|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
10-560 |
0e+00 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 995.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 10 WQCGADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNL 89
Cdd:PRK08617 4 KKYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDS-GPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 90 ITGLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLP 169
Cdd:PRK08617 83 ATGLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 170 MDIVNEPVSAPVLAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVI 249
Cdd:PRK08617 163 QDVVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 250 DVNHFARFAGRVGLFNNQPADQLLQKADLVVSVGYDPIEYDPCMWNSHGRLKLVHIDVLPADIDTCYRPDVELVGNISAT 329
Cdd:PRK08617 243 SRELEDHFFGRVGLFRNQPGDELLKKADLVITIGYDPIEYEPRNWNSEGDATIIHIDVLPAEIDNYYQPERELIGDIAAT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 330 LNMMTETFNEAVcVPPEVELILTDLGRQRTELAERAARRGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYS 409
Cdd:PRK08617 323 LDLLAEKLDGLS-LSPQSLEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIVTDDTTVTVDVGSHYIWMARYFRS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 410 FRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEMQEVNK 489
Cdd:PRK08617 402 YEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEMK 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 490 YQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADNYKLMAQMNFSQM 560
Cdd:PRK08617 482 YGRSSGVDFGPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIKLMEQLLPDQL 552
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
13-552 |
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: 862.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDaPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALED-KGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVLAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVIDVN 252
Cdd:TIGR02418 160 VDSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 253 HFARFAGRVGLFNNQPADQLLQKADLVVSVGYDPIEYDPCMWNSHGRLKLVHIDVLPADIDTCYRPDVELVGNISATLNM 332
Cdd:TIGR02418 240 LEDHFFGRVGLFRNQPGDRLLKQADLVITIGYDPIEYEPRNWNSENDATIVHIDVEPAQIDNNYQPDLELVGDIASTLDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 333 MTETFNEAVcVPPEVELILTDLGRQRTELAERAARRGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRA 412
Cdd:TIGR02418 320 LAERIPGYE-LPPDALAILEDLKQQREALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMARYFRSYRA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 413 RQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQR 492
Cdd:TIGR02418 399 RHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMVEFQEEMKYQR 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 493 KSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADNYKLM 552
Cdd:TIGR02418 479 SSGVDFGPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNPKLM 538
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
13-548 |
5.44e-177 |
|
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: 510.86 E-value: 5.44e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:COG0028 5 GADALVEALEAEGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:COG0028 85 LADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPKDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVlAGCRLPRMGAAAADDIQA---AVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVI 249
Cdd:COG0028 165 QAAEAEEEP-APPELRGYRPRPAPDPEAieeAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGAF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 250 DVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGYDPIEYDPCMWNSH-GRLKLVHIDVLPADIDTCYRPDVELVGNISA 328
Cdd:COG0028 244 PEDH-PLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFaPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 329 TLNMMTETFNEAVCVPPEvelILTDLGRQRTELAERAARRGGmPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLY 408
Cdd:COG0028 323 VLAALLEALEPRADDRAA---WLARIAAWRAEYLAAYAADDG-PIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 409 SFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEMQEVN 488
Cdd:COG0028 399 FRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQEL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 489 KYQ-RKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADN 548
Cdd:COG0028 479 FYGgRYSGTDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
13-554 |
2.72e-160 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 468.15 E-value: 2.72e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08322 3 AADLFVKCLENEGVEYIFGIPGEENLDLLEALRDS-SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK08322 82 VAYAQLGGMPMVAITGQKPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVLAGCRLPRMgAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVIDVN 252
Cdd:PRK08322 162 AAEETDGKPLPRSYSRRP-YASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIPET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 253 HfARFAGRVGL----FNNQPADQllqkADLVVSVGYDPIEYDPCMWNSHGRLKLVHIDVLPADIDTCYRPDVELVGNISA 328
Cdd:PRK08322 241 H-PLSLGTAGLsqgdYVHCAIEH----ADLIINVGHDVIEKPPFFMNPNGDKKVIHINFLPAEVDPVYFPQVEVVGDIAN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 329 TLNMMTEtfneAVCVPPEVELILTDLGRQ--RTELAERAARrGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARY 406
Cdd:PRK08322 316 SLWQLKE----RLADQPHWDFPRFLKIREaiEAHLEEGADD-DRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIWFARN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 407 LYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEMQE 486
Cdd:PRK08322 391 YRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 487 VNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADNYKLMAQ 554
Cdd:PRK08322 471 ENMGFEDFGLDFGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSENDRVLNQ 538
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
375-551 |
6.69e-91 |
|
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: 276.86 E-value: 6.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 375 PLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQ 454
Cdd:cd02010 1 PQRIVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 455 SSMELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQ 534
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFGNPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
170
....*....|....*..
gi 2273381670 535 GPVVVAIPVDYADNYKL 551
Cdd:cd02010 161 GVHVIDCPVDYSENIRL 177
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
13-548 |
9.40e-86 |
|
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: 276.60 E-value: 9.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:TIGR00118 83 IATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVLAGCRLPRMGAAAA---DDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVI 249
Cdd:TIGR00118 163 TTAEIEYPYPEKVNLPGYRPTVKghpLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLGSF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 250 DVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGY--------DPIEYDPcmwnshgRLKLVHIDVLPADIDTCYRPDVE 321
Cdd:TIGR00118 243 PEDH-PLSLGMLGMHGTKTANLAVHECDLIIAVGArfddrvtgNLAKFAP-------NAKIIHIDIDPAEIGKNVRVDIP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 322 LVGNISATLNMMTETFNEAvcVPPEVELILTDLGRQRTELAERAARRGGmPIHPLRIVKELQDIVSDDVTLCVDMGSFHI 401
Cdd:TIGR00118 315 IVGDARNVLEELLKKLFEL--KERKESAWLEQINKWKKEYPLKMDYTEE-GIKPQQVIEELSRVTKDEAIVTTDVGQHQM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 402 WIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLknNI-VHVIWVDNAY- 479
Cdd:TIGR00118 392 WAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQY--DIpVKILILNNRYl 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 480 NMV-EMQEVNKYQRKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADN 548
Cdd:TIGR00118 470 GMVrQWQELFYEERYSHTHMGSLpDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPEN 540
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
13-544 |
3.52e-79 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 259.04 E-value: 3.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08199 10 GGQILVDALRANGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK08199 90 VHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPEDV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVLAGCRlPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVIDVN 252
Cdd:PRK08199 170 LSETAEVPDAPPYR-RVAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 253 HfARFAGRVGLFNNQPADQLLQKADLVVSVG----------YDPIEYDpcmwnsHGRLKLVHIDVLPADIDTCYRPDVEL 322
Cdd:PRK08199 249 H-PNYAGDLGLGINPALAARIREADLVLAVGtrlgevttqgYTLLDIP------VPRQTLVHVHPDAEELGRVYRPDLAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 323 VGNISATLNMMTEtfneavcVPPEVELILTDLGRQR--TELAERAARRGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFH 400
Cdd:PRK08199 322 VADPAAFAAALAA-------LEPPASPAWAEWTAAAhaDYLAWSAPLPGPGAVQLGEVMAWLRERLPADAIITNGAGNYA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 401 IWIARYlYSFR--ARQLLISNGqqTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVhVIWVDNA 478
Cdd:PRK08199 395 TWLHRF-FRFRryRTQLAPTSG--SMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPII-VIVVNNG 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 479 -YNMVEMQEVNKY-QRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK08199 471 mYGTIRMHQEREYpGRVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
13-544 |
1.72e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 250.44 E-value: 1.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDS-DLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK06276 82 IATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPV---SAPVLAGCRLPRMGAAAA---DDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAA 246
Cdd:PRK06276 162 QEGELdleKYPIPAKIDLPGYKPTTFghpLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 247 GVIDVNHFARFaGRVGLFNNQPADQLLQKADLVVSVG---YDPIEYDPCMWNSHGrlKLVHIDVLPADIDTCYRPDVELV 323
Cdd:PRK06276 242 GAFPEDHPLAL-GMVGMHGTKAANYSVTESDVLIAIGcrfSDRTTGDISSFAPNA--KIIHIDIDPAEIGKNVRVDVPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 324 G---NISATLNMMTETFNEAVcVPPEVELIltdlgRQRTELAERAARRGGMPIHPLRIVKELQDIVSD-----DVTLCVD 395
Cdd:PRK06276 319 GdakNVLRDLLAELMKKEIKN-KSEWLERV-----KKLKKESIPRMDFDDKPIKPQRVIKELMEVLREidpskNTIITTD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 396 MGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWV 475
Cdd:PRK06276 393 VGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFD 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273381670 476 DNAYNMVeMQEVNKY--QRKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK06276 473 NRTLGMV-YQWQNLYygKRQSEVHLGETpDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIID 543
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-544 |
8.57e-74 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 245.68 E-value: 8.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 1 MAQEKTGndwqcgaDLVVKNLEAQGVKHVFGIPGAKIDRVFDSL-EDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVAL 79
Cdd:PRK08611 1 MAKIKAG-------EALVKLLQDWGIDHVYGIPGDSIDAVVDALrKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 80 VTSGPGSSNLITGLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAeFG 159
Cdd:PRK08611 74 SIGGPGAIHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTA-YE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 160 RPGASFISLPMDIVNE-----PVSAPVLAgcrLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASrpENSEAVRHLLYR 234
Cdd:PRK08611 153 KKGVAVLTIPDDLPAQkikdtTNKTVDTF---RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAK--HAKEELLAFAEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 235 THMPVVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVG--YDPIEYDPcmwnshGRLKLVHIDVLPADI 312
Cdd:PRK08611 228 AKIPIIHTLPAKGIIPDDH-PYSLGNLGKIGTKPAYEAMQEADLLIMVGtnYPYVDYLP------KKAKAIQIDTDPANI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 313 DTCYRPDVELVGNISATLNMMTETFnEAVCVPPEVELILTDLGRQRTELAERAArRGGMPIHPLRIVKELQDIVSDDVTL 392
Cdd:PRK08611 301 GKRYPVNVGLVGDAKKALHQLTENI-KHVEDRRFLEACQENMAKWWKWMEEDEN-NASTPIKPERVMAAIQKIADDDAVL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 393 CVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHV 472
Cdd:PRK08611 379 SVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273381670 473 IWVDNAYNMVEMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK08611 459 VLNNQQLAFIKYEQQAAGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD 530
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
13-548 |
3.31e-70 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 235.76 E-value: 3.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVkrADSLKQTH--QSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPM 170
Cdd:PRK08527 85 LATAYMDSIPLVLISGQV--PNSLIGTDafQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 171 DI------------VNEPVSAPVLAGcrlprmgaaAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMP 238
Cdd:PRK08527 163 DVtatlgefeypkeISLKTYKPTYKG---------NSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 239 VVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGY---DPIEydpcmwnshGRL-------KLVHIDVL 308
Cdd:PRK08527 234 AVETLMARGVLRSDD-PLLLGMLGMHGSYAANMAMSECDLLISLGArfdDRVT---------GKLsefakhaKIIHVDID 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 309 PADIDTCYRPDVELVGNISATLNMMTETFNEAvcvppevelILTDLGRQRTELAERAArrggmpIHPLR----------- 377
Cdd:PRK08527 304 PSSISKIVNADYPIVGDLKNVLKEMLEELKEE---------NPTTYKEWREILKRYNE------LHPLSyedsdevlkpq 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 378 -IVKELQDIVSDDVTLCVDMGSFHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQS 455
Cdd:PRK08527 369 wVIERVGELLGDDAIISTDVGQHQMWVAQF-YPFnYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMN 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 456 SMELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQRK---SGVEFGPiDFKAYAESCGAVGFAVQSVDDLRPMLRKAMA 532
Cdd:PRK08527 448 IQELMTAVEYKIPVINIILNNNFLGMVRQWQTFFYEERyseTDLSTQP-DFVKLAESFGGIGFRVTTKEEFDKALKEALE 526
|
570
....*....|....*.
gi 2273381670 533 IQGPVVVAIPVDYADN 548
Cdd:PRK08527 527 SDKVALIDVKIDRFEN 542
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
13-548 |
2.76e-66 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 224.76 E-value: 2.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPsIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRA----DSLkqthQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISL 168
Cdd:PRK08978 82 LADALLDSVPVVAITGQVSSPligtDAF----QEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 169 PMDIVNEPVSAPVLAgCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGV 248
Cdd:PRK08978 158 PKDIQLAEGELEPHL-TTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 249 IDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVG--YDpieyDpcmwNSHGRL-------KLVHIDVLPADIDTCYRPD 319
Cdd:PRK08978 237 VEADH-PYYLGMLGMHGTKAANLAVQECDLLIAVGarFD----D----RVTGKLntfaphaKVIHLDIDPAEINKLRQAH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 320 VELVGNISATLnmmtetfnEAVCVPPEVELILTDLGRQRTELAERAARRGGmPIHPLRIVKELQDIVSDDVTLCVDMGSF 399
Cdd:PRK08978 308 VALQGDLNALL--------PALQQPLNIDAWRQHCAQLRAEHAWRYDHPGE-AIYAPALLKQLSDRKPADTVVTTDVGQH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 400 HIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRlKNNIVHVIWVDNA- 478
Cdd:PRK08978 379 QMWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKR-KQLPVKIVLLDNQr 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2273381670 479 YNMV-EMQEVNKYQRKSGVEF--GPiDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADN 548
Cdd:PRK08978 458 LGMVrQWQQLFFDERYSETDLsdNP-DFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELEN 529
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
13-544 |
7.24e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 224.20 E-value: 7.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08155 15 GAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK08155 95 IADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPKDV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVL--AGCRLPrMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVID 250
Cdd:PRK08155 175 QTAVIELEALpaPAEKDA-APAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGMLP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 251 VNHFARFaGRVGLFNNQPADQLLQKADLVVSVG--YDpieyDPCMWNSHG---RLKLVHIDVLPADIDTCYRPDVELVGN 325
Cdd:PRK08155 254 KAHPLSL-GMLGMHGARSTNYILQEADLLIVLGarFD----DRAIGKTEQfcpNAKIIHVDIDRAELGKIKQPHVAIQAD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 326 ISATLNMMTetfneavcvpPEVELILTDLGRQRTELAER----AARRGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFHI 401
Cdd:PRK08155 329 VDDVLAQLL----------PLVEAQPRAEWHQLVADLQRefpcPIPKADDPLSHYGLINAVAACVDDNAIITTDVGQHQM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 402 WIARyLYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYN 480
Cdd:PRK08155 399 WTAQ-AYPLnRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALG 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 481 MVEMQEVNKY-QRKSGVEF-GPIDFKAYAEscgavGFAVQSVD-----DLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK08155 478 LVHQQQSLFYgQRVFAATYpGKINFMQIAA-----GFGLETCDlnneaDPQAALQEAINRPGPALIHVRID 543
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-548 |
7.30e-66 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 224.46 E-value: 7.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 2 AQEKTGNDWQCGADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVT 81
Cdd:PRK06725 6 TYEKLQCEEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYES-GLKHILTRHEQAAIHAAEGYARASGKVGVVFAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 82 SGPGSSNLITGLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRP 161
Cdd:PRK06725 85 SGPGATNLVTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 162 GASFISLPMDIVNEPVSAPVLAGCRLPRMGAAAA---DDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMP 238
Cdd:PRK06725 165 GPVLIDIPKDVQNEKVTSFYNEVVEIPGYKPEPRpdsMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 239 VVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPcmwNSHGRLKL-------VHIDVLPAD 311
Cdd:PRK06725 245 VVSTLMGLGAYPPGD-PLFLGMLGMHGTYAANMAVTECDLLLALG---VRFDD---RVTGKLELfsphskkVHIDIDPSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 312 IDTCYRPDVELVGNISATLNMMtetFNEAVCVPPEVELILTDLGRQRTELAERAARRGGMPIHPLRIVKELqdiVSDDVT 391
Cdd:PRK06725 318 FHKNVAVEYPVVGDVKKALHML---LHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSEL---TNGEAI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 392 LCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVrlKNNI-V 470
Cdd:PRK06725 392 VTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIA--ENNIpV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 471 HVIWVDNAY-NMV-EMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADN 548
Cdd:PRK06725 470 KVFIINNKFlGMVrQWQEMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGEN 549
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
13-544 |
4.60e-65 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 222.41 E-value: 4.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDS-LEDAPS--IETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNL 89
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfVEDLANgeLRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 90 ITGLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLP 169
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 170 MDIVNEPV------SAPVLAGCRlPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTY 243
Cdd:PRK06456 164 RDIFYEKMeeikwpEKPLVKGYR-DFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 244 QAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVG----------YDPIeydpcmwnSHGRLKLVHIDVLPADID 313
Cdd:PRK06456 243 PGKTAIPHDH-PLYFGPMGYYGRAEASMAALESDAMLVVGarfsdrtftsYDEM--------VETRKKFIMVNIDPTDGE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 314 TCYRPDVELVGNISATLNMMTETFNEAVCVPPEVELIltdlgRQRTELAERAAR----RGGMPIHPLRIVKELQDIVSDD 389
Cdd:PRK06456 314 KAIKVDVGIYGNAKIILRELIKAITELGQKRDRSAWL-----KRVKEYKEYYSQfyytEENGKLKPWKIMKTIRQALPRD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 390 VTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNI 469
Cdd:PRK06456 389 AIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPV 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273381670 470 VHVIWVDNAYNMV-EMQEVNKYQRKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK06456 469 ISVIFDNRTLGLVrQVQDLFFGKRIVGVDYGPSpDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVD 545
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
13-552 |
1.23e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 220.80 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK06048 10 GARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDS-DLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK06048 89 IATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVS------------APVLAGcrlprmgaaAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVV 240
Cdd:PRK06048 169 TTAEIDfdypdkvelrgyKPTYKG---------NPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 241 GTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPcmwNSHGRL-------KLVHIDVLPADID 313
Cdd:PRK06048 240 TTLMGIGAIPTEH-PLSLGMLGMHGTKYANYAIQESDLIIAVG---ARFDD---RVTGKLasfapnaKIIHIDIDPAEIS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 314 TCYRPDVELVGNISATLNMMTETFNEavCVPPEVELILTDLgRQRTELAERAARRGgmpIHPLRIVKELQDIVSDDVtLC 393
Cdd:PRK06048 313 KNVKVDVPIVGDAKQVLKSLIKYVQY--CDRKEWLDKINQW-KKEYPLKYKEREDV---IKPQYVIEQIYELCPDAI-IV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 394 VDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVrlKNNI-VHV 472
Cdd:PRK06048 386 TEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAV--QNDIpVIV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 473 IWVDNAY-NMV-EMQEVNKYQRKSGVEFGP-IDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADNY 549
Cdd:PRK06048 464 AILNNGYlGMVrQWQELFYDKRYSHTCIKGsVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENV 543
|
...
gi 2273381670 550 KLM 552
Cdd:PRK06048 544 SPM 546
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
13-543 |
1.66e-63 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 217.19 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPS-IETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLIT 91
Cdd:PRK08266 6 GGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 92 GLATATSEGDAVVAFGGAVKRA---DSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISL 168
Cdd:PRK08266 86 ALLTAYGCNSPVLCLTGQIPSAligKGRGHLHEMPDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 169 PMDIVNEpvSAPVLAGCRLPRMGAAAA--DDIQAAVKLIRQAKCPVLLLGLQASrpENSEAVRHLLYRTHMPVVGTYQAA 246
Cdd:PRK08266 166 PWDVFGQ--RAPVAAAPPLRPAPPPAPdpDAIAAAAALIAAAKNPMIFVGGGAA--GAGEEIRELAEMLQAPVVAFRSGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 247 GVIDVNHFarfagrvgLFNNQPAD-QLLQKADLVVSVGY---DPIEYDPcmWNSHGrLKLVHIDVLPADIdTCYRPDVEL 322
Cdd:PRK08266 242 GIVSDRHP--------LGLNFAAAyELWPQTDVVIGIGSrleLPTFRWP--WRPDG-LKVIRIDIDPTEM-RRLKPDVAI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 323 VGNISATLNMMTEtfneavcvppEVELILTDLGRQRTELAERAARRGGM--PIHP----LRIVKEL---QDIVSDDVTlc 393
Cdd:PRK08266 310 VADAKAGTAALLD----------ALSKAGSKRPSRRAELRELKAAARQRiqAVQPqasyLRAIREAlpdDGIFVDELS-- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 394 vDMGsFHIWIARYLYSfrARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVI 473
Cdd:PRK08266 378 -QVG-FASWFAFPVYA--PRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVV 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 474 WVDNAYNMVEMQEVNKYQ-RKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPV 543
Cdd:PRK08266 454 FNNNAYGNVRRDQKRRFGgRVVASDLVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPV 524
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
13-544 |
1.56e-61 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 212.76 E-value: 1.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPKDC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VN----------EPVSA----PVLAGCRlprmgaaaaDDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMP 238
Cdd:PRK08979 166 LNpailhpyeypESIKMrsynPTTSGHK---------GQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 239 VVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPCMWNSHGRL----KLVHIDVLPADIDT 314
Cdd:PRK08979 237 VVSTLMGLGAFPGTH-KNSLGMLGMHGRYEANMAMHNADLIFGIG---VRFDDRTTNNLEKYcpnaTILHIDIDPSSISK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 315 CYRPDVELVGNISATLNMMTETFNEAVCVPPE--VELILTDLG--RQRTELA-ERAARRggmpIHPLRIVKELQDIVSDD 389
Cdd:PRK08979 313 TVRVDIPIVGSADKVLDSMLALLDESGETNDEaaIASWWNEIEvwRSRNCLAyDKSSER----IKPQQVIETLYKLTNGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 390 VTLCVDMGSFHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAvrLKNN 468
Cdd:PRK08979 389 AYVASDVGQHQMFAALY-YPFdKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTA--LQYD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 469 I-VHVIWVDNAY-NMVEMQEVNKYQ-RKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVV-VAIPV 543
Cdd:PRK08979 466 IpVKIINLNNRFlGMVKQWQDMIYQgRHSHSYMDSVpDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVDINV 545
|
.
gi 2273381670 544 D 544
Cdd:PRK08979 546 D 546
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
13-511 |
1.39e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 210.06 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK07282 12 GSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK07282 92 IADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVSAPVLAGCRLPRMGAAAADDIQAAVKLIRQ---AKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVI 249
Cdd:PRK07282 172 SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQlskAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGTI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 250 DVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGY---DPIEYDPCMWNSHGrlKLVHIDVLPADIDTCYRPDVELVGNI 326
Cdd:PRK07282 252 ATSH-PLFLGMGGMHGSYAANIAMTEADFMINIGSrfdDRLTGNPKTFAKNA--KVAHIDIDPAEIGKIIKTDIPVVGDA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 327 SATLNMMTETfneavcvpPEVELILTDLGRQRTELAERAA--RRGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIA 404
Cdd:PRK07282 329 KKALQMLLAE--------PTVHNNTEKWIEKVTKDKNRVRsyDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 405 RYlYSFR-ARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMV- 482
Cdd:PRK07282 401 QY-YPYQnERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVr 479
|
490 500 510
....*....|....*....|....*....|
gi 2273381670 483 EMQEVNKYQRKSGVEFGPI-DFKAYAESCG 511
Cdd:PRK07282 480 QWQESFYEGRTSESVFDTLpDFQLMAQAYG 509
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
3-555 |
2.38e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 207.60 E-value: 2.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 3 QEKTGNDWQCGADLVVKNLEAQGVKHVFGIPGAKIDRVFDSL---EDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVAL 79
Cdd:PRK07418 11 STTVTPQRATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELykaEAEGWLKHILVRHEQGAAHAADGYARATGKVGVCF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 80 VTSGPGSSNLITGLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFG 159
Cdd:PRK07418 91 GTSGPGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 160 RPGASFISLPMDIVNE-----PV--SAPVLAGCRLPRMGaaAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLL 232
Cdd:PRK07418 171 RPGPVLIDIPKDVGQEefdyvPVepGSVKPPGYRPTVKG--NPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 233 YRTHMPVVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGY---DPI-----EYDPcmwnshgRLKLVH 304
Cdd:PRK07418 249 ERFQIPVTTTLMGKGAFDEHH-PLSVGMLGMHGTAYANFAVTECDLLIAVGArfdDRVtgkldEFAS-------RAKVIH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 305 IDVLPADIDTCYRPDVELVGNISATLNMMTETFNEAVcVPPEVELILTDLGRQRTELAERAARRGGmPIHPLRIVKELQD 384
Cdd:PRK07418 321 IDIDPAEVGKNRRPDVPIVGDVRKVLVKLLERSLEPT-TPPRTQAWLERINRWKQDYPLVVPPYEG-EIYPQEVLLAVRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 385 IVSDD-VTlcVDMGSFHIWIARYLYSfRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAV 463
Cdd:PRK07418 399 LAPDAyYT--TDVGQHQMWAAQFLRN-GPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 464 RLKNNIVHVIwVDNAYN-MVEMQEVNKYQRK---SGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVV 539
Cdd:PRK07418 476 QYGINVKTVI-INNGWQgMVRQWQESFYGERysaSNMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLI 554
|
570 580
....*....|....*....|...
gi 2273381670 540 AIPVDYADNYKLM-------AQM 555
Cdd:PRK07418 555 DVHVRRDENCYPMvppgksnAQM 577
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
13-548 |
1.12e-58 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 205.15 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK06882 86 IATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VN----------EPVSA----PVLAGCRlprmgaaaaDDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMP 238
Cdd:PRK06882 166 VNpankftyeypEEVSLrsynPTVQGHK---------GQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 239 VVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPCMWNSHGRL----KLVHIDVLPADIDT 314
Cdd:PRK06882 237 VTSSLMGLGAYPSTD-KQFLGMLGMHGTYEANNAMHESDLILGIG---VRFDDRTTNNLAKYcpnaKVIHIDIDPTSISK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 315 CYRPDVELVGNISATLNMMTETFNEAVCVPPEVEliLTDLGRQRTELAERAA---RRGGMPIHPLRIVKELQDIVSDDVT 391
Cdd:PRK06882 313 NVPAYIPIVGSAKNVLEEFLSLLEEENLAKSQTD--LTAWWQQINEWKAKKClefDRTSDVIKPQQVVEAIYRLTNGDAY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 392 LCVDMGSFHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIV 470
Cdd:PRK06882 391 VASDVGQHQMFAALH-YPFdKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 471 HVIWVDNAYNMV-EMQEVNKYQRKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVV-VAIPVDYAD 547
Cdd:PRK06882 470 IVSLNNRFLGMVkQWQDLIYSGRHSQVYMNSLpDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETE 549
|
.
gi 2273381670 548 N 548
Cdd:PRK06882 550 H 550
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
13-539 |
3.40e-58 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 204.44 E-value: 3.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK07789 113 IADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPKDA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNE--PVSAPV---LAGCRlPrMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAG 247
Cdd:PRK07789 193 LQAqtTFSWPPrmdLPGYR-P-VTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMARG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 248 VIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVG--YDPieydpcmwNSHGRL-------KLVHIDVLPADIDTCYRP 318
Cdd:PRK07789 271 AFPDSH-PQHLGMPGMHGTVAAVAALQRSDLLIALGarFDD--------RVTGKLdsfapdaKVIHADIDPAEIGKNRHA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 319 DVELVGNISATLNMMTETFN--EAVCVPPEVELILTDLGRQRTELAERAARRGGMPIHPLRIVKELQDIVSDDVTLCVDM 396
Cdd:PRK07789 342 DVPIVGDVKEVIAELIAALRaeHAAGGKPDLTAWWAYLDGWRETYPLGYDEPSDGSLAPQYVIERLGEIAGPDAIYVAGV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 397 GSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVrlKNNI-VHVIWV 475
Cdd:PRK07789 422 GQHQMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCA--IEGIpIKVALI 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273381670 476 DN-AYNMV-EMQEVNKYQRKSGVEFGP-----IDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQG-PVVV 539
Cdd:PRK07789 500 NNgNLGMVrQWQTLFYEERYSNTDLHThshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDrPVVI 571
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
13-538 |
4.46e-58 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 203.88 E-value: 4.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPKDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEPVS------------APVLAGcrlprmgaaAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVV 240
Cdd:PRK06965 183 SKTPCEyeypksvemrsyNPVTKG---------HSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 241 GTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGY---DPIEYDPCMWNSHGRlKLVHIDVLPADIDTCYR 317
Cdd:PRK06965 254 NTLMGLGAYPASD-KKFLGMLGMHGTYEANMAMQHCDVLIAIGArfdDRVIGNPAHFASRPR-KIIHIDIDPSSISKRVK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 318 PDVELVGNISATLNMMTETFNEAVCVPPEvelilTDLGRQRTELAERAAR------RGGMPIHPLRIVKELQDIVSDDVT 391
Cdd:PRK06965 332 VDIPIVGDVKEVLKELIEQLQTAEHGPDA-----DALAQWWKQIEGWRSRdclkydRESEIIKPQYVVEKLWELTDGDAF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 392 LCVDMGSFHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLkNNIV 470
Cdd:PRK06965 407 VCSDVGQHQMWAAQF-YRFnEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQY-DTPV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 471 HVIWVDNAY-NMV-EMQEVNKYQRKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVV 538
Cdd:PRK06965 485 KIISLNNRYlGMVrQWQEIEYSKRYSHSYMDALpDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRTV 555
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
13-544 |
1.18e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 202.28 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK06466 6 GAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK06466 86 IATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPKDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNE----PVSAPVLAGCRL---PRMGaaAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQA 245
Cdd:PRK06466 166 TNPaekfEYEYPKKVKLRSyspAVRG--HSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 246 AGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPCMWNSHGRL----KLVHIDVLPADIDTCYRPDVE 321
Cdd:PRK06466 244 LGGFPGTD-RQFLGMLGMHGTYEANMAMHHADVILAVG---ARFDDRVTNGPAKFcpnaKIIHIDIDPASISKTIKADIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 322 LVGNISATLNMMTETFNEaVCVPPEVELILT-----DLGRQRTELAERAARRGGMpIHPLRIVKELQDIVSDDVTLCVDM 396
Cdd:PRK06466 320 IVGPVESVLTEMLAILKE-IGEKPDKEALAAwwkqiDEWRGRHGLFPYDKGDGGI-IKPQQVVETLYEVTNGDAYVTSDV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 397 GSFHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNiVHVIWV 475
Cdd:PRK06466 398 GQHQMFAAQY-YKFnKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLP-VKIINL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273381670 476 DN-AYNMV----EMQEVNKYQrKSGVEFGPiDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVV-VAIPVD 544
Cdd:PRK06466 476 NNgALGMVrqwqDMQYEGRHS-HSYMESLP-DFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRLVfIDIYVD 548
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
13-532 |
1.53e-56 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 199.31 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVkrADSL--KQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPM 170
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQV--ATSLigYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 171 DIVN----------EPVS----APVLAGCRlprmgaaaaDDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTH 236
Cdd:PRK07979 164 DILNpanklpyvwpESVSmrsyNPTTQGHK---------GQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 237 MPVVGTYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPCMWNSHGRL----KLVHIDVLPADI 312
Cdd:PRK07979 235 LPVVSSLMGLGAFPATH-RQSLGMLGMHGTYEANMTMHNADVIFAVG---VRFDDRTTNNLAKYcpnaTVLHIDIDPTSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 313 DTCYRPDVELVGNISATLNMMTETFNEAVCVPPeveliLTDLGRQRTELAERAAR------RGGMPIHPLRIVKELQDIV 386
Cdd:PRK07979 311 SKTVTADIPIVGDARQVLEQMLELLSQESAHQP-----LDEIRDWWQQIEQWRARqclkydTHSEKIKPQAVIETLWRLT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 387 SDDVTLCVDMGSFHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRL 465
Cdd:PRK07979 386 KGDAYVTSDVGQHQMFAALY-YPFdKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQY 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 466 KNNIVhVIWVDNAY-NMVEMQEVNKY---QRKSGVEFGPiDFKAYAESCGAVGFAVQSVDDLRPMLRKAMA 532
Cdd:PRK07979 465 ELPVL-VLNLNNRYlGMVKQWQDMIYsgrHSQSYMQSLP-DFVRLAEAYGHVGIQISHPDELESKLSEALE 533
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
13-539 |
2.23e-56 |
|
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: 198.91 E-value: 2.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSL-EDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLIT 91
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALsAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 92 GLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAeFGRPGASFISLPMD 171
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRA-YAHNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 172 I------VNEPVSAPVLAgcRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPenSEAVRHLLYRTHMPVVGTYQA 245
Cdd:TIGR02720 160 FgwqeipDNDYYASSVSY--QTPLLPAPDVEAVTRAVQTLKAAERPVIYYGIGARKA--GEELEALSEKLKIPLISTGLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 246 AGVIDVNHFARF--AGRVGlfnNQPADQLLQKADLVVSVGYDpIEYDPCMWNSHGRLKLVHIDVLPADIDTCYRPDVELV 323
Cdd:TIGR02720 236 KGIIEDRYPAYLgsAYRVA---QKPANEALFQADLVLFVGNN-YPFAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 324 GNISATLNMMTETfNEAVCVPPEVELILTDLGRQRTELAERAARRGGmPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWI 403
Cdd:TIGR02720 312 ADAKKALAAILAQ-VEPRESTPWWQANVANVKNWRAYLASLEDKTEG-PLQAYQVYRAINKIAEDDAIYSIDVGDININS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 404 ARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVE 483
Cdd:TIGR02720 390 NRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIK 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 484 MQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQG--PVVV 539
Cdd:TIGR02720 470 DEQEDTNQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIKQgkPVLI 527
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
13-544 |
5.69e-55 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 194.98 E-value: 5.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFG--IPGAkidrVFDSLEdAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLI 90
Cdd:PRK06112 16 VAHAIARALKRHGVEQIFGqsLPSA----LFLAAE-AIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 91 TGLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPM 170
Cdd:PRK06112 91 APLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 171 DIVNEPVSAPV------LAGCRLPRMgAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQ 244
Cdd:PRK06112 171 DLLTAAAAAPAaprsnsLGHFPLDRT-VPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 245 AAGVIDVNHfARFAGRVGLF--NNQPAD---QLLQKADLVVSVGYDPIEYDPCMWNSHGR-LKLVHIDVLPADIDTCYRP 318
Cdd:PRK06112 250 GKGAVDETH-PLSLGVVGSLmgPRSPGRhlrDLVREADVVLLVGTRTNQNGTDSWSLYPEqAQYIHIDVDGEEVGRNYEA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 319 dVELVGNISATLNMMTETfneavcvppeveLILTDLGR---QRTELAE-----RAARRGGM---------PIHPLRIVKE 381
Cdd:PRK06112 329 -LRLVGDARLTLAALTDA------------LRGRDLAAragRRAALEPaiaagREAHREDSapvalsdasPIRPERIMAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 382 LQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQ-LLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELE 460
Cdd:PRK06112 396 LQAVLTGDTIVVADASYSSIWVANFLTARRAGMrFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 461 TAVRLKNNIVHVIWVDNAYNMVEMQEVNKY-QRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVV 539
Cdd:PRK06112 476 TARRMGVPVTIVVLNNGILGFQKHAETVKFgTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLI 555
|
....*
gi 2273381670 540 AIPVD 544
Cdd:PRK06112 556 EVITD 560
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
13-536 |
4.72e-54 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 192.64 E-value: 4.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 V--------NEPVSAPVLAGcRLPRmgAAAADDIQAAVKLIRQAKCPVLLLG---LQAsrpenSEAVRHLLYRTHMPVVG 241
Cdd:PLN02470 175 QqqlavpnwNQPMKLPGYLS-RLPK--PPEKSQLEQIVRLISESKRPVVYVGggcLNS-----SEELREFVELTGIPVAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 242 TYQAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVGydpIEYDPcmwNSHGRL-------KLVHIDVLPADIDT 314
Cdd:PLN02470 247 TLMGLGAFPASD-ELSLQMLGMHGTVYANYAVDSADLLLAFG---VRFDD---RVTGKLeafasraSIVHIDIDPAEIGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 315 CYRPDVELVGNISATLNMMTETFNEAVCVPPEVELILTDLGRQRTELAERAARRGGMpIHPLRIVKELQDIVSDDVTLCV 394
Cdd:PLN02470 320 NKQPHVSVCADVKLALQGLNKLLEERKAKRPDFSAWRAELDEQKEKFPLSYPTFGDA-IPPQYAIQVLDELTDGNAIIST 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 395 DMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETaVRLKNNIVHVIW 474
Cdd:PLN02470 399 GVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELAT-IHVENLPVKIMV 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2273381670 475 VDNAY-NMVEMQEVNKYQRKSG----------VEFGPiDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGP 536
Cdd:PLN02470 478 LNNQHlGMVVQWEDRFYKANRAhtylgdpdaeAEIFP-DFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGP 549
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
13-549 |
2.98e-53 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 189.55 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREE-GIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGavkRADSLK---QTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLP 169
Cdd:PRK05858 86 MAAAQFNQSPLVVLGG---RAPALRwgmGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 170 MDIVNEPVSAPVLAGC--RLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAG 247
Cdd:PRK05858 163 MDHAFSMADDDGRPGAltELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 248 VIDVNH---FARFAGrvglfnnqpadQLLQKADLVVSVGYdPIEYDPCMWNSHGRLKLVHIDVLPADIDTCYRPDVELVG 324
Cdd:PRK05858 243 VVPADHplaFSRARG-----------KALGEADVVLVVGV-PMDFRLGFGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 325 NISATLnmmtETFNEAVCVPPEVELILTDLgrQRTELAERAARRGGM-----PIHPLRIVKELQDIVSDDVTLCVDMGSF 399
Cdd:PRK05858 311 DLSAIL----SALAGAGGDRTDHQGWIEEL--RTAETAARARDAAELaddrdPIHPMRVYGELAPLLDRDAIVIGDGGDF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 400 HIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAY 479
Cdd:PRK05858 385 VSYAGRYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIW 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273381670 480 NMVE--MQEVNKYQRKSGVEFGpidfKAYAESCGAVGFA---VQSVDDLRPMLRKAMAIQGPVVVAIPVDYADNY 549
Cdd:PRK05858 465 GLEKhpMEALYGYDVAADLRPG----TRYDEVVRALGGHgelVTVPAELGPALERAFASGVPYLVNVLTDPSVAY 535
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
11-546 |
3.58e-53 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 189.42 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 11 QCGADLVvKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLI 90
Cdd:PRK07524 3 TCGEALV-RLLEAYGVETVFGIPGVHTVELYRGLAGS-GIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 91 TGLATATSegDAV---VAFGgaVKRADSLKQ----THQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGA 163
Cdd:PRK07524 81 TAMGQAYA--DSIpmlVISS--VNRRASLGKgrgkLHELPDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 164 SFISLPMDIVNEPVSAPVLAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPEnsEAVRHLLYRTHMPVVGTY 243
Cdd:PRK07524 157 VHIEIPLDVLAAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAA--AALRALAERLDAPVALTI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 244 QAAGVIDVNHFARFAGRVGLfnnQPADQLLQKADLVVSVGYD--PIEYDpCMWNSHGRL--KLVHIDVLPADIDTCYRPD 319
Cdd:PRK07524 235 NAKGLLPAGHPLLLGASQSL---PAVRALIAEADVVLAVGTElgETDYD-VYFDGGFPLpgELIRIDIDPDQLARNYPPA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 320 VELVGNISATLNMMTETFNEAVCVPPEVELILTDLgRQrtelAERAARRGGMPIHPL---RIVKELQD--IVSDDVTLcv 394
Cdd:PRK07524 311 LALVGDARAALEALLARLPGQAAAADWGAARVAAL-RQ----ALRAEWDPLTAAQVAlldTILAALPDaiFVGDSTQP-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 395 dmgsfhIWIARYLYSFRA--RQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHV 472
Cdd:PRK07524 384 ------VYAGNLYFDADAprRWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 473 IWVDNAYnmvemQEVNKYQRKSGVEfgPI-------DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDY 545
Cdd:PRK07524 458 LWNNDGY-----GEIRRYMVARDIE--PVgvdpytpDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQAC 530
|
.
gi 2273381670 546 A 546
Cdd:PRK07524 531 W 531
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
15-561 |
5.84e-53 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 189.91 E-value: 5.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 15 DLVVKNleaqGVKHVFGIPGAKIDRVFDSL---EDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLIT 91
Cdd:CHL00099 18 DSLVRH----GVKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 92 GLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMD 171
Cdd:CHL00099 94 GIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 172 I---------VNEPVSAPVLAGCRlPRMGaAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGT 242
Cdd:CHL00099 174 VglekfdyypPEPGNTIIKILGCR-PIYK-PTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 243 YQAAGVIDVNHfaRFA-GRVGLFNNQPADQLLQKADLVVSVGydpIEYDPcmwNSHGRL-------KLVHIDVLPADIDT 314
Cdd:CHL00099 252 LMGKGIFDEDH--PLClGMLGMHGTAYANFAVSECDLLIALG---ARFDD---RVTGKLdefacnaQVIHIDIDPAEIGK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 315 CYRPDVELVGNI----SATLNMMTETFNEavcvpPEVELILTdlGRQRTELAERA----ARRGGMPIHPLRIVKELQDIV 386
Cdd:CHL00099 324 NRIPQVAIVGDVkkvlQELLELLKNSPNL-----LESEQTQA--WRERINRWRKEypllIPKPSTSLSPQEVINEISQLA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 387 SDDVtLCVDMGSFHIWIARYLySFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLK 466
Cdd:CHL00099 397 PDAY-FTTDVGQHQMWAAQFL-KCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 467 NNIvHVIWVDNAYN-MV-EMQEVNKYQR--KSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIP 542
Cdd:CHL00099 475 LPI-KIIIINNKWQgMVrQWQQAFYGERysHSNMEEGAPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQ 553
|
570 580
....*....|....*....|..
gi 2273381670 543 VDYADN-YKLMA--QMNfSQMI 561
Cdd:CHL00099 554 VIEDENcYPMVApgKSN-SQMI 574
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-548 |
6.25e-53 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 189.92 E-value: 6.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 1 MAQEKTGNDWQCGADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALV 80
Cdd:PRK09107 1 SAQKSHMPRQMTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 81 TSGPGSSNLITGLATATSEGDAVVAFGGAVKradslkqTH-------QSMDTVSMFRPVTKYCAEVHAGSAISEVIANAF 153
Cdd:PRK09107 81 TSGPGATNAVTPLQDALMDSIPLVCITGQVP-------THligsdafQECDTVGITRPCTKHNWLVKDVNDLARVIHEAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 154 RRAEFGRPGASFISLPMDI------VNEPVSAPVLAGCRlPRMGaAAADDIQAAVKLIRQAKCPVLLL--GLQASRPENS 225
Cdd:PRK09107 154 HVATSGRPGPVVVDIPKDVqfatgtYTPPQKAPVHVSYQ-PKVK-GDAEAITEAVELLANAKRPVIYSggGVINSGPEAS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 226 EAVRHLLYRTHMPV------VGTYQAAGvidvnhfARFAGRVGLFNNQPADQLLQKADLVVSVGY---DPIEydpcmwns 296
Cdd:PRK09107 232 RLLRELVELTGFPItstlmgLGAYPASG-------KNWLGMLGMHGTYEANMAMHDCDVMLCVGArfdDRIT-------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 297 hGRL-------KLVHIDVLPADIDTCYRPDVELVGNISATLNMMTETFnEAVCVPPEVELI-----LTDLGRQRTELAER 364
Cdd:PRK09107 297 -GRLdafspnsKKIHIDIDPSSINKNVRVDVPIIGDVGHVLEDMLRLW-KARGKKPDKEALadwwgQIARWRARNSLAYT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 365 AARRGGMPIHPLRIVKELQDivSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVV 444
Cdd:PRK09107 375 PSDDVIMPQYAIQRLYELTK--GRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 445 SISGDGGFMQSSMELETAVRLKNNIVHVIwVDNAY-NMV-EMQEV---NKYQRkSGVEFGPiDFKAYAESCGAVGFAVQS 519
Cdd:PRK09107 453 DIAGDASIQMCIQEMSTAVQYNLPVKIFI-LNNQYmGMVrQWQQLlhgNRLSH-SYTEAMP-DFVKLAEAYGAVGIRCEK 529
|
570 580
....*....|....*....|....*....
gi 2273381670 520 VDDLRPMLRKAMAIQGPVVVAIPVDYADN 548
Cdd:PRK09107 530 PGDLDDAIQEMIDVDKPVIFDCRVANLEN 558
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
12-548 |
1.12e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 186.12 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 12 CGADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLIT 91
Cdd:PRK07710 17 TGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDC-GIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 92 GLATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMD 171
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 172 IV--------NEPVSAPVLAGCRLPRMgaaaaDDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTY 243
Cdd:PRK07710 176 MVveegefcyDVQMDLPGYQPNYEPNL-----LQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 244 QAAGVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVG--YDpieyDPCMWN-SH--GRLKLVHIDVLPADIDTCYRP 318
Cdd:PRK07710 251 LGLGGFPADH-PLFLGMAGMHGTYTANMALYECDLLINIGarFD----DRVTGNlAYfaKEATVAHIDIDPAEIGKNVPT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 319 DVELVGNISATLNMMTETFNEavcvPPEVELILTDLGRQRTELAERAARRGGMpIHPLRIVKELQDIVSDDVTLCVDMGS 398
Cdd:PRK07710 326 EIPIVADAKQALQVLLQQEGK----KENHHEWLSLLKNWKEKYPLSYKRNSES-IKPQKAIEMLYEITKGEAIVTTDVGQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 399 FHIWIARYlYSF-RARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELeTAVRLKNNIVHVIWVDN 477
Cdd:PRK07710 401 HQMWAAQY-YPFkTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQEL-SVIKELSLPVKVVILNN 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273381670 478 -AYNMV-EMQEVNKYQRKSGVEFG--PiDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVDYADN 548
Cdd:PRK07710 479 eALGMVrQWQEEFYNQRYSHSLLScqP-DFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEK 552
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
14-544 |
5.90e-48 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 175.40 E-value: 5.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGL 93
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKS-KVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 94 ATATSEGDAVVAFGGAVKrADSLKQTH-QSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRpGASFISLPMDI 172
Cdd:PRK06457 84 YDAKMDHAPVIALTGQVE-SDMIGHDYfQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 VNEpvSAPVLAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASrpENSEAVRHLLYRTHMPVVGTYQAAGVIDvN 252
Cdd:PRK06457 162 LRK--SSEYKGSKNTEVGKVKYSIDFSRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILP-D 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 253 HFARFAGRVGLFNNQPADQLLQKADLVVSVGyDPIEYDPCMwnsHGRLKLVHIDVLPADIDTCYRPDVELVGNISATLNM 332
Cdd:PRK06457 237 LDPKVMGGIGLLGTKPSIEAMDKADLLIMLG-TSFPYVNFL---NKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 333 ----MTETFNEAvcVPPEVELILTDLGRQRTELAEraarrggmPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLY 408
Cdd:PRK06457 313 dieeKSDKFYEE--LKGKKEDWLDSISKQENSLDK--------PMKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 409 SFRARQLLISNGQQTMGVALPWAIGAALVR-PGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEM-QE 486
Cdd:PRK06457 383 ASGEQTFIFSAWLGSMGIGVPGSVGASFAVeNKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFeQE 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 487 VNKYQrKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK06457 463 VMGYP-EWGVDLYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVD 519
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
377-543 |
2.02e-47 |
|
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: 163.20 E-value: 2.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 377 RIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSS 456
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 457 MELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQ-RKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQG 535
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGgRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 2273381670 536 PVVVAIPV 543
Cdd:cd00568 161 PALIEVKT 168
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
395-541 |
2.35e-47 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 162.37 E-value: 2.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 395 DMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIW 474
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273381670 475 VDNAYNMVEMQEVNKY-QRKSGVE---FGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAI 541
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGgGRYSGPSgkiLPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
13-541 |
1.67e-45 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 168.25 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRA---DSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLP 169
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETPyldQDLGYIHEAPDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 170 MDIVNEPVSAPVLAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASrpENSEAVRHLLYRThMPVVGTYQAAGVI 249
Cdd:PRK07064 165 IDIQAAEIELPDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGAR--HAGAEVKRLVDLG-FGVVTSTQGRGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 250 DVNHFARfagrVGLFNNQPA-DQLLQKADLVVSVGydpieydpcmwnSHGR--------LKL----VHIDVLPADIDTCY 316
Cdd:PRK07064 242 PEDHPAS----LGAFNNSAAvEALYKTCDLLLVVG------------SRLRgnetlkysLALprplIRVDADAAADGRGY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 317 RPDVELVGNISATLNMMTETFNEAVCVPPEveliLTDLGRQRTELAERAARRGGMPIHplRIVKELQDIVSDDVTLCVDM 396
Cdd:PRK07064 306 PNDLFVHGDAARVLARLADRLEGRLSVDPA----FAADLRAAREAAVADLRKGLGPYA--KLVDALRAALPRDGNWVRDV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 397 G-SFHIWIARYLYSFRARQLLISNGQqTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWV 475
Cdd:PRK07064 380 TiSNSTWGNRLLPIFEPRANVHALGG-GIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMN 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273381670 476 DNAYN-MVEMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAI 541
Cdd:PRK07064 459 DGGYGvIRNIQDAQYGGRRYYVELHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
13-180 |
4.17e-45 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 157.01 E-value: 4.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRAD-SLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMD 171
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLvGRGALQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*....
gi 2273381670 172 IVNEPVSAP 180
Cdd:pfam02776 161 VLLEEVDED 169
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
15-170 |
8.26e-44 |
|
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: 152.69 E-value: 8.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 15 DLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDaPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGLA 94
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273381670 95 TATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPM 170
Cdd:cd07035 80 NAYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
14-541 |
2.91e-43 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 162.84 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLT-GKAGVALVTSGPGSSNLITG 92
Cdd:PRK11269 7 VDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDMITG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDI 172
Cdd:PRK11269 87 LYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 173 -VNE-----------PVSAPVLAGCRLPRmgaaaaddiqaAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVV 240
Cdd:PRK11269 167 qVAEiefdpdtyeplPVYKPAATRAQIEK-----------ALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 241 GTYQAAGVIDVNHfARFAGRVGLFNNQP-ADQLLQKADLVVSVGYdpieydpcMW-NSH---------GRlKLVHIDVLP 309
Cdd:PRK11269 236 PTLMGWGAIPDDH-PLMAGMVGLQTSHRyGNATLLASDFVLGIGN--------RWaNRHtgsvevytkGR-KFVHVDIEP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 310 ADIDTCYRPDVELVGNISATLNMMTETFNEAvcvppeveliltdlgRQRTELAERAA-------RRGGM---------PI 373
Cdd:PRK11269 306 TQIGRVFGPDLGIVSDAKAALELLVEVAREW---------------KAAGRLPDRSAwvadcqeRKRTLlrkthfdnvPI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 374 HPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQlLISNGQQ-TMGVALPWAIGAALVRPGDKVVSISGDGGF 452
Cdd:PRK11269 371 KPQRVYEEMNKAFGRDTCYVSTIGLSQIAAAQFLHVYKPRH-WINCGQAgPLGWTIPAALGVRAADPDRNVVALSGDYDF 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 453 mQSSMElETAVRLKNNI--VHVIwVDNAY-----------NM----------VEMQEVNKYqrksGVefgpiDFKAYAES 509
Cdd:PRK11269 450 -QFLIE-ELAVGAQFNLpyIHVL-VNNAYlglirqaqrafDMdycvqlafenINSPELNGY----GV-----DHVKVAEG 517
|
570 580 590
....*....|....*....|....*....|....*.
gi 2273381670 510 CGAVGFAVQSVDDLRPMLRKAMAI----QGPVVVAI 541
Cdd:PRK11269 518 LGCKAIRVFKPEDIAPALEQAKALmaefRVPVVVEV 553
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
372-544 |
5.73e-41 |
|
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: 146.14 E-value: 5.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 372 PIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGG 451
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 452 FMQSSMELETAVRLKNNIVHVIWVDNAYNMVEM-QEVNKYQrKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKA 530
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSDLGFIKWeQEVMGQP-EFGVDLPNPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....
gi 2273381670 531 MAIQGPVVVAIPVD 544
Cdd:cd02014 160 LAADGPVVIDVVTD 173
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
14-544 |
2.12e-40 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 154.38 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGL 93
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 94 ATATSEGDAVVAFGGAVKRAD----SLKQTHQSmdtvSMFRPVTKYCAEVHAGSAISEVIANAFRRAeFGRPGASFISLP 169
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQigsgFFQETHPD----RLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 170 MDIVNEPV---SAPVLAGCRLPRMgAAAADDIQAAVKLIRQAKCPVLLLGlqASRPENSEAVRHLLYRTHMPVVGTYQAA 246
Cdd:PRK06546 161 GDIADEPApegFAPSVISPRRPTV-VPDPAEVRALADAINEAKKVTLFAG--AGVRGAHAEVLALAEKIKAPVGHSLRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 247 GVIDV-NHFArfAGRVGLFNNQPADQLLQKADLVVSVGYDpIEYDPCMwnshGRLKLVHIDVLPADIDTCYRPDVELVGN 325
Cdd:PRK06546 238 EWIQYdNPFD--VGMSGLLGYGAAHEAMHEADLLILLGTD-FPYDQFL----PDVRTAQVDIDPEHLGRRTRVDLAVHGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 326 ISATLNmmtetfneavCVPPEVE-----LILTDLGRQRTELAER---AARRG---GMPIHPLRIVKELQDIVSDDVTLCV 394
Cdd:PRK06546 311 VAETIR----------ALLPLVKektdrRFLDRMLKKHARKLEKvvgAYTRKvekHTPIHPEYVASILDELAADDAVFTV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 395 DMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFmqsSM---ELETaVRLKNNIVH 471
Cdd:PRK06546 381 DTGMCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGL---SMllgELLT-VKLYDLPVK 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2273381670 472 VIWVDNA-YNMVEMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK06546 457 VVVFNNStLGMVKLEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
18-534 |
9.07e-40 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 152.84 E-value: 9.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 18 VKNLEAQGVKHVFGIPGAKIDRVFDSLEDApSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGLATA- 96
Cdd:PRK07525 13 VETLQAHGITHAFGIIGSAFMDASDLFPPA-GIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 97 ---------TSE-GDAVVAFGGavkradslkqtHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRpGASFI 166
Cdd:PRK07525 92 wahtpvvlvTPQaGTKTIGQGG-----------FQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 167 SLPMDIVNEPVSAPVLAGCRLPRmGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAA 246
Cdd:PRK07525 160 NIPRDYFYGVIDVEIPQPVRLER-GAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 247 GVIDVNHfARFAGRVGLFNNQPADQLLQKADLVVSVG-----------YDpIEYDPcmwnshGRLKLVHIDVLPADIDTC 315
Cdd:PRK07525 239 DAFPGSH-PLWVGPLGYNGSKAAMELIAKADVVLALGtrlnpfgtlpqYG-IDYWP------KDAKIIQVDINPDRIGLT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 316 YRPDVELVGNISATLNMMTETFNEAVCVPPEVELILTDLGRQR------------------TELAERAARRGGMPIHPLR 377
Cdd:PRK07525 311 KKVSVGICGDAKAVARELLARLAERLAGDAGREERKALIAAEKsaweqelsswdhedddpgTDWNEEARARKPDYMHPRQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 378 IVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSM 457
Cdd:PRK07525 391 ALREIQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMN 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273381670 458 ELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQRK-SGVEF-GPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQ 534
Cdd:PRK07525 471 EVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRfVGTELdNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQ 549
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
14-539 |
1.80e-39 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 151.68 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGL 93
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 94 ATATSEGDAVVAFGGAVKRA----DSLKQTHQSmdtvSMFRPVTKYCAEVHAGSAISEVIANAFRRAeFGRPGASFISLP 169
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSeigsGYFQETHPQ----ELFRECSHYCELVSNPEQLPRVLAIAMRKA-ILNRGVAVVVLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 170 MDIVNEPVSAPVLAGCRLPRMGAAAADDI--QAAVKLIRQAKCPVLLLG--LQASRPENSEAVRHLlyrtHMPVVGTYQA 245
Cdd:PRK09124 161 GDVALKPAPERATPHWYHAPQPVVTPAEEelRKLAALLNGSSNITLLCGsgCAGAHDELVALAETL----KAPIVHALRG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 246 AGVI------DVnhfarfaGRVGLFNNQPADQLLQKADLVVSVGYDpIEYDPcMWNSHGrlKLVHIDVLPADIDTCYRPD 319
Cdd:PRK09124 237 KEHVeydnpyDV-------GMTGLIGFSSGYHAMMNCDTLLMLGTD-FPYRQ-FYPTDA--KIIQIDINPGSLGRRSPVD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 320 VELVGNISATLNMMtetfneavcvppeveLILTDLGRQRTELAE-----RAARRG----------GMPIHPLRIVKELQD 384
Cdd:PRK09124 306 LGLVGDVKATLAAL---------------LPLLEEKTDRKFLDKalehyRKARKGlddlavpsdgGKPIHPQYLARQISE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 385 IVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFmqsSM---ELET 461
Cdd:PRK09124 371 FAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGF---SMlmgDFLS 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 462 AVRLKNNIVHVIWVDNAYNMVEMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVV 539
Cdd:PRK09124 448 LVQLKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALV 525
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
13-531 |
3.14e-39 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 151.12 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPgakIDRVFDSlEDAPSIETVVVRHEANAAFMAAAVGRLTG--KAGVALVTSGPGSSNLI 90
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGFP---VNELFDA-AAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 91 TGLATATSEGDAVVAFGGAVKRadSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPM 170
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPR--GSTDVAPNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 171 DIVNEPVSAPVLAGCRLPRMGAAAADDIQAAV-KLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVI 249
Cdd:PRK06154 176 DVLAEELDELPLDHRPSRRSRPGADPVEVVEAaALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKSAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 250 DVNHFARFaGRVGLFNNQPADQLLQKADLVVSVGYDPIEYDPCMWNSHGRlKLVHIDVLPADIDTCYRPDVELVGNISAT 329
Cdd:PRK06154 256 PEDHPLAL-GSGGRARPATVAHFLREADVLFGIGCSLTRSYYGLPMPEGK-TIIHSTLDDADLNKDYPIDHGLVGDAALV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 330 LNMMTETFNEAVcvppeveliLTDLGRQRTELAE-RAARRGGM------------PIHPLRIVKELQDIVSDDVTLCV-D 395
Cdd:PRK06154 334 LKQMIEELRRRV---------GPDRGRAQQVAAEiEAVRAAWLakwmpkltsdstPINPYRVVWELQHAVDIKTVIIThD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 396 MGSFHIWIARYlysFRARQLL--ISNGQQT-MGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHV 472
Cdd:PRK06154 405 AGSPRDQLSPF---YVASRPGsyLGWGKTTqLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTI 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2273381670 473 IWVDNA---YNMVEMQEVNKYQ--RKSGvefgpiDFKAYAESCGAVGFAVQSVDDLRPMLRKAM 531
Cdd:PRK06154 482 LLNNFSmggYDKVMPVSTTKYRatDISG------DYAAIARALGGYGERVEDPEMLVPALLRAL 539
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
375-544 |
4.73e-36 |
|
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: 132.27 E-value: 4.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 375 PLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQ 454
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 455 SSMELETAVRLKNNIVHVIWVDNAYNMV--EMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMA 532
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGldGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALA 160
|
170
....*....|..
gi 2273381670 533 IQGPVVVAIPVD 544
Cdd:cd02004 161 SGKPALINVIID 172
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
373-552 |
1.81e-34 |
|
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: 128.38 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 373 IHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGF 452
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 453 MQSSMELETAVRLKNNIVHVIwVDNAY-NMV-EMQEVNKYQRKSGVEFGPI-DFKAYAESCGAVGFAVQSVDDLRPMLRK 529
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVI-LNNGSlGMVrQWQELFYEGRYSHTTLDSNpDFVKLAEAYGIKGLRVEKPEELEAALKE 159
|
170 180
....*....|....*....|...
gi 2273381670 530 AMAIQGPVVVAIPVDYADNYKLM 552
Cdd:cd02015 160 ALASDGPVLLDVLVDPEENVLPM 182
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
13-547 |
2.59e-34 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 137.04 E-value: 2.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRvFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVGIPITD-LARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRA--DSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPM 170
Cdd:PRK09259 91 LANATTNCFPMIMISGSSEREivDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 171 DIVNEPVSAPVLAGCRL------PRMgAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQ 244
Cdd:PRK09259 171 KVLAQTMDADEALTSLVkvvdpaPAQ-LPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 245 AAGVIDVNHFARFAGRVGLfnnqpadqLLQKADLVVSVGydpieydpCMWN---SHGR-------LKLVHIDVLPADIDT 314
Cdd:PRK09259 250 AKGLLPDTHPQSAAAARSL--------ALANADVVLLVG--------ARLNwllSHGKgktwgadKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 315 CYRPDVELVGNISATLNMMTETFNEAVCVPPE--VELILTDLGRQRTELAERAARRGgmpiHPLRI---VKELQDIVSD- 388
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLKQNTFKAPAewLDALAERKEKNAAKMAEKLSTDT----QPMNFynaLGAIRDVLKEn 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 389 -DVTLcVDMGSFHIWIARYL---YSFRARqlLISNGQQTMGVALPWAIGAAlVRPGDKVVSISGDGGFMQSSMELETAVR 464
Cdd:PRK09259 390 pDIYL-VNEGANTLDLARNIidmYKPRHR--LDCGTWGVMGIGMGYAIAAA-VETGKPVVAIEGDSAFGFSGMEVETICR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 465 LKNNIVHVIWVDNA-YNMVEMQEVNkyqrksGVEFGPIDFKAYA------ESCGAVGFAVQSVDDLRPMLRKAMAIQGPV 537
Cdd:PRK09259 466 YNLPVTVVIFNNGGiYRGDDVNLSG------AGDPSPTVLVHHArydkmmEAFGGVGYNVTTPDELRHALTEAIASGKPT 539
|
570
....*....|
gi 2273381670 538 VVAIPVDYAD 547
Cdd:PRK09259 540 LINVVIDPAA 549
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
14-172 |
5.77e-31 |
|
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: 118.04 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGL 93
Cdd:cd07039 3 ADVIVETLENWGVKRVYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2273381670 94 ATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAeFGRPGASFISLPMDI 172
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTA-IAKRGVAVLILPGDV 160
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
15-169 |
7.01e-29 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 112.05 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 15 DLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGkAGVALVTSGPGSSNLITGLA 94
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2273381670 95 TATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEfGRPGASFISLP 169
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAY-ASQGPVVVRLP 153
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
14-544 |
8.39e-29 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 120.79 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPS-IETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALGRADDkPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPV-TKYCAEVHAGSAISEVIANAFRRAEFGRPGASFIsLPMD 171
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI-LPND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 172 IVNEPVSAPVLA--------GCRLPRMGAAAADDIQAAVKLIRQAKcpVLLLGLQASRPENSE--AVRHLLyrthmpvvg 241
Cdd:PRK08273 165 VQELEYEPPPHAhgtvhsgvGYTRPRVVPYDEDLRRAAEVLNAGRK--VAILVGAGALGATDEviAVAERL--------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 242 tyqAAGVI----------DVNHFArfAGRVGLFNNQPADQLLQKAD--LVVSVGYDPIEYDPcmwnSHGRLKLVHIDVLP 309
Cdd:PRK08273 234 ---GAGVAkallgkaalpDDLPWV--TGSIGLLGTKPSYELMRECDtlLMVGSSFPYSEFLP----KEGQARGVQIDIDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 310 ADIDTCYRPDVELVGNISATLNMM------------TETFNEAVcvppeveliltdlgRQRTELAERAARRGGMPIHPLR 377
Cdd:PRK08273 305 RMLGLRYPMEVNLVGDAAETLRALlpllerkkdrswRERIEKWV--------------ARWWETLEARAMVPADPVNPQR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 378 IVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSM 457
Cdd:PRK08273 371 VFWELSPRLPDNAILTADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNGM 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 458 -ELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQRKSGVE--FGP------IDFKAYAESCGAVGFAVQSVDDLRPMLR 528
Cdd:PRK08273 451 aELITVAKYWRQWSDPRLIVLVLNNRDLNQVTWEQRVMEGDpkFEAsqdlpdVPYARFAELLGLKGIRVDDPEQLGAAWD 530
|
570
....*....|....*.
gi 2273381670 529 KAMAIQGPVVVAIPVD 544
Cdd:PRK08273 531 EALAADRPVVLEVKTD 546
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
13-545 |
9.88e-27 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 114.33 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSI-----ETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSS 87
Cdd:PRK08327 9 AAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAgrplpEFVICPHEIVAISMAHGYALVTGKPQAVMVHVDVGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 88 NLITGLATATSEGDAVVAFGGAV---------KRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEF 158
Cdd:PRK08327 89 NALGGVHNAARSRIPVLVFAGRSpyteegelgSRNTRIHWTQEMRDQGGLVREYVKWDYEIRRGDQIGEVVARAIQIAMS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 159 GRPGASFISLPMDIVNEPVSAPVLAGCRL--PRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTH 236
Cdd:PRK08327 169 EPKGPVYLTLPREVLAEEVPEVKADAGRQmaPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASLRRLAEELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 237 MPVV---GTYqaagvidVNhfarFAGRVGLFNNQPADQLLQKADLVVSVGYDpIEYDPCMWNSHGRLKLVHIDVLPADID 313
Cdd:PRK08327 249 IPVVeyaGEV-------VN----YPSDHPLHLGPDPRADLAEADLVLVVDSD-VPWIPKKIRPDADARVIQIDVDPLKSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 314 T---CYRPDVELVGNISATLNMMTETF----NEAVCVPPEVELILTDLgRQRTELAERAA---RRGGMPIHPLRIVKELQ 383
Cdd:PRK08327 317 IplwGFPCDLCIQADTSTALDQLEERLkslaSAERRRARRRRAAVREL-RIRQEAAKRAEierLKDRGPITPAYLSYCLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 384 DIVSDDVTLCVDMGSfhiwIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSME--LET 461
Cdd:PRK08327 396 EVADEYDAIVTEYPF----VPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaHWV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 462 AVRLKNNIVHVIWVDNAYNMVEMQEVNKY-----QRKS---GVEFGP-IDFKAYAESCGAVGFAVQSVDDLRPMLRKAMA 532
Cdd:PRK08327 472 AERYGLPVLVVVFNNGGWLAVKEAVLEVYpegyaARKGtfpGTDFDPrPDFAKIAEAFGGYGERVEDPEELKGALRRALA 551
|
570
....*....|....*..
gi 2273381670 533 I----QGPVVVAIPVDY 545
Cdd:PRK08327 552 AvrkgRRSAVLDVIVDR 568
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
202-333 |
1.51e-24 |
|
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: 99.18 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 202 VKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMPVVGTYQAAGVIDVNHFaRFAGRVGLFNNQPADQLLQKADLVVS 281
Cdd:pfam00205 5 AELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHP-LYLGMLGMHGTPAANEALEEADLVLA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2273381670 282 VGYDPIEYDPCMWNSH--GRLKLVHIDVLPADIDTCYRPDVELVGNISATLNMM 333
Cdd:pfam00205 84 VGARFDDIRTTGKLPEfaPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
14-477 |
1.50e-22 |
|
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: 101.39 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 14 ADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGkAGVALVTSGPGSSNLITGL 93
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNG-LGALVTTYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 94 ATATSEGDAVVAFGGA----VKRADSLkqTHQS-----MDTVS-MFRPVTKYCAEVHAGSAISE---VIANAFRRaefGR 160
Cdd:COG3961 87 AGAYAERVPVVHIVGApgtrAQRRGPL--LHHTlgdgdFDHFLrMFEEVTVAQAVLTPENAAAEidrVLAAALRE---KR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 161 PGasFISLPMDIVNEPVSAPV--LAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPENSEAVRHLLYRTHMP 238
Cdd:COG3961 162 PV--YIELPRDVADAPIEPPEapLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 239 VVGTYQAAGVIDVNHfARFAG-RVGLFNNQPADQLLQKADLVVSVGYDPIEYDPCMWNSHGRL-KLVHIDVLPADI-DTC 315
Cdd:COG3961 240 VATTLLGKSVLDESH-PQFIGtYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPeRTIDIQPDSVRVgGHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 316 YrPDVELVGNISAtlnmmtetfneavcvppeveliLTDLGRQRTELAERAARRGGMPI----HPL---RIVKELQDIVSD 388
Cdd:COG3961 319 Y-PGVSLADFLEA----------------------LAELLKKRSAPLPAPAPPPPPPPaapdAPLtqdRLWQRLQAFLDP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 389 DVTLCVDMGSFhiwiarylySFRARQLLISNGQQ--------TMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELE 460
Cdd:COG3961 376 GDIVVADTGTS---------LFGAADLRLPEGATfiaqplwgSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELS 446
|
490
....*....|....*..
gi 2273381670 461 TAVRLKNNIVhVIWVDN 477
Cdd:COG3961 447 TMLRYGLKPI-IFVLNN 462
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
370-544 |
7.71e-21 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 90.65 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 370 GMPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGD 449
Cdd:cd02013 1 GNPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 450 GGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEMQEVNKYQRK-SGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLR 528
Cdd:cd02013 81 GAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRfVGTELESESFAKIAEACGAKGITVDKPEDVGPALQ 160
|
170
....*....|....*....
gi 2273381670 529 KAMAIQG---PVVVAIPVD 544
Cdd:cd02013 161 KAIAMMAegkTTVIEIVCD 179
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
21-544 |
5.45e-19 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 90.40 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 21 LEAQGVKHVFGIPGAKiDRVFdsLEDAPS-IETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITGLATA-TS 98
Cdd:PRK07092 22 LRRFGITTVFGNPGST-ELPF--LRDFPDdFRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAfKN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 99 EGDAVVAFGGAVKRADSLKQTHQSMDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISLPMDIVNEPvs 178
Cdd:PRK07092 99 HTPLVITAGQQARSILPFEPFLAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDQP-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 179 APVLAGCRLPRMGAAAADDIQAAVKLIRQAKCPVLLLGLQASRPE-NSEAVRhLLYRTHMPV-VGTYQAAGVIDVNH--F 254
Cdd:PRK07092 177 AEPLPARTVSSAVRPDPAALARLGDALDAARRPALVVGPAVDRAGaWDDAVR-LAERHRAPVwVAPMSGRCSFPEDHplF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 255 ARF--AGRVGLfnnqpaDQLLQKADLVVSVG--------YDPIEYDPcmwnshGRLKLVHIdvlPADIDTCYRPDV--EL 322
Cdd:PRK07092 256 AGFlpASREKI------SALLDGHDLVLVIGapvftyhvEGPGPHLP------EGAELVQL---TDDPGEAAWAPMgdAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 323 VGNISATLNMMTETFNEAVCVPPEveliltdlGRQRTElaerAARRGGMPIHPLRIVKELQDIVSDDVTLCVDMGSFHIW 402
Cdd:PRK07092 321 VGDIRLALRDLLALLPPSARPAPP--------ARPMPP----PAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRPA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 403 IARYL-------YSFRArqlliSNGqqtMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWV 475
Cdd:PRK07092 389 MQEHLpmrrqgsFYTMA-----SGG---LGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILN 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 476 DNAYN-MVEMQEVNKYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK07092 461 NGRYGaLRWFAPVFGVRDVPGLDLPGLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
373-543 |
1.39e-18 |
|
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: 83.41 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 373 IHPLRIVKELQDIVSDDVTLcVDMGSFHIWIARYLYSFRARQLLISNGQQTMGVALPWAIGAALVRPGDKVVSISGDGGF 452
Cdd:cd02002 1 LTPEYLAAALAAALPEDAII-VDEAVTNGLPLRDQLPLTRPGSYFTLRGGGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 453 MQSSMELETAVRLKNNIVHVIWVDNAYNM--VEMQEVNKYQRKSGVEFGP------IDFKAYAESCGAVGFAVQSVDDLR 524
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGAlrSFLKRVGPEGPGENAPDGLdlldpgIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 2273381670 525 PMLRKAMAIQGPVVVAIPV 543
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
13-539 |
7.14e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 71.06 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 13 GADLVVKNLEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGKAGVALVTSGPGSSNLITG 92
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 93 LATATSEGDAVVAFGG--AVKRA--DSLKQThqsmDTVSMFRPVTKYCAEVHAGSAISEVIANAFRRAEFGRPGASFISL 168
Cdd:PRK12474 87 LHNARRAASPIVNIVGdhAVEHLqyDAPLTS----DIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 169 PMDIV-NEPV-SAPVLAGCRLPRMGAAAADDIQaavKLIRQAKCPVLLL--------GLQ-ASRPENSEAVRhLLYRTHM 237
Cdd:PRK12474 163 PADVAwNEAAyAAQPLRGIGPAPVAAETVERIA---ALLRNGKKSALLLrgsalrgaPLEaAGRIQAKTGVR-LYCDTFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 238 PvvGTYQAAGVIDVNHFARFAGRVGLFnnqpadqlLQKADLVVSVGYDPIEYDPCMWNSHGRLKlvhidvlPA--DIDTC 315
Cdd:PRK12474 239 P--RIERGAGRVPIERIPYFHEQITAF--------LKDVEQLVLVGAKPPVSFFAYPGKPSWGA-------PPgcEIVYL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 316 YRPDVELVGNISaTLNMMTETFNEAVCVPPeveLILTDLGRQRTELAERAarrggmpihplRIVKEL---QDIVSDDVTl 392
Cdd:PRK12474 302 AQPDEDLAQALQ-DLADAVDAPAEPAARTP---LALPALPKGALNSLGVA-----------QLIAHRtpdQAIYADEAL- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 393 cVDMGSFHIWIArylysfRAR---QLLISNGqqTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNI 469
Cdd:PRK12474 366 -TSGLFFDMSYD------RARphtHLPLTGG--SIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDV 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 470 VHVIWVDNAYNM--VEMQEVN------KYQRKSGVEFGPIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVV 539
Cdd:PRK12474 437 TVVIFANRSYAIlnGELQRVGaqgagrNALSMLDLHNPELNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLI 514
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
420-544 |
2.23e-12 |
|
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: 66.17 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 420 GQQTMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVhVIWVDNAynmvEMQEVNKYQRKSGVE-F 498
Cdd:cd02003 46 GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKII-IVLFDNH----GFGCINNLQESTGSGsF 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2273381670 499 G------------------PIDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:cd02003 121 GtefrdrdqesgqldgallPVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
371-548 |
1.75e-10 |
|
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: 60.76 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 371 MPIHPLRIVKELQDIVSDDVTLCVDMGSFHIWIARYLYSFRARQLlISNGQQ-TMGVALPWAIGAALVRPGDKVVSISGD 449
Cdd:cd02006 6 VPIKPQRVYEEMNKAFGRDVRYVTTIGLSQIAGAQMLHVYKPRHW-INCGQAgPLGWTVPAALGVAAADPDRQVVALSGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 450 GGFMQSSMELETAVRLKNNIVHVIwVDNAY-----------NM-----VEMQEVNkyqrKSGVEFGPIDFKAYAESCGAV 513
Cdd:cd02006 85 YDFQFMIEELAVGAQHRIPYIHVL-VNNAYlglirqaqrafDMdyqvnLAFENIN----SSELGGYGVDHVKVAEGLGCK 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2273381670 514 GFAVQSVDDLRPMLRKAMAIQG----PVVVAIPVDYADN 548
Cdd:cd02006 160 AIRVTKPEELAAAFEQAKKLMAehrvPVVVEAILERVTN 198
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
425-536 |
1.69e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 60.24 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 425 GVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLKNNIVHVIWVDNAYNMVEMQevnkYQRKSGVEFGP---- 500
Cdd:PRK07586 388 GQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGE----LARVGAGNPGPrald 463
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2273381670 501 --------IDFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGP 536
Cdd:PRK07586 464 mldlddpdLDWVALAEGMGVPARRVTTAEEFADALAAALAEPGP 507
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
21-169 |
1.60e-08 |
|
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: 54.04 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 21 LEAQGVKHVFGIPGAKIDRVFDSLEDAPSIETVVVRHEANAAFMAAAVGRLTGkAGVALVTSGPGSSNLITGLATATSEG 100
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIAGAYAEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 101 DAVVAFGGAVKRADSLKQT---HQSMDTV-----SMFRPVTkyCAEVH------AGSAISEVIANAFRraeFGRPGasFI 166
Cdd:cd07038 86 VPVVHIVGAPSTKAQASGLllhHTLGDGDfdvflKMFEEIT--CAAARltdpenAAEEIDRVLRTALR---ESRPV--YI 158
|
...
gi 2273381670 167 SLP 169
Cdd:cd07038 159 EIP 161
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
423-539 |
2.24e-07 |
|
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: 51.12 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 423 TMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSME-LETAVRLKNNIVHVIwVDNAYnmVEM---QEVNKYQRKSGVEF 498
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTFFHSGILgLINAVYNKANITVVI-LDNRT--TAMtggQPHPGTGKTLTEPT 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2273381670 499 GPIDFKAYAESCGAVGFAVQSVDDLRPM---LRKAMAIQGPVVV 539
Cdd:cd02008 129 TVIDIEALVRAIGVKRVVVVDPYDLKAIreeLKEALAVPGVSVI 172
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
403-543 |
2.63e-07 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 51.16 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 403 IARYLYSFRARqLLISNGQQ-----TMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELETAVRLK-NNIVHVIWVD 476
Cdd:cd03371 25 TSRELFELRDR-PGGGHAQDfltvgSMGHASQIALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLApANLIHIVLNN 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2273381670 477 NAYNMVEMQEVNKYQrksgvefgpIDFKAYAESCG-AVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPV 543
Cdd:cd03371 104 GAHDSVGGQPTVSFD---------VSLPAIAKACGyRAVYEVPSLEELVAALAKALAADGPAFIEVKV 162
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
423-544 |
1.26e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 49.44 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 423 TMGVALPWAIGAALVRPGDKVVSISGDGGFMQSSMELET-AVRLKNNIVHVIWVDNAYNMVEMQEVNKYQrksgvefgPI 501
Cdd:PRK06163 58 SMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDNGVYQITGGQPTLTSQ--------TV 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2273381670 502 DFKAYAESCG-AVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPVD 544
Cdd:PRK06163 130 DVVAIARGAGlENSHWAADEAHFEALVDQALSGPGPSFIAVRID 173
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
423-544 |
2.22e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 45.36 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 423 TMGVALPWAIGAALVRPgDKVVSISGDGGFMQSSMELET--AVRLKNNIVHVIwvDN-AYNMVEMQEVNKYQRksgvefg 499
Cdd:cd03372 43 SMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATiaAEKPKNLIIVVL--DNgAYGSTGNQPTHAGKK------- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2273381670 500 pIDFKAYAESCG-AVGFAVQSVDDLRPMLrkAMAIQGPVVVAIPVD 544
Cdd:cd03372 113 -TDLEAVAKACGlDNVATVASEEAFEKAV--EQALDGPSFIHVKIK 155
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
377-479 |
2.59e-04 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 42.14 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 377 RIVKELQDIVSDDVTLCVDMGSFhiwiarylySFRARQLLISNGQQ--------TMGVALPWAIGAALVRPGDKVVSISG 448
Cdd:cd02005 6 RLWQQVQNFLKPNDILVAETGTS---------WFGALDLKLPKGTRfisqplwgSIGYSVPAALGAALAAPDRRVILLVG 76
|
90 100 110
....*....|....*....|....*....|.
gi 2273381670 449 DGGFMQSSMELETAVRLKNNIVHVIWVDNAY 479
Cdd:cd02005 77 DGSFQMTVQELSTMIRYGLNPIIFLINNDGY 107
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|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
423-543 |
2.70e-04 |
|
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: 41.70 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273381670 423 TMGVALPWAIGAALVRPgDKVVSISGDGGFMQSSMELETAVRLK-NNIVHVIWVDNAYNMVEMQEVNKyqrksgvefGPI 501
Cdd:cd02001 43 SMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYGSTGGQPTPS---------SNV 112
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2273381670 502 DFKAYAESCGAVGFAVQSVDDLRPMLRKAMAIQGPVVVAIPV 543
Cdd:cd02001 113 NLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPI 154
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