRNEQGMAHAAIAYAKQKNRRRIMACTSsiGPGATNMVTAAALATANRLPVLLLPGdtfatrqpdpv 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 106 --QVESAFKG----REAFQEVD-YvqmfsglakWaveiDRIERiPE----IVGRAFSVATSgrP---GPVVVALPEEIlf 171
Cdd:COG3962 130 lqQLEHFHDPtisvNDAFRPVSrY---------W----DRITR-PEqlmsALPRAMRVLTD--PaetGAVTLALPQDV-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 172 gSAQVADAPE----PRV-LPGRPGAT--AMAELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDL 244
Cdd:COG3962 192 -QAEAYDYPEsffaKRVhRIRRPPPDpaELARAVELIRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 245 FDNRDPHYAGQLGF---GAAPALLerlRQADLLLVVGARLGETPSAGYSLVRSPAPAQTLIHVHP-DSAELNRVYL---A 317
Cdd:COG3962 271 LPWDHPLNLGGIGVtgtLAANALA---AEADLVIGVGTRLQDFTTGSKTLFANPDVRFVNINVARfDAYKHDALPVvadA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 318 RLPIQAtpcaFAEALADLAPlpSSTWQDWREAAHADYLAYSTPAASDPAVQGVDLASVVAYLSENLPDDAVIANGAGNYA 397
Cdd:COG3962 348 REGLEA----LTEALAGWRY--PAAWTDEAAELKAEWDAEVDRLYAPTNGGLPTQAQVIGAVNEAAGPDDIVVCAAGSLP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 398 VWVHRFYRYRQART-QLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLG 476
Cdd:COG3962 422 GDLHKLWRTRDPGTyHVEYGYSCMGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDNHGFG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 477 TIRMHQE--------REYPGRVSAT-RLDNP----DFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDPR 543
Cdd:COG3962 502 CINRLQMstgsqsfgTELRDRDTETgRLDGGllpvDFAANAASLGAKAYRVTTIAELRAALERAKAADRTTVIVIKTDPK 581
|
....
gi 15597231 544 QITP 547
Cdd:COG3962 582 TMTP 585
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
9-539 |
1.62e-36 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 142.32 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 9 NGGQILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGPGATHAAN 88
Cdd:PRK12474 6 NGADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGRPGPVVVALPEE 168
Cdd:PRK12474 86 NLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 169 ILFGSAQVADAPEPRVLPGRPGATAMAELRELLANARRPLLVLGGSGwdsaarkrlgafVEANGLPVATSFRRQDLFDNR 248
Cdd:PRK12474 166 VAWNEAAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRGSA------------LRGAPLEAAGRIQAKTGVRLY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 249 DPHYAGQLGFGAAPALLER-----------LRQADLLLVVGARlgeTPSAGYSLVRSPApaqtliHVHPDSAELnrVYLA 317
Cdd:PRK12474 234 CDTFAPRIERGAGRVPIERipyfheqitafLKDVEQLVLVGAK---PPVSFFAYPGKPS------WGAPPGCEI--VYLA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 318 RlPIQatpcAFAEALADLAPLPSstwqdwreaAHADYLAYSTPAASDPAVQGVDLASVVAYLSENLPDDAVIANGAGNYA 397
Cdd:PRK12474 303 Q-PDE----DLAQALQDLADAVD---------APAEPAARTPLALPALPKGALNSLGVAQLIAHRTPDQAIYADEALTSG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 398 VWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGT 477
Cdd:PRK12474 369 LFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAI 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597231 478 IRMHQER---EYPGR--VSATRLDNP--DFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELL 539
Cdd:PRK12474 449 LNGELQRvgaQGAGRnaLSMLDLHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAM 517
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
374-541 |
2.16e-35 |
|
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: 130.34 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 374 SVVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAP-TNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYP 452
Cdd:cd02004 3 RVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAgTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 453 QELATAAQFGATPVVIVVNNGMLGTIRMHQEREYP-GRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESG 531
Cdd:cd02004 83 MELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGlGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASG 162
|
170
....*....|
gi 15597231 532 RPALLELLTD 541
Cdd:cd02004 163 KPALINVIID 172
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
373-540 |
4.12e-35 |
|
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: 130.02 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 373 ASVVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYP 452
Cdd:cd02002 4 EYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRGGGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 453 QELATAAQFGATPVVIVVNNGMLGTIRMHQEREYPGRVSA-----TRLDNP--DFVALARAFGAHAERVECSADFPAAFR 525
Cdd:cd02002 84 QALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGEnapdgLDLLDPgiDFAAIAKAFGVEAERVETPEELDEALR 163
|
170
....*....|....*
gi 15597231 526 RARESGRPALLELLT 540
Cdd:cd02002 164 EALAEGGPALIEVVV 178
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
375-541 |
1.68e-34 |
|
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: 128.17 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 375 VVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLApTNG--AMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYP 452
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLI-SNGlaTMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 453 QELATAAQFGATPVVIVVNNGMLGTIRMHQEREYpGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRARESGR 532
Cdd:cd02010 83 QELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEY-GRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
....*....
gi 15597231 533 PALLELLTD 541
Cdd:cd02010 162 VHVIDCPVD 170
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
195-332 |
1.19e-33 |
|
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: 124.60 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 195 AELRELLANARRPLLVLGGSGWDSAARKRLGAFVEANGLPVATSFRRQDLFDNRDPHYAGQLGFGAAPALLERLRQADLL 274
Cdd:pfam00205 2 EKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADLV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15597231 275 LVVGARLGETPSAGYSlvRSPAPAQTLIHVHPDSAELNRVYLARLPIQATPCAFAEAL 332
Cdd:pfam00205 82 LAVGARFDDIRTTGKL--PEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
373-547 |
2.61e-26 |
|
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: 106.24 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 373 ASVVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQART-QLAPTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMY 451
Cdd:cd02003 2 TEVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGyHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 452 PQELATAAQFGATPVVIVVNNGMLGTIRMHQE-------------REYPGRVSATRLDNPDFVALARAFGAHAERVECSA 518
Cdd:cd02003 82 HSEIVTAVQEGLKIIIVLFDNHGFGCINNLQEstgsgsfgtefrdRDQESGQLDGALLPVDFAANARSLGARVEKVKTIE 161
|
170 180
....*....|....*....|....*....
gi 15597231 519 DFPAAFRRARESGRPALLELLTDPRQITP 547
Cdd:cd02003 162 ELKAALAKAKASDRTTVIVIKTDPKSMTP 190
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
12-167 |
4.47e-25 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 101.27 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 12 QILVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPgICFVTRGPGATHAANGVH 91
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPP-VVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597231 92 TAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEIVGRAFSVATSGrPGPVVVALPE 167
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
379-547 |
8.21e-22 |
|
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: 93.34 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 379 LSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAP-TNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELAT 457
Cdd:cd02013 13 LEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPlSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMMEIMT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 458 AAQFGaTPVVIVV-NNGMLGTIRMHQEREYPGRVSATRLDNPDFVALARAFGAHAERVECSADFPAAFRRA---RESGRP 533
Cdd:cd02013 93 AVRHK-LPVTAVVfRNRQWGAEKKNQVDFYNNRFVGTELESESFAKIAEACGAKGITVDKPEDVGPALQKAiamMAEGKT 171
|
170
....*....|....
gi 15597231 534 ALLELLTDPRQITP 547
Cdd:cd02013 172 TVIEIVCDQELGDP 185
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
384-547 |
1.91e-18 |
|
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: 83.35 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 384 PDDAVIA-NGAGNYAVWVHRFyryrQARTQLA--PTNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQ 460
Cdd:cd02005 17 PNDILVAeTGTSWFGALDLKL----PKGTRFIsqPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 461 FGATPVVIVVNNGmlG-TIrmhqEREYPGRVSA-TRLDNPDFVALARAFGA----HAERVECSADFPAAFRRARE-SGRP 533
Cdd:cd02005 93 YGLNPIIFLINND--GyTI----ERAIHGPEASyNDIANWNYTKLPEVFGGggggLSFRVKTEGELDEALKDALFnRDKL 166
|
170
....*....|....
gi 15597231 534 ALLELLTDPRQITP 547
Cdd:cd02005 167 SLIEVILPKDDAPE 180
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
418-539 |
2.64e-14 |
|
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: 71.93 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 418 GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELATAAQFGATPVVIVVNNGMLGTIRMHQ---EREYPGRVSATR 494
Cdd:cd02006 57 GPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafDMDYQVNLAFEN 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15597231 495 LDNP-------DFVALARAFGAHAERVECSADFPAAFRRAR----ESGRPALLELL 539
Cdd:cd02006 137 INSSelggygvDHVKVAEGLGCKAIRVTKPEELAAAFEQAKklmaEHRVPVVVEAI 192
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
14-473 |
9.62e-14 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 73.97 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 14 LVEAlrrnAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGrPGICFVTRGPGATHAANGVHTA 93
Cdd:PLN02573 26 LVEI----GVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 94 QQDSTPMILFVGQVESAFKGR-----------------EAFQEVDYVQmfsglakwAVeIDRIERIPEIVGRAFSVATsG 156
Cdd:PLN02573 101 YSENLPVICIVGGPNSNDYGTnrilhhtiglpdfsqelRCFQTVTCYQ--------AV-INNLEDAHELIDTAISTAL-K 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 157 RPGPV-------VVALPEEIlFGSAQVADAPEPRVlPGRPGATAMAELR-ELLANARRPLLVLGGSGWDSAARKRLGAFV 228
Cdd:PLN02573 171 ESKPVyisvscnLAAIPHPT-FSREPVPFFLTPRL-SNKMSLEAAVEAAaEFLNKAVKPVLVGGPKLRVAKACKAFVELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 229 EANGLPVATSFRRQDLFDNRDPHYAGQLgFGAA--PALLERLRQADLLLVVGARLGETPSAGYSLVRSPAPAqtlIHVHP 306
Cdd:PLN02573 249 DASGYPVAVMPSAKGLVPEHHPHFIGTY-WGAVstPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKA---IIVQP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 307 DsaelnRVYLARLPiqATPCA----FAEALADLAPLPSSTWQDWREAahadYLAYSTPAASDPavqGVDLASVVAY---- 378
Cdd:PLN02573 325 D-----RVTIGNGP--AFGCVlmkdFLEALAKRVKKNTTAYENYKRI----FVPEGEPLKSEP---GEPLRVNVLFkhiq 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 379 --LSenlPDDAVIA---------------NGAGnyavwvhrfYRYrQARTqlaptnGAMGYGLPAAIAASLRDPQRSVVC 441
Cdd:PLN02573 391 kmLS---GDTAVIAetgdswfncqklklpEGCG---------YEF-QMQY------GSIGWSVGATLGYAQAAPDKRVIA 451
|
490 500 510
....*....|....*....|....*....|..
gi 15597231 442 FAGDGCFMMYPQELATAAQFGATPVVIVVNNG 473
Cdd:PLN02573 452 CIGDGSFQVTAQDVSTMIRCGQKSIIFLINNG 483
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
14-105 |
2.56e-11 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 62.13 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 14 LVEALRRNAVDTVYCIPGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGrPGICFVTRGPGATHAANGVHTA 93
Cdd:cd07038 3 LLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGA 81
|
90
....*....|..
gi 15597231 94 QQDSTPMILFVG 105
Cdd:cd07038 82 YAEHVPVVHIVG 93
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
376-550 |
7.19e-07 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 49.62 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 376 VAYLSENLPDDAVIANGAGnyavWVHR-FYRYRQARTQLAPTN----GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMM 450
Cdd:cd03371 5 IEIVLSRAPATAAVVSTTG----MTSReLFELRDRPGGGHAQDfltvGSMGHASQIALGIALARPDRKVVCIDGDGAALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 451 YPQELAT-AAQFGATPVVIVVNNG---MLGTirmhqereypgrvSATRLDNPDFVALARAFGAHAERVECS-ADFPAAFR 525
Cdd:cd03371 81 HMGGLATiGGLAPANLIHIVLNNGahdSVGG-------------QPTVSFDVSLPAIAKACGYRAVYEVPSlEELVAALA 147
|
170 180
....*....|....*....|....*
gi 15597231 526 RARESGRPALLELLTDPRQITPQAR 550
Cdd:cd03371 148 KALAADGPAFIEVKVRPGSRSDLGR 172
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
416-536 |
1.29e-05 |
|
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: 45.73 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 416 TNGAMGYGLPAAIAASLRDPQRSVVCFAGDGCFM-MYPQELATAAQFGATPVVIVVNNG---MLGtirmHQEREYPGRVS 491
Cdd:cd02008 49 TCTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFhSGILGLINAVYNKANITVVILDNRttaMTG----GQPHPGTGKTL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15597231 492 ATRLDNPDFVALARAFGAHAERVECSADFPA---AFRRARESGRPALL 536
Cdd:cd02008 125 TEPTTVIDIEALVRAIGVKRVVVVDPYDLKAireELKEALAVPGVSVI 172
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
418-542 |
1.78e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 45.17 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 418 GAMGYGLPAAIAASLRDPqRSVVCFAGDGCFMMYPQELATAAQFGATPVV-IVVNNGMLGTirMHQEREYPGRVsatrld 496
Cdd:cd02001 42 GSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTPLNLIlVVLDNRAYGS--TGGQPTPSSNV------ 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15597231 497 npDFVALARAFGAHAERVECSADFPAAFRRARESGRPALLELLTDP 542
Cdd:cd02001 113 --NLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPIAP 156
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
415-540 |
4.16e-05 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 45.56 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 415 PTNGAMGYGLP----AAIAASLRDPQRSVVCFAGDGcfmmypqelAT-----------AAQFGAtPVVIVVNNGMLGtIR 479
Cdd:cd02000 101 GGNGIVGGQVPlaagAALALKYRGEDRVAVCFFGDG---------ATnegdfhealnfAALWKL-PVIFVCENNGYA-IS 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597231 480 MHQEREYPGrvsatrldnPDFVALARAFGAHAERVEcSADFPA-------AFRRARESGRPALLELLT 540
Cdd:cd02000 170 TPTSRQTAG---------TSIADRAAAYGIPGIRVD-GNDVLAvyeaakeAVERARAGGGPTLIEAVT 227
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
418-541 |
4.62e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 44.44 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 418 GAMGYGLPAAIAASLRDPQRSVVCFAGDGCFMMYPQELAT-AAQFGATPVVIVVNNGMLgtirmhqerEYPGRVSATRLD 496
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVY---------QITGGQPTLTSQ 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15597231 497 NPDFVALARAFG-AHAERVECSADFPAAFRRARESGRPALLELLTD 541
Cdd:PRK06163 128 TVDVVAIARGAGlENSHWAADEAHFEALVDQALSGPGPSFIAVRID 173
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
12-166 |
7.45e-05 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 43.26 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 12 QILVEALRRNAVDTVyCI-PGESYLPVLDALYDTDGIRTVVTRHEGAASNMADAYGKLTGRPGICFVTRGpgaTHAAN-- 88
Cdd:cd07037 1 QALVEELKRLGVRDV-VIsPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSG---TAVANll 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 89 -GVHTAQQDSTPMILFVGQVESAFKGREAFQEVDYVQMFSGLAKWAVEIDRIERIPEI------VGRAFSVATSGRPGPV 161
Cdd:cd07037 77 pAVVEAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLwyllrlANRAVLEALSAPPGPV 156
|
....*
gi 15597231 162 VVALP 166
Cdd:cd07037 157 HLNLP 161
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
415-540 |
1.39e-04 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 44.36 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 415 PTNGAMGYGLP----AAIAASLRDPQRSVVCFAGDGcfmmypqelAT-----------AAQFGAtPVVIVVNNGMLGtIR 479
Cdd:COG1071 124 GGSGIVGGQLPhavgAALAAKLRGEDEVAVAFFGDG---------ATsegdfhealnfAAVWKL-PVVFVCENNGYA-IS 192
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597231 480 MHQEREYPGrvsatrldnPDFVALARAFGAHAERVECSaDFPA-------AFRRARESGRPALLELLT 540
Cdd:COG1071 193 TPVERQTAV---------ETIADRAAGYGIPGVRVDGN-DVLAvyaavkeAVERARAGEGPTLIEAKT 250
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
373-541 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 373 ASVVAYLSENLPDDAVIANGAGNYAVWVHRFYRYRQARTQLAPTNGAMGY--GLPAAIAASLRDPQRsVVCFAGDGCFMM 450
Cdd:cd02009 4 PALARALPDHLPEGSQLFVGNSMPIRDLDLFALPSDKTVRVFANRGASGIdgTLSTALGIALATDKP-TVLLTGDLSFLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 451 YPQELATAAQFGATPVVIVVNNGMlGTI-RM---HQEREYPGRVSATRLDNpDFVALARAFGAHAERVECSADFPAAFRR 526
Cdd:cd02009 83 DLNGLLLGKQEPLNLTIVVINNNG-GGIfSLlpqASFEDEFERLFGTPQGL-DFEHLAKAYGLEYRRVSSLDELEQALES 160
|
170
....*....|....*
gi 15597231 527 ARESGRPALLELLTD 541
Cdd:cd02009 161 ALAQDGPHVIEVKTD 175
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
375-529 |
2.70e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 41.89 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 375 VVAYLSENLPDDAVIAN-GAGNYAVWVHR-----FYRYrqartqlaptnGAMGYGLPAAIAASLRDPQRsVVCFAGDGCF 448
Cdd:cd03372 4 AIKTLIADLKDELVVSNiGFPSKELYAAGdrplnFYML-----------GSMGLASSIGLGLALAQPRK-VIVIDGDGSL 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 449 MMYPQELATAAQfgATP---VVIVVNNGMLGTIRMhqEREYPGRVSatrldnpDFVALARAFGAHAERVECSADfpaAFR 525
Cdd:cd03372 72 LMNLGALATIAA--EKPknlIIVVLDNGAYGSTGN--QPTHAGKKT-------DLEAVAKACGLDNVATVASEE---AFE 137
|
....
gi 15597231 526 RARE 529
Cdd:cd03372 138 KAVE 141
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|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
416-540 |
2.88e-03 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 39.79 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597231 416 TNGAMGYGLPA----AIAASLRDPQRSVVCFAGDGCFmmypQE------LATAAQFGATP-VVIVVNNGMlgTIRmhqer 484
Cdd:cd02012 103 TTGSLGQGLSVavgmALAEKLLGFDYRVYVLLGDGEL----QEgsvweaASFAGHYKLDNlIAIVDSNRI--QID----- 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 15597231 485 eypGRVSATrLDNPDFVALARAFGAHAERVE--CSADFPAAFRRARES-GRPALLELLT 540
Cdd:cd02012 172 ---GPTDDI-LFTEDLAKKFEAFGWNVIEVDghDVEEILAALEEAKKSkGKPTLIIAKT 226
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