|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
7-558 |
0e+00 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 973.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 7 MRQWAHGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCS 86
Cdd:PRK08617 1 TDKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 87 NLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVS 166
Cdd:PRK08617 81 NLATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 167 LPQDIVDQPAQGNILPAGNAPKLGPAPDACIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAG 246
Cdd:PRK08617 161 LPQDVVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AVNQEHFTRFAGRVGLFNNQAGDRLLHLADLIICIGYSPVEYEPAMWNC-GNATLVHIDVLPAYEESHYAPEIELVGDIA 325
Cdd:PRK08617 241 VISRELEDHFFGRVGLFRNQPGDELLKKADLVITIGYDPIEYEPRNWNSeGDATIIHIDVLPAEIDNYYQPERELIGDIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 326 GTLEKLAGRIeQPLVLSDRASEILIDRQNQRELLARRGAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYL 405
Cdd:PRK08617 321 ATLDLLAEKL-DGLSLSPQSLEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWMARYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 406 YSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNMVAIQEE 485
Cdd:PRK08617 400 RSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEE 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495122918 486 KKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNPLLMGQLHLSQI 558
Cdd:PRK08617 480 MKYGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIKLMEQLLPDQL 552
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
13-551 |
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: 930.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDIV 172
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 173 DQPAQGNILPAGNAPKLGPAPDACIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAVNQEH 252
Cdd:TIGR02418 161 DSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSREL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 253 FTRFAGRVGLFNNQAGDRLLHLADLIICIGYSPVEYEPAMWNCGN-ATLVHIDVLPAYEESHYAPEIELVGDIAGTLEKL 331
Cdd:TIGR02418 241 EDHFFGRVGLFRNQPGDRLLKQADLVITIGYDPIEYEPRNWNSENdATIVHIDVEPAQIDNNYQPDLELVGDIASTLDLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 332 AGRIEQPlVLSDRASEILIDRQNQRELLARRGAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRAR 411
Cdd:TIGR02418 321 AERIPGY-ELPPDALAILEDLKQQREALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSYRAR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 412 QVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNMVAIQEEKKYQRL 491
Cdd:TIGR02418 400 HLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRS 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 492 SGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNPLLMG 551
Cdd:TIGR02418 480 SGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNPKLMS 539
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
13-547 |
1.89e-165 |
|
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: 481.20 E-value: 1.89e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLD-SSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:COG0028 5 GADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:COG0028 85 LADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPAQGN---ILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAV 248
Cdd:COG0028 165 QAAEAEEEpapPELRGYRPRPAPDPEA-IEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGAF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 249 NQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGYSPVEYEPAMWN--CGNATLVHIDVLPAYEESHYAPEIELVGDIAG 326
Cdd:COG0028 244 PEDH-PLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDefAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 327 TLEKLAGRIEQ-PLVLSDRASEIlidRQNQRELLARRGAqlNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYL 405
Cdd:COG0028 323 VLAALLEALEPrADDRAAWLARI---AAWRAEYLAAYAA--DDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 406 YSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNMVAIQEE 485
Cdd:COG0028 398 RFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495122918 486 KKYQ-RLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNP 547
Cdd:COG0028 478 LFYGgRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENP 540
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
13-546 |
2.33e-151 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 445.43 E-value: 2.33e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGG--AVKRADKARqvHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQD 170
Cdd:PRK08322 83 AYAQLGGMPMVAITGqkPIKRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQPAQGNILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAVNQ 250
Cdd:PRK08322 161 IAAEETDGKPLPRSYSRRPYASPKA-IERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 251 EHfTRFAGRVGLfnnQAGD---RLLHLADLIICIGYSPVEYEPAMWN-CGNATLVHIDVLPAYEESHYAPEIELVGDIAG 326
Cdd:PRK08322 240 TH-PLSLGTAGL---SQGDyvhCAIEHADLIINVGHDVIEKPPFFMNpNGDKKVIHINFLPAEVDPVYFPQVEVVGDIAN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 327 TLEKLAGRI-EQPLVLSDRASEIlidRQNQRELLARrGAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYL 405
Cdd:PRK08322 316 SLWQLKERLaDQPHWDFPRFLKI---REAIEAHLEE-GADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFARNY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 406 YSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNMVAIQEE 485
Cdd:PRK08322 392 RAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQE 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495122918 486 KKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDN 546
Cdd:PRK08322 472 NMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSEN 532
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
13-550 |
3.86e-91 |
|
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: 290.47 E-value: 3.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL-LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALyNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPAQGNI-----LPaGNAPKLGPAPdACIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAG 246
Cdd:TIGR00118 163 TTAEIEYPYpekvnLP-GYRPTVKGHP-LQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGyspVEYEPAMWN-----CGNATLVHIDVLPAYEESHYAPEIELV 321
Cdd:TIGR00118 241 SFPEDH-PLSLGMLGMHGTKTANLAVHECDLIIAVG---ARFDDRVTGnlakfAPNAKIIHIDIDPAEIGKNVRVDIPIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 322 GDIAGTLEKLAGRIEQPLVLSDRASEILIDRQNQRELLArrgAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWI 401
Cdd:TIGR00118 317 GDARNVLEELLKKLFELKERKESAWLEQINKWKKEYPLK---MDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 402 ARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIwVDNAY-NMV 480
Cdd:TIGR00118 394 AQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILI-LNNRYlGMV 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495122918 481 AIQEEKKY-QRLSGVSFGPV-DFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNPLLM 550
Cdd:TIGR00118 473 RQWQELFYeERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPM 544
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
373-549 |
3.26e-84 |
|
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: 259.53 E-value: 3.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 373 PLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQ 452
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 453 SSMELETAVRLKANVLHIIWVDNAYNMVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVD 532
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|....*..
gi 495122918 533 GPAVVAIPVDYSDNPLL 549
Cdd:cd02010 161 GVHVIDCPVDYSENIRL 177
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
13-542 |
4.60e-76 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 251.60 E-value: 4.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDIV 172
Cdd:PRK06276 83 ATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 173 DQ-------PAQGNILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAA 245
Cdd:PRK06276 163 EGeldlekyPIPAKIDLPGYKPTTFGHPLQ-IKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 246 GAVNQEHFTRFaGRVGLFNNQAGDRLLHLADLIICIG--YS------PVEYEPamwncgNATLVHIDVLPAYEESHYAPE 317
Cdd:PRK06276 242 GAFPEDHPLAL-GMVGMHGTKAANYSVTESDVLIAIGcrFSdrttgdISSFAP------NAKIIHIDIDPAEIGKNVRVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 318 IELVGDIAGTLEKL-AGRIEQPLVLSDRASEILIDRQNqrELLARrgAQLNQFALHPLRIVRAMQDIINN-----DVTLT 391
Cdd:PRK06276 315 VPIVGDAKNVLRDLlAELMKKEIKNKSEWLERVKKLKK--ESIPR--MDFDDKPIKPQRVIKELMEVLREidpskNTIIT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 392 VDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHII 471
Cdd:PRK06276 391 TDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICI 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495122918 472 WVDNAYNMVAIQEEKKY-QRLSGVSFGPV-DFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:PRK06276 471 FDNRTLGMVYQWQNLYYgKRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIID 543
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-542 |
8.13e-74 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 245.17 E-value: 8.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 1 MDNENRMRqwaHGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDS-SIQIIPVRHEANAAFMAAAVGRITGKAGVALV 79
Cdd:PRK08199 1 MTSTPRAR---TGGQILVDALRANGVERVFCVPGESYLAVLDALHDEtDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 80 TSGPGCSNLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGR 159
Cdd:PRK08199 78 TRGPGATNASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 160 PGSAFVSLPQDIVDQPAQGNILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVT 239
Cdd:PRK08199 158 PGPVVLALPEDVLSETAEVPDAPPYRRVAAAPGAAD-LARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 240 STYQAAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG----------YSPVEY-EPAmwncgnATLVHIDvlPA 308
Cdd:PRK08199 237 CAFRRQDLFDNRH-PNYAGDLGLGINPALAARIREADLVLAVGtrlgevttqgYTLLDIpVPR------QTLVHVH--PD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 309 YEE--SHYAPEIELVGDIAGTLEKLAGRIEQPLVLSDRASEilidrQNQRELLARRGAQLNQFALHPLRIVRAMQDIINN 386
Cdd:PRK08199 308 AEElgRVYRPDLAIVADPAAFAAALAALEPPASPAWAEWTA-----AAHADYLAWSAPLPGPGAVQLGEVMAWLRERLPA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 387 DVTLTVDMGSFHIWIARYlYSFR--ARQVMISNGqqTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLK 464
Cdd:PRK08199 383 DAIITNGAGNYATWLHRF-FRFRryRTQLAPTSG--SMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 465 ANVLhIIWVDNA-YNMVAIQEEKKY-QRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:PRK08199 460 LPII-VIVVNNGmYGTIRMHQEREYpGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
13-550 |
1.13e-70 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 236.91 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDS-SIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQStQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPAQGNILPAGNAPKLGPAPDA-CIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAVNQ 250
Cdd:PRK08155 175 QTAVIELEALPAPAEKDAAPAFDEeSIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGMLPK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 251 EHFTRFaGRVGLFNNQAGDRLLHLADLIICIG--YSPVEYEPAMWNCGNATLVHIDVLPAYEESHYAPEIELVGDIAGTL 328
Cdd:PRK08155 255 AHPLSL-GMLGMHGARSTNYILQEADLLIVLGarFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 329 EKLAGRIEQPlvlsdraseiliDRQNQRELLA--RRGAQLNQFALH----PLRIVRAMQDIINNDVTLTVDMGSFHIWIA 402
Cdd:PRK08155 334 AQLLPLVEAQ------------PRAEWHQLVAdlQREFPCPIPKADdplsHYGLINAVAACVDDNAIITTDVGQHQMWTA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 403 RyLYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNMVA 481
Cdd:PRK08155 402 Q-AYPLnRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVH 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495122918 482 IQEEKKY-QRLSGVSF-GPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNPLLM 550
Cdd:PRK08155 481 QQQSLFYgQRVFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPM 551
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
6-559 |
1.18e-68 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 231.59 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 6 RMRqwahGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGC 85
Cdd:PRK06048 7 KMT----GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 86 SNLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFV 165
Cdd:PRK06048 83 TNLVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 166 SLPQDIV------DQPAQGNIlpAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVT 239
Cdd:PRK06048 163 DLPKDVTtaeidfDYPDKVEL--RGYKPTYKGNPQQ-IKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 240 STYQAAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGY--------SPVEYEPamwncgNATLVHIDVLPAYEE 311
Cdd:PRK06048 240 TTLMGIGAIPTEH-PLSLGMLGMHGTKYANYAIQESDLIIAVGArfddrvtgKLASFAP------NAKIIHIDIDPAEIS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 312 SHYAPEIELVGDIAGTLEKLAGRIEQplvlsdRASEILIDRQNQ--REL----LARRGAQLNQFALHplRIVRAMQDIIn 385
Cdd:PRK06048 313 KNVKVDVPIVGDAKQVLKSLIKYVQY------CDRKEWLDKINQwkKEYplkyKEREDVIKPQYVIE--QIYELCPDAI- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 386 ndvtLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKA 465
Cdd:PRK06048 384 ----IVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 466 NVLHIIwVDNAY-NMVAIQEEKKY-QRLSGVSFGP-VDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:PRK06048 460 PVIVAI-LNNGYlGMVRQWQELFYdKRYSHTCIKGsVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVE 538
|
570
....*....|....*....
gi 495122918 543 YSDN--PLLMGQLHLSQIL 559
Cdd:PRK06048 539 CEENvsPMVPAGAAINEIL 557
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
13-548 |
7.02e-66 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 224.49 E-value: 7.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL--LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLIT 90
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 91 GMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAeHGRPGSAFVSLPQD 170
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTA-YEKKGVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQPAQ-GNILPAGNAPKLGPAPD-ACIDHVAGLIRNAKNPVILLGLMASqpENSRALHRLLEKSHIPVTSTYQAAGAV 248
Cdd:PRK08611 165 LPAQKIKdTTNKTVDTFRPTVPSPKpKDIKKAAKLINKAKKPVILAGLGAK--HAKEELLAFAEKAKIPIIHTLPAKGII 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 249 NQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG--YSPVEYEPAmwncgNATLVHIDVLPAYEESHYAPEIELVGDIAG 326
Cdd:PRK08611 243 PDDH-PYSLGNLGKIGTKPAYEAMQEADLLIMVGtnYPYVDYLPK-----KAKAIQIDTDPANIGKRYPVNVGLVGDAKK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 327 TLEKLAGRIEqpLVLSDRASEILIDR-QNQRELLARRgAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYL 405
Cdd:PRK08611 317 ALHQLTENIK--HVEDRRFLEACQENmAKWWKWMEED-ENNASTPIKPERVMAAIQKIADDDAVLSVDVGTVTVWSARYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 406 YSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVlhIIWVDNAYNMVAIQEE 485
Cdd:PRK08611 394 NLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPI--VVVVLNNQQLAFIKYE 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495122918 486 kkyQRLSG-----VSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNPL 548
Cdd:PRK08611 472 ---QQAAGeleyaIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNAAPL 536
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
7-545 |
4.37e-64 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 218.82 E-value: 4.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 7 MRQWAHGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCS 86
Cdd:PRK05858 1 PAQTGHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 87 NLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVS 166
Cdd:PRK05858 81 NGMSAMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 167 LPQDIVDQPAQGNILPAG--NAPK-LGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQ 243
Cdd:PRK05858 161 FPMDHAFSMADDDGRPGAltELPAgPTPDPDA-LARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 244 AAGAVNQEH---FTRFAGRVglfnnqagdrlLHLADLIICIGySPVEYEPAM-WNCGNATLVHIDVLPAYEESHYAPEIE 319
Cdd:PRK05858 240 GRGVVPADHplaFSRARGKA-----------LGEADVVLVVG-VPMDFRLGFgVFGGTAQLVHVDDAPPQRAHHRPVAAG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 320 LVGDIAGTLEKLAGRIEQPlvlSDRASEILIDRQNQRELLARRGAQLNQFA--LHPLRIVRAMQDIINNDVTLTVDMGSF 397
Cdd:PRK05858 308 LYGDLSAILSALAGAGGDR---TDHQGWIEELRTAETAARARDAAELADDRdpIHPMRVYGELAPLLDRDAIVIGDGGDF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 398 HIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHI-----IW 472
Cdd:PRK05858 385 VSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVignngIW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 473 --------VDNAYNMVA-IQEEKKYQRLSGVSFGPVDFkvyaeafgaagfaVESAEALEPTLRAAMDVDGPAVVAIPVDY 543
Cdd:PRK05858 465 glekhpmeALYGYDVAAdLRPGTRYDEVVRALGGHGEL-------------VTVPAELGPALERAFASGVPYLVNVLTDP 531
|
..
gi 495122918 544 SD 545
Cdd:PRK05858 532 SV 533
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
13-550 |
5.80e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 218.82 E-value: 5.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLL-DSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYkQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK08527 85 LATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPAQGNI-----LPA------GNAPKLGPAPDAcidhvaglIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTS 240
Cdd:PRK08527 165 TATLGEFEYpkeisLKTykptykGNSRQIKKAAEA--------IKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 241 TYQAAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGyspveyepAMWN----------CGNATLVHIDVLPAYE 310
Cdd:PRK08527 237 TLMARGVLRSDD-PLLLGMLGMHGSYAANMAMSECDLLISLG--------ARFDdrvtgklsefAKHAKIIHVDIDPSSI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 311 ESHYAPEIELVGDIAGTLEKLAGRIEqplvlsdraSEILIDRQNQRELLARRGaqlnqfALHPLR------------IVR 378
Cdd:PRK08527 308 SKIVNADYPIVGDLKNVLKEMLEELK---------EENPTTYKEWREILKRYN------ELHPLSyedsdevlkpqwVIE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 379 AMQDIINNDVTLTVDMGSFHIWIARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMEL 457
Cdd:PRK08527 373 RVGELLGDDAIISTDVGQHQMWVAQF-YPFnYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQEL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 458 ETAVRLKANVLHIIWVDNAYNMVAIQEEKKY-QRLSG--VSFGPvDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGP 534
Cdd:PRK08527 452 MTAVEYKIPVINIILNNNFLGMVRQWQTFFYeERYSEtdLSTQP-DFVKLAESFGGIGFRVTTKEEFDKALKEALESDKV 530
|
570
....*....|....*.
gi 495122918 535 AVVAIPVDYSDNPLLM 550
Cdd:PRK08527 531 ALIDVKIDRFENVLPM 546
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
13-541 |
7.00e-64 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 218.34 E-value: 7.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSS--IQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLIT 90
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 91 GMATANSEGDPVVALGGAVKRA--DKAR-QVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSL 167
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGQIPSAliGKGRgHLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 168 PQDIVDQPAQGNILPAGN-APKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASqpENSRALHRLLEKSHIPVTSTYQAAG 246
Cdd:PRK08266 166 PWDVFGQRAPVAAAPPLRpAPPPAPDPDA-IAAAAALIAAAKNPMIFVGGGAA--GAGEEIRELAEMLQAPVVAFRSGRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AVNQEHFTRFagrvglfNNQAGDRLLHLADLIICIGySPVEyEPAM---WNCGNATLVHIDVLPAyEESHYAPEIELVGD 323
Cdd:PRK08266 243 IVSDRHPLGL-------NFAAAYELWPQTDVVIGIG-SRLE-LPTFrwpWRPDGLKVIRIDIDPT-EMRRLKPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 324 IAGTLEKLAGRIEQPL-VLSDRASEIlidrqnqRELLARRGAQLnqFALHP----LRIVRAM---QDIINNDVTltvDMG 395
Cdd:PRK08266 313 AKAGTAALLDALSKAGsKRPSRRAEL-------RELKAAARQRI--QAVQPqasyLRAIREAlpdDGIFVDELS---QVG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 396 sFHIWIARYLYSfrARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDN 475
Cdd:PRK08266 381 -FASWFAFPVYA--PRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNN 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495122918 476 AY-NMVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPV 541
Cdd:PRK08266 458 AYgNVRRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
13-550 |
1.99e-61 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 212.52 E-value: 1.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDIV 172
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 173 DQPAQGNILPAGNAP--KLGPAPDAC-IDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAVN 249
Cdd:PRK06725 177 NEKVTSFYNEVVEIPgyKPEPRPDSMkLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGAYP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 250 QEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG-------------YSPveyepamwncgNATLVHIDVLPAYEESHYAP 316
Cdd:PRK06725 257 PGD-PLFLGMLGMHGTYAANMAVTECDLLLALGvrfddrvtgklelFSP-----------HSKKVHIDIDPSEFHKNVAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 317 EIELVGDIAGTLEKLAgrieqPLVLSDRASEILIDRQNQRELLArRGAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGS 396
Cdd:PRK06725 325 EYPVVGDVKKALHMLL-----HMSIHTQTDEWLQKVKTWKEEYP-LSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 397 FHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNA 476
Cdd:PRK06725 399 HQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKF 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495122918 477 YNMVAIQEEKKYQ-RLSGVSFGPVDF-KVYAEAFGAAGFAVESAEALEpTLRAAMDVDGPAVVAIPVDYSDNPLLM 550
Cdd:PRK06725 479 LGMVRQWQEMFYEnRLSESKIGSPDFvKVAEAYGVKGLRATNSTEAKQ-VMLEAFAHEGPVVVDFCVEEGENVFPM 553
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
13-475 |
2.37e-61 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 211.66 E-value: 2.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDIv 172
Cdd:PRK08978 83 ADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKDI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 173 dQPAQGNILPAGNAPKLGPAPDAC-IDHVAGLIRNAKNPVILLG---LMASQPEnsrALHRLLEKSHIPVTSTYQAAGAV 248
Cdd:PRK08978 162 -QLAEGELEPHLTTVENEPAFPAAeLEQARALLAQAKKPVLYVGggvGMAGAVP---ALREFLAATGMPAVATLKGLGAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 249 NQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG-------------YSPveyepamwncgNATLVHIDVLPAYEESHYA 315
Cdd:PRK08978 238 EADH-PYYLGMLGMHGTKAANLAVQECDLLIAVGarfddrvtgklntFAP-----------HAKVIHLDIDPAEINKLRQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 316 PEIELVGDIAGTLEKLagriEQPLvlsdraseiliDRQNQRELLARRGAQlNQF-------ALHPLRIVRAMQDIINNDV 388
Cdd:PRK08978 306 AHVALQGDLNALLPAL----QQPL-----------NIDAWRQHCAQLRAE-HAWrydhpgeAIYAPALLKQLSDRKPADT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 389 TLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVl 468
Cdd:PRK08978 370 VVTTDVGQHQMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPV- 448
|
....*..
gi 495122918 469 HIIWVDN 475
Cdd:PRK08978 449 KIVLLDN 455
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
13-457 |
3.02e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 208.91 E-value: 3.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLD-SSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK07282 12 GSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNfEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK07282 92 IADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPAQGNILPAGNAPKLGPAPDACIDHVAGLIRN---AKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAV 248
Cdd:PRK07282 172 SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQlskAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 249 NQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGY--------SPVEYEPamwncgNATLVHIDVLPAYEESHYAPEIEL 320
Cdd:PRK07282 252 ATSH-PLFLGMGGMHGSYAANIAMTEADFMINIGSrfddrltgNPKTFAK------NAKVAHIDIDPAEIGKIIKTDIPV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 321 VGDIAGTLEKLagrIEQPLVLSDRASEILIDRQNQRELlarRGAQLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIW 400
Cdd:PRK07282 325 VGDAKKALQML---LAEPTVHNNTEKWIEKVTKDKNRV---RSYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 495122918 401 IARYlYSFR-ARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMEL 457
Cdd:PRK07282 399 AAQY-YPYQnERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQEL 455
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
13-542 |
7.34e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 208.15 E-value: 7.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLD----SSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNL 88
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAFVEdlanGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 89 ITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLP 168
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 169 QDIVDQPAQGNILPAGNAPKLGPAPDACIDHV-----AGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQ 243
Cdd:PRK06456 164 RDIFYEKMEEIKWPEKPLVKGYRDFPTRIDRLalkkaAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 244 AAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGYSPVEYEPAMWNCGNAT---LVHIDVLPAYEESHYAPEIEL 320
Cdd:PRK06456 244 GKTAIPHDH-PLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrkkFIMVNIDPTDGEKAIKVDVGI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 321 VGDIAGTLEKLAGRIEQplvlsdraseilIDRQNQRELLARRGAQLNQF-----------ALHPLRIVRAMQDIINNDVT 389
Cdd:PRK06456 323 YGNAKIILRELIKAITE------------LGQKRDRSAWLKRVKEYKEYysqfyyteengKLKPWKIMKTIRQALPRDAI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 390 LTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLH 469
Cdd:PRK06456 391 VTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVIS 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495122918 470 IIWVDNAYNMV-AIQEEKKYQRLSGVSFGPV-DFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:PRK06456 471 VIFDNRTLGLVrQVQDLFFGKRIVGVDYGPSpDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVD 545
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
2-546 |
2.64e-58 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 204.90 E-value: 2.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 2 DNENRMRQWAHGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLL----DSSIQIIPVRHEANAAFMAAAVGRITGKAGVA 77
Cdd:PRK07418 10 DSTTVTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYARATGKVGVC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 78 LVTSGPGCSNLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEH 157
Cdd:PRK07418 90 FGTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 158 GRPGSAFVSLPQDIVD-----QPAQ-GNILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLL 231
Cdd:PRK07418 170 GRPGPVLIDIPKDVGQeefdyVPVEpGSVKPPGYRPTVKGNPRQ-INAALKLIEEAERPLLYVGGGAISAGAHAELKELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 232 EKSHIPVTSTYQAAGAVNqEHFTRFAGRVGLFNNQAGDRLLHLADLIICIG-------------YSPveyepamwncgNA 298
Cdd:PRK07418 249 ERFQIPVTTTLMGKGAFD-EHHPLSVGMLGMHGTAYANFAVTECDLLIAVGarfddrvtgkldeFAS-----------RA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 299 TLVHIDVLPAYEESHYAPEIELVGDIAGTLEKLAGRIEQPLVlSDRASEIL--IDRQNQRellarrgaqlnqfalHPLRI 376
Cdd:PRK07418 317 KVIHIDIDPAEVGKNRRPDVPIVGDVRKVLVKLLERSLEPTT-PPRTQAWLerINRWKQD---------------YPLVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 377 VRAMQDIINNDVTL-----------TVDMGSFHIWIARYLYSfRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVS 445
Cdd:PRK07418 381 PPYEGEIYPQEVLLavrdlapdayyTTDVGQHQMWAAQFLRN-GPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 446 GDGGFLQSSMELETAVRLKANVLHIIwVDNAYN-MVAIQEEKKY-QRLSG--VSFGPVDFKVYAEAFGAAGFAVESAEAL 521
Cdd:PRK07418 460 GDASFLMNIQELGTLAQYGINVKTVI-INNGWQgMVRQWQESFYgERYSAsnMEPGMPDFVKLAEAFGVKGMVISERDQL 538
|
570 580
....*....|....*....|....*
gi 495122918 522 EPTLRAAMDVDGPAVVAIPVDYSDN 546
Cdd:PRK07418 539 KDAIAEALAHDGPVLIDVHVRRDEN 563
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-480 |
1.48e-57 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 202.24 E-value: 1.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 1 MDNENRMRQWAHGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLL-DSSIQIIPVRHEANAAFMAAAVGRITGKAGVALV 79
Cdd:PRK09107 1 SAQKSHMPRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 80 TSGPGCSNLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGR 159
Cdd:PRK09107 81 TSGPGATNAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 160 PGSAFVSLPQDIvdQPAQGNILPAGNA-------PKLGPAPDAcIDHVAGLIRNAKNPVILL--GLMASQPENSRALHRL 230
Cdd:PRK09107 161 PGPVVVDIPKDV--QFATGTYTPPQKApvhvsyqPKVKGDAEA-ITEAVELLANAKRPVIYSggGVINSGPEASRLLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 231 LEKSHIPVTSTYQAAGA--VNQEHFTRFAGRVGLFN-NQAgdrlLHLADLIICIG-------------YSPveyepamwn 294
Cdd:PRK09107 238 VELTGFPITSTLMGLGAypASGKNWLGMLGMHGTYEaNMA----MHDCDVMLCVGarfddritgrldaFSP--------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 295 cgNATLVHIDVLPAYEESHYAPEIELVGDIAGTLE------KLAGRIEQPLVLSDRASEilIDRQNQRELLARRGAQ--- 365
Cdd:PRK09107 305 --NSKKIHIDIDPSSINKNVRVDVPIIGDVGHVLEdmlrlwKARGKKPDKEALADWWGQ--IARWRARNSLAYTPSDdvi 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 366 LNQFALHplRIVRAMQDiinNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVS 445
Cdd:PRK09107 381 MPQYAIQ--RLYELTKG---RDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIA 455
|
490 500 510
....*....|....*....|....*....|....*.
gi 495122918 446 GDGGFLQSSMELETAVRLKANVlHIIWVDNAY-NMV 480
Cdd:PRK09107 456 GDASIQMCIQEMSTAVQYNLPV-KIFILNNQYmGMV 490
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
13-547 |
2.74e-57 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 201.53 E-value: 2.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFG--IPGAkidkVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLIT 90
Cdd:PRK06112 16 VAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 91 GMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQD 170
Cdd:PRK06112 92 PLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLPAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQPAQGNILPAGNApkLGPAP-------DACIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQ 243
Cdd:PRK06112 172 LLTAAAAAPAAPRSNS--LGHFPldrtvpaPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 244 AAGAVNQEHftrfAGRVGLFNNQAGDRLL--HL------ADLIICIGYSPVEYEPAMWNC--GNATLVHIDVLPAYEESH 313
Cdd:PRK06112 250 GKGAVDETH----PLSLGVVGSLMGPRSPgrHLrdlvreADVVLLVGTRTNQNGTDSWSLypEQAQYIHIDVDGEEVGRN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 314 YApEIELVGDIAGTLEKL---AGRIEQPLVLSDRAS-EILIDRQNQRELLARRGAQLNQFA-LHPLRIVRAMQDIINNDV 388
Cdd:PRK06112 326 YE-ALRLVGDARLTLAALtdaLRGRDLAARAGRRAAlEPAIAAGREAHREDSAPVALSDASpIRPERIMAELQAVLTGDT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 389 TLTVDMGSFHIWIARYLYSFRARQVMIS-NGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANV 467
Cdd:PRK06112 405 IVVADASYSSIWVANFLTARRAGMRFLTpRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 468 LhIIWVDNAynMVAIQ---EEKKY-QRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDY 543
Cdd:PRK06112 485 T-IVVLNNG--ILGFQkhaETVKFgTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDP 561
|
....
gi 495122918 544 SDNP 547
Cdd:PRK06112 562 SAFP 565
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
9-550 |
1.04e-56 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 199.60 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 9 QWAHGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNL 88
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 89 ITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLP 168
Cdd:PRK07710 94 VTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 169 QDIV--------DQPAQgniLPaGNAPKLGPApDACIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTS 240
Cdd:PRK07710 174 KDMVveegefcyDVQMD---LP-GYQPNYEPN-LLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 241 TYQAAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG-------------YSPveyepamwncgNATLVHIDVLP 307
Cdd:PRK07710 249 TLLGLGGFPADH-PLFLGMAGMHGTYTANMALYECDLLINIGarfddrvtgnlayFAK-----------EATVAHIDIDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 308 AYEESHYAPEIELVGDIAGTLEKLAGRIEQPlVLSDRASEILIDRQNQRELLARRGAQlnqfALHPLRIVRAMQDIINND 387
Cdd:PRK07710 317 AEIGKNVPTEIPIVADAKQALQVLLQQEGKK-ENHHEWLSLLKNWKEKYPLSYKRNSE----SIKPQKAIEMLYEITKGE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 388 VTLTVDMGSFHIWIARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKAN 466
Cdd:PRK07710 392 AIVTTDVGQHQMWAAQY-YPFkTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 467 VLHIIWVDNAYNMVAIQEEKKYQRLSGVSFGPV--DFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYS 544
Cdd:PRK07710 471 VKVVILNNEALGMVRQWQEEFYNQRYSHSLLSCqpDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQS 550
|
....*.
gi 495122918 545 DNPLLM 550
Cdd:PRK07710 551 EKVMPM 556
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
13-557 |
3.31e-56 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 198.12 E-value: 3.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL-LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALhEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDqPAQGNILPAGNAPKLGPAPDACIDHvAGLIR-------NAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQA 244
Cdd:PRK08979 166 LN-PAILHPYEYPESIKMRSYNPTTSGH-KGQIKrglqallAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 245 AGAVNQEHFTRFaGRVGLFNNQAGDRLLHLADLIICIGyspVEYEPAMWN-----CGNATLVHIDVLPAYEESHYAPEIE 319
Cdd:PRK08979 244 LGAFPGTHKNSL-GMLGMHGRYEANMAMHNADLIFGIG---VRFDDRTTNnlekyCPNATILHIDIDPSSISKTVRVDIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 320 LVGDIAGTLEKLAGRIEQPLVLSDRA------SEILIDRqnQRELLARrgaQLNQFALHPLRIVRAMQDIINNDVTLTVD 393
Cdd:PRK08979 320 IVGSADKVLDSMLALLDESGETNDEAaiaswwNEIEVWR--SRNCLAY---DKSSERIKPQQVIETLYKLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 394 MGSFHIWIARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVlHIIW 472
Cdd:PRK08979 395 VGQHQMFAALY-YPFdKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPV-KIIN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 473 VDNAY-NMVAIQEEKKYQ-RLSGVSFGPV-DFKVYAEAFGAAGFAVESAEALEPTLRAAMDV-DGPAVVAIPVDYSDN-- 546
Cdd:PRK08979 473 LNNRFlGMVKQWQDMIYQgRHSHSYMDSVpDFAKIAEAYGHVGIRISDPDELESGLEKALAMkDRLVFVDINVDETEHvy 552
|
570
....*....|....*.
gi 495122918 547 PLL-----MGQLHLSQ 557
Cdd:PRK08979 553 PMQirggaMNEMWLSK 568
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
18-543 |
1.67e-55 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 195.58 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 18 VGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANS 97
Cdd:PRK07524 9 VRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMGQAYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 98 EGDPVVALGGAVKRADKAR---QVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDIVDQ 174
Cdd:PRK07524 89 DSIPMLVISSVNRRASLGKgrgKLHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLDVLAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 175 PAQGNILPAGNAPKLGPAPDACIDHVAGLIRNAKNPVILLGLMASQPENsrALHRLLEKSHIPVTSTYQAAGAVNQEHFT 254
Cdd:PRK07524 169 PADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAA--ALRALAERLDAPVALTINAKGLLPAGHPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 255 RFAGRVGLfnnQAGDRLLHLADLIICIG--YSPVEYEpAMWNCG---NATLVHIDVLPAYEESHYAPEIELVGDIAGTLE 329
Cdd:PRK07524 247 LLGASQSL---PAVRALIAEADVVLAVGteLGETDYD-VYFDGGfplPGELIRIDIDPDQLARNYPPALALVGDARAALE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 330 KLAGRIEQPLVLSDRASEiLIDRQNQRELLARRGAQLNQFALHPlRIVRAMQD-IINNDVTLTVDMGSFHIWIARYLYSF 408
Cdd:PRK07524 323 ALLARLPGQAAAADWGAA-RVAALRQALRAEWDPLTAAQVALLD-TILAALPDaIFVGDSTQPVYAGNLYFDADAPRRWF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 409 RArqvmiSNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYnmvaiQEEKKY 488
Cdd:PRK07524 401 NA-----STGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGY-----GEIRRY 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 489 QR-----LSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDY 543
Cdd:PRK07524 471 MVardiePVGVDPYTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
13-480 |
4.80e-55 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 195.35 E-value: 4.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLL-DSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK06466 86 IATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDqPAQGNILPAGNAPKLGPAPDACIDHvAGLIRN-------AKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQA 244
Cdd:PRK06466 166 TN-PAEKFEYEYPKKVKLRSYSPAVRGH-SGQIRKavemllaAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 245 AGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGY---SPVEYEPAMWnCGNATLVHIDVLPAYEESHYAPEIELV 321
Cdd:PRK06466 244 LGGFPGTD-RQFLGMLGMHGTYEANMAMHHADVILAVGArfdDRVTNGPAKF-CPNAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 322 GDIAGTLEKLAGRIEQplvlsdraseilIDRQNQRELLARRGAQLNQF---------------ALHPLRIVRAMQDIINN 386
Cdd:PRK06466 322 GPVESVLTEMLAILKE------------IGEKPDKEALAAWWKQIDEWrgrhglfpydkgdggIIKPQQVVETLYEVTNG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 387 DVTLTVDMGSFHIWIARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKA 465
Cdd:PRK06466 390 DAYVTSDVGQHQMFAAQY-YKFnKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGL 468
|
490
....*....|....*.
gi 495122918 466 NVlHIIWVDN-AYNMV 480
Cdd:PRK06466 469 PV-KIINLNNgALGMV 483
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
13-477 |
6.63e-55 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 194.68 E-value: 6.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLD-SSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDqpaqgnilPAGNAPKLGPapdaciDHVA------------GLIR-------NAKNPVILLGLMASQPENSRALHRLLE 232
Cdd:PRK07979 166 LN--------PANKLPYVWP------ESVSmrsynpttqghkGQIKralqtlvAAKKPVVYVGGGAINAACHQQLKELVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 233 KSHIPVTSTYQAAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGyspVEYEPAMWN-----CGNATLVHIDVLP 307
Cdd:PRK07979 232 KLNLPVVSSLMGLGAFPATH-RQSLGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNnlakyCPNATVLHIDIDP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 308 AYEESHYAPEIELVGDIAGTLEKLAGRIEQPLVLSD----RASEILIDRQNQRELLarrGAQLNQFALHPLRIVRAMQDI 383
Cdd:PRK07979 308 TSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPldeiRDWWQQIEQWRARQCL---KYDTHSEKIKPQAVIETLWRL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 384 INNDVTLTVDMGSFHIWIARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVR 462
Cdd:PRK07979 385 TKGDAYVTSDVGQHQMFAALY-YPFdKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQ 463
|
490
....*....|....*
gi 495122918 463 LKANVLhIIWVDNAY 477
Cdd:PRK07979 464 YELPVL-VLNLNNRY 477
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
13-546 |
1.68e-54 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 193.59 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLD-SSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDqpaqgnilPAGNAPKLGP------APDACIDHVAGLIRN-------AKNPVILLGLMASQPENSRALHRLLEKSHIPV 238
Cdd:PRK06882 166 VN--------PANKFTYEYPeevslrSYNPTVQGHKGQIKKalkallvAKKPVLFVGGGVITAECSEQLTQFAQKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 239 TSTYQAAGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGyspVEYEPAMWN-----CGNATLVHIDVLPAYEESH 313
Cdd:PRK06882 238 TSSLMGLGAYPSTD-KQFLGMLGMHGTYEANNAMHESDLILGIG---VRFDDRTTNnlakyCPNAKVIHIDIDPTSISKN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 314 YAPEIELVGDIAGTLEKLAGRIEQPlVLSDRASEILIDRQNQRELLARRGAQLNQF--ALHPLRIVRAMQDIINNDVTLT 391
Cdd:PRK06882 314 VPAYIPIVGSAKNVLEEFLSLLEEE-NLAKSQTDLTAWWQQINEWKAKKCLEFDRTsdVIKPQQVVEAIYRLTNGDAYVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 392 VDMGSFHIWIARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLhI 470
Cdd:PRK06882 393 SDVGQHQMFAALH-YPFdKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVV-I 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 471 IWVDNAY-NMVAIQEEKKYQ-RLSGVSFGPV-DFKVYAEAFGAAGFAVESAEALEPTLRAAMDV-DGPAVVAIPVDYSDN 546
Cdd:PRK06882 471 VSLNNRFlGMVKQWQDLIYSgRHSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIkDKLVFVDVNVDETEH 550
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
25-546 |
2.56e-52 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 187.98 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 25 GVKQVFGIPGAKIDKVFDSLL----DSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGD 100
Cdd:CHL00099 24 GVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 101 PVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI------VDQ 174
Cdd:CHL00099 104 PLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVglekfdYYP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 175 PAQGN--ILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAVNQEH 252
Cdd:CHL00099 184 PEPGNtiIKILGCRPIYKPTIKR-IEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIFDEDH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 253 ftRFA-GRVGLFNNQAGDRLLHLADLIICIGY---SPVEYEPAMWNCgNATLVHIDVLPAYEESHYAPEIELVGDIAGTL 328
Cdd:CHL00099 263 --PLClGMLGMHGTAYANFAVSECDLLIALGArfdDRVTGKLDEFAC-NAQVIHIDIDPAEIGKNRIPQVAIVGDVKKVL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 329 EKLagrieqpLVLSDRASEILIDRQNQ--RELLARRGAQlnqfalHPLRIVR-----AMQDIINN------DVTLTVDMG 395
Cdd:CHL00099 340 QEL-------LELLKNSPNLLESEQTQawRERINRWRKE------YPLLIPKpstslSPQEVINEisqlapDAYFTTDVG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 396 SFHIWIARYLySFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVlHIIWVDN 475
Cdd:CHL00099 407 QHQMWAAQFL-KCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPI-KIIIINN 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495122918 476 AYN-MVAIQEEKKY-QRL--SGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDN 546
Cdd:CHL00099 485 KWQgMVRQWQQAFYgERYshSNMEEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDEN 559
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
13-529 |
5.41e-50 |
|
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: 181.19 E-value: 5.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDS--SIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLIT 90
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAErdRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 91 GMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAeHGRPGSAFVSLPQD 170
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRA-YAHNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQPAQGNILPAGNAPK---LGPAPDA-CIDHVAGLIRNAKNPVILLGLMASQPenSRALHRLLEKSHIPVTSTYQAAG 246
Cdd:TIGR02720 160 FGWQEIPDNDYYASSVSYqtpLLPAPDVeAVTRAVQTLKAAERPVIYYGIGARKA--GEELEALSEKLKIPLISTGLAKG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AV--NQEHFTRFAGRVGlfnNQAGDRLLHLADLIICIGySPVEYEPAMWNCGNAT-LVHIDVLPAYEESHYAPEIELVGD 323
Cdd:TIGR02720 238 IIedRYPAYLGSAYRVA---QKPANEALFQADLVLFVG-NNYPFAEVSKAFKNTKyFIQIDIDPAKLGKRHHTDIAVLAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 324 ----IAGTLEKLAGRIEQPLVLSDRAseiliDRQNQRELLARrgaqLNQFALHPLR---IVRAMQDIINNDVTLTVDMGS 396
Cdd:TIGR02720 314 akkaLAAILAQVEPRESTPWWQANVA-----NVKNWRAYLAS----LEDKTEGPLQayqVYRAINKIAEDDAIYSIDVGD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 397 FHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNA 476
Cdd:TIGR02720 385 ININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCT 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 495122918 477 YNMVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAM 529
Cdd:TIGR02720 465 YGFIKDEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAK 517
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
13-528 |
4.99e-49 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 178.84 E-value: 4.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLL-DSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPA-----QGNILPAGNAPKLGPAPDacIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAG 246
Cdd:PRK06965 183 SKTPCeyeypKSVEMRSYNPVTKGHSGQ--IRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIGY---SPVEYEPAMWNCGNATLVHIDVLPAYEESHYAPEIELVGD 323
Cdd:PRK06965 261 AYPASD-KKFLGMLGMHGTYEANMAMQHCDVLIAIGArfdDRVIGNPAHFASRPRKIIHIDIDPSSISKRVKVDIPIVGD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 324 IAGTLEKLAGRIEQPLVLSDRASeiLIDRQNQRELLARRGA---QLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIW 400
Cdd:PRK06965 340 VKEVLKELIEQLQTAEHGPDADA--LAQWWKQIEGWRSRDClkyDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMW 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 401 IARYlYSF-RARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVlHIIWVDNAY-N 478
Cdd:PRK06965 418 AAQF-YRFnEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPV-KIISLNNRYlG 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 495122918 479 MVAIQEEKKYQRLSGVSFGPV--DFKVYAEAFGAAGFAVESAEALEPTLRAA 528
Cdd:PRK06965 496 MVRQWQEIEYSKRYSHSYMDAlpDFVKLAEAYGHVGMRIEKTSDVEPALREA 547
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-488 |
1.67e-48 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 177.24 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSS-IQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 VDQPA-----QGNILPaGNAPKLGPAP-DACIDHVAGLIRNAKNPVILL--GLMASQPEnsraLHRLLEKSHIPVTSTYQ 243
Cdd:PLN02470 175 QQQLAvpnwnQPMKLP-GYLSRLPKPPeKSQLEQIVRLISESKRPVVYVggGCLNSSEE----LREFVELTGIPVASTLM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 244 AAGAVNQE-----HFTRFAGRVglFNNQAGDRllhlADLIICIGyspVEYEPAMWN-----CGNATLVHIDVLPAYEESH 313
Cdd:PLN02470 250 GLGAFPASdelslQMLGMHGTV--YANYAVDS----ADLLLAFG---VRFDDRVTGkleafASRASIVHIDIDPAEIGKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 314 YAPEIELVGDIAGTLEKLAGRIEQPLVLSDRASEILIDRQNQRELLARRGAQLNQfALHPLRIVRAMQDIINNDVTLTVD 393
Cdd:PLN02470 321 KQPHVSVCADVKLALQGLNKLLEERKAKRPDFSAWRAELDEQKEKFPLSYPTFGD-AIPPQYAIQVLDELTDGNAIISTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 394 MGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETaVRLKANVLHIIWV 473
Cdd:PLN02470 400 VGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELAT-IHVENLPVKIMVL 478
|
490
....*....|....*
gi 495122918 474 DNAYNMVAIQEEKKY 488
Cdd:PLN02470 479 NNQHLGMVVQWEDRF 493
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
13-460 |
1.49e-47 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 175.17 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSS-IQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTkVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDI 171
Cdd:PRK07789 113 IADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPKDA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 172 vdQPAQGN-------ILPaGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQA 244
Cdd:PRK07789 193 --LQAQTTfswpprmDLP-GYRPVTKPHGKQ-IREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 245 AGAVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG-------------YSPveyepamwncgNATLVHIDVLPAYEE 311
Cdd:PRK07789 269 RGAFPDSH-PQHLGMPGMHGTVAAVAALQRSDLLIALGarfddrvtgkldsFAP-----------DAKVIHADIDPAEIG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 312 SHYAPEIELVGDIAGTLEKLAGRIEqplvlSDRASEILIDrqnqrelLARRGAQLNQF--------------ALHPLRIV 377
Cdd:PRK07789 337 KNRHADVPIVGDVKEVIAELIAALR-----AEHAAGGKPD-------LTAWWAYLDGWretyplgydepsdgSLAPQYVI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 378 RAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMEL 457
Cdd:PRK07789 405 ERLGEIAGPDAIYVAGVGQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQEL 484
|
...
gi 495122918 458 ETA 460
Cdd:PRK07789 485 ATC 487
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
15-169 |
9.22e-47 |
|
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: 160.78 E-value: 9.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 15 DMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMAT 94
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495122918 95 ANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQ 169
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
13-539 |
4.13e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 164.98 E-value: 4.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPgakIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITG--KAGVALVTSGPGCSNLIT 90
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 91 GMATANSEGDPVVALGGAVKRADKArqVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQD 170
Cdd:PRK06154 99 GVAQAYGDSVPVLFLPTGYPRGSTD--VAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQPAQGniLPAGNAP----KLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAG 246
Cdd:PRK06154 177 VLAEELDE--LPLDHRPsrrsRPGADPVE-VVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AVNQEHFTRFaGRVGLFNNQAGDRLLHLADLIICIGYSPVEYEPAMWNCGNATLVHIDVLPAYEESHYAPEIELVGDIAG 326
Cdd:PRK06154 254 AFPEDHPLAL-GSGGRARPATVAHFLREADVLFGIGCSLTRSYYGLPMPEGKTIIHSTLDDADLNKDYPIDHGLVGDAAL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 327 TL----EKLAGRI-EQPLVLSDRASEIlidRQNQRELLARRGAQL--NQFALHPLRIVRAMQDIIN-NDVTLTVDMGSFH 398
Cdd:PRK06154 333 VLkqmiEELRRRVgPDRGRAQQVAAEI---EAVRAAWLAKWMPKLtsDSTPINPYRVVWELQHAVDiKTVIITHDAGSPR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 399 IWIARYlysFRARQVM--ISNGQQT-MGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDN 475
Cdd:PRK06154 410 DQLSPF---YVASRPGsyLGWGKTTqLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNF 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495122918 476 -----AYNMVAIQEEKKYQRLSGvsfgpvDFKVYAEAFGAAGFAVESAEALEPTLRAAMDV--DG-PAVVAI 539
Cdd:PRK06154 487 smggyDKVMPVSTTKYRATDISG------DYAAIARALGGYGERVEDPEMLVPALLRALRKvkEGtPALLEV 552
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
13-176 |
9.08e-44 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 153.16 E-value: 9.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDS-SIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQS-MDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQD 170
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*.
gi 495122918 171 IVDQPA 176
Cdd:pfam02776 161 VLLEEV 166
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
14-548 |
1.57e-42 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 160.00 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 14 ADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMA 93
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 94 TANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRpGSAFVSLPQDIVD 173
Cdd:PRK06457 85 DAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDILR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 174 QPAQgnILPAGNAPKlgPAPDACID--HVAGLIRNAKNPVILLGLMASqpENSRALHRLLEKSHIPVTSTYQAAGAVNQE 251
Cdd:PRK06457 164 KSSE--YKGSKNTEV--GKVKYSIDfsRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 252 HfTRFAGRVGLFNNQAGDRLLHLADLIICIGYS-P-VEYEPAmwncgNATLVHIDVLPAYEESHYAPEIELVGDIAgtlE 329
Cdd:PRK06457 238 D-PKVMGGIGLLGTKPSIEAMDKADLLIMLGTSfPyVNFLNK-----SAKVIQVDIDNSNIGKRLDVDLSYPIPVA---E 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 330 KLAGRIEQPlvlSDR-ASEILIDRQNQRELLARRGAQLNQfALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSF 408
Cdd:PRK06457 309 FLNIDIEEK---SDKfYEELKGKKEDWLDSISKQENSLDK-PMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRAS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 409 RARQVMISNGQQTMGVALPWAIGAWLV-DPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNMVAIQEEKK 487
Cdd:PRK06457 385 GEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVM 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495122918 488 YQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVDYSDNPL 548
Cdd:PRK06457 465 GYPEWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPM 525
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
375-541 |
4.39e-40 |
|
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: 143.16 E-value: 4.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 375 RIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSS 454
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 455 MELETAVRLKANVLHIIWVDNAYNMVAIQEEKKYQ-RLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDG 533
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGgRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 495122918 534 PAVVAIPV 541
Cdd:cd00568 161 PALIEVKT 168
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
21-462 |
1.08e-39 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 152.46 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 21 LEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGMATANSEGD 100
Cdd:PRK07525 16 LQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYWAHT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 101 PVVA-----------LGGavkradkarqvHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRpGSAFVSLPQ 169
Cdd:PRK07525 96 PVVLvtpqagtktigQGG-----------FQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 170 DIVDQPAQGNILPAGNAPKlGPAPDACIDHVAGLIRNAKNPVILLG---LMASQPENSRALHRLLEKshiPVTSTYQAAG 246
Cdd:PRK07525 164 DYFYGVIDVEIPQPVRLER-GAGGEQSLAEAAELLSEAKFPVILSGagvVLSDAIEECKALAERLDA---PVACGYLHND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 247 AVNQEHfTRFAGRVGLFNNQAGDRLLHLADLIICIG--YSP--------VEYEPAmwncgNATLVHIDVLPAYEESHYAP 316
Cdd:PRK07525 240 AFPGSH-PLWVGPLGYNGSKAAMELIAKADVVLALGtrLNPfgtlpqygIDYWPK-----DAKIIQVDINPDRIGLTKKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 317 EIELVGDIA----GTLEKLAGRIEQPLVLSDRASEILIDRQNQRELLAR-------RGAQLNQFA-------LHPLRIVR 378
Cdd:PRK07525 314 SVGICGDAKavarELLARLAERLAGDAGREERKALIAAEKSAWEQELSSwdhedddPGTDWNEEArarkpdyMHPRQALR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 379 AMQDIINNDVTLTVDMGSFHIwIARYLYSFRARQVMISNGQ-QTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMEL 457
Cdd:PRK07525 394 EIQKALPEDAIVSTDIGNNCS-IANSYLRFEKGRKYLAPGSfGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEV 472
|
....*
gi 495122918 458 ETAVR 462
Cdd:PRK07525 473 MTAVR 477
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
13-539 |
2.38e-39 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 150.91 E-value: 2.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL-LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIgRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRA--DKARQ-VHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLP 168
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETPylDQDLGyIHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 169 QDIvdQPAQGNiLPAGNAPKLGPAPDAC---IDHVAGLIRNAKNPVILLGLMASQPenSRALHRLLEKShIPVTSTYQAA 245
Cdd:PRK07064 165 IDI--QAAEIE-LPDDLAPVHVAVPEPDaaaVAELAERLAAARRPLLWLGGGARHA--GAEVKRLVDLG-FGVVTSTQGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 246 GAVNQEHftrfAGRVGLFNNQ-AGDRLLHLADLIICIG-----YSPVEYEPAMwncgNATLVHIDVLPAYEESHYAPEIE 319
Cdd:PRK07064 239 GVVPEDH----PASLGAFNNSaAVEALYKTCDLLLVVGsrlrgNETLKYSLAL----PRPLIRVDADAAADGRGYPNDLF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 320 LVGDIAGTLEKLAGRIEQPL-VLSDRASEILIDRQNQRELLarrGAQLNQFAlhplRIVRAMQDIINNDVTLTVDMG-SF 397
Cdd:PRK07064 311 VHGDAARVLARLADRLEGRLsVDPAFAADLRAAREAAVADL---RKGLGPYA----KLVDALRAALPRDGNWVRDVTiSN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 398 HIWIARYLYSFRARQVMISNGqQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAY 477
Cdd:PRK07064 384 STWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGY 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495122918 478 N-MVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAI 539
Cdd:PRK07064 463 GvIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
14-537 |
4.23e-39 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 150.91 E-value: 4.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 14 ADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL-LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLrRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEhGRPGSAFVSLPQDIV 172
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAI-LNRGVAVVVLPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 173 DQPAQGNILPAGNAPKLG---PApDACIDHVAGLIRNAKNPVILLG---------LMA-SQPENSRALHRLLEKSHIPVT 239
Cdd:PRK09124 165 LKPAPERATPHWYHAPQPvvtPA-EEELRKLAALLNGSSNITLLCGsgcagahdeLVAlAETLKAPIVHALRGKEHVEYD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 240 STYQAagavnqehftrfaGRVGLFNNQAGDRLLHLADLIICIG----YSPveYEPAmwncgNATLVHIDVLPAYEESHYA 315
Cdd:PRK09124 244 NPYDV-------------GMTGLIGFSSGYHAMMNCDTLLMLGtdfpYRQ--FYPT-----DAKIIQIDINPGSLGRRSP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 316 PEIELVGDIAGTLEKLAGRIEqplVLSDRAseiLIDRQNQRELLARRG------AQLNQFALHPLRIVRAMQDIINNDVT 389
Cdd:PRK09124 304 VDLGLVGDVKATLAALLPLLE---EKTDRK---FLDKALEHYRKARKGlddlavPSDGGKPIHPQYLARQISEFAADDAI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 390 LTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFlqsSM---ELETAVRLKAN 466
Cdd:PRK09124 378 FTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGF---SMlmgDFLSLVQLKLP 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495122918 467 VLHIIWVDNAYNMVAIqEEKKYQRL-SGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVV 537
Cdd:PRK09124 455 VKIVVFNNSVLGFVAM-EMKAGGYLtDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALV 525
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
393-539 |
1.25e-38 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 138.87 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 393 DMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIW 472
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495122918 473 VDNAYNMVAIQEEKKYQR----LSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAI 539
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGrysgPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
14-542 |
3.33e-38 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 148.21 E-value: 3.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 14 ADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDS-SIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTgGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAeHGRPGSAFVSLPQDIV 172
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTLPGDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 173 DQPAQ---GNILPAGNAPKLGPAPDAcIDHVAGLIRNAKNPVILLGlmaSQPENSRA-LHRLLEKSHIPVTSTYqaAGAV 248
Cdd:PRK06546 165 DEPAPegfAPSVISPRRPTVVPDPAE-VRALADAINEAKKVTLFAG---AGVRGAHAeVLALAEKIKAPVGHSL--RGKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 249 NQEHFTRF-AGRVGLFNNQAGDRLLHLADLIICIG----YSpvEYEPamwncgNATLVHIDVLPAYEESHYAPEIELVGD 323
Cdd:PRK06546 239 WIQYDNPFdVGMSGLLGYGAAHEAMHEADLLILLGtdfpYD--QFLP------DVRTAQVDIDPEHLGRRTRVDLAVHGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 324 IAGTLEKLAGRIEQPlvlSDRAseiLIDRQ--NQRELLAR------RGAQlNQFALHPLRIVRAMQDIINNDVTLTVDMG 395
Cdd:PRK06546 311 VAETIRALLPLVKEK---TDRR---FLDRMlkKHARKLEKvvgaytRKVE-KHTPIHPEYVASILDELAADDAVFTVDTG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 396 SFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFlqsSM---ELETAVRLKANVLHIIW 472
Cdd:PRK06546 384 MCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGL---SMllgELLTVKLYDLPVKVVVF 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495122918 473 VDNAYNMVAIqeEKKYQRLS--GVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:PRK06546 461 NNSTLGMVKL--EMLVDGLPdfGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
6-477 |
7.65e-38 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 147.43 E-value: 7.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 6 RMRqwahGADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDS-SIQIIPVRHEANAAFMAAAVGRIT-GKAGVALVTSGP 83
Cdd:PRK11269 3 KMR----AVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHgGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 84 GCSNLITGMATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSA 163
Cdd:PRK11269 79 AGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 164 FVSLPQDIvdQPAQGNILPAGNAPKLGPAPDAC---IDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTS 240
Cdd:PRK11269 159 LIDLPFDV--QVAEIEFDPDTYEPLPVYKPAATraqIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 241 TYQAAGAVNQEHfTRFAGRVGLFNNQA-GDRLLHLADLIICIGyspveyepAMWN----------CGNATLVHIDVLPAY 309
Cdd:PRK11269 237 TLMGWGAIPDDH-PLMAGMVGLQTSHRyGNATLLASDFVLGIG--------NRWAnrhtgsvevyTKGRKFVHVDIEPTQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 310 EESHYAPEIELVGDIAGTLE---------KLAGRieqplvLSDRaSEILIDRQNQRELLARRgAQLNQFALHPLRIVRAM 380
Cdd:PRK11269 308 IGRVFGPDLGIVSDAKAALEllvevarewKAAGR------LPDR-SAWVADCQERKRTLLRK-THFDNVPIKPQRVYEEM 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 381 QDIINNDVTLTVDMGSFHIWIARYLYSFRARQvMISNGQQ-TMGVALPWAIGAWLVDPSRKVVSVSGDGGFlQSSMElET 459
Cdd:PRK11269 380 NKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRH-WINCGQAgPLGWTIPAALGVRAADPDRNVVALSGDYDF-QFLIE-EL 456
|
490 500
....*....|....*....|
gi 495122918 460 AVRLKANV--LHIIwVDNAY 477
Cdd:PRK11269 457 AVGAQFNLpyIHVL-VNNAY 475
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
14-462 |
2.54e-34 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 136.96 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 14 ADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL--LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITG 91
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 92 MATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPV-TKYSVEVSSSDAIAEVVSNAFRVAeHGRPGSAFVSLPQD 170
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTA-LAERTVTAVILPND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQPAQG-----NILPAG---NAPKLGPAPDAcIDHVAGLIrNAKNPVILL---GLMASQPENSRALHR--------LL 231
Cdd:PRK08273 165 VQELEYEPpphahGTVHSGvgyTRPRVVPYDED-LRRAAEVL-NAGRKVAILvgaGALGATDEVIAVAERlgagvakaLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 232 EKSHIPVTSTYqaagavnqehftrFAGRVGLFNNQAGDRLLHLADLIICIG----YSpvEYEPAmwnCGNATLVHIDVLP 307
Cdd:PRK08273 243 GKAALPDDLPW-------------VTGSIGLLGTKPSYELMRECDTLLMVGssfpYS--EFLPK---EGQARGVQIDIDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 308 AYEESHYAPEIELVGDIAGTLEKLAGRIEQPlvlSDRA--SEILIDRQNQRELLARRgAQLNQFALHPLRIVRAMQDIIN 385
Cdd:PRK08273 305 RMLGLRYPMEVNLVGDAAETLRALLPLLERK---KDRSwrERIEKWVARWWETLEAR-AMVPADPVNPQRVFWELSPRLP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 386 NDVTLTVDMGSFHIWIARYLysfRARQVM---ISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSM-ELETAV 461
Cdd:PRK08273 381 DNAILTADSGSCANWYARDL---RMRRGMmasLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGMaELITVA 457
|
.
gi 495122918 462 R 462
Cdd:PRK08273 458 K 458
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
15-169 |
3.30e-34 |
|
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: 126.69 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 15 DMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLD-SSIQIIPVRHEANAAFMAAAVGRITGkAGVALVTSGPGCSNLITGMA 93
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREgDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495122918 94 TANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAeHGRPGSAFVSLPQ 169
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTA-YASQGPVVVRLPR 154
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
13-471 |
2.23e-33 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 133.96 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 13 GADMVVGQLEAQGVKQVFGIPGAKIDKVFDSLLDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRA--DKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQD 170
Cdd:PRK09259 92 ANATTNCFPMIMISGSSEREivDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 171 IVDQ-----PAQGNILPAGN-APKLGPAPDAcIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQA 244
Cdd:PRK09259 172 VLAQtmdadEALTSLVKVVDpAPAQLPAPEA-VDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 245 AGAVNQEHFTRFAGRVGLfnnqagdrLLHLADLIICIG----YSPVEYEPAMWNcGNATLVHIDVLPAYEESHYAPEIEL 320
Cdd:PRK09259 251 KGLLPDTHPQSAAAARSL--------ALANADVVLLVGarlnWLLSHGKGKTWG-ADKKFIQIDIEPQEIDSNRPIAAPV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 321 VGDIAGTLEKLAGRIEQ-PLVLSDRASEILIDRQNQ-----RELLARRGAQLNQF-ALHPLRIVraMQDiiNNDVTLtVD 393
Cdd:PRK09259 322 VGDIGSVMQALLAGLKQnTFKAPAEWLDALAERKEKnaakmAEKLSTDTQPMNFYnALGAIRDV--LKE--NPDIYL-VN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 394 MGSFHIWIARYL---YSFRARQVMISNGqqTMGVALPWAIGAwLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHI 470
Cdd:PRK09259 397 EGANTLDLARNIidmYKPRHRLDCGTWG--VMGIGMGYAIAA-AVETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVV 473
|
.
gi 495122918 471 I 471
Cdd:PRK09259 474 I 474
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
14-175 |
3.77e-30 |
|
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: 115.73 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 14 ADMVVGQLEAQGVKQVFGIPGAKIDKVFDSL-LDSSIQIIPVRHEANAAFMAAAVGRITGKAGVALVTSGPGCSNLITGM 92
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALrREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 93 ATANSEGDPVVALGGAVKRADKARQVHQSMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAeHGRPGSAFVSLPQDIV 172
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTA-IAKRGVAVLILPGDVQ 161
|
...
gi 495122918 173 DQP 175
Cdd:cd07039 162 DAP 164
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
197-331 |
5.26e-28 |
|
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: 108.81 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 197 IDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIPVTSTYQAAGAVNQEHFtRFAGRVGLFNNQAGDRLLHLAD 276
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHP-LYLGMLGMHGTPAANEALEEAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 495122918 277 LIICIG----YSPVEYEPAMWNCgNATLVHIDVLPAYEESHYAPEIELVGDIAGTLEKL 331
Cdd:pfam00205 80 LVLAVGarfdDIRTTGKLPEFAP-DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
371-542 |
8.56e-28 |
|
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: 109.54 E-value: 8.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 371 LHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGF 450
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 451 LQSSMELETAVRLKANVLHIIWVDNAYNMVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPTLRAAMD 530
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|..
gi 495122918 531 VDGPAVVAIPVD 542
Cdd:cd02014 162 ADGPVVIDVVTD 173
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-554 |
4.37e-26 |
|
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: 112.17 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 14 ADMVVGQLEAQGVKQVFGIPGakiDKVFdSLLDssiQII---PVRHeanaafmaaaVG---------------RITGkAG 75
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPG---DYNL-PFLD---AIEahpGIRW----------VGccnelnagyaadgyaRVNG-LG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 76 VALVTSGPGCSNLITGMATANSEGDPVVALGGAVKRADKAR--QVHQS-----MDTVA-MFSPVTKYSVEVSSSDAIAE- 146
Cdd:COG3961 70 ALVTTYGVGELSAINGIAGAYAERVPVVHIVGAPGTRAQRRgpLLHHTlgdgdFDHFLrMFEEVTVAQAVLTPENAAAEi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 147 --VVSNAFRvaeHGRPGsaFVSLPQDIVDQPaqgnILPAGNAPKLGPAP------DACIDHVAGLIRNAKNPVILLGLMA 218
Cdd:COG3961 150 drVLAAALR---EKRPV--YIELPRDVADAP----IEPPEAPLPLPPPAsdpaalAAAVAAAAERLAKAKRPVILAGVEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 219 SQPENSRALHRLLEKSHIPVTSTYQAAGAVNQEHftrfAGRVGLFNNQAGD----RLLHLADLIICIGYSPVEYEPAMW- 293
Cdd:COG3961 221 HRFGLQEELLALAEKTGIPVATTLLGKSVLDESH----PQFIGTYAGAASSpevrEYVENADCVLCLGVVFTDTNTGGFt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 294 ------NCGNATLVHIDVlpayeESHYAPEIELVGDIAGTLEKLAGRIEQPLVLSDRASeilidrqnqrELLARRGAQLN 367
Cdd:COG3961 297 aqldpeRTIDIQPDSVRV-----GGHIYPGVSLADFLEALAELLKKRSAPLPAPAPPPP----------PPPAAPDAPLT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 368 QFALHPlrivrAMQDIINNDVTLTVDMG--SFHIWIARyLYsfRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVS 445
Cdd:COG3961 362 QDRLWQ-----RLQAFLDPGDIVVADTGtsLFGAADLR-LP--EGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 446 GDGGFLQSSMELETAVRLKANVLhIIWVDN--------------AYNMVAiqeEKKYQRLSGVsFGPVDFKVYaeafgaa 511
Cdd:COG3961 434 GDGAFQLTAQELSTMLRYGLKPI-IFVLNNdgytieraihgpdgPYNDIA---NWDYAKLPEA-FGGGNALGF------- 501
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 495122918 512 gfAVESAEALEPTLRAAM-DVDGPAVVAIPVDYSDNPLLMGQLH 554
Cdd:COG3961 502 --RVTTEGELEEALAAAEaNTDRLTLIEVVLDKMDAPPLLKRLG 543
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
71-544 |
2.85e-25 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 109.70 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 71 TGKAGVALVTSGPGCSNLITGMATANSEGDPVVALGGAVKRADKAR------QVH--QSM-DTVAMFSPVTKYSVEVSSS 141
Cdd:PRK08327 73 TGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntRIHwtQEMrDQGGLVREYVKWDYEIRRG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 142 DAIAEVVSNAFRVAEHGRPGSAFVSLPQDIVDQPAQGNILPAGNAPKL---GPAPDAcIDHVAGLIRNAKNPVILLGLMA 218
Cdd:PRK08327 153 DQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPappAPDPED-IARAAEMLAAAERPVIITWRAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 219 SQPENSRALHRLLEKSHIPVTSTyqaagavnqehftrfagrVGLFNNQAGDRLLHL----------ADLIICIG----YS 284
Cdd:PRK08327 232 RTAEGFASLRRLAEELAIPVVEY------------------AGEVVNYPSDHPLHLgpdpradlaeADLVLVVDsdvpWI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 285 PVEYEPAMwncgNATLVHIDVLPAYEES---HYAPEIELVGDIAGTLEKLAGRI-----EQPLVLSDRASEILIDRQNQR 356
Cdd:PRK08327 294 PKKIRPDA----DARVIQIDVDPLKSRIplwGFPCDLCIQADTSTALDQLEERLkslasAERRRARRRRAAVRELRIRQE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 357 ELLARRGAQLNQF-ALHPLRIVRAMQDIINNDVTLTVDmgsfhiwiarylYSFRARQV-------MISNGQQ-TMGVALP 427
Cdd:PRK08327 370 AAKRAEIERLKDRgPITPAYLSYCLGEVADEYDAIVTE------------YPFVPRQArlnkpgsYFGDGSAgGLGWALG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 428 WAIGAWLVDPSRKVVSVSGDGGFLQSSME--LETAVRLKANVLHIIWVDNAYNMVAIQEEKKY--------QRLSGVSFG 497
Cdd:PRK08327 438 AALGAKLATPDRLVIATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYpegyaarkGTFPGTDFD 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 495122918 498 P-VDFKVYAEAFGAAGFAVESAEALEPTLRAAMDV----DGPAVVAIPVDYS 544
Cdd:PRK08327 518 PrPDFAKIAEAFGGYGERVEDPEELKGALRRALAAvrkgRRSAVLDVIVDRV 569
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
371-550 |
7.61e-25 |
|
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: 101.81 E-value: 7.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 371 LHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGF 450
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 451 LQSSMELETAVRLKANVLhIIWVDNAY-NMVAIQEEKKY-QRLSGVSFGP-VDFKVYAEAFGAAGFAVESAEALEPTLRA 527
Cdd:cd02015 81 QMNIQELATAAQYNLPVK-IVILNNGSlGMVRQWQELFYeGRYSHTTLDSnPDFVKLAEAYGIKGLRVEKPEELEAALKE 159
|
170 180
....*....|....*....|...
gi 495122918 528 AMDVDGPAVVAIPVDYSDNPLLM 550
Cdd:cd02015 160 ALASDGPVLLDVLVDPEENVLPM 182
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
373-542 |
1.72e-22 |
|
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: 94.52 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 373 PLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQ 452
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 453 SSMELETAVRLKANVLHIIWVDNAYNMVA-IQEEKKYQRLSGVSFGP-VDFKVYAEAFGAAGFAVESAEALEPTLRAAMD 530
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLdGQQLSYGLGLPVTTLLPdTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 495122918 531 VDGPAVVAIPVD 542
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
130-542 |
8.35e-19 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 89.63 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 130 PVTKYSVEVSSSDAIAEVVSNAFRVAEHGRPGSAFVSLPQDIVDQPAQgNILPAGNAPKLGPAPDAcIDHVAGLIRNAKN 209
Cdd:PRK07092 131 PYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDQPAE-PLPARTVSSAVRPDPAA-LARLGDALDAARR 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 210 PVILLGlmasqPENSRA-----LHRLLEKSHIPV-TSTYQAAGAVNQEH--FTRF--AGRVGLfnnqagDRLLHLADLII 279
Cdd:PRK07092 209 PALVVG-----PAVDRAgawddAVRLAERHRAPVwVAPMSGRCSFPEDHplFAGFlpASREKI------SALLDGHDLVL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 280 CIGySPV----EYEPAMWNCGNATLVHIDVLPayEESHYAPE-IELVGDIAGTLEKLAGRIEQplvlSDRAseilidRQN 354
Cdd:PRK07092 278 VIG-APVftyhVEGPGPHLPEGAELVQLTDDP--GEAAWAPMgDAIVGDIRLALRDLLALLPP----SARP------APP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 355 QRELLARRGAQ----LNQFALHPLRIVRAMQDIINNDVTLTVD-MGSFHIWIARYLYSFrarqvMISNGqqtMGVALPWA 429
Cdd:PRK07092 345 ARPMPPPAPAPgeplSVAFVLQTLAALRPADAIVVEEAPSTRPaMQEHLPMRRQGSFYT-----MASGG---LGYGLPAA 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 430 IGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLHIIWVDNAYNmvAIQEEKK---YQRLSGVSFGPVDFKVYAE 506
Cdd:PRK07092 417 VGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYG--ALRWFAPvfgVRDVPGLDLPGLDFVALAR 494
|
410 420 430
....*....|....*....|....*....|....*.
gi 495122918 507 AFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:PRK07092 495 GYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
7-486 |
1.50e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 82.61 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 7 MRQWAHGADMVVGQLEAQGVKQVFGIPGAKiDKVFDSLLDSSIQIIPVR--HEANAAFMAAAVGRITGKAGVALVTSGPG 84
Cdd:PRK12474 1 MGQTMNGADSVVDTLLNCGVEVCFANPGTS-EMHFVAALDRVPRMRPVLclFEGVVTGAADGYGRIAGKPAVTLLHLGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 85 CSNLITGMATANSEGDPVVALGGavkraDKARQVHQ-----SMDTVAMFSPVTKYSVEVSSSDAIAEVVSNAFRVAEHGR 159
Cdd:PRK12474 80 LANGLANLHNARRAASPIVNIVG-----DHAVEHLQydaplTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 160 PGSAFVSLPQDIVDQPAQGNilpAGNAPKLGPAPDA--CIDHVAGLIRNAKNPVILLGLMASQPENSRALHRLLEKSHIP 237
Cdd:PRK12474 155 GGIATLIMPADVAWNEAAYA---AQPLRGIGPAPVAaeTVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 238 VTSTyQAAGavnqeHFTRFAGRVGL----FNNQAGDRLLHLADLIICIGYS-PVEY--EPAMWNCGNATLVHIDVLPAYE 310
Cdd:PRK12474 232 LYCD-TFAP-----RIERGAGRVPIeripYFHEQITAFLKDVEQLVLVGAKpPVSFfaYPGKPSWGAPPGCEIVYLAQPD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 311 EshyapeielvgDIAGTLEKLAGRIEQPLVLSDRAseilidrqnQRELLARRGAQLNQFALHPLRIVRAMQDIINNDVTL 390
Cdd:PRK12474 306 E-----------DLAQALQDLADAVDAPAEPAART---------PLALPALPKGALNSLGVAQLIAHRTPDQAIYADEAL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 391 TvDMGSFHIWIArylysfRAR---QVMISNGqqTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANV 467
Cdd:PRK12474 366 T-SGLFFDMSYD------RARphtHLPLTGG--SIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDV 436
|
490
....*....|....*....
gi 495122918 468 LHIIWVDNAYNMVAIQEEK 486
Cdd:PRK12474 437 TVVIFANRSYAILNGELQR 455
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
371-530 |
1.96e-12 |
|
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: 66.38 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 371 LHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGF 450
Cdd:cd02013 4 MHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 451 LQSSMELETAVRLKANVLHIIWVDNAYNmvaiqEEKKYQ------RLSGVSFGPVDFKVYAEAFGAAGFAVESAEALEPT 524
Cdd:cd02013 84 GMSMMEIMTAVRHKLPVTAVVFRNRQWG-----AEKKNQvdfynnRFVGTELESESFAKIAEACGAKGITVDKPEDVGPA 158
|
....*.
gi 495122918 525 LRAAMD 530
Cdd:cd02013 159 LQKAIA 164
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
371-541 |
2.02e-11 |
|
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: 63.00 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 371 LHPLRIVRAMQDIINNDVTLtVDMGSFHIWIARYLYSFRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGF 450
Cdd:cd02002 1 LTPEYLAAALAAALPEDAII-VDEAVTNGLPLRDQLPLTRPGSYFTLRGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 451 LQSSMELETAVRLKANVLHIIWVDNAYN--------MVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAVESAEALE 522
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGalrsflkrVGPEGPGENAPDGLDLLDPGIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 495122918 523 PTLRAAMDVDGPAVVAIPV 541
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
68-537 |
4.81e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 58.70 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 68 GRITGKAGVALVTSGPGCSNLITGMATANSEGDPVVALGGavkraDKARQVHQ-----SMDTVAMFSPVTKYSVEVSSSD 142
Cdd:PRK07586 59 ARMAGKPAATLLHLGPGLANGLANLHNARRARTPIVNIVG-----DHATYHRKydaplTSDIEALARPVSGWVRRSESAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 143 AIAEVVSNAFRVAEHGRPGSAFVSLPQDIVDQPAqGNILPAGNAPKLGPAPDACIDHVAGLIRNAKNPVILLGLMASQPE 222
Cdd:PRK07586 134 DVAADAAAAVAAARGAPGQVATLILPADVAWSEG-GPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRER 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 223 NSRALHRLLEKSHIPV-TSTYQA-----AGAVNQEhftrfagRVGLFNNQAGDRLLHlADLIICIGY-SPVEYEpamwnc 295
Cdd:PRK07586 213 GLAAAARIAAATGARLlAETFPArmergAGRPAVE-------RLPYFAEQALAQLAG-VRHLVLVGAkAPVAFF------ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 296 gnatlvhidvlpAYEE--SHYAPE----IELVG---DIAGTLEKLAGRIEQPLVLSDRASEIlidrqnqrELLARRGAqL 366
Cdd:PRK07586 279 ------------AYPGkpSRLVPEgcevHTLAGpgeDAAAALEALADALGAKPAAPPLAAPA--------RPPLPTGA-L 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 367 NQFALhPLRIVRAMQD---IINNDVTLTVDmgsFHIWIARylysfRARQVMISNGQQTMGVALPWAIGAWLVDPSRKVVS 443
Cdd:PRK07586 338 TPEAI-AQVIAALLPEnaiVVDESITSGRG---FFPATAG-----AAPHDWLTLTGGAIGQGLPLATGAAVACPDRKVLA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 444 VSGDGGFLQSSMELETAVRLKANVLHIIWVDNAY--------NMVAIQEEKKYQRLSGVSFGPVDFKVYAEAFGAAGFAV 515
Cdd:PRK07586 409 LQGDGSAMYTIQALWTQARENLDVTTVIFANRAYailrgelaRVGAGNPGPRALDMLDLDDPDLDWVALAEGMGVPARRV 488
|
490 500
....*....|....*....|..
gi 495122918 516 ESAEALEPTLRAAMDVDGPAVV 537
Cdd:PRK07586 489 TTAEEFADALAAALAEPGPHLI 510
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
365-477 |
2.62e-08 |
|
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: 54.21 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 365 QLNQFALHPLRIVRAMQDIINNDVTLTVDMGSFHIWIARYLYSFRARQvMISNGQQ-TMGVALPWAIGAWLVDPSRKVVS 443
Cdd:cd02006 2 HFDDVPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRH-WINCGQAgPLGWTVPAALGVAAADPDRQVVA 80
|
90 100 110
....*....|....*....|....*....|....
gi 495122918 444 VSGDGGFLQSSMELETAVRLKANVLHIIwVDNAY 477
Cdd:cd02006 81 LSGDYDFQFMIEELAVGAQHRIPYIHVL-VNNAY 113
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
21-161 |
1.07e-07 |
|
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: 51.73 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 21 LEAQGVKQVFGIPGAKIDKVFDSLLDSS-IQIIPVRHEANAAFMAAAVGRITGkAGVALVTSGPGCSNLITGMATANSEG 99
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPgLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495122918 100 DPVVALGGAVKRAD--KARQVHQS-----MDTVA-MFSPVTKYSVEVSSSDAIAEVVSNAFRVA-EHGRPG 161
Cdd:cd07038 86 VPVVHIVGAPSTKAqaSGLLLHHTlgdgdFDVFLkMFEEITCAAARLTDPENAAEEIDRVLRTAlRESRPV 156
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
418-542 |
1.64e-07 |
|
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: 51.92 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 418 GQQTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLKANVLhIIWVDNA--------YNMVAIQ----EE 485
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKII-IVLFDNHgfgcinnlQESTGSGsfgtEF 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 486 KKYQRLSGVSFG---PVDFKVYAEAFGAAGFAVESAEALEPTLRAAMDVDGPAVVAIPVD 542
Cdd:cd02003 125 RDRDQESGQLDGallPVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
421-483 |
9.06e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 46.75 E-value: 9.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495122918 421 TMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELET-AVRLKANVLHIIWVDNAYNMVAIQ 483
Cdd:PRK06163 58 SMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVYQITGGQ 121
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
401-541 |
5.38e-04 |
|
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: 41.14 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495122918 401 IARYLYSFRARQVMISNGQ----QTMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSMELETAVRLK-ANVLHIIWVDN 475
Cdd:cd03371 25 TSRELFELRDRPGGGHAQDfltvGSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLApANLIHIVLNNG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495122918 476 AYNMVAIQEEKKYQ-RLSGVSFGPVDFKVYaeafgaagfAVESAEALEPTLRAAMDVDGPAVVAIPV 541
Cdd:cd03371 105 AHDSVGGQPTVSFDvSLPAIAKACGYRAVY---------EVPSLEELVAALAKALAADGPAFIEVKV 162
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
421-477 |
6.88e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 40.72 E-value: 6.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 495122918 421 TMGVALPWAIGAWLVDPSRKVVSVSGDGGFLQSSME-LETAVRLKANVLHIIwVDNAY 477
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSGILgLINAVYNKANITVVI-LDNRT 108
|
|
| |
