|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
11-561 |
0e+00 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 1066.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 11 KTKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSN 90
Cdd:PRK08617 2 DKKKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 91 LATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSL 170
Cdd:PRK08617 82 LATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 171 PQDVMTAETTVESIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGA 250
Cdd:PRK08617 162 PQDVVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 251 ISRELEDHFFGRVGLFRNQPGDILLEEADLVISMGYDPIEYDPKFWNKLGDRTIIHLDDHQADIDHDYQPERELIGDIAL 330
Cdd:PRK08617 242 ISRELEDHFFGRVGLFRNQPGDELLKKADLVITIGYDPIEYEPRNWNSEGDATIIHIDVLPAEIDNYYQPERELIGDIAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 331 TVNSIAEKLPKLVLSTKSEAVLERLRAKLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRS 410
Cdd:PRK08617 322 TLDLLAEKLDGLSLSPQSLEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWMARYFRS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 411 YEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAFQQMMK 490
Cdd:PRK08617 402 YEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMK 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446025664 491 YGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNIKLSEKLLPNQL 561
Cdd:PRK08617 482 YGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIKLMEQLLPDQL 552
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
16-554 |
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: 899.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGL 95
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 96 VTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDVM 175
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 176 TAETTVESIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAISREL 255
Cdd:TIGR02418 161 DSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSREL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 256 EDHFFGRVGLFRNQPGDILLEEADLVISMGYDPIEYDPKFWNKLGDRTIIHLDDHQADIDHDYQPERELIGDIALTVNSI 335
Cdd:TIGR02418 241 EDHFFGRVGLFRNQPGDRLLKQADLVITIGYDPIEYEPRNWNSENDATIVHIDVEPAQIDNNYQPDLELVGDIASTLDLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 336 AEKLPKLVLSTKSEAVLERLRAKLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRR 415
Cdd:TIGR02418 321 AERIPGYELPPDALAILEDLKQQREALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSYRARH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 416 LLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAFQQMMKYGRTS 495
Cdd:TIGR02418 401 LLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQRSS 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446025664 496 ATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNIKLSE 554
Cdd:TIGR02418 481 GVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNPKLMS 539
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
12-549 |
0e+00 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 581.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 12 TKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQER-GPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSN 90
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQsGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 91 LATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSL 170
Cdd:COG0028 81 LVTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 171 PQDVMTAETTVE--SIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAA 248
Cdd:COG0028 161 PKDVQAAEAEEEpaPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 249 GAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGYDPIEYDPKFWNKL-GDRTIIHLDDHQADIDHDYQPERELI 325
Cdd:COG0028 241 GAFP---EDHplYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFaPDAKIIHIDIDPAEIGKNYPVDLPIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 326 GDIALTVNSIAEKLPKlvLSTKSEAVLERLRAkLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIGSHSIWMA 405
Cdd:COG0028 318 GDAKAVLAALLEALEP--RADDRAAWLARIAA-WRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 406 RCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAF 485
Cdd:COG0028 395 RYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQ 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446025664 486 QQMMKYG-RTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDN 549
Cdd:COG0028 475 WQELFYGgRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
15-556 |
1.28e-174 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 504.75 E-value: 1.28e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 15 KGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPrTDRLKRT-HQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQD 173
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKP-IKRSKQGsFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 174 VMTAETTVESIgALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAISr 253
Cdd:PRK08322 161 IAAEETDGKPL-PRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIP- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 254 elEDH--FFGRVGLfrnQPGDIL---LEEADLVISMGYDPIEYDPKFWNKLGDRTIIHLDDHQADIDHDYQPERELIGDI 328
Cdd:PRK08322 239 --ETHplSLGTAGL---SQGDYVhcaIEHADLIINVGHDVIEKPPFFMNPNGDKKVIHINFLPAEVDPVYFPQVEVVGDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 329 ALTVNSIAEKLPKLvlSTKSEAVLERLRAKLSEQ-AEVPNRPSEGVThPLQVIRTLRSLISDDTTVTCDIGSHSIWMARC 407
Cdd:PRK08322 314 ANSLWQLKERLADQ--PHWDFPRFLKIREAIEAHlEEGADDDRFPMK-PQRIVADLRKVMPDDDIVILDNGAYKIWFARN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 408 FRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAFQQ 487
Cdd:PRK08322 391 YRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQ 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 488 MMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNIK-LSEKL 556
Cdd:PRK08322 471 ENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSENDRvLNQEL 540
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
15-550 |
5.92e-108 |
|
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: 334.38 E-value: 5.92e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 15 KGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLAT 93
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGiEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 94 GLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQD 173
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 174 VMTAETTVESIGALSKPqlGIAPT---H--DITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAA 248
Cdd:TIGR00118 162 VTTAEIEYPYPEKVNLP--GYRPTvkgHplQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 249 GAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQPER 322
Cdd:TIGR00118 240 GSFP---EDHplSLGMLGMHGTKTANLAVHECDLIIAVG---ARFDDRVTGNLAkfapNAKIIHIDIDPAEIGKNVRVDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 323 ELIGDialtVNSIAEKLPKLVLSTKSEAVLERLRAKLSEQAEVPNRPS--EGVTHPLQVIRTLRSLISDDTTVTCDIGSH 400
Cdd:TIGR00118 314 PIVGD----ARNVLEELLKKLFELKERKESAWLEQINKWKKEYPLKMDytEEGIKPQQVIEELSRVTKDEAIVTTDVGQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 401 SIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTY 480
Cdd:TIGR00118 390 QMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYL 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446025664 481 DMVA-FQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNI 550
Cdd:TIGR00118 470 GMVRqWQELFYEERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENV 541
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
15-545 |
2.98e-103 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 322.86 E-value: 2.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 15 KGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDV 174
Cdd:PRK06276 82 IATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 175 MTAETTVESIGALSKPQL-GIAPT---HD--ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAA 248
Cdd:PRK06276 162 QEGELDLEKYPIPAKIDLpGYKPTtfgHPlqIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 249 GAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGY--------DPIEYDPkfwnklgDRTIIHLDDHQADIDHDY 318
Cdd:PRK06276 242 GAFP---EDHplALGMVGMHGTKAANYSVTESDVLIAIGCrfsdrttgDISSFAP-------NAKIIHIDIDPAEIGKNV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 319 QPERELIGDIALTVNSIAEKLPKLVLSTKSEAV--LERLRAKLSEQAEVPNRPsegvTHPLQVIRTLRSLISD-----DT 391
Cdd:PRK06276 312 RVDVPIVGDAKNVLRDLLAELMKKEIKNKSEWLerVKKLKKESIPRMDFDDKP----IKPQRVIKELMEVLREidpskNT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 392 TVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIV 471
Cdd:PRK06276 388 IITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVV 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446025664 472 HLVWRDGTYDMVAFQQMMKYG-RTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK06276 468 ICIFDNRTLGMVYQWQNLYYGkRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIID 543
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
376-552 |
8.84e-95 |
|
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: 286.88 E-value: 8.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 376 PLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLF 455
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 456 SAMELETAVRLNSPIVHLVWRDGTYDMVAFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAAD 535
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|....*..
gi 446025664 536 GPVIIDIPIDYRDNIKL 552
Cdd:cd02010 161 GVHVIDCPVDYSENIRL 177
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
12-545 |
3.27e-92 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 293.32 E-value: 3.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 12 TKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSN 90
Cdd:PRK08199 6 RARTGGQILVDALRANGVERVFCVPGESYLAVLDALHDETDiRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 91 LATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSL 170
Cdd:PRK08199 86 ASIGVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 171 PQDVMTAETTVESIGALSKPQlgIAPT-HDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAG 249
Cdd:PRK08199 166 PEDVLSETAEVPDAPPYRRVA--AAPGaADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 250 AISRELeDHFFGRVGLFRNqPGdiLLE---EADLVI----------SMGYDPIEYD-PKfwnklgdRTIIHLDDHQADID 315
Cdd:PRK08199 244 LFDNRH-PNYAGDLGLGIN-PA--LAArirEADLVLavgtrlgevtTQGYTLLDIPvPR-------QTLVHVHPDAEELG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 316 HDYQPERELIGDIALTVNSIAEKLPKLVLSTKSEAvlERLRAKLseQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTC 395
Cdd:PRK08199 313 RVYRPDLAIVADPAAFAAALAALEPPASPAWAEWT--AAAHADY--LAWSAPLPGPGAVQLGEVMAWLRERLPADAIITN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 396 DIGSHSIWMARCFRSYEPRRLL--FSNGMqtlGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHL 473
Cdd:PRK08199 389 GAGNYATWLHRFFRFRRYRTQLapTSGSM---GYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVI 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 474 VWRDGTYDMVAFQQMMKY-GRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK08199 466 VVNNGMYGTIRMHQEREYpGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
11-544 |
6.41e-90 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 286.91 E-value: 6.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 11 KTKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPEL--IVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGT 88
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDRIrvIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 89 SNLATGLVTANAESDPVVALAGAVPrTDRLKR----THQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPG 164
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIP-SALIGKgrghLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 165 ATLVSLPQDVMTAETTVESIGALSKPQlgiAPTHD---ITYVVEKIKAAKLPVILLGMRAStnEVTKAVRELIADTELPV 241
Cdd:PRK08266 160 PVALEMPWDVFGQRAPVAAAPPLRPAP---PPAPDpdaIAAAAALIAAAKNPMIFVGGGAA--GAGEEIRELAEMLQAPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 242 VETYQAAGAISrelEDHFfgrvgLFRNQP-GDILLEEADLVISMGYDPIeyDPKF-WNKLGDR-TIIHLDDHQADIDHdY 318
Cdd:PRK08266 235 VAFRSGRGIVS---DRHP-----LGLNFAaAYELWPQTDVVIGIGSRLE--LPTFrWPWRPDGlKVIRIDIDPTEMRR-L 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 319 QPERELIGDIALTVNSIAEKLPKLVLSTKS-EAVLERLRAKLSEQAEVpnrpsegVTHPLQVIRTLRSLISDDTTVT--- 394
Cdd:PRK08266 304 KPDVAIVADAKAGTAALLDALSKAGSKRPSrRAELRELKAAARQRIQA-------VQPQASYLRAIREALPDDGIFVdel 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 395 CDIGSHSiWMArcFRSYEPRRLLFSnGMQ-TLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHL 473
Cdd:PRK08266 377 SQVGFAS-WFA--FPVYAPRTFVTC-GYQgTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446025664 474 VWRDGTYDMV-AFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPI 544
Cdd:PRK08266 453 VFNNNAYGNVrRDQKRRFGGRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
13-550 |
2.67e-89 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 285.90 E-value: 2.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 13 KTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLA 92
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 93 TGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQ 172
Cdd:PRK06048 87 TGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 173 DVMTAET------TVESIGalSKPQLGIAPtHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQ 246
Cdd:PRK06048 167 DVTTAEIdfdypdKVELRG--YKPTYKGNP-QQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 247 AAGAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQP 320
Cdd:PRK06048 244 GIGAIP---TEHplSLGMLGMHGTKYANYAIQESDLIIAVG---ARFDDRVTGKLAsfapNAKIIHIDIDPAEISKNVKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 321 ERELIGDialtVNSIAEKLPKLVLSTKSEAVLERLrAKLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTcDIGSH 400
Cdd:PRK06048 318 DVPIVGD----AKQVLKSLIKYVQYCDRKEWLDKI-NQWKKEYPLKYKEREDVIKPQYVIEQIYELCPDAIIVT-EVGQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 401 SIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTY 480
Cdd:PRK06048 392 QMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYL 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446025664 481 DMVAFQQMMKYG-RTSATEFGD-VDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNI 550
Cdd:PRK06048 472 GMVRQWQELFYDkRYSHTCIKGsVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENV 543
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
16-550 |
2.68e-89 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 285.62 E-value: 2.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFmaAAIG--RLTGKPGVCLVTSGPGTSNLAT 93
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAM--AAIGyaRATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 94 GLVTANAESDPVVALAGAVPR----TDRLkrthQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVS 169
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSpligTDAF----QEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 170 LPQDVMTAETTVESIgALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAG 249
Cdd:PRK08978 157 IPKDIQLAEGELEPH-LTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 250 AISRElEDHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQPERELI 325
Cdd:PRK08978 236 AVEAD-HPYYLGMLGMHGTKAANLAVQECDLLIAVG---ARFDDRVTGKLNtfapHAKVIHLDIDPAEINKLRQAHVALQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 326 GDIaltvNSIaekLPKLVLSTKSEAVLERLRAKLSEQAEVPNRPSEGVTHPLqVIRTLRSLISDDTTVTCDIGSHSIWMA 405
Cdd:PRK08978 312 GDL----NAL---LPALQQPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPA-LLKQLSDRKPADTVVTTDVGQHQMWVA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 406 RCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMV-A 484
Cdd:PRK08978 384 QHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVrQ 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446025664 485 FQQMMKYGRTSATEFGD-VDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNI 550
Cdd:PRK08978 464 WQQLFFDERYSETDLSDnPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENV 530
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
16-545 |
4.61e-89 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 285.58 E-value: 4.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPG----AKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNL 91
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGlsnmQIYDAFVEDLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 92 ATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLP 171
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QDVMTaeTTVESIGALSKPQL-GIAPTHDITYVVEKIKAAKL------PVILLGMRASTNEVTKAVRELIADTELPVVET 244
Cdd:PRK06456 164 RDIFY--EKMEEIKWPEKPLVkGYRDFPTRIDRLALKKAAEIlinaerPIILVGTGVVWSNATPEVLELAELLHIPIVST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 245 YQAAGAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGydpieydpkfwNKLGDRTIIHLDDHQ----------- 311
Cdd:PRK06456 242 FPGKTAIP---HDHplYFGPMGYYGRAEASMAALESDAMLVVG-----------ARFSDRTFTSYDEMVetrkkfimvni 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 312 --ADIDHDYQPERELIGDIALTVNSIAEKLPKLVLSTKSEAVLERLRAKLSEQAEVPNRPSEGVTHPLQVIRTLRSLISD 389
Cdd:PRK06456 308 dpTDGEKAIKVDVGIYGNAKIILRELIKAITELGQKRDRSAWLKRVKEYKEYYSQFYYTEENGKLKPWKIMKTIRQALPR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 390 DTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSP 469
Cdd:PRK06456 388 DAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIP 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446025664 470 IVHLVWRDGTYDMV-AFQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK06456 468 VISVIFDNRTLGLVrQVQDLFFGKRIVGVDYGPSpDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVD 545
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
13-550 |
9.50e-88 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 281.99 E-value: 9.50e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 13 KTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFD-VLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNL 91
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDeIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 92 ATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLP 171
Cdd:PRK08527 82 VTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QDVmTAEttvesIGALSKPQLGIAPTHDITY---------VVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVV 242
Cdd:PRK08527 162 KDV-TAT-----LGEFEYPKEISLKTYKPTYkgnsrqikkAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 243 ETYQAAGAISRELEdHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLGD----RTIIHLDDHQADIDHDY 318
Cdd:PRK08527 236 ETLMARGVLRSDDP-LLLGMLGMHGSYAANMAMSECDLLISLG---ARFDDRVTGKLSEfakhAKIIHVDIDPSSISKIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 319 QPERELIGDIALTVNSIAEKLpKLVLSTKSEAVLERLRaKLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIG 398
Cdd:PRK08527 312 NADYPIVGDLKNVLKEMLEEL-KEENPTTYKEWREILK-RYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 399 SHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDG 478
Cdd:PRK08527 390 QHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNN 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446025664 479 TYDMVAFQQMMKYG-RTSATEFG-DVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNI 550
Cdd:PRK08527 470 FLGMVRQWQTFFYEeRYSETDLStQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENV 543
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
12-545 |
1.42e-86 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 279.19 E-value: 1.42e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 12 TKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL--QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTS 89
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 90 NLATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATsTNPGATLVS 169
Cdd:PRK08611 82 HLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAY-EKKGVAVLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 170 LPQDVMTAE---TTVESIGALSKPQLGIAPThDITYVVEKIKAAKLPVILLGMraSTNEVTKAVRELIADTELPVVETYQ 246
Cdd:PRK08611 161 IPDDLPAQKikdTTNKTVDTFRPTVPSPKPK-DIKKAAKLINKAKKPVILAGL--GAKHAKEELLAFAEKAKIPIIHTLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 247 AAGAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMG--YDPIEYDPKfwnklgDRTIIHLDDHQADIDHDYQPER 322
Cdd:PRK08611 238 AKGIIP---DDHpySLGNLGKIGTKPAYEAMQEADLLIMVGtnYPYVDYLPK------KAKAIQIDTDPANIGKRYPVNV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 323 ELIGDIALTVNSIAEKLpKLVLSTKS-EAVLERLR------AKLSEQAEVPNRPSegvthplQVIRTLRSLISDDTTVTC 395
Cdd:PRK08611 309 GLVGDAKKALHQLTENI-KHVEDRRFlEACQENMAkwwkwmEEDENNASTPIKPE-------RVMAAIQKIADDDAVLSV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 396 DIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVW 475
Cdd:PRK08611 381 DVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 476 RDGTYDMVAFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK08611 461 NNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD 530
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
6-558 |
3.74e-86 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 277.74 E-value: 3.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 6 KANDVKTKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL-QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTS 84
Cdd:PRK08155 5 GTTSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALsQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 85 GPGTSNLATGLVTANAESDPVVALAGAVPR----TDRLkrthQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATS 160
Cdd:PRK08155 85 GPGATNLVTAIADARLDSIPLVCITGQVPAsmigTDAF----QEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 161 TNPGATLVSLPQDVMTAETTVESIGALSKPQLGIAP-THDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTEL 239
Cdd:PRK08155 161 GRPGPVWIDIPKDVQTAVIELEALPAPAEKDAAPAFdEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 240 PVVETYQAAGAISReleDH--FFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQAD 313
Cdd:PRK08155 241 PTTMTLMALGMLPK---AHplSLGMLGMHGARSTNYILQEADLLIVLG---ARFDDRAIGKTEqfcpNAKIIHVDIDRAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 314 IDHDYQPERELIGDIALTvnsIAEKLPkLVLSTKSEAVLERLRaklSEQAEVP-NRPseGVTHPLQ---VIRTLRSLISD 389
Cdd:PRK08155 315 LGKIKQPHVAIQADVDDV---LAQLLP-LVEAQPRAEWHQLVA---DLQREFPcPIP--KADDPLShygLINAVAACVDD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 390 DTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAV--RLN 467
Cdd:PRK08155 386 NAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAenQLD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 468 SPIVhlVWRDGTYDMVAFQQMMKYG-RTSATEF-GDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK08155 466 VKII--LMNNEALGLVHQQQSLFYGqRVFAATYpGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRID 543
|
570
....*....|...
gi 446025664 546 yrdnikLSEKLLP 558
Cdd:PRK08155 544 ------AEEKVYP 550
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
16-550 |
7.71e-86 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 277.23 E-value: 7.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGL 95
Cdd:PRK06725 17 GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVTGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 96 VTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDVM 175
Cdd:PRK06725 97 ADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKDVQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 176 TAETTVESIGALSKPQLGIAPTHD---ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAIS 252
Cdd:PRK06725 177 NEKVTSFYNEVVEIPGYKPEPRPDsmkLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGAYP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 253 RElEDHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQPERELIGDi 328
Cdd:PRK06725 257 PG-DPLFLGMLGMHGTYAANMAVTECDLLLALG---VRFDDRVTGKLElfspHSKKVHIDIDPSEFHKNVAVEYPVVGD- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 329 altVNSIAEKLPKLVLSTKSEAVLERLRAkLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCF 408
Cdd:PRK06725 332 ---VKKALHMLLHMSIHTQTDEWLQKVKT-WKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 409 RSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMV-AFQQ 487
Cdd:PRK06725 408 KAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVrQWQE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 488 MMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNI 550
Cdd:PRK06725 488 MFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENV 550
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
13-545 |
3.36e-76 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 252.05 E-value: 3.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 13 KTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQER-GPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNL 91
Cdd:PRK08979 3 MLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKsGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 92 ATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLP 171
Cdd:PRK08979 83 ITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QDVMTAETTVESIGALSKPQLGIAPT---H--DITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQ 246
Cdd:PRK08979 163 KDCLNPAILHPYEYPESIKMRSYNPTtsgHkgQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 247 AAGAISRElEDHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQPER 322
Cdd:PRK08979 243 GLGAFPGT-HKNSLGMLGMHGRYEANMAMHNADLIFGIG---VRFDDRTTNNLEkycpNATILHIDIDPSSISKTVRVDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 323 ELIGdialTVNSIAEKLPKLVLSTKSEAVLERLRAKLSEQAEVPNR------PSEGVTHPLQVIRTLRSLISDDTTVTCD 396
Cdd:PRK08979 319 PIVG----SADKVLDSMLALLDESGETNDEAAIASWWNEIEVWRSRnclaydKSSERIKPQQVIETLYKLTNGDAYVASD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 397 IGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWR 476
Cdd:PRK08979 395 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLN 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446025664 477 DGTYDMVA-FQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALA-ADGPVIIDIPID 545
Cdd:PRK08979 475 NRFLGMVKqWQDMIYQGRHSHSYMDSVpDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVD 546
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
16-549 |
5.96e-75 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 249.24 E-value: 5.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL-QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIfQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPrtdrlkrTH-------QSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATL 167
Cdd:PRK09107 93 LQDALMDSIPLVCITGQVP-------THligsdafQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 168 VSLPQDVMTAEttvesiGALSKPQlgIAPTHD------------ITYVVEKIKAAKLPVILL--GMRASTNEVTKAVREL 233
Cdd:PRK09107 166 VDIPKDVQFAT------GTYTPPQ--KAPVHVsyqpkvkgdaeaITEAVELLANAKRPVIYSggGVINSGPEASRLLREL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 234 IADTELPVVETYQAAGAISRELEDhFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLGD----RTIIHLDD 309
Cdd:PRK09107 238 VELTGFPITSTLMGLGAYPASGKN-WLGMLGMHGTYEANMAMHDCDVMLCVG---ARFDDRITGRLDAfspnSKKIHIDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 310 HQADIDHDYQPERELIGDIALTVNSIAEKLPKLVLSTKSEAV------LERLRAKLSeqaeVPNRPSEGVTHPLQVIRTL 383
Cdd:PRK09107 314 DPSSINKNVRVDVPIIGDVGHVLEDMLRLWKARGKKPDKEALadwwgqIARWRARNS----LAYTPSDDVIMPQYAIQRL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 384 RSLISD-DTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELET 462
Cdd:PRK09107 390 YELTKGrDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMST 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 463 AVRLNSPIVHLVWRDGTYDMV-AFQQMMKYGRTSATeFGDV--DIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVI 539
Cdd:PRK09107 470 AVQYNLPVKIFILNNQYMGMVrQWQQLLHGNRLSHS-YTEAmpDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVI 548
|
570
....*....|
gi 446025664 540 IDIPIDYRDN 549
Cdd:PRK09107 549 FDCRVANLEN 558
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
16-542 |
1.19e-74 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 248.81 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL---QERGpEL--IVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSN 90
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGGAILPIYDELykaEAEG-WLkhILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 91 LATGLVTANAESDPVVALAGAVPR----TDRLKRThqsmDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGAT 166
Cdd:PRK07418 100 LVTGIATAQMDSVPMVVITGQVPRpaigTDAFQET----DIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 167 LVSLPQDVMTAE---TTVESiGALSKPqlGIAPT-----HDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTE 238
Cdd:PRK07418 176 LIDIPKDVGQEEfdyVPVEP-GSVKPP--GYRPTvkgnpRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 239 LPVVETYQAAGAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLGD----RTIIHLDDHQA 312
Cdd:PRK07418 253 IPVTTTLMGKGAFD---EHHplSVGMLGMHGTAYANFAVTECDLLIAVG---ARFDDRVTGKLDEfasrAKVIHIDIDPA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 313 DIDHDYQPERELIGDIALTVNSIAEKLPKLVLSTKSEAVLERL-RAKLSEQAEVPnrPSEGVTHPLQVIRTLRSLiSDDT 391
Cdd:PRK07418 327 EVGKNRRPDVPIVGDVRKVLVKLLERSLEPTTPPRTQAWLERInRWKQDYPLVVP--PYEGEIYPQEVLLAVRDL-APDA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 392 TVTCDIGSHSIWMARCFRSyEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIV 471
Cdd:PRK07418 404 YYTTDVGQHQMWAAQFLRN-GPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVK 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446025664 472 HLVWRDGTYDMVAFQQMMKYG-RTSAT--EFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDI 542
Cdd:PRK07418 483 TVIINNGWQGMVRQWQESFYGeRYSASnmEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDV 556
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
16-545 |
2.35e-73 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 244.27 E-value: 2.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL-QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGAVLHIYDALfKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDV 174
Cdd:PRK06466 86 IATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 175 MTAETTVE-------SIGALSKPQLGiaPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQA 247
Cdd:PRK06466 166 TNPAEKFEyeypkkvKLRSYSPAVRG--HSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 248 AGAISRElEDHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQPERE 323
Cdd:PRK06466 244 LGGFPGT-DRQFLGMLGMHGTYEANMAMHHADVILAVG---ARFDDRVTNGPAkfcpNAKIIHIDIDPASISKTIKADIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 324 LIGDIALTVNSIAEKLpKLVLSTKSEAVLERLRAKLSEQAEVP-----NRPSEGVTHPLQVIRTLRSLISDDTTVTCDIG 398
Cdd:PRK06466 320 IVGPVESVLTEMLAIL-KEIGEKPDKEALAAWWKQIDEWRGRHglfpyDKGDGGIIKPQQVVETLYEVTNGDAYVTSDVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 399 SHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDG 478
Cdd:PRK06466 399 QHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNG 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 479 TYDMVAFQQMMKYGRTSATEFGDV--DIVKYAESFGATGLRVNTPDELEGVLKSALA-ADGPVIIDIPID 545
Cdd:PRK06466 479 ALGMVRQWQDMQYEGRHSHSYMESlpDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVD 548
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
11-558 |
1.05e-72 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 242.74 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 11 KTKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSN 90
Cdd:PRK07710 13 EKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 91 LATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSL 170
Cdd:PRK07710 93 VVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 171 PQDVMTAETTVESIGALSKPqlGIAPTHD-----ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETY 245
Cdd:PRK07710 173 PKDMVVEEGEFCYDVQMDLP--GYQPNYEpnllqIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 246 QAAGAISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGY---DPIEYDPKFWNKlgDRTIIHLDDHQADIDHDYQP 320
Cdd:PRK07710 251 LGLGGFP---ADHplFLGMAGMHGTYTANMALYECDLLINIGArfdDRVTGNLAYFAK--EATVAHIDIDPAEIGKNVPT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 321 ERELIGDIALTVNSIAEKLPKlvlSTKSEAVLERLrAKLSEQAEVPNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIGSH 400
Cdd:PRK07710 326 EIPIVADAKQALQVLLQQEGK---KENHHEWLSLL-KNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 401 SIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTY 480
Cdd:PRK07710 402 QMWAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEAL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 481 DMV-AFQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIpidyrdNIKLSEKLLP 558
Cdd:PRK07710 482 GMVrQWQEEFYNQRYSHSLLSCQpDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDC------RVLQSEKVMP 555
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
16-545 |
8.30e-72 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 240.14 E-value: 8.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGiDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDV 174
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 175 MTAETTVESIGALSKPQLGIAPT---H--DITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAG 249
Cdd:PRK07979 166 LNPANKLPYVWPESVSMRSYNPTtqgHkgQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMGLG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 250 AISrELEDHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDYQPERELI 325
Cdd:PRK07979 246 AFP-ATHRQSLGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLAkycpNATVLHIDIDPTSISKTVTADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 326 GDIALTVNSIAEKLPKLVLSTKSEAV------LERLRAKlseQAEVPNRPSEGVThPLQVIRTLRSLISDDTTVTCDIGS 399
Cdd:PRK07979 322 GDARQVLEQMLELLSQESAHQPLDEIrdwwqqIEQWRAR---QCLKYDTHSEKIK-PQAVIETLWRLTKGDAYVTSDVGQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 400 HSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGT 479
Cdd:PRK07979 398 HQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRY 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446025664 480 YDMV-AFQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALA---ADGPVIIDIPID 545
Cdd:PRK07979 478 LGMVkQWQDMIYSGRHSQSYMQSLpDFVRLAEAYGHVGIQISHPDELESKLSEALEqvrNNRLVFVDVTVD 548
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
8-549 |
7.68e-71 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 238.06 E-value: 7.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 8 NDVKTKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL----QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVT 83
Cdd:CHL00099 4 QLTLREKTGAFALIDSLVRHGVKHIFGYPGGAILPIYDELyaweKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 84 SGPGTSNLATGLVTANAESDPVVALAGAVPR----TDRLkrthQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSAT 159
Cdd:CHL00099 84 SGPGATNLVTGIATAQMDSVPLLVITGQVGRafigTDAF----QEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 160 STNPGATLVSLPQDVMTAETTVESI--GALSKPQLGIAPTHD-----ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRE 232
Cdd:CHL00099 160 HGRPGPVLIDIPKDVGLEKFDYYPPepGNTIIKILGCRPIYKptikrIEQAAKLILQSSQPLLYVGGGAIISDAHQEITE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 233 LIADTELPVVETYQAAGAISrelEDHFF--GRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLGD----RTIIH 306
Cdd:CHL00099 240 LAELYKIPVTTTLMGKGIFD---EDHPLclGMLGMHGTAYANFAVSECDLLIALG---ARFDDRVTGKLDEfacnAQVIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 307 LDDHQADIDHDYQPERELIGDIALTVNSIAEKL---PKLVLSTKSEAVLERL-RAKLSEQAEVPnRPSEGVThPLQVIRT 382
Cdd:CHL00099 314 IDIDPAEIGKNRIPQVAIVGDVKKVLQELLELLknsPNLLESEQTQAWRERInRWRKEYPLLIP-KPSTSLS-PQEVINE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 383 LrSLISDDTTVTCDIGSHSIWMARcFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELET 462
Cdd:CHL00099 392 I-SQLAPDAYFTTDVGQHQMWAAQ-FLKCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 463 AVRLNSPIVHLVWRDGTYDMVAFQQMMKYGRT---SATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVI 539
Cdd:CHL00099 470 IAQYNLPIKIIIINNKWQGMVRQWQQAFYGERyshSNMEEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVL 549
|
570
....*....|
gi 446025664 540 IDIPIDYRDN 549
Cdd:CHL00099 550 IDCQVIEDEN 559
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
13-550 |
2.08e-70 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 236.73 E-value: 2.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 13 KTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNL 91
Cdd:PRK06882 3 KLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGiEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 92 ATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLP 171
Cdd:PRK06882 83 ITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QDVMT----------AETTVESIGALSKPQLGiapthDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPV 241
Cdd:PRK06882 163 KDMVNpankftyeypEEVSLRSYNPTVQGHKG-----QIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 242 VETYQAAGAISRElEDHFFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHD 317
Cdd:PRK06882 238 TSSLMGLGAYPST-DKQFLGMLGMHGTYEANNAMHESDLILGIG---VRFDDRTTNNLAkycpNAKVIHIDIDPTSISKN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 318 YQPERELIGDIALTVNSIAEKLPKLVLStKSEAVLERLRAKLSEQAEVPN---RPSEGVTHPLQVIRTLRSLISDDTTVT 394
Cdd:PRK06882 314 VPAYIPIVGSAKNVLEEFLSLLEEENLA-KSQTDLTAWWQQINEWKAKKClefDRTSDVIKPQQVVEAIYRLTNGDAYVA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 395 CDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLV 474
Cdd:PRK06882 393 SDVGQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVS 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446025664 475 WRDGTYDMVA-FQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKSALA-ADGPVIIDIPIDYRDNI 550
Cdd:PRK06882 473 LNNRFLGMVKqWQDLIYSGRHSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSiKDKLVFVDVNVDETEHV 551
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
16-541 |
6.67e-70 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 236.03 E-value: 6.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKI----DSVFDVLQERGpelIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNL 91
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAIlpvyDPLFDSTKVRH---VLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 92 ATGLVTANAESDPVVALAGAVPR----TDRLkrthQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATL 167
Cdd:PRK07789 110 VTPIADANMDSVPVVAITGQVGRgligTDAF----QEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 168 VSLPQDVMTAETTVESIGALSKPqlGIAPT---H--DITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVV 242
Cdd:PRK07789 186 VDIPKDALQAQTTFSWPPRMDLP--GYRPVtkpHgkQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 243 ETYQAAGAISRELEDHfFGRVGLFRNQPGDILLEEADLVISMGydpIEYDPKFWNKLG----DRTIIHLDDHQADIDHDY 318
Cdd:PRK07789 264 TTLMARGAFPDSHPQH-LGMPGMHGTVAAVAALQRSDLLIALG---ARFDDRVTGKLDsfapDAKVIHADIDPAEIGKNR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 319 QPERELIGDialtvnsIAEKLPKLVLSTKSEAV------LERLRAKLSE-QAEVP---NRPSEGVTHPLQVIRTLRSLIS 388
Cdd:PRK07789 340 HADVPIVGD-------VKEVIAELIAALRAEHAaggkpdLTAWWAYLDGwRETYPlgyDEPSDGSLAPQYVIERLGEIAG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 389 DDTTVTCDIGSHSIWMARcFRSYE-PRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLN 467
Cdd:PRK07789 413 PDAIYVAGVGQHQMWAAQ-FIDYEkPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEG 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 468 SPIVHLVWRDGTYDMVAFQQMMKY-GRTSATEFGD-----VDIVKYAESFGATGLRVNTPDELEGVLKSALAA-DGPVII 540
Cdd:PRK07789 492 IPIKVALINNGNLGMVRQWQTLFYeERYSNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAInDRPVVI 571
|
.
gi 446025664 541 D 541
Cdd:PRK07789 572 D 572
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-545 |
9.68e-66 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 224.25 E-value: 9.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 1 MSTGVKANDVKTKTKGADLVVDCLIKQGVTHVFG--IPGAkidsVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPG 78
Cdd:PRK06112 1 LSKPLSAPGFTLNGTVAHAIARALKRHGVEQIFGqsLPSA----LFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 79 VCLVTSGPGTSNLATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSA 158
Cdd:PRK06112 77 VVTAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 159 TSTNPGATLVSLPQDVMTAETtvESIGALSKPQLG-------IAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVR 231
Cdd:PRK06112 157 TSGRPGPVVLLLPADLLTAAA--AAPAAPRSNSLGhfpldrtVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 232 ELIADTELPVVETYQAAGAISrelEDH---------FFGRVGLFRNQPGdiLLEEADLVISMGYDPIEYDPKFWNKL-GD 301
Cdd:PRK06112 235 ALQSLAGLPVATTNMGKGAVD---ETHplslgvvgsLMGPRSPGRHLRD--LVREADVVLLVGTRTNQNGTDSWSLYpEQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 302 RTIIHLDDHQADIDHDYQPEReLIGDIALTVNSIAEKLPKLVLSTKS------EAVLERLRAK-LSEQAEVpnRPSEGV- 373
Cdd:PRK06112 310 AQYIHIDVDGEEVGRNYEALR-LVGDARLTLAALTDALRGRDLAARAgrraalEPAIAAGREAhREDSAPV--ALSDASp 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 374 THPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPR-RLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGG 452
Cdd:PRK06112 387 IRPERIMAELQAVLTGDTIVVADASYSSIWVANFLTARRAGmRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 453 FLFSAMELETAVRLNSPIVHLVWRDGtydMVAFQ---QMMKYGR-TSATEFGDVDIVKYAESFGATGLRVNTPDELEGVL 528
Cdd:PRK06112 467 FAHVWAELETARRMGVPVTIVVLNNG---ILGFQkhaETVKFGThTDACHFAAVDHAAIARACGCDGVRVEDPAELAQAL 543
|
570
....*....|....*..
gi 446025664 529 KSALAADGPVIIDIPID 545
Cdd:PRK06112 544 AAAMAAPGPTLIEVITD 560
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
16-544 |
2.22e-65 |
|
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: 223.17 E-value: 2.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPEL--IVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLAT 93
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAERDRIhyIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 94 GLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNpGATLVSLPQD 173
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYAHN-GVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 174 VMTAETTVESIGALSKP-QLGIAPTHD---ITYVVEKIKAAKLPVILLGM--RASTNEVTKAVRELiadtELPVVETYQA 247
Cdd:TIGR02720 160 FGWQEIPDNDYYASSVSyQTPLLPAPDveaVTRAVQTLKAAERPVIYYGIgaRKAGEELEALSEKL----KIPLISTGLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 248 AGAIsrelEDHFFGRVG-LFR--NQPGDILLEEADLVISMGYD-----------------PIEYDPKfwnKLGDRTiiHL 307
Cdd:TIGR02720 236 KGII----EDRYPAYLGsAYRvaQKPANEALFQADLVLFVGNNypfaevskafkntkyfiQIDIDPA---KLGKRH--HT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 308 DdhqADIDHDYQPERELIgdiaLTVNSIAEKLPKLVLSTKSEAVLERLRAKLSEQAEVPNRPSegvthplQVIRTLRSLI 387
Cdd:TIGR02720 307 D---IAVLADAKKALAAI----LAQVEPRESTPWWQANVANVKNWRAYLASLEDKTEGPLQAY-------QVYRAINKIA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 388 SDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLN 467
Cdd:TIGR02720 373 EDDAIYSIDVGDININSNRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYH 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446025664 468 SPIVHLVWRDGTYDMVAFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSA--LAADGPVIIDIPI 544
Cdd:TIGR02720 453 LPVINIVFSNCTYGFIKDEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKI 531
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
10-550 |
1.44e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 220.85 E-value: 1.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 10 VKTKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL-QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGT 88
Cdd:PRK07282 6 LESPKSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIyNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 89 SNLATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLV 168
Cdd:PRK07282 86 TNAITGIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 169 SLPQDVMTAETTVESIGALSKP--QLGIAPT-HDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETY 245
Cdd:PRK07282 166 DLPKDVSALETDFIYDPEVNLPsyQPTLEPNdMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 246 QAAG--AISRELedhFFGRVGLFRNQPGDILLEEADLVISMGY---DPIEYDPKFWNKlgDRTIIHLDDHQADIDHDYQP 320
Cdd:PRK07282 246 LGQGtiATSHPL---FLGMGGMHGSYAANIAMTEADFMINIGSrfdDRLTGNPKTFAK--NAKVAHIDIDPAEIGKIIKT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 321 ERELIGDIALTVNSIAEkLPKlvLSTKSEAVLERLrakLSEQAEVPN-RPSEGVTHPLQVIRTLRSLISDDTTVTCDIGS 399
Cdd:PRK07282 321 DIPVVGDAKKALQMLLA-EPT--VHNNTEKWIEKV---TKDKNRVRSyDKKERVVQPQAVIERIGELTNGDAIVVTDVGQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 400 HSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGT 479
Cdd:PRK07282 395 HQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHS 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 480 YDMV-AFQQMMKYGRTSATEFGDV-DIVKYAESFGATGLRVNTPDELEGVLKsALAADGPVIIDIPIDYRDNI 550
Cdd:PRK07282 475 LGMVrQWQESFYEGRTSESVFDTLpDFQLMAQAYGIKHYKFDNPETLAQDLE-VITEDVPMLIEVDISRKEHV 546
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
15-542 |
1.81e-64 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 220.76 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 15 KGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQeRGPEL--IVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLA 92
Cdd:PLN02470 14 KGADILVEALEREGVDTVFAYPGGASMEIHQALT-RSNCIrnVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 93 TGLVTANAESDPVVALAGAVPR----TDRLKRThqsmDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLV 168
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRrmigTDAFQET----PIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 169 SLPQDVMTA------ETTVESIGALSKpqLGIAPTHD-ITYVVEKIKAAKLPVILLG---MRAStnevtKAVRELIADTE 238
Cdd:PLN02470 169 DIPKDIQQQlavpnwNQPMKLPGYLSR--LPKPPEKSqLEQIVRLISESKRPVVYVGggcLNSS-----EELREFVELTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 239 LPVVETYQAAGAI--SRELEDHFFGRVG-LFRNQPGDilleEADLVISMGydpIEYDPKFWNKL----GDRTIIHLDDHQ 311
Cdd:PLN02470 242 IPVASTLMGLGAFpaSDELSLQMLGMHGtVYANYAVD----SADLLLAFG---VRFDDRVTGKLeafaSRASIVHIDIDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 312 ADIDHDYQPERELIGDIAL---TVNSIAEKLPKLVLSTKSeavlerLRAKLSEQ-AEVPNR-PSEGVTHPLQ-VIRTLRS 385
Cdd:PLN02470 315 AEIGKNKQPHVSVCADVKLalqGLNKLLEERKAKRPDFSA------WRAELDEQkEKFPLSyPTFGDAIPPQyAIQVLDE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 386 LISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVR 465
Cdd:PLN02470 389 LTDGNAIISTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 466 LNSPIVHLVWRDGTYDMVAFQQMMKYGRTSA-TEFGD--------VDIVKYAESFGATGLRVNTPDELEGVLKSALAADG 536
Cdd:PLN02470 469 ENLPVKIMVLNNQHLGMVVQWEDRFYKANRAhTYLGDpdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPG 548
|
....*.
gi 446025664 537 PVIIDI 542
Cdd:PLN02470 549 PYLLDV 554
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
12-542 |
1.84e-64 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 219.85 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 12 TKTKGADLVvDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNL 91
Cdd:PRK07524 1 MTTCGEALV-RLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 92 ATGLVTANAESDPVVALAGaVPRTDRLK----RTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATL 167
Cdd:PRK07524 80 ATAMGQAYADSIPMLVISS-VNRRASLGkgrgKLHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 168 VSLPQDVMTAETTVESIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEvtKAVRELIADTELPVVETYQA 247
Cdd:PRK07524 159 IEIPLDVLAAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAA--AALRALAERLDAPVALTINA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 248 AGAISReleDHFFgRVGlfRNQ---PGDILLEEADLVISMGYD--PIEYDPKFWNKLG-DRTIIHLDDHQADIDHDYQPE 321
Cdd:PRK07524 237 KGLLPA---GHPL-LLG--ASQslpAVRALIAEADVVLAVGTElgETDYDVYFDGGFPlPGELIRIDIDPDQLARNYPPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 322 RELIGDIALTVNSIAEKLPKLVLSTKSEAV-LERLRAKLSEQAEVPNRPSEGVthplqvIRTLRSLISD-----DTTVTC 395
Cdd:PRK07524 311 LALVGDARAALEALLARLPGQAAAADWGAArVAALRQALRAEWDPLTAAQVAL------LDTILAALPDaifvgDSTQPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 396 DIGSHSIWMARcfrsyePRRLL-FSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLV 474
Cdd:PRK07524 385 YAGNLYFDADA------PRRWFnASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 475 WRDGTYdmvafQQMMKYGRTSATEFGDVDI-----VKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDI 542
Cdd:PRK07524 459 WNNDGY-----GEIRRYMVARDIEPVGVDPytpdfIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
16-550 |
1.31e-63 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 218.52 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVL-QERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIYDELyKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDV 174
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 175 ---MTAETTVESIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAI 251
Cdd:PRK06965 183 sktPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGLGAY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 252 sRELEDHFFGRVGLFRNQPGDILLEEADLVISMGY---DPIEYDPKFWNKLgDRTIIHLDDHQADIDHDYQPERELIGDI 328
Cdd:PRK06965 263 -PASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGArfdDRVIGNPAHFASR-PRKIIHIDIDPSSISKRVKVDIPIVGDV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 329 ALTVNSIAEKLPKLVLSTKSEAV---LERLRAKLSEQAEVPNRPSEgVTHPLQVIRTLRSLISDDTTVTCDIGSHSIWMA 405
Cdd:PRK06965 341 KEVLKELIEQLQTAEHGPDADALaqwWKQIEGWRSRDCLKYDRESE-IIKPQYVVEKLWELTDGDAFVCSDVGQHQMWAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 406 RCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAF 485
Cdd:PRK06965 420 QFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVRQ 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446025664 486 QQMMKYGRTSATEFGDV--DIVKYAESFGATGLRVNTPDELEGVLKSALA-ADGPVIIDIPIDYRDNI 550
Cdd:PRK06965 500 WQEIEYSKRYSHSYMDAlpDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDFQTDPTENV 567
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
17-545 |
2.43e-63 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 217.00 E-value: 2.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 17 ADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGLV 96
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 97 TANAESDPVVALAGAVpRTDRLKRTH-QSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNpGATLVSLPQDV- 174
Cdd:PRK06457 85 DAKMDHAPVIALTGQV-ESDMIGHDYfQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDIl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 175 -MTAETTVESIGALSKPQLGIapthDITYVVEKIKAAKLPVILL--GMRASTNEVTKAVRELIAdtelPVVETYQAAGAI 251
Cdd:PRK06457 163 rKSSEYKGSKNTEVGKVKYSI----DFSRAKELIKESEKPVLLIggGTRGLGKEINRFAEKIGA----PIIYTLNGKGIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 252 SrELEDHFFGRVGLFRNQPGDILLEEADLVISMGyDPIEYdPKFWNKlgDRTIIHLDDHQADIDHDYQPERELIGDIA-- 329
Cdd:PRK06457 235 P-DLDPKVMGGIGLLGTKPSIEAMDKADLLIMLG-TSFPY-VNFLNK--SAKVIQVDIDNSNIGKRLDVDLSYPIPVAef 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 330 LTVNsIAEKLPKLVLSTKSEavLERLRAKLSEQAEVPNRPSEgvthPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFR 409
Cdd:PRK06457 310 LNID-IEEKSDKFYEELKGK--KEDWLDSISKQENSLDKPMK----PQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 410 SYEPRRLLFSNGMQTLGVALPWAIAATLV-EPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAF-QQ 487
Cdd:PRK06457 383 ASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFeQE 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446025664 488 MMKYgrtsaTEFG----DVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK06457 463 VMGY-----PEWGvdlyNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVD 519
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
18-172 |
5.25e-62 |
|
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: 201.22 E-value: 5.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 18 DLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGLVT 97
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446025664 98 ANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQ 172
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
16-545 |
1.39e-61 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 212.27 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGL 95
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 96 VTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQDVM 175
Cdd:PRK05858 87 AAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 176 TAETTVESI-GALSKPQLGIAPTHD-ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAISR 253
Cdd:PRK05858 167 FSMADDDGRpGALTELPAGPTPDPDaLARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 254 eleDH--FFGRVglfRNQPgdilLEEADLVISMGYdPIEYDPKFWNKLGDRTIIHLDDHQADIDHDYQPERELIGDIALT 331
Cdd:PRK05858 247 ---DHplAFSRA---RGKA----LGEADVVLVVGV-PMDFRLGFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 332 VNSIAEKLPKLV--------LSTKSEAVLERLRAKLSEQAeVPnrpsegvTHPLQVIRTLRSLISDDTTVTCDIGSHSIW 403
Cdd:PRK05858 316 LSALAGAGGDRTdhqgwieeLRTAETAARARDAAELADDR-DP-------IHPMRVYGELAPLLDRDAIVIGDGGDFVSY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 404 MARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMV 483
Cdd:PRK05858 388 AGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLE 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 484 AFQQMMKYGRTSATEFG-DVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK05858 468 KHPMEALYGYDVAADLRpGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTD 530
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
14-545 |
2.87e-60 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 209.07 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 14 TKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLAT 93
Cdd:PRK09259 10 TDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 94 GLVTANAESDPVVALAGAVPR--TDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLP 171
Cdd:PRK09259 90 ALANATTNCFPMIMISGSSEReiVDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QD----VMTAETTVESIGALSKPQLGIAPTHD-ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQ 246
Cdd:PRK09259 170 AKvlaqTMDADEALTSLVKVVDPAPAQLPAPEaVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 247 AAGAISrelEDHFFGrVGLFRNqpgdILLEEADLVI----------SMGydpieyDPKFWNklGDRTIIHLDDHQADIDH 316
Cdd:PRK09259 250 AKGLLP---DTHPQS-AAAARS----LALANADVVLlvgarlnwllSHG------KGKTWG--ADKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 317 DYQPERELIGDIALTVNSIAEKLPKL----------VLSTKSEAVLERLRAKLSEqaevpnrpsegVTHPLQ---VIRTL 383
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQNtfkapaewldALAERKEKNAAKMAEKLST-----------DTQPMNfynALGAI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 384 RSLISD--DTTV------TCDIGSHSIWMarcfrsYEPRRLLFSNGMQTLGVALPWAIAATlVEPGKKVVSVSGDGGFLF 455
Cdd:PRK09259 383 RDVLKEnpDIYLvneganTLDLARNIIDM------YKPRHRLDCGTWGVMGIGMGYAIAAA-VETGKPVVAIEGDSAFGF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 456 SAMELETAVRLNSPIVHLVWRDGTYdmvafqqmmkYGRTSATEFGDVDIV-----------KYAESFGATGLRVNTPDEL 524
Cdd:PRK09259 456 SGMEVETICRYNLPVTVVIFNNGGI----------YRGDDVNLSGAGDPSptvlvhharydKMMEAFGGVGYNVTTPDEL 525
|
570 580
....*....|....*....|.
gi 446025664 525 EGVLKSALAADGPVIIDIPID 545
Cdd:PRK09259 526 RHALTEAIASGKPTLINVVID 546
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
21-558 |
1.80e-59 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 207.41 E-value: 1.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 21 VDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGLVTANA 100
Cdd:TIGR03457 9 VEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVTAIAAAYW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 101 ESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNpGATLVSLPQDVMTAETT 180
Cdd:TIGR03457 89 AHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRDYFYGEID 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 181 VEsIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAI--SRELedh 258
Cdd:TIGR03457 168 VE-IPRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFpaSHPL--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 259 FFGRVGLFRNQPGDILLEEADLVISMG--YDPI----EYDPKFWNKlgDRTIIhlddhQADIDHDYQPERE-----LIGD 327
Cdd:TIGR03457 244 WVGPLGYQGSKAAMKLISDADVVLALGtrLGPFgtlpQYGIDYWPK--NAKII-----QVDANAKMIGLVKkvtvgICGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 328 IALTVNSIAEKLPKLVLSTKSEAVLERLRA-------KLSEQAEVPNRPSEGVT-----------HPLQVIRTLRSLISD 389
Cdd:TIGR03457 317 AKAAAAEILQRLAGKAGDANRAERKAKIQAersaweqELSEMTHERDPFSLDMIveqrqeegnwlHPRQVLRELEKAMPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 390 DTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSP 469
Cdd:TIGR03457 397 DAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 470 IVHLVWRDGTYDMVAFQQMMKYGRT-SATEF-GDVDIVKYAESFGATGLRVNTPDELEGVLKSALA--ADG-PVIIDIPI 544
Cdd:TIGR03457 477 VTAVVFRNRQWGAEKKNQVDFYNNRfVGTELeSELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAaqAEGkTTVIEIVC 556
|
570 580
....*....|....*....|.
gi 446025664 545 D-------YRDNIKLSEKLLP 558
Cdd:TIGR03457 557 TrelgdpfRRDALSKPVRLLD 577
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
16-182 |
2.80e-58 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 191.68 E-value: 2.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQER-GPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPRTDRLK-RTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQD 173
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRgALQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*....
gi 446025664 174 VMTAETTVE 182
Cdd:pfam02776 161 VLLEEVDED 169
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
396-542 |
3.18e-58 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 190.87 E-value: 3.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 396 DIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVW 475
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446025664 476 RDGTYDMVAFQQMMKYGRTSATEFG----DVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDI 542
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSGkilpPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
17-545 |
5.44e-57 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 200.91 E-value: 5.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 17 ADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERG--PELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATG 94
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADdkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 95 LVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPI-TKYSVEVEHPDNVPEALSNAFRSATSTNpGATLVSLPQD 173
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 174 VMTAE---------TTVESIGaLSKPQLgIAPTHDITYVVEKIKAAKLPVILLGM--RASTNEVTKAVRELIA------- 235
Cdd:PRK08273 165 VQELEyeppphahgTVHSGVG-YTRPRV-VPYDEDLRRAAEVLNAGRKVAILVGAgaLGATDEVIAVAERLGAgvakall 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 236 -----DTELPVVetyqaAGAIsreledhffgrvGLFRNQPGDILLEEAD--LVISMGYDPIEYDPKFwnklGD-RTIihl 307
Cdd:PRK08273 243 gkaalPDDLPWV-----TGSI------------GLLGTKPSYELMRECDtlLMVGSSFPYSEFLPKE----GQaRGV--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 308 ddhQADIDHD-----YQPERELIGDIALTVNSIaekLPKLVLST------KSEAVLERLRAKLSEQAEVPNRPsegvTHP 376
Cdd:PRK08273 299 ---QIDIDGRmlglrYPMEVNLVGDAAETLRAL---LPLLERKKdrswreRIEKWVARWWETLEARAMVPADP----VNP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 377 LQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFS 456
Cdd:PRK08273 369 QRVFWELSPRLPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 457 AM-ELETAVRL-----NSPIVHLVWRDGTYDMVAFQQ--MMKYGRTSAT-EFGDVDIVKYAESFGATGLRVNTPDELEGV 527
Cdd:PRK08273 449 GMaELITVAKYwrqwsDPRLIVLVLNNRDLNQVTWEQrvMEGDPKFEASqDLPDVPYARFAELLGLKGIRVDDPEQLGAA 528
|
570
....*....|....*...
gi 446025664 528 LKSALAADGPVIIDIPID 545
Cdd:PRK08273 529 WDEALAADRPVVLEVKTD 546
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
21-558 |
7.89e-57 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 200.22 E-value: 7.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 21 VDCLIKQGVTHVFGIPGAKIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGLVTANA 100
Cdd:PRK07525 13 VETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 101 ESDPVVAL---AGavprtdrlKRT-----HQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNpGATLVSLPQ 172
Cdd:PRK07525 93 AHTPVVLVtpqAG--------TKTigqggFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 173 DVMTAETTVEsIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRAStneVTKAVRELIADTEL---PVVETYQAAG 249
Cdd:PRK07525 164 DYFYGVIDVE-IPQPVRLERGAGGEQSLAEAAELLSEAKFPVILSGAGVV---LSDAIEECKALAERldaPVACGYLHND 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 250 AISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMG-----------YDpIEYDPKfwnklgDRTIIhlddhQADIDH 316
Cdd:PRK07525 240 AFP---GSHplWVGPLGYNGSKAAMELIAKADVVLALGtrlnpfgtlpqYG-IDYWPK------DAKII-----QVDINP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 317 D-----YQPERELIGDIALTVNSIAEKL-PKLVLSTKSEAVLERLRA-------KLSEQAEVPNRPS-----------EG 372
Cdd:PRK07525 305 DrigltKKVSVGICGDAKAVARELLARLaERLAGDAGREERKALIAAeksaweqELSSWDHEDDDPGtdwneeararkPD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 373 VTHPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRR----LLFSNgmqtLGVALPWAIAATLVEPGKKVVSVS 448
Cdd:PRK07525 385 YMHPRQALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKylapGSFGN----CGYAFPAIIGAKIACPDRPVVGFA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 449 GDGGFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAFQQMMKYG-RTSATEF-GDVDIVKYAESFGATGLRVNTPDELEG 526
Cdd:PRK07525 461 GDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNnRFVGTELdNNVSYAGIAEAMGAEGVVVDTQEELGP 540
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 446025664 527 VLKSALAADG---PVIIDIPIDY-------RDNIKLSEKLLP 558
Cdd:PRK07525 541 ALKRAIDAQNegkTTVIEIMCNQelgepfrRDALKKPVRVLG 582
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
15-542 |
6.90e-56 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 197.34 E-value: 6.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 15 KGADLVVDCLIKQGVTHVFGIPgakIDSVFDVLQERGPELIVCRHEQNAAFMAAAIGRLTG--KPGVCLVTSGPGTSNLA 92
Cdd:PRK06154 21 KVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 93 TGLVTANAESDPVVALAGAVPRtdRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVSLPQ 172
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPR--GSTDVAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 173 DVMtaETTVESIGALSKPQLGIAPTHDITYVVEKIK---AAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAG 249
Cdd:PRK06154 176 DVL--AEELDELPLDHRPSRRSRPGADPVEVVEAAAlllAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 250 AISrelEDH--FFGRVGLFRNQPGDILLEEADLVISMGYDPIEYD-----PKfwnklgDRTIIHLDDHQADIDHDYQPER 322
Cdd:PRK06154 254 AFP---EDHplALGSGGRARPATVAHFLREADVLFGIGCSLTRSYyglpmPE------GKTIIHSTLDDADLNKDYPIDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 323 ELIGDIALTVNSIAEKLPKLVLSTKSE-----AVLERLRAKLSEQAEvPNRPSEGV-THPLQVIRTLRSLISDDTT-VTC 395
Cdd:PRK06154 325 GLVGDAALVLKQMIEELRRRVGPDRGRaqqvaAEIEAVRAAWLAKWM-PKLTSDSTpINPYRVVWELQHAVDIKTViITH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 396 DIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVW 475
Cdd:PRK06154 404 DAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILL 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 476 RD---GTYDMVAFQQMMKYGRTSATefGDVDIVkyAESFGATGLRVNTPDELEGVLKSAL--AADG-PVIIDI 542
Cdd:PRK06154 484 NNfsmGGYDKVMPVSTTKYRATDIS--GDYAAI--ARALGGYGERVEDPEMLVPALLRALrkVKEGtPALLEV 552
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
378-544 |
8.42e-54 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 180.14 E-value: 8.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 378 QVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSA 457
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 458 MELETAVRLNSPIVHLVWRDGTYDMVAFQQMMKY-GRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADG 536
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYgGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 446025664 537 PVIIDIPI 544
Cdd:cd00568 161 PALIEVKT 168
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
12-550 |
2.88e-53 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 190.58 E-value: 2.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 12 TKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLT-GKPGVCLVTSGPGTS 89
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGiRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 90 NLATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLVS 169
Cdd:PRK11269 82 DMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 170 LPQDVMTAE-----TTVESIgALSKPqlgiAPTH-DITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVE 243
Cdd:PRK11269 162 LPFDVQVAEiefdpDTYEPL-PVYKP----AATRaQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 244 TYQAAGAISrelEDH--FFGRVGLFRNQP-GDILLEEADLVISMGydpieydPKFWNK--------LGDRTIIHLDDHQA 312
Cdd:PRK11269 237 TLMGWGAIP---DDHplMAGMVGLQTSHRyGNATLLASDFVLGIG-------NRWANRhtgsvevyTKGRKFVHVDIEPT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 313 DIDHDYQPERELIGD--IALTV-------NSIAEKLPKlvLSTKSEAVLERLRAKL--SEQAEVPNRPSegvthplQVIR 381
Cdd:PRK11269 307 QIGRVFGPDLGIVSDakAALELlvevareWKAAGRLPD--RSAWVADCQERKRTLLrkTHFDNVPIKPQ-------RVYE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 382 TLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELE 461
Cdd:PRK11269 378 EMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 462 TAVRLNSPIVHLVWRDG----------TYDMvAFQQMMKYGRTSATEFGD--VDIVKYAESFGATGLRVNTPDELEGVLK 529
Cdd:PRK11269 458 VGAQFNLPYIHVLVNNAylglirqaqrAFDM-DYCVQLAFENINSPELNGygVDHVKVAEGLGCKAIRVFKPEDIAPALE 536
|
570 580
....*....|....*....|....*
gi 446025664 530 SA--LAADG--PVIIDIPIDYRDNI 550
Cdd:PRK11269 537 QAkaLMAEFrvPVVVEVILERVTNI 561
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
17-542 |
3.88e-52 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 187.12 E-value: 3.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 17 ADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGL 95
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTiEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 96 VTANAESDPVVALAGAVPRT----DRLKRTHQSmdnaALFEPITKYSVEVEHPDNVPEALSNAFRSATStNPGATLVSLP 171
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSeigsGYFQETHPQ----ELFRECSHYCELVSNPEQLPRVLAIAMRKAIL-NRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QDVMTAETTVESIGALSKPQLGIA--PTHDITYVVEKIKAAKlPVILL---GMRASTNEVTKAVRELIAdtelPVVETYQ 246
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVtpAEEELRKLAALLNGSS-NITLLcgsGCAGAHDELVALAETLKA----PIVHALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 247 AAGAIsrELEDHF-FGRVGLFRNQPGDILLEEADLVISMGYDpIEYDPkFWNKlgDRTIIHLDDHQADIDHDYQPERELI 325
Cdd:PRK09124 236 GKEHV--EYDNPYdVGMTGLIGFSSGYHAMMNCDTLLMLGTD-FPYRQ-FYPT--DAKIIQIDINPGSLGRRSPVDLGLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 326 GDIALTVNSIaekLPKLVLST------KSEAVLERLRAKLSEQAeVPNRPSEGVtHPLQVIRTLRSLISDDTTVTCDIGS 399
Cdd:PRK09124 310 GDVKATLAAL---LPLLEEKTdrkfldKALEHYRKARKGLDDLA-VPSDGGKPI-HPQYLARQISEFAADDAIFTCDVGT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 400 HSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGT 479
Cdd:PRK09124 385 PTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446025664 480 YDMVAFQqmMKYG--RTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDI 542
Cdd:PRK09124 465 LGFVAME--MKAGgyLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDV 527
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
375-550 |
5.74e-51 |
|
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: 173.07 E-value: 5.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 375 HPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFL 454
Cdd:cd02015 2 KPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 455 FSAMELETAVRLNSPIVHLVWRDGTYDMVA-FQQMMKYGRTSATEFGD-VDIVKYAESFGATGLRVNTPDELEGVLKSAL 532
Cdd:cd02015 82 MNIQELATAAQYNLPVKIVILNNGSLGMVRqWQELFYEGRYSHTTLDSnPDFVKLAEAYGIKGLRVEKPEELEAALKEAL 161
|
170
....*....|....*...
gi 446025664 533 AADGPVIIDIPIDYRDNI 550
Cdd:cd02015 162 ASDGPVLLDVLVDPEENV 179
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
12-542 |
5.54e-50 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 180.57 E-value: 5.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 12 TKTKGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSN 90
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKiRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 91 LATGLVTANAESDPVVALAGAVPRT--DR-LKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATL 167
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPylDQdLGYIHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 168 VSLPQDVMTAETTVESIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGmrASTNEVTKAVRELiADTELPVVETYQA 247
Cdd:PRK07064 161 VEIPIDIQAAEIELPDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLG--GGARHAGAEVKRL-VDLGFGVVTSTQG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 248 AGAISrelEDHFfGRVGLFRNQPG-DILLEEADLVISMG-----YDPIEYDPKFwnklgDRTIIHLDDHQADIDHDYQPE 321
Cdd:PRK07064 238 RGVVP---EDHP-ASLGAFNNSAAvEALYKTCDLLLVVGsrlrgNETLKYSLAL-----PRPLIRVDADAAADGRGYPND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 322 RELIGDIALTVNSIAEKLPK----------LVLSTKSEAVlERLRAKLSEQAEVPNrpsegvthplqvirTLRSLISDDT 391
Cdd:PRK07064 309 LFVHGDAARVLARLADRLEGrlsvdpafaaDLRAAREAAV-ADLRKGLGPYAKLVD--------------ALRAALPRDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 392 TVTCDIG-SHSIWMARCFRSYEPRRLLFSNGmQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPI 470
Cdd:PRK07064 374 NWVRDVTiSNSTWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANM 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446025664 471 VHLVWRDGTYD-MVAFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDI 542
Cdd:PRK07064 453 VIVLMNDGGYGvIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
16-534 |
1.03e-48 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 177.88 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPG---AKIDSVFDVLQERG---PELIVCRHEqNAAfMAAAIG--RLTGKPGVCLVTSGPG 87
Cdd:PRK08327 9 AAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGrplPEFVICPHE-IVA-ISMAHGyaLVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 88 TSNLATGLVTANAESDPVVALAGAVP---------RTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSA 158
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFAGRSPyteegelgsRNTRIHWTQEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 159 TSTNPGATLVSLPQDVMtaETTVESIGALSKPQLGIAPTH----DITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELI 234
Cdd:PRK08327 167 MSEPKGPVYLTLPREVL--AEEVPEVKADAGRQMAPAPPApdpeDIARAAEMLAAAERPVIITWRAGRTAEGFASLRRLA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 235 ADTELPVVETyqaagaISRELE---DHffgrvGLFRNQPGDILLEEADLVISMGYD----PIEYDPKFwnklgDRTIIHL 307
Cdd:PRK08327 245 EELAIPVVEY------AGEVVNypsDH-----PLHLGPDPRADLAEADLVLVVDSDvpwiPKKIRPDA-----DARVIQI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 308 DdhqADIDHDYQPERE------LIGDIALTVNSIAEKL-------PKLVLSTKSEAVLERLRAKLSEQAEVPNRPSEGVT 374
Cdd:PRK08327 309 D---VDPLKSRIPLWGfpcdlcIQADTSTALDQLEERLkslasaeRRRARRRRAAVRELRIRQEAAKRAEIERLKDRGPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 375 HPLQVIRTLRSLISDDTTVtcdigshsiwmarcFRSYEPR----RL-----LFSNGMQ-TLGVALPWAIAATLVEPGKKV 444
Cdd:PRK08327 386 TPAYLSYCLGEVADEYDAI--------------VTEYPFVprqaRLnkpgsYFGDGSAgGLGWALGAALGAKLATPDRLV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 445 VSVSGDGGFLFSAME--LETAVRLNSPIVHLVWRDGTYDMVAFQQMMKY--------GRTSATEFG-DVDIVKYAESFGA 513
Cdd:PRK08327 452 IATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYpegyaarkGTFPGTDFDpRPDFAKIAEAFGG 531
|
570 580
....*....|....*....|.
gi 446025664 514 TGLRVNTPDELEGVLKSALAA 534
Cdd:PRK08327 532 YGERVEDPEELKGALRRALAA 552
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
17-545 |
1.69e-47 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 174.41 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 17 ADLVVDCLIKQGVTHVFGIPGAKIDSVFD-VLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGL 95
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDaVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 96 VTANAESDPVVALAGAVPR----TDRLKRTHQSmdnaALFEPITKYSVEVEHPDNVPEALSNAFRSATsTNPGATLVSLP 171
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSaqigSGFFQETHPD----RLFVECSGYCEMVSSAEQAPRVLHSAIQHAV-AGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 172 QDVMT---AETTVESIGALSKPQLGIAPThDITYVVEKIKAAKLPVILLGmrASTNEVTKAVRELIADTELPVVETYQAA 248
Cdd:PRK06546 161 GDIADepaPEGFAPSVISPRRPTVVPDPA-EVRALADAINEAKKVTLFAG--AGVRGAHAEVLALAEKIKAPVGHSLRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 249 GAISReleDHFF--GRVGLFRNQPGDILLEEADLVISMG----YDP---------IEYDPKfwnKLGDRTIIHLDDHqad 313
Cdd:PRK06546 238 EWIQY---DNPFdvGMSGLLGYGAAHEAMHEADLLILLGtdfpYDQflpdvrtaqVDIDPE---HLGRRTRVDLAVH--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 314 idhdyqpereliGDIALTVNSIaekLPkLVLSTKSEAVLERLrakLSEQAEVPNRPSEGVT---------HPLQVIRTLR 384
Cdd:PRK06546 309 ------------GDVAETIRAL---LP-LVKEKTDRRFLDRM---LKKHARKLEKVVGAYTrkvekhtpiHPEYVASILD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 385 SLISDDTTVTCDIGSHSIWMARCFRSYEPRRLL--FSNGmqTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELET 462
Cdd:PRK06546 370 ELAADDAVFTVDTGMCNVWAARYITPNGRRRVIgsFRHG--SMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 463 AVRLNSPIVHLVWRDGTYDMVAFqQMMKYGRTS-ATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIID 541
Cdd:PRK06546 448 VKLYDLPVKVVVFNNSTLGMVKL-EMLVDGLPDfGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVD 526
|
....
gi 446025664 542 IPID 545
Cdd:PRK06546 527 VVTD 530
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
375-545 |
2.94e-45 |
|
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: 157.69 E-value: 2.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 375 HPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFL 454
Cdd:cd02014 3 HPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 455 FSAMELETAVRLNSPIVHLVWRDGTYDMVAF-QQMMKYGRtSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALA 533
Cdd:cd02014 83 MLMGDLITAVKYNLPVIVVVFNNSDLGFIKWeQEVMGQPE-FGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALA 161
|
170
....*....|..
gi 446025664 534 ADGPVIIDIPID 545
Cdd:cd02014 162 ADGPVVIDVVTD 173
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
15-178 |
2.91e-44 |
|
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: 154.25 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 15 KGADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLAT 93
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKiEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 94 GLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATStNPGATLVSLPQD 173
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIA-KRGVAVLILPGD 159
|
....*
gi 446025664 174 VMTAE 178
Cdd:cd07039 160 VQDAP 164
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
376-545 |
3.99e-40 |
|
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: 143.44 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 376 PLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLF 455
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 456 SAMELETAVRLNSPIVHLVWRDGTYDMVAFQQ--MMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALA 533
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 446025664 534 ADGPVIIDIPID 545
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
18-545 |
1.18e-35 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 140.09 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 18 DLVVDCLIKQGVTHVFGIPGAKidsvfdvlqergpEL------------IVCRHEQNAAFMAAAIGRLTGKPGVCLVTSG 85
Cdd:PRK07092 16 DATIDLLRRFGITTVFGNPGST-------------ELpflrdfpddfryVLGLQEAVVVGMADGYAQATGNAAFVNLHSA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 86 PGTSNLATGLVTANAESDPVVALAGAVPRtdrlkrthqSM----------DNAALFEPITKYSVEVEHPDNVPEALSNAF 155
Cdd:PRK07092 83 AGVGNAMGNLFTAFKNHTPLVITAGQQAR---------SIlpfepflaavQAAELPKPYVKWSIEPARAEDVPAAIARAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 156 RSATSTNPGATLVSLPQDVMTAET------TVESIGALSKPQLgiapthdiTYVVEKIKAAKLPVILLGM---RASTNEv 226
Cdd:PRK07092 154 HIAMQPPRGPVFVSIPYDDWDQPAeplparTVSSAVRPDPAAL--------ARLGDALDAARRPALVVGPavdRAGAWD- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 227 tKAVReliadtelpVVETYQAAGAISREL------EDHffgrvGLFRN----QPGDI--LLEEADLVISMG--------Y 286
Cdd:PRK07092 225 -DAVR---------LAERHRAPVWVAPMSgrcsfpEDH-----PLFAGflpaSREKIsaLLDGHDLVLVIGapvftyhvE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 287 DPIEYDPkfwnklGDRTIIHL-DDHQAdidHDYQPERE-LIGDIALTVNSIAEKLPklvlstkseavlERLRAKLSEQAE 364
Cdd:PRK07092 290 GPGPHLP------EGAELVQLtDDPGE---AAWAPMGDaIVGDIRLALRDLLALLP------------PSARPAPPARPM 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 365 VPNRPSEGVT-HPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLF--SNGmqtLGVALPWAIAATLVEPG 441
Cdd:PRK07092 349 PPPAPAPGEPlSVAFVLQTLAALRPADAIVVEEAPSTRPAMQEHLPMRRQGSFYTmaSGG---LGYGLPAAVGVALAQPG 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 442 KKVVSVSGDGGFLFSAMELETAVRLNSPIVHLVWRDGTYD-MVAFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNT 520
Cdd:PRK07092 426 RRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGaLRWFAPVFGVRDVPGLDLPGLDFVALARGYGCEAVRVSD 505
|
570 580
....*....|....*....|....*
gi 446025664 521 PDELEGVLKSALAADGPVIIDIPID 545
Cdd:PRK07092 506 AAELADALARALAADGPVLVEVEVA 530
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
17-545 |
1.21e-35 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 140.29 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 17 ADLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGkPGVCLVTSGPGTSNLATGL 95
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGiRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 96 VTANAESDPVVALAGAVPRTDRLKRT--HQSM------DNAALFEPITKYSVEVEhPDNVPEALSNAFRSATSTN-PGat 166
Cdd:COG3961 87 AGAYAERVPVVHIVGAPGTRAQRRGPllHHTLgdgdfdHFLRMFEEVTVAQAVLT-PENAAAEIDRVLAAALREKrPV-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 167 LVSLPQDVmtAETTVESIGALSKPQlgiAPTHD-------ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTEL 239
Cdd:COG3961 164 YIELPRDV--ADAPIEPPEAPLPLP---PPASDpaalaaaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 240 PVVETYQAAGAISrelEDH--FfgrVGLFRNQPGDI----LLEEADLVISMGYDPIEYDPKFW-NKLGDRTIIHLDDHQA 312
Cdd:COG3961 239 PVATTLLGKSVLD---ESHpqF---IGTYAGAASSPevreYVENADCVLCLGVVFTDTNTGGFtAQLDPERTIDIQPDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 313 DIDHDYQPereligDIALT--VNSIAEKLPKLVlstkseavlERLRAKLSEQAEVPNRPSEGVTHPlQVIRTLRSLISDD 390
Cdd:COG3961 313 RVGGHIYP------GVSLAdfLEALAELLKKRS---------APLPAPAPPPPPPPAAPDAPLTQD-RLWQRLQAFLDPG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 391 TTVTCDIGSHSIWMARcfrsyeprrLLFSNGM----QTL----GVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELET 462
Cdd:COG3961 377 DIVVADTGTSLFGAAD---------LRLPEGAtfiaQPLwgsiGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELST 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 463 AVRLN-SPIVHLVWRDGtYdmvAFQQMM--KYGRtsateFGDV---DIVKYAESFGAT---GLRVNTPDELEGVLKSALA 533
Cdd:COG3961 448 MLRYGlKPIIFVLNNDG-Y---TIERAIhgPDGP-----YNDIanwDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEA 518
|
570
....*....|...
gi 446025664 534 -ADGPVIIDIPID 545
Cdd:COG3961 519 nTDRLTLIEVVLD 531
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
18-172 |
5.71e-32 |
|
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: 120.53 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 18 DLVVDCLIKQGVTHVFGIPGAKIDSVFDVLQER-GPELIVCRHEQNAAFMAAAIGRLTGkPGVCLVTSGPGTSNLATGLV 96
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446025664 97 TANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTnPGATLVSLPQ 172
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
375-544 |
1.33e-26 |
|
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: 106.53 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 375 HPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQtLGVALPWAIAATLVEPGKKVVSVSGDGGFL 454
Cdd:cd02002 2 TPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRGGG-LGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 455 FSAMELETAVRLNSPIVHLVWRDGTY--DMVAFQQMMKYGRTSATEFG------DVDIVKYAESFGATGLRVNTPDELEG 526
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYgaLRSFLKRVGPEGPGENAPDGldlldpGIDFAAIAKAFGVEAERVETPEELDE 160
|
170
....*....|....*...
gi 446025664 527 VLKSALAADGPVIIDIPI 544
Cdd:cd02002 161 ALREALAEGGPALIEVVV 178
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
375-545 |
2.29e-23 |
|
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: 97.97 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 375 HPLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFL 454
Cdd:cd02013 5 HPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 455 FSAMELETAVRLNSPIVHLVWRDGTYDMVAFQQMMKYG-RTSATEFGDVDIVKYAESFGATGLRVNTPDELEGVLKSALA 533
Cdd:cd02013 85 MSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNnRFVGTELESESFAKIAEACGAKGITVDKPEDVGPALQKAIA 164
|
170
....*....|....*
gi 446025664 534 --ADG-PVIIDIPID 545
Cdd:cd02013 165 mmAEGkTTVIEIVCD 179
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
200-332 |
6.95e-23 |
|
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: 94.55 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 200 ITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVETYQAAGAISrelEDH--FFGRVGLFRNQPGDILLEE 277
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFP---EDHplYLGMLGMHGTPAANEALEE 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 278 ADLVISMG--YDPI---EYDPKFWNklgDRTIIHLDDHQADIDHDYQPERELIGDIALTV 332
Cdd:pfam00205 78 ADLVLAVGarFDDIrttGKLPEFAP---DAKIIHIDIDPAEIGKNYPVDVPIVGDAKETL 134
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
16-541 |
8.98e-20 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 92.60 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPG-------AKIDSVfdvlqeRGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGt 88
Cdd:PRK07586 3 GAESLVRTLVDGGVDVCFANPGtsemhfvAALDRV------PGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 89 snLATGLvtAN------AESdPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTN 162
Cdd:PRK07586 76 --LANGL--ANlhnarrART-PIVNIVGDHATYHRKYDAPLTSDIEALARPVSGWVRRSESAADVAADAAAAVAAARGAP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 163 PG-ATLVsLPQDVMTAETTVeSIGALSKPQLGIAPTHDITYVVEKIKAAKLPVILLGMRASTNEVTKAVRELIADTELPV 241
Cdd:PRK07586 151 GQvATLI-LPADVAWSEGGP-PAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATGARL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 242 -VETYQA-----AGAISREledhffgRVGLFRNQPGDIlLEEADLVISMGY-DPIEY----DPKFWNKLGDRTIIHLDDH 310
Cdd:PRK07586 229 lAETFPArmergAGRPAVE-------RLPYFAEQALAQ-LAGVRHLVLVGAkAPVAFfaypGKPSRLVPEGCEVHTLAGP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 311 QADIDHdyqpereligdiALtvnsiaEKLPKLVLSTKSEAVLERLRAklseqaevPNRPSEGVTHP--LQVIRTL---RS 385
Cdd:PRK07586 301 GEDAAA------------AL------EALADALGAKPAAPPLAAPAR--------PPLPTGALTPEaiAQVIAALlpeNA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 386 LISDDtTVTCDIGSHSiWMARCfrsyePRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVR 465
Cdd:PRK07586 355 IVVDE-SITSGRGFFP-ATAGA-----APHDWLTLTGGAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQAR 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 466 LNSPIVHLVWRDGTYDMVafqqMMKYGRTSATEFG------------DVDIVKYAESFGATGLRVNTPDELEGVLKSALA 533
Cdd:PRK07586 428 ENLDVTTVIFANRAYAIL----RGELARVGAGNPGpraldmldlddpDLDWVALAEGMGVPARRVTTAEEFADALAAALA 503
|
....*...
gi 446025664 534 ADGPVIID 541
Cdd:PRK07586 504 EPGPHLIE 511
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
378-545 |
1.45e-19 |
|
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: 86.98 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 378 QVIRTLRSLISDDTTVTCDIGS-----HSIWMARCFRSYEprrLLFsnGMQTLGVALPWAIAATLVEPGKKVVSVSGDGG 452
Cdd:cd02003 3 EVLGALNEAIGDDDVVINAAGSlpgdlHKLWRARTPGGYH---LEY--GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 453 FLFSAMELETAVRLNSPIVHLVWRDGTYDMVAFQQMMKYGRTSATEFGD--------------VDIVKYAESFGATGLRV 518
Cdd:cd02003 78 YLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDrdqesgqldgallpVDFAANARSLGARVEKV 157
|
170 180
....*....|....*....|....*..
gi 446025664 519 NTPDELEGVLKSALAADGPVIIDIPID 545
Cdd:cd02003 158 KTIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
16-541 |
2.61e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 88.01 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 16 GADLVVDCLIKQGVTHVFGIPG-------AKIDSVfdvlqeRGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGT 88
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGtsemhfvAALDRV------PRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 89 SNLATGLVTANAESDPVVALAGAVPRTDRLKRTHQSMDNAALFEPITKYSVEVEHPDNVPEALSNAFRSATSTNPGATLV 168
Cdd:PRK12474 81 ANGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 169 SLPQDVMTAETtvesiGALSKPQLGIAPTHDITYVVEKIKAA----KLPVILL--------GMRASTNEVTKAVRELIAD 236
Cdd:PRK12474 161 IMPADVAWNEA-----AYAAQPLRGIGPAPVAAETVERIAALlrngKKSALLLrgsalrgaPLEAAGRIQAKTGVRLYCD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 237 TELPVVEtyQAAGAISREledhffgRVGLFRNQpGDILLEEADLVISMGYDPIEYDPKFWNKLGdrtiiHLDDHQADIDH 316
Cdd:PRK12474 236 TFAPRIE--RGAGRVPIE-------RIPYFHEQ-ITAFLKDVEQLVLVGAKPPVSFFAYPGKPS-----WGAPPGCEIVY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 317 DYQPEREL---IGDIALTVNSIAEKLPKLVLStkseavlerlraklseqaeVPNRPSEGVThPLQVIRTLRSLISDDTTV 393
Cdd:PRK12474 301 LAQPDEDLaqaLQDLADAVDAPAEPAARTPLA-------------------LPALPKGALN-SLGVAQLIAHRTPDQAIY 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 394 TCDIGSHSIWMARCFRSYEPRRLLFSNGmQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAMELETAVRLNSPIVHL 473
Cdd:PRK12474 361 ADEALTSGLFFDMSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVV 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446025664 474 VWRDGTYDMVaFQQMMKYGRTSATEFG---------DVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIID 541
Cdd:PRK12474 440 IFANRSYAIL-NGELQRVGAQGAGRNAlsmldlhnpELNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIE 515
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
21-158 |
4.55e-16 |
|
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: 75.61 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 21 VDCLIKQGVTHVFGIPGAKIDSVFDVLQERGP-ELIVCRHEQNAAFMAAAIGRLTGkPGVCLVTSGPGTSNLATGLVTAN 99
Cdd:cd07038 4 LERLKQLGVKHVFGVPGDYNLPLLDAIEENPGlRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAY 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446025664 100 AESDPVVALAGAVPRTDRLKRT--HQS-----MDNAA-LFEPITKYSVEVEHPDNVPEALSNAFRSA 158
Cdd:cd07038 83 AEHVPVVHIVGAPSTKAQASGLllHHTlgdgdFDVFLkMFEEITCAAARLTDPENAAEEIDRVLRTA 149
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
376-553 |
1.67e-13 |
|
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: 69.62 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 376 PLQVIRTLRSLISDDTTVTCDIGSHSIWMARCFRSYEPRRLLFSNGMQTLGVALPWAIAATLVEPGKKVVSVSGDGGFLF 455
Cdd:cd02006 10 PQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 456 SAMELETAVRLNSPIVHLVWRDG----------TYDMvAFQQMMKYGRTSATEFG--DVDIVKYAESFGATGLRVNTPDE 523
Cdd:cd02006 90 MIEELAVGAQHRIPYIHVLVNNAylglirqaqrAFDM-DYQVNLAFENINSSELGgyGVDHVKVAEGLGCKAIRVTKPEE 168
|
170 180 190
....*....|....*....|....*....|....
gi 446025664 524 LEGVLKSA--LAADG--PVIIDIPIDYRDNIKLS 553
Cdd:cd02006 169 LAAAFEQAkkLMAEHrvPVVVEAILERVTNISMG 202
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
381-540 |
1.36e-11 |
|
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: 63.45 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 381 RTLRSLISDDTTVTCDIGSH--SIWMarcfrsyePRRLLFSNGmqTLGVALPWAIAATLVEPGKKVVSVSGDGGFLFSAM 458
Cdd:cd02008 17 YALRKAFKKDSIVSGDIGCYtlGALP--------PLNAIDTCT--CMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 459 E-LETAVRLNSPIVHLVWRDGTYDMVAFQQMMKYGRTSATEFGDVDIVKYAESFGATGLRVNTPDELEGV---LKSALAA 534
Cdd:cd02008 87 LgLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTVIDIEALVRAIGVKRVVVVDPYDLKAIreeLKEALAV 166
|
....*..
gi 446025664 535 DGP-VII 540
Cdd:cd02008 167 PGVsVII 173
|
|
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
8-557 |
1.85e-11 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 66.73 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 8 NDVKTKTKGADLVVDCLIKQGVTHVFgI----------------PGAKIDSVFDvlqERGpelivcrheqnAAFMAAAIG 71
Cdd:COG1165 1 SDKNSNTLWARVLVEELVRLGVRHVV-IspgsrstpltlafarhPDLRLHSHVD---ERS-----------AAFFALGLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 72 RLTGKPGVCLVTSGPGTSNLATGLVTANaESD-PVVALagavprT-DRLKRTHQSMDN-----AALFEPITKYSVEVEHP 144
Cdd:COG1165 66 KASGRPVALVCTSGTAAANYYPAVIEAF-YSGvPLIVL------TaDRPPELRDCGANqtidqVGLFGNHVRWSADLPLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 145 DNVPEAL-------SNAFRSATSTNPGAtlVSLpqDVMTAE-----TTVESIGALSKPQLGIAPT------HDITYVVEK 206
Cdd:COG1165 139 EADPDALrylrrtiNRALAAALGPPPGP--VHI--NVPFREplypdPDEEDPLAAGGPWIRVTPPepapspEALAQLADE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 207 IKAAKLPVILLGMRASTNEVTKAVRELIADTELPVVetyqaAGAISRELEDHFFGRVGLFRNQPGDILLEEADLVISMGY 286
Cdd:COG1165 215 LERAKRGLIVAGPLPPPEELAEALAALAEALGWPVL-----ADPLSNLRHPNVISTYDLLLRNPEFAELLQPDLVIRFGG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 287 DPIEYDPKFW-NKLGDRTIIHLDDHQADIDHDYQPERELIGDIaltvNSIAEKLPKLVLSTKSE-----AVLERLRAKLS 360
Cdd:COG1165 290 PPVSKRLKQFlRRHPPAEHWVVDPSGEWRDPFHSLTRVIEADP----EAFLEALAERLPPADSAwlarwLAAEQKARAAI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 361 EQAEVPNRPSEGvthplQVIRTLRSLISDDTTVTcdIG-SHSI-WMARCFRSYEPRRLLFSN-G-------MQT-LGVAL 429
Cdd:COG1165 366 DEYLAEDPLSEG-----AVARRLLEALPEGSTLF--VGnSMPVrDLDLFARPLPKGVRVYANrGasgidgtVSTaLGAAL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 430 pwaiaATlvepGKKVVSVSGDGGFLfsameletavrlnspivhlvwrdgtYDMVAFqqMMKY------------------ 491
Cdd:COG1165 439 -----AS----GKPTVLLTGDLSFL-------------------------HDLNGL--LLLYelppnltivvvnndgggi 482
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446025664 492 -----GRTSATEFG-------DVDIVKYAESFGATGLRVNTPDELEGVLKSALAADGPVIIDIPIDYRDNIKLSEKLL 557
Cdd:COG1165 483 fsmlpGAKFEPEFErffgtphGLDFEHLAAMYGLDYARVSSWEELREALAEFLPSDGPRVLEVRTDREENAELLKALF 560
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
19-164 |
1.46e-09 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 57.12 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 19 LVVDCLIKQGVTHVFGIPGAKidS---VFDVLQERGPELIVCRHEQNAAFMAAAIGRLTGKPGVCLVTSGPGTSNLATGL 95
Cdd:cd07037 2 ALVEELKRLGVRDVVISPGSR--SaplALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446025664 96 VTANAESDPVVALAGAVPRtdRLKRTH--QSMDNAALFEPITKYSVEVEHPDNVPE------ALSNAFRSATSTNPG 164
Cdd:cd07037 80 VEAYYSGVPLLVLTADRPP--ELRGTGanQTIDQVGLFGDYVRWSVDLPPPEDDDDlwyllrLANRAVLEALSAPPG 154
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
425-544 |
3.27e-08 |
|
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: 53.86 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 425 LGVALpwaiaatlVEPGKKVVSVSGDGGFLFSAMELETAVRLNSP-IVHLVWRDGTYDMVAFQqmmkygrtsATEFGDVD 503
Cdd:cd03371 58 LGIAL--------ARPDRKVVCIDGDGAALMHMGGLATIGGLAPAnLIHIVLNNGAHDSVGGQ---------PTVSFDVS 120
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446025664 504 IVKYAESFG-ATGLRVNTPDELEGVLKSALAADGPVIIDIPI 544
Cdd:cd03371 121 LPAIAKACGyRAVYEVPSLEELVAALAKALAADGPAFIEVKV 162
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
366-557 |
3.98e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 53.68 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 366 PNRPSEGVTHPLQVIRTLRSLISDDTTVTCDIGS--HSIWMArcfrSYEPRRLLFSNGMqtlGVALPWAIAATLVEPGKK 443
Cdd:PRK06163 5 VTRSNAKVMNRFDLTCRLVAKLKDEEAVIGGIGNtnFDLWAA----GQRPQNFYMLGSM---GLAFPIALGVALAQPKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 444 VVSVSGDGGFLFSAMELET-AVRLNSPIVHLVWRDGTYDMVAFQqmmkygRTSATefGDVDIVKYAEsfgATGLR----V 518
Cdd:PRK06163 78 VIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVYQITGGQ------PTLTS--QTVDVVAIAR---GAGLEnshwA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446025664 519 NTPDELEGVLKSALAADGPVIIDIPID--------YRDNIKLSEKLL 557
Cdd:PRK06163 147 ADEAHFEALVDQALSGPGPSFIAVRIDdkpgvgttERDPAQIRERFM 193
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
442-544 |
4.96e-07 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 49.79 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 442 KKVVSVSGDGGFLFSAMELETAVRLNS-PIVHLVWRDGTYDMVAFQQmmkygrtsaTEFGDVDIVKYAESFGATGLRVNT 520
Cdd:cd02001 60 RKVIVVDGDGSLLMNPGVLLTAGEFTPlNLILVVLDNRAYGSTGGQP---------TPSSNVNLEAWAAACGYLVLSAPL 130
|
90 100
....*....|....*....|....
gi 446025664 521 PDELEGVLKSALAADGPVIIDIPI 544
Cdd:cd02001 131 LGGLGSEFAGLLATTGPTLLHAPI 154
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
419-542 |
8.98e-04 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 40.59 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 419 SNGMQTL-GVALPWAIAATLVEPGKKVVSVSGDG-GFLFSAMELETAVRLNSPIVHLVWRDGTYDMVAfQQM----MKYG 492
Cdd:cd03375 46 TYGFHTLhGRALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTK-GQAspttPEGF 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446025664 493 RTSATEFG----DVDIVKYAESFGATGL-RVNT--PDELEGVLKSALAADGPVIIDI 542
Cdd:cd03375 125 KTKTTPYGnieePFNPLALALAAGATFVaRGFSgdIKQLKEIIKKAIQHKGFSFVEV 181
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
419-542 |
3.60e-03 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 39.48 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446025664 419 SNGMQTL-GVALPWAIAATLVEPGKKVVSVSGDGGFL------FSAmeletAVRLNSPIVHLVWRDGTYDMVAFQ---QM 488
Cdd:PRK05778 65 SHGLHTLhGRAIAFATGAKLANPDLEVIVVGGDGDLAsiggghFIH-----AGRRNIDITVIVENNGIYGLTKGQaspTT 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446025664 489 MKYGRTSATEFG----DVDIVKYAESFGATGL-R--VNTPDELEGVLKSALAADGPVIIDI 542
Cdd:PRK05778 140 PEGSKTKTAPYGniepPIDPCALALAAGATFVaRsfAGDVKQLVELIKKAISHKGFAFIDV 200
|
|
| |
