|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
4-553 |
0e+00 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 1085.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 4 KFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLAT 83
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 84 GLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VVDSQVQVKAIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAGIVSR 243
Cdd:PRK08617 165 VVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVISR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 244 ELEEaTFFGRVGLFRNQPGDMLLKKSDLVIAIGYDPIEYEARNWNAEISARVIVIDVEPAEIDTYFQPERELIGDIANTL 323
Cdd:PRK08617 245 ELED-HFFGRVGLFRNQPGDELLKKADLVITIGYDPIEYEPRNWNSEGDATIIHIDVLPAEIDNYYQPERELIGDIAATL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 324 DLLLPAINGYQLPEGSREYLQVLRDKMDGDVKFDRsQAEKGRLHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSY 403
Cdd:PRK08617 324 DLLAEKLDGLSLSPQSLEILEELRAQLEELAERPA-RLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWMARYFRSY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 404 EPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKY 483
Cdd:PRK08617 403 EPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMKY 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 484 GRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDYKDSSTLGETILPDEF 553
Cdd:PRK08617 483 GRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIKLMEQLLPDQL 552
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-546 |
0e+00 |
|
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: 948.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDVV 165
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 DSQVQVKAIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAGIVSREL 245
Cdd:TIGR02418 161 DSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSREL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 246 eEATFFGRVGLFRNQPGDMLLKKSDLVIAIGYDPIEYEARNWNAEISARVIVIDVEPAEIDTYFQPERELIGDIANTLDL 325
Cdd:TIGR02418 241 -EDHFFGRVGLFRNQPGDRLLKQADLVITIGYDPIEYEPRNWNSENDATIVHIDVEPAQIDNNYQPDLELVGDIASTLDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 326 LLPAINGYQLPEGSREYLQVLRDKMDG--DVKFDRSQAekgRLHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSY 403
Cdd:TIGR02418 320 LAERIPGYELPPDALAILEDLKQQREAldRVPATLKQA---HLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 404 EPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKY 483
Cdd:TIGR02418 397 RARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKY 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568064214 484 GRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDYKDSSTLGE 546
Cdd:TIGR02418 477 QRSSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNPKLMS 539
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
6-538 |
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: 568.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDK-GPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:COG0028 5 GADALVEALEAEGVETVFGVPGGAILPLYDALRRQsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDV 164
Cdd:COG0028 85 LADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 165 VDSQVQVKAIKPLTDP--QLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAGIVS 242
Cdd:COG0028 165 QAAEAEEEPAPPELRGyrPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGAFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 243 RELEeaTFFGRVGLFRNQPGDMLLKKSDLVIAIGYDPIEYEARNWNAEI-SARVIVIDVEPAEIDTYFQPERELIGDIAN 321
Cdd:COG0028 245 EDHP--LYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFApDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 322 TLDLLLPAINGYQLPEGS-REYLQVLRDKmdgdvKFDRSQAEKGRLHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYF 400
Cdd:COG0028 323 VLAALLEALEPRADDRAAwLARIAAWRAE-----YLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 401 KSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEE 480
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 481 MKYG-RSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDY 538
Cdd:COG0028 478 LFYGgRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDP 536
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
6-540 |
1.71e-165 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 481.25 E-value: 1.71e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQV--KRSDllKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PRK08322 83 AYAQLGGMPMVAITGQKpiKRSK--QGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VVDSQVQVKAIKPlTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAGIV-- 241
Cdd:PRK08322 161 IAAEETDGKPLPR-SYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIpe 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 242 SRELeeatFFGRVGLfrnQPGDML---LKKSDLVIAIGYDPIEYEARNWNAEISARVIVIDVEPAEIDTYFQPERELIGD 318
Cdd:PRK08322 240 THPL----SLGTAGL---SQGDYVhcaIEHADLIINVGHDVIEKPPFFMNPNGDKKVIHINFLPAEVDPVYFPQVEVVGD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 319 IANTLDLLLPAINGYQLPEgsREYLQVLRDKMDGDVKfDRSQAEKGRLHPLDIVEVLQENTTDDMTVTVDVGTHYIWMAR 398
Cdd:PRK08322 313 IANSLWQLKERLADQPHWD--FPRFLKIREAIEAHLE-EGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFAR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 399 YFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQ 478
Cdd:PRK08322 390 NYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568064214 479 EEMKYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDYKD 540
Cdd:PRK08322 470 QENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSE 531
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
6-540 |
4.04e-121 |
|
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: 367.90 E-value: 4.04e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTL-EDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALyNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDV 164
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 165 --------VDSQVQVKAIKPLTDPqlgssSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ 236
Cdd:TIGR00118 163 ttaeieypYPEKVNLPGYRPTVKG-----HPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGivSRELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIG--YDP-----IEYEARNwnaeisARVIVIDVEPAEIDTYF 309
Cdd:TIGR00118 238 GLG--SFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGarFDDrvtgnLAKFAPN------AKIIHIDIDPAEIGKNV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 310 QPERELIGDIANTLDLLLPAINGYQLPEGSREYLQVLRDKMDGDVKFDRsqaEKGRLHPLDIVEVLQENTTDDMTVTVDV 389
Cdd:TIGR00118 310 RVDIPIVGDARNVLEELLKKLFELKERKESAWLEQINKWKKEYPLKMDY---TEEGIKPQQVIEELSRVTKDEAIVTTDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 390 GTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWND 469
Cdd:TIGR00118 387 GQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNN 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568064214 470 GHYNMVEFQEEMKY-GRSSGVDFGPV-DFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDYKD 540
Cdd:TIGR00118 467 RYLGMVRQWQELFYeERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPE 539
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
6-537 |
1.05e-104 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 326.33 E-value: 1.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDVV 165
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 DSQVQVKAIKPLTDPQLGSSSVA------DINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAG 239
Cdd:PRK06276 163 EGELDLEKYPIPAKIDLPGYKPTtfghplQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 240 IVSRELEEAtfFGRVGLFRNQPGDMLLKKSDLVIAIG---YDPIEYEARNWNAEisARVIVIDVEPAEIDTYFQPERELI 316
Cdd:PRK06276 243 AFPEDHPLA--LGMVGMHGTKAANYSVTESDVLIAIGcrfSDRTTGDISSFAPN--AKIIHIDIDPAEIGKNVRVDVPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 317 GDIANTLDLLLPAINGYQLPEGSR--EYLQVLRDKMDGDVKFDRSqaekgRLHPLDIVEVLQENTTD-----DMTVTVDV 389
Cdd:PRK06276 319 GDAKNVLRDLLAELMKKEIKNKSEwlERVKKLKKESIPRMDFDDK-----PIKPQRVIKELMEVLREidpskNTIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 390 GTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWND 469
Cdd:PRK06276 394 GQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDN 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 470 GHYNMV-EFQEEMKYGRSSGVDFGPV-DFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK06276 474 RTLGMVyQWQNLYYGKRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIID 543
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-536 |
9.58e-98 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 306.94 E-value: 9.58e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQL--IVARHEQNAAFMAQGIGRITGEPGVVIATSGPGA 78
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIrvIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKrSDLLKRA----HQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPG 154
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIP-SALIGKGrghlHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 155 ASFISIPQDVVDSQVQVKAI---KPLTDPQLGSSSVADInylAQAIKNAVLPVLLLGNGASSAkvTASIRQLLEQVQLPV 231
Cdd:PRK08266 160 PVALEMPWDVFGQRAPVAAApplRPAPPPAPDPDAIAAA---AALIAAAKNPMIFVGGGAAGA--GEEIRELAEMLQAPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 232 VETFQGAGIVSRELEeatffgrvgLFRNQP-GDMLLKKSDLVIAIGYD-PIEYEARNWNAEiSARVIVIDVEPAEIdTYF 309
Cdd:PRK08266 235 VAFRSGRGIVSDRHP---------LGLNFAaAYELWPQTDVVIGIGSRlELPTFRWPWRPD-GLKVIRIDIDPTEM-RRL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 310 QPERELIGDIANTLDLLLPAINGYQLPEGSREYlQVLRDKMDGDVKFDRSQAEKGRLHPldIVEVLQENT--TDDMTvtv 387
Cdd:PRK08266 304 KPDVAIVADAKAGTAALLDALSKAGSKRPSRRA-ELRELKAAARQRIQAVQPQASYLRA--IREALPDDGifVDELS--- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 388 DVGtHYIWMAryFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIW 467
Cdd:PRK08266 378 QVG-FASWFA--FPVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVF 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 468 NDGHY-NMVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPV 536
Cdd:PRK08266 455 NNNAYgNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-538 |
9.19e-96 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 302.46 E-value: 9.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKF-GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGAS 79
Cdd:PRK06048 4 STEKMtGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 80 NLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFIS 159
Cdd:PRK06048 84 NLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLID 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 160 IPQDVVDSQ--------VQVKAIKPLT--DPQlgsssvaDINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQL 229
Cdd:PRK06048 164 LPKDVTTAEidfdypdkVELRGYKPTYkgNPQ-------QIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 230 PVVETFQGAGIVSRelEEATFFGRVGLFRNQPGDMLLKKSDLVIAIG--YD-----PIEYEARNwnaeisARVIVIDVEP 302
Cdd:PRK06048 237 PVTTTLMGIGAIPT--EHPLSLGMLGMHGTKYANYAIQESDLIIAVGarFDdrvtgKLASFAPN------AKIIHIDIDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 303 AEIDTYFQPERELIGDIANTLDLLLPAINgyqlPEGSREYLQVLRD-KMDGDVKFDRSQaekGRLHPLDIVEVLQENTTD 381
Cdd:PRK06048 309 AEISKNVKVDVPIVGDAKQVLKSLIKYVQ----YCDRKEWLDKINQwKKEYPLKYKERE---DVIKPQYVIEQIYELCPD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 382 DMTVTvDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLP 461
Cdd:PRK06048 382 AIIVT-EVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIP 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 462 IVHLIWNDGHYNMVEFQEEMKYGRSSGVDF--GPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDY 538
Cdd:PRK06048 461 VIVAILNNGYLGMVRQWQELFYDKRYSHTCikGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVEC 539
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
6-537 |
1.52e-95 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 302.14 E-value: 1.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDT----LEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNL 81
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 82 ATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIP 161
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 162 QDVVDSQVQ---------VKAIKP---LTDPQlgsssvaDINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQL 229
Cdd:PRK06456 164 RDIFYEKMEeikwpekplVKGYRDfptRIDRL-------ALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 230 PVVETFQGAGIVSRelEEATFFGRVGLFRNQPGDMLLKKSDLVIAIG--YDPIEYEARNWNAEISARVIVIDVEPAEIDT 307
Cdd:PRK06456 237 PIVSTFPGKTAIPH--DHPLYFGPMGYYGRAEASMAALESDAMLVVGarFSDRTFTSYDEMVETRKKFIMVNIDPTDGEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 308 YFQPERELIGDIANTLDLLLPAINGYQLPEGSREYLQVLRDKMDGDVKFDRSQaEKGRLHPLDIVEVLQENTTDDMTVTV 387
Cdd:PRK06456 315 AIKVDVGIYGNAKIILRELIKAITELGQKRDRSAWLKRVKEYKEYYSQFYYTE-ENGKLKPWKIMKTIRQALPRDAIVTT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 388 DVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIW 467
Cdd:PRK06456 394 GVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIF 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568064214 468 NDGHYNMV-EFQEEMKYGRSSGVDFGPV-DFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK06456 474 DNRTLGLVrQVQDLFFGKRIVGVDYGPSpDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVD 545
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-536 |
5.33e-95 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 300.91 E-value: 5.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK07710 18 GAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDVV 165
Cdd:PRK07710 98 ADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDMV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 --------DSQVQVKAIKPLTDPQLgsssvADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQG 237
Cdd:PRK07710 178 veegefcyDVQMDLPGYQPNYEPNL-----LQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 238 AGIVSRELEeaTFFGRVGLFRNQPGDMLLKKSDLVIAIG--YDP-----IEYEARNwnaeisARVIVIDVEPAEIDTYFQ 310
Cdd:PRK07710 253 LGGFPADHP--LFLGMAGMHGTYTANMALYECDLLINIGarFDDrvtgnLAYFAKE------ATVAHIDIDPAEIGKNVP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 311 PERELIGDIANTLDLLLpAINGYqlPEGSREYLQVLRD-KMDGDVKFDRsqaEKGRLHPLDIVEVLQENTTDDMTVTVDV 389
Cdd:PRK07710 325 TEIPIVADAKQALQVLL-QQEGK--KENHHEWLSLLKNwKEKYPLSYKR---NSESIKPQKAIEMLYEITKGEAIVTTDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 390 GTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWND 469
Cdd:PRK07710 399 GQHQMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNN 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 470 GHYNMV-EFQEEMKYGRSSGVDFG--PvDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPV 536
Cdd:PRK07710 479 EALGMVrQWQEEFYNQRYSHSLLScqP-DFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRV 547
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
6-537 |
7.18e-95 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 300.09 E-value: 7.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFD-TLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAILNIYDeIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDV 164
Cdd:PRK08527 85 LATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 165 V--------DSQVQVKAIKPLTDpqlGSSSvaDINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ 236
Cdd:PRK08527 165 TatlgefeyPKEISLKTYKPTYK---GNSR--QIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGIVSRELEeaTFFGRVGLFRNQPGDMLLKKSDLVIAIGY---DPI-----EYeARNwnaeisARVIVIDVEPAEIDTY 308
Cdd:PRK08527 240 ARGVLRSDDP--LLLGMLGMHGSYAANMAMSECDLLISLGArfdDRVtgklsEF-AKH------AKIIHVDIDPSSISKI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 309 FQPERELIGDIANTLDLLLPAINGYQlPEGSREYLQVLRDkmdgdvkfdrsqaeKGRLHPL---DIVEVLQ--------- 376
Cdd:PRK08527 311 VNADYPIVGDLKNVLKEMLEELKEEN-PTTYKEWREILKR--------------YNELHPLsyeDSDEVLKpqwviervg 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 377 ENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAV 456
Cdd:PRK08527 376 ELLGDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 457 RLQLPIVHLIWNDGHYNMVEFQEEMKYG-RSSGVD--FGPvDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIID 533
Cdd:PRK08527 456 EYKIPVINIILNNNFLGMVRQWQTFFYEeRYSETDlsTQP-DFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALID 534
|
....
gi 568064214 534 VPVD 537
Cdd:PRK08527 535 VKID 538
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
3-550 |
3.22e-94 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 298.81 E-value: 3.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 3 EKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLA 82
Cdd:PRK06725 14 EVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 83 TGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQ 162
Cdd:PRK06725 94 TGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 163 DVVDSQ--------VQVKAIKPltDPQLGSSSVADInylAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVET 234
Cdd:PRK06725 174 DVQNEKvtsfynevVEIPGYKP--EPRPDSMKLREV---AKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 235 FQGAGivSRELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEAR-NWNAEI---SARVIVIDVEPAEIDTYFQ 310
Cdd:PRK06725 249 LMGLG--AYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALG---VRFDDRvTGKLELfspHSKKVHIDIDPSEFHKNVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 311 PERELIGDIANTLDLLLPAIngyqLPEGSREYLQVLRdkmDGDVKFDRS-QAEKGRLHPLDIVEVLQENTTDDMTVTVDV 389
Cdd:PRK06725 324 VEYPVVGDVKKALHMLLHMS----IHTQTDEWLQKVK---TWKEEYPLSyKQKESELKPQHVINLVSELTNGEAIVTTEV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 390 GTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWND 469
Cdd:PRK06725 397 GQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 470 GHYNMVEFQEEMKY-GRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDYkdsstlGETI 548
Cdd:PRK06725 477 KFLGMVRQWQEMFYeNRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEE------GENV 550
|
..
gi 568064214 549 LP 550
Cdd:PRK06725 551 FP 552
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
368-540 |
5.84e-93 |
|
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: 281.87 E-value: 5.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 368 PLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLF 447
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 448 SAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKEN 527
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|...
gi 568064214 528 GPVIIDVPVDYKD 540
Cdd:cd02010 161 GVHVIDCPVDYSE 173
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
6-537 |
1.00e-90 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 289.09 E-value: 1.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDVV 165
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDIQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 DSQVQVKAIkPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAGIVSRel 245
Cdd:PRK08978 163 LAEGELEPH-LTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEA-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 246 EEATFFGRVGLFRNQPGDMLLKKSDLVIAIGydpieyeAR---------NWNAEiSARVIVIDVEPAEIDTYFQPERELI 316
Cdd:PRK08978 240 DHPYYLGMLGMHGTKAANLAVQECDLLIAVG-------ARfddrvtgklNTFAP-HAKVIHLDIDPAEINKLRQAHVALQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 317 GDiantLDLLLPAINGYQLPEGSREYLQVLRdkmdgdVKFD-RSQAEKGRLHPLDIVEVLQENTTDDMTVTVDVGTHYIW 395
Cdd:PRK08978 312 GD----LNALLPALQQPLNIDAWRQHCAQLR------AEHAwRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMW 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 396 MARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMV 475
Cdd:PRK08978 382 VAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568064214 476 EFQEEMKY-GRSSGVDF--GPvDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK08978 462 RQWQQLFFdERYSETDLsdNP-DFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSID 525
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-537 |
2.58e-90 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 288.82 E-value: 2.58e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQL--IVARHEQNAAFMAQGIGRITGEPGVVIATSGPGA 78
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIkfIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSgMPGASFI 158
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYE-KKGVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 159 SIPQDVVDSQVQVKAIKP--LTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKvtASIRQLLEQVQLPVVETFQ 236
Cdd:PRK08611 160 TIPDDLPAQKIKDTTNKTvdTFRPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKAKIPIIHTLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGIVSREleEATFFGRVGLFRNQPGDMLLKKSDLVIAIGYDpieYEARNWNAEiSARVIVIDVEPAEIDTYFQPERELI 316
Cdd:PRK08611 238 AKGIIPDD--HPYSLGNLGKIGTKPAYEAMQEADLLIMVGTN---YPYVDYLPK-KAKAIQIDTDPANIGKRYPVNVGLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 317 GDIANTLDLLLPAINgyqlPEGSREYLQVLRDKM---DGDVKFDRSQAEKgRLHPLDIVEVLQENTTDDMTVTVDVGTHY 393
Cdd:PRK08611 312 GDAKKALHQLTENIK----HVEDRRFLEACQENMakwWKWMEEDENNAST-PIKPERVMAAIQKIADDDAVLSVDVGTVT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 394 IWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYN 473
Cdd:PRK08611 387 VWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLA 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568064214 474 MVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK08611 467 FIKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD 530
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-537 |
2.86e-90 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 288.14 E-value: 2.86e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKF-GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGP-QLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGA 78
Cdd:PRK08155 9 TRKRFtGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQiRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFI 158
Cdd:PRK08155 89 TNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 159 SIPQDVVDSQVQVKAIKPLTDPQ-LGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQG 237
Cdd:PRK08155 169 DIPKDVQTAVIELEALPAPAEKDaAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 238 AGIVSreLEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGydpieyeARNWNAEI--------SARVIVIDVEPAEIDTYF 309
Cdd:PRK08155 249 LGMLP--KAHPLSLGMLGMHGARSTNYILQEADLLIVLG-------ARFDDRAIgkteqfcpNAKIIHVDIDRAELGKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 310 QPERELIGDIANTLDLLLPAINgyqlPEGSREYLQVLRDkMDGDVKFDRSQAEKGRLHpLDIVEVLQENTTDDMTVTVDV 389
Cdd:PRK08155 320 QPHVAIQADVDDVLAQLLPLVE----AQPRAEWHQLVAD-LQREFPCPIPKADDPLSH-YGLINAVAACVDDNAIITTDV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 390 GTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWND 469
Cdd:PRK08155 394 GQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNN 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 470 GHYNMVEFQEEMKYG-RSSGVDF-GPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK08155 474 EALGLVHQQQSLFYGqRVFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRID 543
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-537 |
1.07e-88 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 284.07 E-value: 1.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGP-QLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGAS 79
Cdd:PRK08199 5 PRARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDiRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 80 NLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFIS 159
Cdd:PRK08199 85 NASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 160 IPQDVVDSQVQVkAIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAG 239
Cdd:PRK08199 165 LPEDVLSETAEV-PDAPPYRRVAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 240 IVSRELeeATFFGRVGLFRNQPGDMLLKKSDLVIAIG----------YDPIEYEARnwnaeiSARVIVIDVEPAEIDTYF 309
Cdd:PRK08199 244 LFDNRH--PNYAGDLGLGINPALAARIREADLVLAVGtrlgevttqgYTLLDIPVP------RQTLVHVHPDAEELGRVY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 310 QPERELIGDIANTLDLLLPAINGYQLP------EGSREYLQVLrdkmdgdvkfdRSQAEKGRLHPLDIVEVLQENTTDDM 383
Cdd:PRK08199 316 RPDLAIVADPAAFAAALAALEPPASPAwaewtaAAHADYLAWS-----------APLPGPGAVQLGEVMAWLRERLPADA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 384 TVTVDVGTHYIWMARYFKSYEPR-HLLFSNGmqTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPI 462
Cdd:PRK08199 385 IITNGAGNYATWLHRFFRFRRYRtQLAPTSG--SMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPI 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064214 463 VHLIWNDGHYNMVEFQEEMKY-GRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK08199 463 IVIVVNNGMYGTIRMHQEREYpGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
6-536 |
1.44e-87 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 282.71 E-value: 1.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTL---EDKGP-QLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNL 81
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIYDELykaEAEGWlKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 82 ATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIP 161
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 162 QDV----VDSQ-VQVKAIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ 236
Cdd:PRK07418 181 KDVgqeeFDYVpVEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTLM 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGIVSRelEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGY---DPI-----EYEARnwnaeisARVIVIDVEPAEIDTY 308
Cdd:PRK07418 261 GKGAFDE--HHPLSVGMLGMHGTAYANFAVTECDLLIAVGArfdDRVtgkldEFASR-------AKVIHIDIDPAEVGKN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 309 FQPERELIGDIANTLDLLLPAINGYQLPEGSREYL-QVLRDKMDGDVKFDRsqaEKGRLHPLDIVEVLQENTTDDMtVTV 387
Cdd:PRK07418 332 RRPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLeRINRWKQDYPLVVPP---YEGEIYPQEVLLAVRDLAPDAY-YTT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 388 DVGTHYIWMARYFKSyEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIW 467
Cdd:PRK07418 408 DVGQHQMWAAQFLRN-GPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVII 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568064214 468 NDGHYNMVEFQEEMKYGR---SSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPV 536
Cdd:PRK07418 487 NNGWQGMVRQWQESFYGErysASNMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHV 558
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
3-536 |
5.35e-85 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 275.04 E-value: 5.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 3 EKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTL---EDKG-PQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGA 78
Cdd:CHL00099 9 EKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyawEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFI 158
Cdd:CHL00099 89 TNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 159 SIPQDV------------VDSQVQVKAIKPLTDPqlgsssvaDINYLAQA---IKNAVLPVLLLGNGASSAKVTASIRQL 223
Cdd:CHL00099 169 DIPKDVglekfdyyppepGNTIIKILGCRPIYKP--------TIKRIEQAaklILQSSQPLLYVGGGAIISDAHQEITEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 224 LEQVQLPVVETFQGAGIVSRELEEAtfFGRVGLFRNQPGDMLLKKSDLVIAIG--YD-----PIEYEARNwnaeisARVI 296
Cdd:CHL00099 241 AELYKIPVTTTLMGKGIFDEDHPLC--LGMLGMHGTAYANFAVSECDLLIALGarFDdrvtgKLDEFACN------AQVI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 297 VIDVEPAEIDTYFQPERELIGDIANTLdlllpaingyqlpegsREYLQVLrDKMDGDVKFDRSQAEKGRLH------PLD 370
Cdd:CHL00099 313 HIDIDPAEIGKNRIPQVAIVGDVKKVL----------------QELLELL-KNSPNLLESEQTQAWRERINrwrkeyPLL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 371 I---------VEVLQE--NTTDDMTVTVDVGTHYIWMARYFKSYePRHLLFSNGMQTLGVALPWAISAALVRPNTKIISV 439
Cdd:CHL00099 376 IpkpstslspQEVINEisQLAPDAYFTTDVGQHQMWAAQFLKCK-PRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 440 SGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKYGRS---SGVDFGPVDFVKYAESFGAKGFRATSPAEL 516
Cdd:CHL00099 455 SGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQAFYGERyshSNMEEGAPDFVKLAEAYGIKGLRIKSRKDL 534
|
570 580
....*....|....*....|
gi 568064214 517 TQLLQKALKENGPVIIDVPV 536
Cdd:CHL00099 535 KSSLKEALDYDGPVLIDCQV 554
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
6-537 |
2.03e-80 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 262.83 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDK-GPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKsGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDV 164
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 165 VDSQ----------VQVKAIKPLTDPQLGSssvadINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVET 234
Cdd:PRK08979 166 LNPAilhpyeypesIKMRSYNPTTSGHKGQ-----IKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 235 FQGAGIVSRELEEAtfFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEARNWNAE----ISARVIVIDVEPAEIDTYFQ 310
Cdd:PRK08979 241 LMGLGAFPGTHKNS--LGMLGMHGRYEANMAMHNADLIFGIG---VRFDDRTTNNLekycPNATILHIDIDPSSISKTVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 311 PERELIGDIANTLDLLL------PAINGYQLPEGSREYLQVLRDKmdGDVKFDRSQaekGRLHPLDIVEVLQENTTDDMT 384
Cdd:PRK08979 316 VDIPIVGSADKVLDSMLalldesGETNDEAAIASWWNEIEVWRSR--NCLAYDKSS---ERIKPQQVIETLYKLTNGDAY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 385 VTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVH 464
Cdd:PRK08979 391 VASDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKI 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064214 465 LIWNDGHYNMVEFQEEMKY-GRSSGVDFGPV-DFVKYAESFGAKGFRATSPAELTQLLQKALK-ENGPVIIDVPVD 537
Cdd:PRK08979 471 INLNNRFLGMVKQWQDMIYqGRHSHSYMDSVpDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVD 546
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
6-537 |
1.35e-79 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 260.55 E-value: 1.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLED-KGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDV 164
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 165 VD----------SQVQVKAIKPLTDPQLGSssvadINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVET 234
Cdd:PRK07979 166 LNpanklpyvwpESVSMRSYNPTTQGHKGQ-----IKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 235 FQGAGIVSRELEEAtfFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEARNWNAEI----SARVIVIDVEPAEIDTYFQ 310
Cdd:PRK07979 241 LMGLGAFPATHRQS--LGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLAkycpNATVLHIDIDPTSISKTVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 311 PERELIGDIANTLDL---LLPAINGYQLPEGSREYLQVLRDKMDGD-VKFDRsqaEKGRLHPLDIVEVLQENTTDDMTVT 386
Cdd:PRK07979 316 ADIPIVGDARQVLEQmleLLSQESAHQPLDEIRDWWQQIEQWRARQcLKYDT---HSEKIKPQAVIETLWRLTKGDAYVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 387 VDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLI 466
Cdd:PRK07979 393 SDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLN 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568064214 467 WNDGHYNMVEFQEEMKY-GR--SSGVDFGPvDFVKYAESFGAKGFRATSPAELTQLLQKALKE---NGPVIIDVPVD 537
Cdd:PRK07979 473 LNNRYLGMVKQWQDMIYsGRhsQSYMQSLP-DFVRLAEAYGHVGIQISHPDELESKLSEALEQvrnNRLVFVDVTVD 548
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
4-550 |
1.21e-78 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 257.83 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 4 KFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLED-KGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLA 82
Cdd:PRK07282 10 KSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNfEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 83 TGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQ 162
Cdd:PRK07282 90 TGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 163 DVV--------DSQVQVKAIKPLTDPqlgssSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVET 234
Cdd:PRK07282 170 DVSaletdfiyDPEVNLPSYQPTLEP-----NDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 235 FQGAGIVSreLEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGY--------DPIEYeARNwnaeisARVIVIDVEPAEID 306
Cdd:PRK07282 245 LLGQGTIA--TSHPLFLGMGGMHGSYAANIAMTEADFMINIGSrfddrltgNPKTF-AKN------AKVAHIDIDPAEIG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 307 TYFQPERELIGDIANTLDLLLpaingyQLPE---GSREYLQ-VLRDKmdgdvKFDRSQAEKGR-LHPLDIVEVLQENTTD 381
Cdd:PRK07282 316 KIIKTDIPVVGDAKKALQMLL------AEPTvhnNTEKWIEkVTKDK-----NRVRSYDKKERvVQPQAVIERIGELTNG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 382 DMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLP 461
Cdd:PRK07282 385 DAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 462 IVHLIWNDGHYNMV-EFQEEMKYGRSSGVDFGPV-DFVKYAESFGAKGFRATSPAELTQLLqKALKENGPVIIDVPVDYK 539
Cdd:PRK07282 465 IKVVMLNNHSLGMVrQWQESFYEGRTSESVFDTLpDFQLMAQAYGIKHYKFDNPETLAQDL-EVITEDVPMLIEVDISRK 543
|
570
....*....|.
gi 568064214 540 dsstlgETILP 550
Cdd:PRK07282 544 ------EHVLP 548
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
6-537 |
7.89e-77 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 253.51 E-value: 7.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTL--EDKGPQLIVaRHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLAT 83
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGAVLHIYDALfkQDKVEHILV-RHEQAATHMADGYARATGKTGVVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 84 GLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PRK06466 85 GIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VVDSQVQVKAIKP-------LTDPQLGSSsvADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ 236
Cdd:PRK06466 165 MTNPAEKFEYEYPkkvklrsYSPAVRGHS--GQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGIVSRELEEatFFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEARNWNAEI----SARVIVIDVEPAEIDTYFQPE 312
Cdd:PRK06466 243 GLGGFPGTDRQ--FLGMLGMHGTYEANMAMHHADVILAVG---ARFDDRVTNGPAkfcpNAKIIHIDIDPASISKTIKAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 313 RELIGDIANTLDLLLPAINGyqlpEGSREYLQVLRD---------KMDGDVKFDRSQAEKgrLHPLDIVEVLQENTTDDM 383
Cdd:PRK06466 318 IPIVGPVESVLTEMLAILKE----IGEKPDKEALAAwwkqidewrGRHGLFPYDKGDGGI--IKPQQVVETLYEVTNGDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 384 TVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIV 463
Cdd:PRK06466 392 YVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVK 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568064214 464 HLIWNDGHYNMVEFQEEMKY-GR--SSGVDFGPvDFVKYAESFGAKGFRATSPAELTQLLQKALK-ENGPVIIDVPVD 537
Cdd:PRK06466 472 IINLNNGALGMVRQWQDMQYeGRhsHSYMESLP-DFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVD 548
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-537 |
7.44e-76 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 250.60 E-value: 7.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLED-KGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGAS 79
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 80 NLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFIS 159
Cdd:PRK06882 81 NAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 160 IPQDVVD----------SQVQVKAIKPLTDPQLGSssvadINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQL 229
Cdd:PRK06882 161 IPKDMVNpankftyeypEEVSLRSYNPTVQGHKGQ-----IKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 230 PVVETFQGAGivSRELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEARNWNAEI----SARVIVIDVEPAEI 305
Cdd:PRK06882 236 PVTSSLMGLG--AYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIG---VRFDDRTTNNLAkycpNAKVIHIDIDPTSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 306 DTYFQPERELIGDIANTLDLLLPAINGYQLPEGSRE----YLQVLRDKMDGDVKFDRSqaeKGRLHPLDIVEVLQENTTD 381
Cdd:PRK06882 311 SKNVPAYIPIVGSAKNVLEEFLSLLEEENLAKSQTDltawWQQINEWKAKKCLEFDRT---SDVIKPQQVVEAIYRLTNG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 382 DMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLP 461
Cdd:PRK06882 388 DAYVASDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIP 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 462 IVHLIWNDGHYNMVEFQEEMKY-GRSSGVDFGPV-DFVKYAESFGAKGFRATSPAELTQLLQKALK-ENGPVIIDVPVD 537
Cdd:PRK06882 468 VVIVSLNNRFLGMVKQWQDLIYsGRHSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSiKDKLVFVDVNVD 546
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-537 |
4.77e-75 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 249.24 E-value: 4.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTekfGADLIVDSLINHKVDYVFGIPGAKIDRVFDTL-EDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGAS 79
Cdd:PRK09107 11 MT---GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 80 NLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFIS 159
Cdd:PRK09107 88 NAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 160 IPQDV-----VDSQVQVKAIKPLTDPQLGsSSVADINYLAQAIKNAVLPVLLLGNGA--SSAKVTASIRQLLEQVQLPVV 232
Cdd:PRK09107 168 IPKDVqfatgTYTPPQKAPVHVSYQPKVK-GDAEAITEAVELLANAKRPVIYSGGGVinSGPEASRLLRELVELTGFPIT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 233 ETFQGAGivSRELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGydpieyeARnWNAEISARV---------IVIDVEPA 303
Cdd:PRK09107 247 STLMGLG--AYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVG-------AR-FDDRITGRLdafspnskkIHIDIDPS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 304 EIDTYFQPERELIGDIANTLDLLL------------PAINGYQLPEGSREYLQVLRDKMDGDVkfdrsqaekgrLHPLDI 371
Cdd:PRK09107 317 SINKNVRVDVPIIGDVGHVLEDMLrlwkargkkpdkEALADWWGQIARWRARNSLAYTPSDDV-----------IMPQYA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 372 VEVLQENTTD-DMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQ 450
Cdd:PRK09107 386 IQRLYELTKGrDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 451 ELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKYGR---SSGVDFGPvDFVKYAESFGAKGFRATSPAELTQLLQKALKEN 527
Cdd:PRK09107 466 EMSTAVQYNLPVKIFILNNQYMGMVRQWQQLLHGNrlsHSYTEAMP-DFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVD 544
|
570
....*....|
gi 568064214 528 GPVIIDVPVD 537
Cdd:PRK09107 545 KPVIFDCRVA 554
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
6-536 |
1.22e-74 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 248.36 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLED-KGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDsTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDV 164
Cdd:PRK07789 113 IADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPKDA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 165 VDSQ--------VQVKAIKPLTDPQLGSSSVAdinylAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ 236
Cdd:PRK07789 193 LQAQttfswpprMDLPGYRPVTKPHGKQIREA-----AKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLM 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGIV--SRELEeatfFGRVGLFRNQPGDMLLKKSDLVIAIG--YD-----PIEYEARNwnaeisARVIVIDVEPAEIDT 307
Cdd:PRK07789 268 ARGAFpdSHPQH----LGMPGMHGTVAAVAALQRSDLLIALGarFDdrvtgKLDSFAPD------AKVIHADIDPAEIGK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 308 YFQPERELIGDIANTLDLLLPAINGYQLPEGS------REYLQVLRDKMdgDVKFDRSqaEKGRLHPLDIVEVLQENTTD 381
Cdd:PRK07789 338 NRHADVPIVGDVKEVIAELIAALRAEHAAGGKpdltawWAYLDGWRETY--PLGYDEP--SDGSLAPQYVIERLGEIAGP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 382 DMTVTVDVGTHYIWMARyFKSYE-PRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQL 460
Cdd:PRK07789 414 DAIYVAGVGQHQMWAAQ-FIDYEkPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGI 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 461 PI-VHLIwNDGHYNMVEFQEEMKY-GRSSGVDFGP-----VDFVKYAESFGAKGFRATSPAELTQLLQKALKENG-PVII 532
Cdd:PRK07789 493 PIkVALI-NNGNLGMVRQWQTLFYeERYSNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDrPVVI 571
|
....
gi 568064214 533 DVPV 536
Cdd:PRK07789 572 DFVV 575
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
6-537 |
9.80e-73 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 242.74 E-value: 9.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFG--IPGAkidrVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLAT 83
Cdd:PRK06112 16 VAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 84 GLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VVDSQVQVKAikPLTDPQLGS-------SSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ 236
Cdd:PRK06112 172 LLTAAAAAPA--APRSNSLGHfpldrtvPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 237 GAGIVSrELEE------ATFFGRVGLFRNQPGdmLLKKSDLVIAIGYDPIEYEARNWNA-EISARVIVIDVEPAEIDTYF 309
Cdd:PRK06112 250 GKGAVD-ETHPlslgvvGSLMGPRSPGRHLRD--LVREADVVLLVGTRTNQNGTDSWSLyPEQAQYIHIDVDGEEVGRNY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 310 QPEReLIGDIANTLDLLLPAINGYQLP--EGSREYLQ----VLRDKMDGDVKfDRSQAEKGRLHPLDIVEVLQENTTDDM 383
Cdd:PRK06112 327 EALR-LVGDARLTLAALTDALRGRDLAarAGRRAALEpaiaAGREAHREDSA-PVALSDASPIRPERIMAELQAVLTGDT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 384 TVTVDVGTHYIWMARYFKSYEPR-HLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPI 462
Cdd:PRK06112 405 IVVADASYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 463 VHLIWNDGhynMVEFQ---EEMKYGR-SSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK06112 485 TIVVLNNG---ILGFQkhaETVKFGThTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD 560
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
7-538 |
4.35e-71 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 237.18 E-value: 4.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLV 86
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 87 TATAEGDPVLALAGqVKRSDLLKRA----HQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQ 162
Cdd:PRK07524 85 QAYADSIPMLVISS-VNRRASLGKGrgklHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 163 DVVDSQVQVKAIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAkvTASIRQLLEQVQLPVVETFQGAGIVS 242
Cdd:PRK07524 164 DVLAAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAA--AAALRALAERLDAPVALTINAKGLLP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 243 RE--LeeatffgRVGlfRNQ---PGDMLLKKSDLVIAIGYD--PIEYEArNWN--AEISARVIVIDVEPAEIDTYFQPER 313
Cdd:PRK07524 242 AGhpL-------LLG--ASQslpAVRALIAEADVVLAVGTElgETDYDV-YFDggFPLPGELIRIDIDPDQLARNYPPAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 314 ELIGDIANTLDLLLPAINGYQLPE--GSREYL---QVLRDKMDGDVkfdRSQAekgrlHPLD-IVEVLQENT-TDDMTVT 386
Cdd:PRK07524 312 ALVGDARAALEALLARLPGQAAAAdwGAARVAalrQALRAEWDPLT---AAQV-----ALLDtILAALPDAIfVGDSTQP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 387 VDVGTHYIWMA---RYFKSyeprhllfSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIV 463
Cdd:PRK07524 384 VYAGNLYFDADaprRWFNA--------STGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 464 HLIWNDGHYnmvefQEEMKYGRSS-----GVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDY 538
Cdd:PRK07524 456 VLLWNNDGY-----GEIRRYMVARdiepvGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
3-537 |
3.86e-67 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 227.76 E-value: 3.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 3 EKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTL-EDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNL 81
Cdd:PRK06965 20 DSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELyKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 82 ATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIP 161
Cdd:PRK06965 100 VTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 162 QDV--------VDSQVQVKAIKPLTDPQLGSssvadINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVE 233
Cdd:PRK06965 180 KDVsktpceyeYPKSVEMRSYNPVTKGHSGQ-----IRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 234 TFQGAGivSRELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGY--------DPIEYearnwnAEISARVIVIDVEPAEI 305
Cdd:PRK06965 255 TLMGLG--AYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGArfddrvigNPAHF------ASRPRKIIHIDIDPSSI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 306 DTYFQPERELIGDIANTLDLLLPAINGYQL---PEGSREYLQVLRDKMDGD-VKFDRSQAekgRLHPLDIVEVLQENTTD 381
Cdd:PRK06965 327 SKRVKVDIPIVGDVKEVLKELIEQLQTAEHgpdADALAQWWKQIEGWRSRDcLKYDRESE---IIKPQYVVEKLWELTDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 382 DMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLP 461
Cdd:PRK06965 404 DAFVCSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTP 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 462 IVHLIWNDGHYNMVEFQEEMKY-GR--SSGVDFGPvDFVKYAESFGAKGFRATSPAELTQLLQKALK-ENGPVIIDVPVD 537
Cdd:PRK06965 484 VKIISLNNRYLGMVRQWQEIEYsKRysHSYMDALP-DFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDFQTD 562
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-550 |
3.99e-66 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 225.00 E-value: 3.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEdKGPQL--IVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLAT 83
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALT-RSNCIrnVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 84 GLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PLN02470 94 GLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VvdsQVQVkAI----KPLTDPQLGS-----SSVADINYLAQAIKNAVLPVLLLGNGASSAkvTASIRQLLEQVQLPVVET 234
Cdd:PLN02470 174 I---QQQL-AVpnwnQPMKLPGYLSrlpkpPEKSQLEQIVRLISESKRPVVYVGGGCLNS--SEELREFVELTGIPVAST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 235 FQGAGIV----SRELEEATFFGRVglFRNQPGDmllkKSDLVIAIG--YD-----PIEYEARNwnaeisARVIVIDVEPA 303
Cdd:PLN02470 248 LMGLGAFpasdELSLQMLGMHGTV--YANYAVD----SADLLLAFGvrFDdrvtgKLEAFASR------ASIVHIDIDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 304 EIDTYFQPERELIGDIA---NTLDLLLPAiNGYQLPEGS--REYLQVLRdkmdgdVKFDRSQAEKGR-LHPLDIVEVLQE 377
Cdd:PLN02470 316 EIGKNKQPHVSVCADVKlalQGLNKLLEE-RKAKRPDFSawRAELDEQK------EKFPLSYPTFGDaIPPQYAIQVLDE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 378 NTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVR 457
Cdd:PLN02470 389 LTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 458 LQLPIVHLIWNDGHYNMVEFQEEMKYGRSSG----------VDFGPvDFVKYAESFGAKGFRATSPAELTQLLQKALKEN 527
Cdd:PLN02470 469 ENLPVKIMVLNNQHLGMVVQWEDRFYKANRAhtylgdpdaeAEIFP-DFLKFAEGCKIPAARVTRKSDLREAIQKMLDTP 547
|
570 580
....*....|....*....|...
gi 568064214 528 GPVIIDVPVDYKdsstlgETILP 550
Cdd:PLN02470 548 GPYLLDVIVPHQ------EHVLP 564
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
7-537 |
2.23e-63 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 217.00 E-value: 2.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLV 86
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 87 TATAEGDPVLALAGQVKrSDLLKRAH-QSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMpGASFISIPQDVV 165
Cdd:PRK06457 85 DAKMDHAPVIALTGQVE-SDMIGHDYfQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 DSQVQVKAIKPLTDPQLGSSsvADINYLAQAIKNAVLPVLLLGNGASSAkvTASIRQLLEQVQLPVVETFQGAGIVSRel 245
Cdd:PRK06457 163 RKSSEYKGSKNTEVGKVKYS--IDFSRAKELIKESEKPVLLIGGGTRGL--GKEINRFAEKIGAPIIYTLNGKGILPD-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 246 EEATFFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEARNWNAEiSARVIVIDVEPAEIDTYFQPERELIGDIANTLDL 325
Cdd:PRK06457 237 LDPKVMGGIGLLGTKPSIEAMDKADLLIMLG---TSFPYVNFLNK-SAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 326 llpaingyQLPEGSREYLQVLRDKMDgDVKFDRSQAEKGRLHPLD---IVEVLQENTTDDMTVTVDVGTHYIWMARYFKS 402
Cdd:PRK06457 313 --------DIEEKSDKFYEELKGKKE-DWLDSISKQENSLDKPMKpqrVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 403 YEPRHLLFSNGMQTLGVALPWAISAALVRPNT-KIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEM 481
Cdd:PRK06457 384 SGEQTFIFSAWLGSMGIGVPGSVGASFAVENKrQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 568064214 482 KYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK06457 464 MGYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVD 519
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
2-544 |
3.45e-63 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 216.13 E-value: 3.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 2 TEKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNL 81
Cdd:PRK05858 3 QTGHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 82 ATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIP 161
Cdd:PRK05858 83 MSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 162 QDVVDSQVQVKAiKPLTDPQLGSSSVADINYLAQA---IKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGA 238
Cdd:PRK05858 163 MDHAFSMADDDG-RPGALTELPAGPTPDPDALARAaglLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 239 GIVSRELEEAtfFGRVglfRNQPgdmlLKKSDLVIAIGYdPIEYEARNWNAEISARVIVIDVEPAEIDTYFQPERELIGD 318
Cdd:PRK05858 242 GVVPADHPLA--FSRA---RGKA----LGEADVVLVVGV-PMDFRLGFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 319 IANTLDLLLPAINGyqlPEGSREYLQVLRDKMDGDVKFDRSQ--AEKGRLHPLDIVEVLQENTTDDMTVTVDVGTHYIWM 396
Cdd:PRK05858 312 LSAILSALAGAGGD---RTDHQGWIEELRTAETAARARDAAElaDDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 397 ARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVE 476
Cdd:PRK05858 389 GRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEK 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568064214 477 FQEEMKYGRSSGVDFGP-VDFVKYAESFGAKGFRATSPAELTQLLQKALKENGP----VIIDVPVDYKDSSTL 544
Cdd:PRK05858 469 HPMEALYGYDVAADLRPgTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPylvnVLTDPSVAYPRRSNL 541
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-162 |
1.82e-59 |
|
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: 194.29 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 8 DLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLVT 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568064214 88 ATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQ 162
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
6-537 |
2.18e-59 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 206.76 E-value: 2.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRS--DLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PRK09259 92 ANATTNCFPMIMISGSSEREivDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VV----DSQVQVKAIKPLTDP---QLGSSSVAD--INYLAQAIKnavlPVLLLGNGASSAKVTASIRQLLEQVQLPVVET 234
Cdd:PRK09259 172 VLaqtmDADEALTSLVKVVDPapaQLPAPEAVDraLDLLKKAKR----PLIILGKGAAYAQADEQIREFVEKTGIPFLPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 235 FQGAGIVSRELEEATFFGRvglfrnqpgDMLLKKSDLVIAIGydpieyeAR-----------NWNAeiSARVIVIDVEPA 303
Cdd:PRK09259 248 SMAKGLLPDTHPQSAAAAR---------SLALANADVVLLVG-------ARlnwllshgkgkTWGA--DKKFIQIDIEPQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 304 EIDTYFQPERELIGDIANTLDLLLPAI--NGYQLPEgsrEYLQVLRDKMDGDV-KFDRSQAEkgRLHPLD-------IVE 373
Cdd:PRK09259 310 EIDSNRPIAAPVVGDIGSVMQALLAGLkqNTFKAPA---EWLDALAERKEKNAaKMAEKLST--DTQPMNfynalgaIRD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 374 VLQENTtdDMTV------TVDVGTHYIWMaryfksYEPRHLLFSNGMQTLGVALPWAISAAlVRPNTKIISVSGDGGFLF 447
Cdd:PRK09259 385 VLKENP--DIYLvneganTLDLARNIIDM------YKPRHRLDCGTWGVMGIGMGYAIAAA-VETGKPVVAIEGDSAFGF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 448 SAQELETAVRLQLPIVHLIW-NDGHYNMVEFQeemkygRSSGVDFGPVDFVKYA------ESFGAKGFRATSPAELTQLL 520
Cdd:PRK09259 456 SGMEVETICRYNLPVTVVIFnNGGIYRGDDVN------LSGAGDPSPTVLVHHArydkmmEAFGGVGYNVTTPDELRHAL 529
|
570
....*....|....*..
gi 568064214 521 QKALKENGPVIIDVPVD 537
Cdd:PRK09259 530 TEAIASGKPTLINVVID 546
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
388-534 |
5.88e-59 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 192.80 E-value: 5.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 388 DVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIW 467
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568064214 468 NDGHYNMVEFQEEMKYGRS----SGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDV 534
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRysgpSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
19-534 |
3.30e-58 |
|
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: 203.53 E-value: 3.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 19 VDYVFGIPGAKIDRVFDTL--EDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLVTATAEGDPVL 96
Cdd:TIGR02720 14 VDHIYGIPGGSFNSTMDALsaERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYDAKEDHVPVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 97 ALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSgMPGASFISIPQDV----VDSQVQVK 172
Cdd:TIGR02720 94 ALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVDFgwqeIPDNDYYA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 173 AIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAkvTASIRQLLEQVQLPVVETFQGAGIVSRELEeaTFFG 252
Cdd:TIGR02720 173 SSVSYQTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKA--GEELEALSEKLKIPLISTGLAKGIIEDRYP--AYLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 253 RVGLFRNQPGDMLLKKSDLVIAIGYDpIEYEARNWNAEISARVIVIDVEPAEIDTYFQPERELIGDIANTLDLLLPAINg 332
Cdd:TIGR02720 249 SAYRVAQKPANEALFQADLVLFVGNN-YPFAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKALAAILAQVE- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 333 yqlPEGSREYLQV-LRDKMDGD---VKFDRSQaeKGRLHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHL 408
Cdd:TIGR02720 327 ---PRESTPWWQAnVANVKNWRaylASLEDKT--EGPLQAYQVYRAINKIAEDDAIYSIDVGDININSNRHLKMTPKNKW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 409 LFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKYGRSSG 488
Cdd:TIGR02720 402 ITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTNQPLIG 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 568064214 489 VDFGPVDFVKYAESFGAKGFRATSPAELTQLLQ--KALKENGPVIIDV 534
Cdd:TIGR02720 482 VDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEqaKAIKQGKPVLIDA 529
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
6-534 |
1.49e-55 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 195.59 E-value: 1.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGP-QLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKiRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRA---HQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIP 161
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETPYLDQDLgyiHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 162 QDV----VDSQVQVKAIKpltdPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAkvTASIRQLLEqVQLPVVETFQG 237
Cdd:PRK07064 165 IDIqaaeIELPDDLAPVH----VAVPEPDAAAVAELAERLAAARRPLLWLGGGARHA--GAEVKRLVD-LGFGVVTSTQG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 238 AGIVSrELEEATffgrVGLFRNQPG-DMLLKKSDLVIAIGYDPIEYEARNWNAEISARVIVIDVEPAEIDTYFQPERELI 316
Cdd:PRK07064 238 RGVVP-EDHPAS----LGAFNNSAAvEALYKTCDLLLVVGSRLRGNETLKYSLALPRPLIRVDADAAADGRGYPNDLFVH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 317 GDIANTLDLLlpaingyqlpegsreyLQVLRDKMDGDVKFD------RSQAEKGRLHPL----DIVEVLQENTTDDMT-- 384
Cdd:PRK07064 313 GDAARVLARL----------------ADRLEGRLSVDPAFAadlraaREAAVADLRKGLgpyaKLVDALRAALPRDGNwv 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 385 --VTVDVGThyiWMARYFKSYEPRHLLFSNGmQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPI 462
Cdd:PRK07064 377 rdVTISNST---WGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANM 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568064214 463 VHLIWNDGHYN-MVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDV 534
Cdd:PRK07064 453 VIVLMNDGGYGvIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-169 |
1.19e-54 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 182.05 E-value: 1.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPGAKIDRVFDTLED-KGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQS-MDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*.
gi 568064214 164 VVDSQV 169
Cdd:pfam02776 161 VLLEEV 166
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
366-537 |
1.89e-54 |
|
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: 182.31 E-value: 1.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 366 LHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGF 445
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 446 LFSAQELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKY-GRSSGVDFGP-VDFVKYAESFGAKGFRATSPAELTQLLQKA 523
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYeGRYSHTTLDSnPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170
....*....|....
gi 568064214 524 LKENGPVIIDVPVD 537
Cdd:cd02015 161 LASDGPVLLDVLVD 174
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-534 |
2.44e-54 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 193.27 E-value: 2.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKFGADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGP-QLIVARHEQNAAFMAQGIGRIT-GEPGVVIATSGPGA 78
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGiRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFI 158
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 159 SIPQDVvdsQVQVKAIKPLTDPQLGSSSVAD--------INYLAQAIKnavlPVLLLGNGASSAKVTASIRQLLEQVQLP 230
Cdd:PRK11269 161 DLPFDV---QVAEIEFDPDTYEPLPVYKPAAtraqiekaLEMLNAAER----PLIVAGGGVINADASDLLVEFAELTGVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 231 VVETFQGAGIVSRELEeaTFFGRVGLFRNQP-GDMLLKKSDLVIAIGydpieyeARNWNAEISA--------RVIVIDVE 301
Cdd:PRK11269 234 VIPTLMGWGAIPDDHP--LMAGMVGLQTSHRyGNATLLASDFVLGIG-------NRWANRHTGSvevytkgrKFVHVDIE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 302 PAEIDTYFQPERELIGDIANTLDLLLpaingyqlpEGSREYlqvlrdKMDGDVKfDRS------QAEKGRLH-------- 367
Cdd:PRK11269 305 PTQIGRVFGPDLGIVSDAKAALELLV---------EVAREW------KAAGRLP-DRSawvadcQERKRTLLrkthfdnv 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 368 PLDIVEVLQE-NTT---DDMTVTVdVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDG 443
Cdd:PRK11269 369 PIKPQRVYEEmNKAfgrDTCYVST-IGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDY 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 444 GFLFSAQELETAVRLQLPIVHLIWNDG--------------------HYNMVEFQEEMKYGrssgvdfgpVDFVKYAESF 503
Cdd:PRK11269 448 DFQFLIEELAVGAQFNLPYIHVLVNNAylglirqaqrafdmdycvqlAFENINSPELNGYG---------VDHVKVAEGL 518
|
570 580 590
....*....|....*....|....*....|....*
gi 568064214 504 GAKGFRATSPAELTQLLQKALKENG----PVIIDV 534
Cdd:PRK11269 519 GCKAIRVFKPEDIAPALEQAKALMAefrvPVVVEV 553
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
370-536 |
2.50e-54 |
|
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: 181.30 E-value: 2.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 370 DIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSA 449
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 450 QELETAVRLQLPIVHLIWNDGHYNMVEFQEEMKY-GRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENG 528
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 568064214 529 PVIIDVPV 536
Cdd:cd00568 161 PALIEVKT 168
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
11-546 |
6.25e-54 |
|
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: 192.00 E-value: 6.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 11 VDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLVTATA 90
Cdd:TIGR03457 9 VEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAIAAAYW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 91 EGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMpGASFISIPQDVVDSQVQ 170
Cdd:TIGR03457 89 AHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYFYGEID 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 171 VKAIKPlTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ--GAGIVSRELeea 248
Cdd:TIGR03457 168 VEIPRP-VRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLhnDSFPASHPL--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 249 tFFGRVGLFRNQPGDMLLKKSDLVIAIG-----------YDpIEYEARNwnaeisARVIVIDVEPAEIDTYFQPERELIG 317
Cdd:TIGR03457 244 -WVGPLGYQGSKAAMKLISDADVVLALGtrlgpfgtlpqYG-IDYWPKN------AKIIQVDANAKMIGLVKKVTVGICG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 318 D----IANTLDLLLPAI-------NGYQLPEGSREYLQVL------RDKMDGDVKFDRSQAEKGRLHPLDIVEVLQENTT 380
Cdd:TIGR03457 316 DakaaAAEILQRLAGKAgdanraeRKAKIQAERSAWEQELsemtheRDPFSLDMIVEQRQEEGNWLHPRQVLRELEKAMP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 381 DDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQL 460
Cdd:TIGR03457 396 EDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 461 PIVHLI-----WNDGHYNMVEFQEEmkygRSSGVDF-GPVDFVKYAESFGAKGFRATSPAELTQLLQKALK---ENGPVI 531
Cdd:TIGR03457 476 PVTAVVfrnrqWGAEKKNQVDFYNN----RFVGTELeSELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaqaEGKTTV 551
|
570
....*....|....*
gi 568064214 532 IDVPVDykdsSTLGE 546
Cdd:TIGR03457 552 IEIVCT----RELGD 562
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
7-534 |
2.84e-53 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 190.20 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGP-QLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTiEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAkSGMPGASFISIPQDVV 165
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 DSQVQVKAIKPLTDPQLG--SSSVADINYLAQAIKNAVLPVLLLGNGASSAKvtASIRQLLEQVQLPVVETFQGAGIVsr 243
Cdd:PRK09124 165 LKPAPERATPHWYHAPQPvvTPAEEELRKLAALLNGSSNITLLCGSGCAGAH--DELVALAETLKAPIVHALRGKEHV-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 244 ELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGYDpieYEARNWNAEiSARVIVIDVEPAEIDTYFQPERELIGDIANTL 323
Cdd:PRK09124 241 EYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTD---FPYRQFYPT-DAKIIQIDINPGSLGRRSPVDLGLVGDVKATL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 324 DLLLPAINGYQ---LPEGSREYLQVLRDKMDgdvkfDRSQAEKGR--LHPLDIVEVLQENTTDDMTVTVDVGTHYIWMAR 398
Cdd:PRK09124 317 AALLPLLEEKTdrkFLDKALEHYRKARKGLD-----DLAVPSDGGkpIHPQYLARQISEFAADDAIFTCDVGTPTVWAAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 399 YFKSYEPRHLL--FSNGmqTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNMVE 476
Cdd:PRK09124 392 YLKMNGKRRLLgsFNHG--SMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVA 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 477 FqeEMKYG--RSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDV 534
Cdd:PRK09124 470 M--EMKAGgyLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDV 527
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
10-534 |
6.62e-52 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 186.74 E-value: 6.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 10 IVDSLINHKVDYVFGIPGAKIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLVTAT 89
Cdd:PRK07525 12 FVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 90 AEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMpGASFISIPQDVVDSQV 169
Cdd:PRK07525 92 WAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYFYGVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 170 QVKAIKPLtDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQ--GAGIVSRELee 247
Cdd:PRK07525 171 DVEIPQPV-RLERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLhnDAFPGSHPL-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 248 atFFGRVGLFRNQPGDMLLKKSDLVIAIG-----------YDpIEYEARNwnaeisARVIVIDVEPAEIDTYFQPERELI 316
Cdd:PRK07525 248 --WVGPLGYNGSKAAMELIAKADVVLALGtrlnpfgtlpqYG-IDYWPKD------AKIIQVDINPDRIGLTKKVSVGIC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 317 GDIANTLDLLLPAINGYQLPEGSRE------------YLQVL------RDKMDGDVKFDRSQAEKGRLHPLDIVEVLQEN 378
Cdd:PRK07525 319 GDAKAVARELLARLAERLAGDAGREerkaliaaeksaWEQELsswdheDDDPGTDWNEEARARKPDYMHPRQALREIQKA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 379 TTDDMTVTVDVGTHYIWMARYFKSYEPRH----LLFSNgmqtLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELET 454
Cdd:PRK07525 399 LPEDAIVSTDIGNNCSIANSYLRFEKGRKylapGSFGN----CGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 455 AVRLQLPIVHLIWNDGHY-----NMVEFQEEmkygRSSGVDF-GPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENG 528
Cdd:PRK07525 475 AVRHNWPVTAVVFRNYQWgaekkNQVDFYNN----RFVGTELdNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQN 550
|
....*....
gi 568064214 529 ---PVIIDV 534
Cdd:PRK07525 551 egkTTVIEI 559
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
7-537 |
4.68e-50 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 181.34 E-value: 4.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTL-EDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVrRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGmPGASFISIPQDVV 165
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHAVAG-GGVSVVTLPGDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 166 DSQVQVKAIKPLTDPQLGS--SSVADINYLAQAIKNAVLPVLLLGNGASSAKvtASIRQLLEQVQLPVVETFQGAGIVsr 243
Cdd:PRK06546 165 DEPAPEGFAPSVISPRRPTvvPDPAEVRALADAINEAKKVTLFAGAGVRGAH--AEVLALAEKIKAPVGHSLRGKEWI-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 244 ELEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGYD-PieyearnWNAEI-SARVIVIDVEPAEIDTYFQPERELIGDIAN 321
Cdd:PRK06546 241 QYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDfP-------YDQFLpDVRTAQVDIDPEHLGRRTRVDLAVHGDVAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 322 TLDLLLPAINgyqlPEGSREYL-QVLR---DKMDGDVKFDRSQAEKGR-LHPLDIVEVLQENTTDDMTVTVDVGTHYIWM 396
Cdd:PRK06546 314 TIRALLPLVK----EKTDRRFLdRMLKkhaRKLEKVVGAYTRKVEKHTpIHPEYVASILDELAADDAVFTVDTGMCNVWA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 397 ARYFKSYEPRHLL--FSNGmqTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHLIWNDGHYNM 474
Cdd:PRK06546 390 ARYITPNGRRRVIgsFRHG--SMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGM 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568064214 475 VEFqEEMKYGRSS-GVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK06546 468 VKL-EMLVDGLPDfGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
6-534 |
1.04e-47 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 174.61 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPgakIDRVFDTLEDKGPQLIVARHEQNAAFMAQGIGRITG--EPGVVIATSGPGASNLAT 83
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 84 GLVTATAEGDPVLALAGQVKRSdlLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQD 163
Cdd:PRK06154 99 GVAQAYGDSVPVLFLPTGYPRG--STDVAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VVDSQVQ--------VKAIKPLTDPqlgsssvADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETF 235
Cdd:PRK06154 177 VLAEELDelpldhrpSRRSRPGADP-------VEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 236 QGAGIVSRELEEAtfFGRVGLFRNQPGDMLLKKSDLVIAIGydpIEYEARNWNAEISA--RVIVIDVEPAEIDTYFQPER 313
Cdd:PRK06154 250 NGKSAFPEDHPLA--LGSGGRARPATVAHFLREADVLFGIG---CSLTRSYYGLPMPEgkTIIHSTLDDADLNKDYPIDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 314 ELIGDIANTLDLLLPAINGYQLPEGSReylqvlRDKMDGDVKFDRSQ----------AEKGRLHPLDIVEVLQENTTDDM 383
Cdd:PRK06154 325 GLVGDAALVLKQMIEELRRRVGPDRGR------AQQVAAEIEAVRAAwlakwmpkltSDSTPINPYRVVWELQHAVDIKT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 384 T-VTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPI 462
Cdd:PRK06154 399 ViITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 463 VHLIWND---GHYNMVEFQEEMKYG--RSSGvdfgpvDFVKYAESFGAKGFRATSPAELTQLLQKAL---KENGPVIIDV 534
Cdd:PRK06154 479 LTILLNNfsmGGYDKVMPVSTTKYRatDISG------DYAAIARALGGYGERVEDPEMLVPALLRALrkvKEGTPALLEV 552
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
366-537 |
6.00e-46 |
|
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: 159.23 E-value: 6.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 366 LHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGF 445
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 446 LFSAQELETAVRLQLPIVHLIWNDGHYNMVEF-QEEMKYGRsSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKAL 524
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWeQEVMGQPE-FGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEAL 160
|
170
....*....|...
gi 568064214 525 KENGPVIIDVPVD 537
Cdd:cd02014 161 AADGPVVIDVVTD 173
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-538 |
1.57e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 165.94 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 1 MTEKFGADLIVDSLINHKVDYVFGIPG---AKIDRVFDTLEDKG---PQLIVARHEQNAAFMAQGIGRITGEPGVVIATS 74
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGrplPEFVICPHEIVAISMAHGYALVTGKPQAVMVHV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 75 GPGASNLATGLVTATAEGDPVLALAGqvkRSDLLKRAH-----------QSM-DNAALFKPITKYSVEVQDGNTLSEIIA 142
Cdd:PRK08327 84 DVGTANALGGVHNAARSRIPVLVFAG---RSPYTEEGElgsrntrihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 143 NAYRHAKSGMPGASFISIPQDVVDSQVQVKAI--KPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASI 220
Cdd:PRK08327 161 RAIQIAMSEPKGPVYLTLPREVLAEEVPEVKAdaGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 221 RQLLEQVQLPVVEtFQGagivsrelEEATFFGRVGLFRNQPGDMLLKKSDLVIAIGYDPIEYEARNWNAEiSARVIVIDV 300
Cdd:PRK08327 241 RRLAEELAIPVVE-YAG--------EVVNYPSDHPLHLGPDPRADLAEADLVLVVDSDVPWIPKKIRPDA-DARVIQIDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 301 EPAEIDT---YFQPERELIGDIANTLDLLLPAI-----NGYQLPEGSREYLQVLRDKMDgdvKFDRSQAEK----GRLHP 368
Cdd:PRK08327 311 DPLKSRIplwGFPCDLCIQADTSTALDQLEERLkslasAERRRARRRRAAVRELRIRQE---AAKRAEIERlkdrGPITP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 369 LDIVEVLQENTTDDMTVTvdvgTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFS 448
Cdd:PRK08327 388 AYLSYCLGEVADEYDAIV----TEYPFVPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 449 AQE--LETAVRLQLPIVHLIWNDGHYNMVEFQEEMKY--------GRSSGVDFGP-VDFVKYAESFGAKGFRATSPAELT 517
Cdd:PRK08327 464 VPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYpegyaarkGTFPGTDFDPrPDFAKIAEAFGGYGERVEDPEELK 543
|
570 580
....*....|....*....|....*
gi 568064214 518 QLLQKAL----KENGPVIIDVPVDY 538
Cdd:PRK08327 544 GALRRALaavrKGRRSAVLDVIVDR 568
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
7-537 |
1.66e-44 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 166.24 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTLE--DKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGraDDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPI-TKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFIsIPQD 163
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI-LPND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 164 VVDSqvqvkaikPLTDPQ---------LGSSS---VADINYLAQA--IKNAVLPV-LLLGNGASSAkvTASIRQLLEQVQ 228
Cdd:PRK08273 165 VQEL--------EYEPPPhahgtvhsgVGYTRprvVPYDEDLRRAaeVLNAGRKVaILVGAGALGA--TDEVIAVAERLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 229 LPVVETFQGAGIVSRELEEATffGRVGLFRNQPGDMLLKKSD--LVIAIGYDPIEYEARnwnaEISARVIVIDVEPAEID 306
Cdd:PRK08273 235 AGVAKALLGKAALPDDLPWVT--GSIGLLGTKPSYELMRECDtlLMVGSSFPYSEFLPK----EGQARGVQIDIDGRMLG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 307 TYFQPERELIGDIANTLDLLLPAINgyqlPEGSREYlqvlRDKMDGDVKF------DRSQAEKGRLHPLDIVEVLQENTT 380
Cdd:PRK08273 309 LRYPMEVNLVGDAAETLRALLPLLE----RKKDRSW----RERIEKWVARwwetleARAMVPADPVNPQRVFWELSPRLP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 381 DDMTVTVDVGTHYIWMAryfksyepRHLLFSNGMQ--------TLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQ-E 451
Cdd:PRK08273 381 DNAILTADSGSCANWYA--------RDLRMRRGMMaslsgtlaTMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGMaE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 452 LETAVRLQ-----LPIVHLIWNDGHYNMVEF-QEEM----KYGRSSgvDFGPVDFVKYAESFGAKGFRATSPAELTQLLQ 521
Cdd:PRK08273 453 LITVAKYWrqwsdPRLIVLVLNNRDLNQVTWeQRVMegdpKFEASQ--DLPDVPYARFAELLGLKGIRVDDPEQLGAAWD 530
|
570
....*....|....*.
gi 568064214 522 KALKENGPVIIDVPVD 537
Cdd:PRK08273 531 EALAADRPVVLEVKTD 546
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
7-164 |
9.77e-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: 144.62 E-value: 9.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTL-EDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGL 85
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALrREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 86 VTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMpGASFISIPQDV 164
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGDV 160
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
368-537 |
2.09e-37 |
|
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: 136.12 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 368 PLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLF 447
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 448 SAQELETAVRLQLPIVHLIWNDGHYNM-VEFQEEM-KYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALK 525
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQgLDGQQLSyGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 568064214 526 ENGPVIIDVPVD 537
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
8-537 |
3.33e-36 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 141.63 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 8 DLIVDSLINHKVDYVFGIPGAKIDRVFDTLEDkGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATGLVT 87
Cdd:PRK07092 16 DATIDLLRRFGITTVFGNPGSTELPFLRDFPD-DFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 88 ATAEGDPVLALAGQVKRSDLLKRAH-QSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFISIPQDVVD 166
Cdd:PRK07092 95 AFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 167 SQVQvkaikPLTDPQLGSSSVAD---INYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPV-VETFQGagivs 242
Cdd:PRK07092 175 QPAE-----PLPARTVSSAVRPDpaaLARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAPMSG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 243 releEATFFGRVGLFRN-QPGDM-----LLKKSDLVIAIG--------YDPIEYEARNwnaeisARVIVIDVEPAEidTY 308
Cdd:PRK07092 245 ----RCSFPEDHPLFAGfLPASRekisaLLDGHDLVLVIGapvftyhvEGPGPHLPEG------AELVQLTDDPGE--AA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 309 FQPERE-LIGDIANTLDLLLPaingyQLPEGSREYLQVLrdkmdgdVKFDRSQAEKGRLHPLDIVEVLQENTTDDMTVTV 387
Cdd:PRK07092 313 WAPMGDaIVGDIRLALRDLLA-----LLPPSARPAPPAR-------PMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 388 DVGTHYIWMARYFKSYEPRHLLF--SNGmqtLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIVHL 465
Cdd:PRK07092 381 EAPSTRPAMQEHLPMRRQGSFYTmaSGG---LGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568064214 466 IWNDGHYN-MVEFQEEMKYGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:PRK07092 458 ILNNGRYGaLRWFAPVFGVRDVPGLDLPGLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
7-542 |
3.28e-35 |
|
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: 139.14 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 7 ADLIVDSLINHKVDYVFGIPGAKIDRVFDTLE-DKGPQLIVARHEQNAAFMAQGIGRITGePGVVIATSGPGASNLATGL 85
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEaHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 86 VTATAEGDPVLALAG----QVKRSDLLkrAHQSM------DNAALFKPITKYSVEVQDGNTLSEI---IANAYRHAKsgm 152
Cdd:COG3961 87 AGAYAERVPVVHIVGapgtRAQRRGPL--LHHTLgdgdfdHFLRMFEEVTVAQAVLTPENAAAEIdrvLAAALREKR--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 153 PGasFISIPQDVVDSQVqVKAIKPLTDPQLGSSSVAD---INYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQL 229
Cdd:COG3961 162 PV--YIELPRDVADAPI-EPPEAPLPLPPPASDPAALaaaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 230 PVVETFQGAGIVSrelEEATFFgrVGLFRnqpGDM-------LLKKSDLVIAIGYDPIEYEARNWNAEIS-ARVIVIDVE 301
Cdd:COG3961 239 PVATTLLGKSVLD---ESHPQF--IGTYA---GAAsspevreYVENADCVLCLGVVFTDTNTGGFTAQLDpERTIDIQPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 302 PAEI-DTYFQPERelIGDIANTL-DLLLPAINGYQLPEGSREYLQVLRDKmdgdvkfdrsqaekgrlhPLDIVEV---LQ 376
Cdd:COG3961 311 SVRVgGHIYPGVS--LADFLEALaELLKKRSAPLPAPAPPPPPPPAAPDA------------------PLTQDRLwqrLQ 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 377 ENTTDDMTVTVDVGTHYIWMARYfksYEPRHLLFSNGMQ--TLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELET 454
Cdd:COG3961 371 AFLDPGDIVVADTGTSLFGAADL---RLPEGATFIAQPLwgSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELST 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 455 AVRLQL-PIVHLIWNDGhYnMVE---FQEEMKYgrssgVDFGPVDFVKYAESFGAK---GFRATSPAELTQLLQKALKE- 526
Cdd:COG3961 448 MLRYGLkPIIFVLNNDG-Y-TIEraiHGPDGPY-----NDIANWDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEANt 520
|
570
....*....|....*.
gi 568064214 527 NGPVIIDVPVDYKDSS 542
Cdd:COG3961 521 DRLTLIEVVLDKMDAP 536
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-162 |
2.30e-29 |
|
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: 113.21 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 8 DLIVDSLINHKVDYVFGIPGAKIDRVFDTL-EDKGPQLIVARHEQNAAFMAQGIGRITGePGVVIATSGPGASNLATGLV 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALrEGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064214 87 TATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGmPGASFISIPQ 162
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
6-533 |
3.69e-28 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 118.05 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPG-------AKIDRVfdtledKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGA 78
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGtsemhfvAALDRV------PRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPGASFI 158
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 159 SIPQDVVDSQvQVKAIKPLTDPQLGSSSVADINYLAQAIKNAVLPVLLL-GNGASSAKVTASIR-------QLLEQVQLP 230
Cdd:PRK12474 161 IMPADVAWNE-AAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLrGSALRGAPLEAAGRiqaktgvRLYCDTFAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 231 VVEtfQGAGIVSREleeatffgRVGLFRNQpGDMLLKKSDLVIAIGYDP----IEYEAR-NWNAEisarvividvEPAEI 305
Cdd:PRK12474 240 RIE--RGAGRVPIE--------RIPYFHEQ-ITAFLKDVEQLVLVGAKPpvsfFAYPGKpSWGAP----------PGCEI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 306 DTYFQPEREL---IGDIANTLD-----LLLPAINGYQLPegsreylqvlrdkmdgdvkfdrsqaeKGRLHPLDIVEVLQE 377
Cdd:PRK12474 299 VYLAQPDEDLaqaLQDLADAVDapaepAARTPLALPALP--------------------------KGALNSLGVAQLIAH 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 378 NTTDDMTVTVDVGTHYIWMARYFKSYEPR-HLLFSNGmqTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAV 456
Cdd:PRK12474 353 RTPDQAIYADEALTSGLFFDMSYDRARPHtHLPLTGG--SIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMA 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 457 RLQLPIVHLIWNDGHYNMVEFqEEMKYGRSSG---------VDFGPVDFVKYAESFGAKGFRATSPAELTQLLQKALKEN 527
Cdd:PRK12474 431 RENLDVTVVIFANRSYAILNG-ELQRVGAQGAgrnalsmldLHNPELNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQR 509
|
....*.
gi 568064214 528 GPVIID 533
Cdd:PRK12474 510 GPRLIE 515
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
190-326 |
1.03e-26 |
|
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: 105.34 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 190 INYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVETFQGAGIVSRELEeaTFFGRVGLFRNQPGDMLLKKS 269
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHP--LYLGMLGMHGTPAANEALEEA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 270 DLVIAIGYDPIEYEARNWNAEIS--ARVIVIDVEPAEIDTYFQPERELIGDIANTLDLL 326
Cdd:pfam00205 79 DLVLAVGARFDDIRTTGKLPEFApdAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
366-536 |
3.41e-23 |
|
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: 96.51 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 366 LHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQtLGVALPWAISAALVRPNTKIISVSGDGGF 445
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRGGG-LGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 446 LFSAQELETAVRLQLPIVHLIWNDGHYNM--VEFQEEMKYGRSSGVDFGP------VDFVKYAESFGAKGFRATSPAELT 517
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGAlrSFLKRVGPEGPGENAPDGLdlldpgIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 568064214 518 QLLQKALKENGPVIIDVPV 536
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
365-553 |
6.41e-21 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 90.65 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 365 RLHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGG 444
Cdd:cd02013 3 PMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 445 FLFSAQELETAVRLQLPIVHLI-----WNDGHYNMVEFQEemkyGRSSGVDFGPVDFVKYAESFGAKGFRATSPAELTQL 519
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVfrnrqWGAEKKNQVDFYN----NRFVGTELESESFAKIAEACGAKGITVDKPEDVGPA 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 568064214 520 LQKAL---KENGPVIIDVPVDykdsSTLGETILPDEF 553
Cdd:cd02013 159 LQKAIammAEGKTTVIEIVCD----QELGDPFRRDAL 191
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
6-534 |
9.01e-21 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 95.68 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 6 GADLIVDSLINHKVDYVFGIPG-------AKIDRVfdtledKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGA 78
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGtsemhfvAALDRV------PGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 79 SNLATGLVTATAEGDPVLALAGQVKRSDLLKRAHQSMDNAALFKPITKYSVEVQDGNTLSEIIANAYRHAKSGMPG-ASF 157
Cdd:PRK07586 77 ANGLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAPGQvATL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 158 IsIPQDVVDSQVQVKAIkPLTDPQLGSSSVADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPV-VETF- 235
Cdd:PRK07586 157 I-LPADVAWSEGGPPAP-PPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATGARLlAETFp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 236 ----QGAGIVSREleeatffgRVGLFRNQPGDMLLKKSDLVIAIGYDPIEYEA----RNWNAEISARVIVIDvEPAEidt 307
Cdd:PRK07586 235 armeRGAGRPAVE--------RLPYFAEQALAQLAGVRHLVLVGAKAPVAFFAypgkPSRLVPEGCEVHTLA-GPGE--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 308 yfqpereligDIANTLDLLLPAINgyqlPEGSREYLQVLRdkmdgdvkfdRSQAEKGRLHPLDIVEVLQENTTDDMTVTV 387
Cdd:PRK07586 303 ----------DAAAALEALADALG----AKPAAPPLAAPA----------RPPLPTGALTPEAIAQVIAALLPENAIVVD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 388 DVGTH----YIWMARyfksyEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLPIV 463
Cdd:PRK07586 359 ESITSgrgfFPATAG-----AAPHDWLTLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 464 HLIWNDGHYNMVEfqeeMKYGRSSGVDFGP------------VDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVI 531
Cdd:PRK07586 434 TVIFANRAYAILR----GELARVGAGNPGPraldmldlddpdLDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHL 509
|
...
gi 568064214 532 IDV 534
Cdd:PRK07586 510 IEA 512
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
371-537 |
1.02e-17 |
|
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: 81.58 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 371 IVEVLQENTTDDMTVTVDVGT-----HYIWMARYFKSYeprHLLFsnGMQTLGVALPWAISAALVRPNTKIISVSGDGGF 445
Cdd:cd02003 4 VLGALNEAIGDDDVVINAAGSlpgdlHKLWRARTPGGY---HLEY--GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 446 LFSAQELETAVRLQLPIVHLIWNDGHY----------NMVEFQEEMKY-GRSSGVDFG---PVDFVKYAESFGAKGFRAT 511
Cdd:cd02003 79 LMLHSEIVTAVQEGLKIIIVLFDNHGFgcinnlqestGSGSFGTEFRDrDQESGQLDGallPVDFAANARSLGARVEKVK 158
|
170 180
....*....|....*....|....*.
gi 568064214 512 SPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:cd02003 159 TIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
366-534 |
7.62e-15 |
|
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: 73.47 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 366 LHPLDIVEVLQENTTDDMTVTVDVGTHYIWMARYFKSYEPRHLLFSNGMQTLGVALPWAISAALVRPNTKIISVSGDGGF 445
Cdd:cd02006 8 IKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 446 LFSAQELETAVRLQLPIVHLIWNDGHYNMV---------EFQEEMKYG--RSSGVDFGPVDFVKYAESFGAKGFRATSPA 514
Cdd:cd02006 88 QFMIEELAVGAQHRIPYIHVLVNNAYLGLIrqaqrafdmDYQVNLAFEniNSSELGGYGVDHVKVAEGLGCKAIRVTKPE 167
|
170 180
....*....|....*....|....
gi 568064214 515 ELTQLLQKALK----ENGPVIIDV 534
Cdd:cd02006 168 ELAAAFEQAKKlmaeHRVPVVVEA 191
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
418-534 |
6.94e-14 |
|
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: 69.87 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 418 GVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQL-PIVHLIWNDGhYnMVEfqEEMKYGRSSGVDFGPVDF 496
Cdd:cd02005 53 GYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLnPIIFLINNDG-Y-TIE--RAIHGPEASYNDIANWNY 128
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568064214 497 VKYAESFGA----KGFRATSPAELTQLLQKALKE-NGPVIIDV 534
Cdd:cd02005 129 TKLPEVFGGggggLSFRVKTEGELDEALKDALFNrDKLSLIEV 171
|
|
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
53-544 |
9.75e-13 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 70.58 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 53 AAFMAQGIGRITGEPGVVIATSGPGASNLATGLVTATAEGDPVLAL------------AGqvkrsdllkrahQSMDNAAL 120
Cdd:COG1165 57 AAFFALGLAKASGRPVALVCTSGTAAANYYPAVIEAFYSGVPLIVLtadrppelrdcgAN------------QTIDQVGL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 121 FKPITKYSVEV-QDGNTLSE------IIANAYRHAKSGMPGASFISIP-----QDVVDSQVQVKAIKPLTDPQLGSSSV- 187
Cdd:COG1165 125 FGNHVRWSADLpLPEADPDAlrylrrTINRALAAALGPPPGPVHINVPfreplYPDPDEEDPLAAGGPWIRVTPPEPAPs 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 188 -ADINYLAQAIKNAVLPVLLLGNGASSAKVTASIRQLLEQVQLPVVetfqgAGIVSReLEEATFFGRVGLFRNQPGDMLL 266
Cdd:COG1165 205 pEALAQLADELERAKRGLIVAGPLPPPEELAEALAALAEALGWPVL-----ADPLSN-LRHPNVISTYDLLLRNPEFAEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 267 KKSDLVIAIGYDPIEYEARNWNAEIS-ARVIVIDVEPAEIDTYFQPERELIGDIANTLDLLLPaingyQLPEGSREYLQV 345
Cdd:COG1165 279 LQPDLVIRFGGPPVSKRLKQFLRRHPpAEHWVVDPSGEWRDPFHSLTRVIEADPEAFLEALAE-----RLPPADSAWLAR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 346 LRDKmdgdvkfDRSQAEKgrlhpldIVEVLQENTTDDMTVTVDVgthyiwmaryFKSYEPRHLLF-SNGM-----QTLGV 419
Cdd:COG1165 354 WLAA-------EQKARAA-------IDEYLAEDPLSEGAVARRL----------LEALPEGSTLFvGNSMpvrdlDLFAR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 420 ALP-----WA----------------ISAALVRPNTKIIsvsGD-------GGFLFSAQeletaVRLQLPIVhLIWNDG- 470
Cdd:COG1165 410 PLPkgvrvYAnrgasgidgtvstalgAALASGKPTVLLT---GDlsflhdlNGLLLLYE-----LPPNLTIV-VVNNDGg 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 471 ---HY-----NMVEFQE--EMKYGrssgvdfgpVDFVKYAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVDYKD 540
Cdd:COG1165 481 gifSMlpgakFEPEFERffGTPHG---------LDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDREE 551
|
....
gi 568064214 541 SSTL 544
Cdd:COG1165 552 NAEL 555
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
19-161 |
4.56e-12 |
|
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: 64.05 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 19 VDYVFGIPGAKIDRVFDTLED-KGPQLIVARHEQNAAFMAQGIGRITGePGVVIATSGPGASNLATGLVTATAEGDPVLA 97
Cdd:cd07038 12 VKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEHVPVVH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568064214 98 LAGQVKRSDLLKRA--HQS-----MDNAA-LFKPITKYSVEVQDGNT-LSEI---IANAYRHAKsgmPGasFISIP 161
Cdd:cd07038 91 IVGAPSTKAQASGLllHHTlgdgdFDVFLkMFEEITCAAARLTDPENaAEEIdrvLRTALRESR---PV--YIEIP 161
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
9-161 |
8.43e-11 |
|
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: 60.59 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 9 LIVDSLINHKVDYVFGIPGAkidR----VFDTLEDKGPQLIVARHEQNAAFMAQGIGRITGEPGVVIATSGPGASNLATG 84
Cdd:cd07037 2 ALVEELKRLGVRDVVISPGS---RsaplALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 85 LVTATAEGDPVLALAGQvkRSDLLK--RAHQSMDNAALFKPITKYSVEVQ------DGNTLSEIIANAYRHAKSGMPGAS 156
Cdd:cd07037 79 VVEAYYSGVPLLVLTAD--RPPELRgtGANQTIDQVGLFGDYVRWSVDLPppedddDLWYLLRLANRAVLEALSAPPGPV 156
|
....*
gi 568064214 157 FISIP 161
Cdd:cd07037 157 HLNLP 161
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
416-539 |
2.91e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 57.15 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 416 TLGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELET-AVRLQLPIVHLIWNDGHYNMVEFQEEMkygrSSGVdfgpV 494
Cdd:PRK06163 58 SMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVYQITGGQPTL----TSQT----V 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568064214 495 DFVKYAESFG-AKGFRATSPAELTQLLQKALKENGPVIIDVPVDYK 539
Cdd:PRK06163 130 DVVAIARGAGlENSHWAADEAHFEALVDQALSGPGPSFIAVRIDDK 175
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
406-536 |
1.76e-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: 51.54 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 406 RHLLFSNGMqtlGVALPWAISAALVRPNTKIISVSGDGGFLFSAQELETAVRLQLP-IVHLIWNDGHYNMVEFQEEMkyg 484
Cdd:cd03371 42 QDFLTVGSM---GHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAHDSVGGQPTV--- 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568064214 485 rSSGVDFGPVdfvkyAESFG-AKGFRATSPAELTQLLQKALKENGPVIIDVPV 536
Cdd:cd03371 116 -SFDVSLPAI-----AKACGyRAVYEVPSLEELVAALAKALAADGPAFIEVKV 162
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
395-534 |
2.46e-07 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 51.37 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 395 WMARYFKSYeprhllfsnGMQTL-GVALPWAISAALVRPNTKIISVSGDG-GFLFSAQELETAVRLQLPIVHLIWNDGHY 472
Cdd:cd03375 39 RLPYYFNTY---------GFHTLhGRALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIY 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568064214 473 NMVEFQ-----EEMKYGRSS--GVDFGPVDFVKYAESFGAkGF--RATS--PAELTQLLQKALKENGPVIIDV 534
Cdd:cd03375 110 GLTKGQaspttPEGFKTKTTpyGNIEEPFNPLALALAAGA-TFvaRGFSgdIKQLKEIIKKAIQHKGFSFVEV 181
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
407-534 |
2.18e-06 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 49.49 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 407 HLLFSNGMQTL-GVALPWAISAALVRPNTKIISVSGDGGFL------FSAqeletAVRLQLPIVHLIWNDGHYNMVEFQ- 478
Cdd:PRK05778 61 GYFLSHGLHTLhGRAIAFATGAKLANPDLEVIVVGGDGDLAsiggghFIH-----AGRRNIDITVIVENNGIYGLTKGQa 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568064214 479 -----EEMKyGRSS--GVDFGPVDFVKYAESFGAkGF--RATS--PAELTQLLQKALKENGPVIIDV 534
Cdd:PRK05778 136 spttpEGSK-TKTApyGNIEPPIDPCALALAAGA-TFvaRSFAgdVKQLVELIKKAISHKGFAFIDV 200
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
407-534 |
1.16e-04 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 43.98 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 407 HLLFSNGMQTL-GVALPWAISAALVRPNTKIISVSGDG-GFLFSAQELETAVRLQLPIVHLIwndgHYNMVefqeemkYG 484
Cdd:PRK11866 50 EFLNTYGIHGIhGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAARRNVDITYIV----SNNQV-------YG 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568064214 485 RSSG--------------VDFG----PVDFVKYA----ESFGAKGFrATSPAELTQLLQKALKENGPVIIDV 534
Cdd:PRK11866 119 LTTGqaspttprgvktktTPDGnieePFNPIALAlaagATFVARGF-SGDVKHLKEIIKEAIKHKGFSFIDV 189
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
425-537 |
2.93e-03 |
|
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: 38.73 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064214 425 ISAALVRPNTKIIsvsGDGGFLFSAQELETAVRLQLPIVHLIWNDG------HYNMVEFQEEMK--YGRSSGVDFGPVdf 496
Cdd:cd02009 63 IALATDKPTVLLT---GDLSFLHDLNGLLLGKQEPLNLTIVVINNNgggifsLLPQASFEDEFErlFGTPQGLDFEHL-- 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568064214 497 vkyAESFGAKGFRATSPAELTQLLQKALKENGPVIIDVPVD 537
Cdd:cd02009 138 ---AKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
423-476 |
8.89e-03 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 38.91 E-value: 8.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568064214 423 WAISAAL----VRPNTKIISVSGDGGFLFSAQELETAVRL-QLPIVHLIWNDGHYNMVE 476
Cdd:PLN02573 432 WSVGATLgyaqAAPDKRVIACIGDGSFQVTAQDVSTMIRCgQKSIIFLINNGGYTIEVE 490
|
|
| |
