|
Name |
Accession |
Description |
Interval |
E-value |
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
1-637 |
0e+00 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 1095.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 1 MGKKIRLTTAQALIKFLNQQYIHVDGKEEPFVEGIFTIFGHGNVLGIGQALEQDAGHLKVYQGKNEQGMAHAAMAYSKQM 80
Cdd:COG3962 1 MMKTIRLTVAQALVRFLANQYVERDGEEQPLFAGVFGIFGHGNVAGLGQALEQDPDELPTYQGRNEQGMAHAAIAYAKQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 81 LRRKIYAVSTSVGPGAANLVAAAGTALANNIPVLLIPADTFATRQPDPVLQQMEQEYSAAITTNDALKPVSRYWDRITRP 160
Cdd:COG3962 81 NRRRIMACTSSIGPGATNMVTAAALATANRLPVLLLPGDTFATRQPDPVLQQLEHFHDPTISVNDAFRPVSRYWDRITRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 161 EQLMSSLLRAFEVMTDPAKAGPATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGG 240
Cdd:COG3962 161 EQLMSALPRAMRVLTDPAETGAVTLALPQDVQAEAYDYPESFFAKRVHRIRRPPPDPAELARAVELIRAAKRPLIIAGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 241 AKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDF 320
Cdd:COG3962 241 VRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTRLQDFTTGSKTLFAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 321 DKAKFLNINVSRMQAYKLDAFQVVADAKVTLGKLHGLLEG--YESEFGTTFRELKDEWLAERERLskvtfkreafdpeik 398
Cdd:COG3962 321 PDVRFVNINVARFDAYKHDALPVVADAREGLEALTEALAGwrYPAAWTDEAAELKAEWDAEVDRL--------------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 399 nhfsqevlneYADALNTELPQTTALLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGL 478
Cdd:COG3962 386 ----------YAPTNGGLPTQAQVIGAVNEAAGPDDIVVCAAGSLPGDLHKLWRTRDPGTYHVEYGYSCMGYEIAGGLGV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 479 KLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRT-------DDNQILN 551
Cdd:COG3962 456 KLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDNHGFGCINRLQMSTGSQSFGTELRDrdtetgrLDGGLLP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 552 VDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLPKTMTDGYDSWWHVGVAEVSEQESVQKAYEAKEKKL 631
Cdd:COG3962 536 VDFAANAASLGAKAYRVTTIAELRAALERAKAADRTTVIVIKTDPKTMTPGGGSWWDVGVAEVSERESVRAARAEYEEAR 615
|
....*.
gi 504294315 632 ESAKQY 637
Cdd:COG3962 616 AKQRRY 621
|
|
| myo_inos_iolD |
TIGR04377 |
3,5/4-trihydroxycyclohexa-1,2-dione hydrolase; Members of this protein family, 3,5 ... |
6-635 |
0e+00 |
|
3,5/4-trihydroxycyclohexa-1,2-dione hydrolase; Members of this protein family, 3,5/4-trihydroxycyclohexa-1,2-dione hydrolase (iolD), represent one of eight enzymes in a pathway converting myo-inositol to acetyl-CoA. IolD hydrolyzes the cyclic molecule 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione to yield 5-deoxy-D-glucuronic acid. TPP is a cofactor. [Energy metabolism, Sugars]
Pssm-ID: 275170 [Multi-domain] Cd Length: 615 Bit Score: 1001.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 6 RLTTAQALIKFLNQQYIHVDGKEEPFVEGIFTIFGHGNVLGIGQALEQDAGHLKVYQGKNEQGMAHAAMAYSKQMLRRKI 85
Cdd:TIGR04377 1 RLTMAQALVRFLAAQYVERDGEEVPFFAGVFAIFGHGNVAGLGEALEEDPDDLPTYRGRNEQGMAHAAIAYAKQKNRRRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 86 YAVSTSVGPGAANLVAAAGTALANNIPVLLIPADTFATRQPDPVLQQMEQEYSAAITTNDALKPVSRYWDRITRPEQLMS 165
Cdd:TIGR04377 81 MACTSSIGPGATNMVTAAALATVNRLPVLLLPGDTFATRQPDPVLQQLEDFSDLTVSVNDAFRPVSRYFDRITRPEQLMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 166 SLLRAFEVMTDPAKAGPATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSG 245
Cdd:TIGR04377 161 ALPNAMRVLTDPAETGAVTLALPQDVQAEAYDYPESFFAKRVHRIRRPEPDPAELERAVAAIRAAKKPLIVAGGGVHYSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 246 ARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDFDKAKF 325
Cdd:TIGR04377 241 AGEALAAFAEKHGIPVAETQAGKGALPWDHPLNLGAIGVTGTLAANALAAEADLVIAVGTRLQDFTTASKTLFQNPDVRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 326 LNINVSRMQAYKLDAFQVVADAKVTLGKLHGLLEGYE--SEFGTTFRELKDEWLAERERLSKVTFKreafdpeiknhfsq 403
Cdd:TIGR04377 321 VNINVARFDAYKHDALPLVADARAGLEALSEALGGYRadSAWAAEAAAAKAAWDAEVDRLYAAEYT-------------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 404 evlneyadalNTELP-QTTALLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAH 482
Cdd:TIGR04377 387 ----------AGGLPtQAEVIGAVNRAAGPDDVVVCAAGSLPGDLHKLWRTRDPGGYHMEYGYSCMGYEIAGGLGVKLAE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 483 PDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRTDDNQ-----ILNVDYAKV 557
Cdd:TIGR04377 457 PDREVYVMVGDGSYLMLNSELATSVQEGKKIIVVLLDNRGFGCINNLQMSTGGASFNTELRYEDTGrldggLLPVDFAAH 536
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504294315 558 AEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLPKTMTDGYDSWWHVGVAEVSEQESVQKAYEAKEKKLESAK 635
Cdd:TIGR04377 537 AAALGAKTYKVTTIAELEAALARAKAADRTTLIVIDTDPKTMTEGYGSWWDVGVAEVSERESVRKAREEYEEAKKAQR 614
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
419-616 |
1.25e-118 |
|
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: 351.61 E-value: 1.25e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 419 QTTALLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLM 498
Cdd:cd02003 1 QTEVLGALNEAIGDDDVVINAAGSLPGDLHKLWRARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 499 LHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRTDDN-------QILNVDYAKVAEGYGAKTYRANTV 571
Cdd:cd02003 81 LHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGTEFRDRDQesgqldgALLPVDFAANARSLGARVEKVKTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504294315 572 EELKAALEDAKKQNVSTLIEMKVLPKTMTDGYDSWWHVGVAEVSE 616
Cdd:cd02003 161 EELKAALAKAKASDRTTVIVIKTDPKSMTPGYGSWWDVGVAEVSE 205
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
6-596 |
3.32e-113 |
|
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: 349.84 E-value: 3.32e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 6 RLTTAQALIKFLNQqyihvdgkeepfvEGIFTIFGH--GNVLGIGQALEQDAGhLKVYQGKNEQGMAHAAMAYSKqmLRR 83
Cdd:COG0028 2 KMTGADALVEALEA-------------EGVETVFGVpgGAILPLYDALRRQSG-IRHILVRHEQGAAFMADGYAR--ATG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 84 KIYAVSTSVGPGAANLVAAAGTALANNIPVLLI----PADTFATRQpdpvLQQMEQeysAAITtndalKPVSRYWDRITR 159
Cdd:COG0028 66 KPGVCLVTSGPGATNLVTGLADAYMDSVPVLAItgqvPTSLIGRGA----FQEVDQ---VGLF-----RPITKWSYLVTD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 160 PEQLMSSLLRAFEVMTDPaKAGPATICISQDVEGEAYDFdESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGG 239
Cdd:COG0028 134 PEDLPEVLRRAFRIATSG-RPGPVVLDIPKDVQAAEAEE-EPAPPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 240 GAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFD 319
Cdd:COG0028 212 GARRAGAAEELRALAERLGAPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 320 fDKAKFLNINVSRMQ---AYKLDAFqVVADAKVTLGKLHGLLEGYESEfgttfrelKDEWLAERERLSKvtfkreafdpe 396
Cdd:COG0028 292 -PDAKIIHIDIDPAEigkNYPVDLP-IVGDAKAVLAALLEALEPRADD--------RAAWLARIAAWRA----------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 397 iknhfsqEVLNEYADALNTELPQtTALLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTL 476
Cdd:COG0028 351 -------EYLAAYAADDGPIKPQ-RVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAI 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 477 GLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYY-CEFRtddnqilNVDYA 555
Cdd:COG0028 423 GAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGGRYSgTDLP-------NPDFA 495
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 504294315 556 KVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:COG0028 496 KLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDP 536
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
33-594 |
4.83e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 202.25 E-value: 4.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGI-GQALEQDagHLKVYQGKNEQGMAHAAMAYSKQMLRRKIyAVSTSvGPGAANLVAAAGTALAN 109
Cdd:PRK08527 16 EGVKVVFGYpgGAILNIyDEIYKQN--YFKHILTRHEQAAVHAADGYARASGKVGV-AIVTS-GPGFTNAVTGLATAYMD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 110 NIPVLLIPAdtfatrqpdpvlqqmeQEYSAAITTnDALKPVSRYwdRITRP-----------EQLMSSLLRAFEVMTDpA 178
Cdd:PRK08527 92 SIPLVLISG----------------QVPNSLIGT-DAFQEIDAV--GISRPcvkhnylvksiEELPRILKEAFYIARS-G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 179 KAGPATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYN 258
Cdd:PRK08527 152 RPGPVHIDIPKDVTATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 259 IPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDfDKAKFLNINVSRMQAYKL 338
Cdd:PRK08527 232 IPAVETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFA-KHAKIIHVDIDPSSISKI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 339 DA--FQVVADAKVTLGKLHGLLEGYESEFGTTFRELkdewLAERERLSKVTFKReafdpeiknhfSQEVLNeyadalnte 416
Cdd:PRK08527 311 VNadYPIVGDLKNVLKEMLEELKEENPTTYKEWREI----LKRYNELHPLSYED-----------SDEVLK--------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 417 lPQtTALLTINETIPEDSVIICSAGSlpgdlQRLWHS-----NVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIV 491
Cdd:PRK08527 367 -PQ-WVIERVGELLGDDAIISTDVGQ-----HQMWVAqfypfNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFT 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 492 GDGSFLMLHSELITAIQYNKK-INVLLfDNSGFGCINNLQMdhgsgSYYCEFRTDDNQILNVDYAKVAEGYGAKTYRANT 570
Cdd:PRK08527 440 GDGSILMNIQELMTAVEYKIPvINIIL-NNNFLGMVRQWQT-----FFYEERYSETDLSTQPDFVKLAESFGGIGFRVTT 513
|
570 580
....*....|....*....|....
gi 504294315 571 VEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK08527 514 KEEFDKALKEALESDKVALIDVKI 537
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
33-601 |
8.02e-57 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 201.01 E-value: 8.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFG--HGNVLGIGQALEQDAGHLKVYQGKNEQGMAHAAMAYSKQMLRRKIYAVSTsvGPGAANLVAAAGTALANN 110
Cdd:PRK08266 17 HGVDTVFGlpGAQLYWLFDALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVP--GPGVLNAGAALLTAYGCN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 111 IPVLL----IPADTFAtrQPDPVLQQMEQEYSAaittndaLKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATIC 186
Cdd:PRK08266 95 SPVLCltgqIPSALIG--KGRGHLHEMPDQLAT-------LRSFTKWAERIEHPSEAPALVAEAFQQMLS-GRPRPVALE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 187 ISQDVEGEAYDFDEsffVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAkySGARDELVAISEAYNIPLVETQA 266
Cdd:PRK08266 165 MPWDVFGQRAPVAA---APPLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 267 GKSTVEADFANNLGgmgitgTLAANKAARQADLIIGIGTRYTDfaTSSKTAFDFDKAKFLNINV--SRMQAYKLDAfQVV 344
Cdd:PRK08266 240 GRGIVSDRHPLGLN------FAAAYELWPQTDVVIGIGSRLEL--PTFRWPWRPDGLKVIRIDIdpTEMRRLKPDV-AIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 345 ADAKvtlgklHGLlegyesefgttfRELKDewlAERERLSKVTFKREAFdpeiknhfsqEVLNEYADALNTEL-PQTTAL 423
Cdd:PRK08266 311 ADAK------AGT------------AALLD---ALSKAGSKRPSRRAEL----------RELKAAARQRIQAVqPQASYL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 424 LTINETIPEDSVI---ICSAGslpgdlqrlWHSNV------PNTYhLEYGYS-CMGYEVSGTLGLKLAHPDREVYSIVGD 493
Cdd:PRK08266 360 RAIREALPDDGIFvdeLSQVG---------FASWFafpvyaPRTF-VTCGYQgTLGYGFPTALGAKVANPDRPVVSITGD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 494 GSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYyceFRTDdnqILNVDYAKVAEGYGAKTYRANTVEE 573
Cdd:PRK08266 430 GGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRV---VASD---LVNPDFVKLAESFGVAAFRVDSPEE 503
|
570 580
....*....|....*....|....*...
gi 504294315 574 LKAALEDAKKQNVSTLIEMKVLPKTMTD 601
Cdd:PRK08266 504 LRAALEAALAHGGPVLIEVPVPRGSEAS 531
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-594 |
7.28e-56 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 198.85 E-value: 7.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 2 GKKIRLTTAQALIKFLNQqyihvdgkeepfvEGIFTIFGH--GNVLGIGQAL-EQDAGHLKVyqgKNEQGMAHAAMAYSK 78
Cdd:PRK06048 3 GSTEKMTGARAIIKCLEK-------------EGVEVIFGYpgGAIIPVYDELyDSDLRHILV---RHEQAAAHAADGYAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 79 QMLRRKIyAVSTSvGPGAANLVAAAGTALANNIPVL---------LIPADTFatrqpdpvlqqmeQEysAAITtnDALKP 149
Cdd:PRK06048 67 ATGKVGV-CVATS-GPGATNLVTGIATAYMDSVPIValtgqvprsMIGNDAF-------------QE--ADIT--GITMP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 150 VSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKS 229
Cdd:PRK06048 128 ITKHNYLVQDAKDLPRIIKEAFHIAST-GRPGPVLIDLPKDVTTAEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 230 SKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTD 309
Cdd:PRK06048 207 AERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 310 FATSSKTAFDfDKAKFLNINVSRMQAYKLDAFQV--VADAKVTLGKLHGLLEgyesefgttfRELKDEWlaererLSKVt 387
Cdd:PRK06048 287 RVTGKLASFA-PNAKIIHIDIDPAEISKNVKVDVpiVGDAKQVLKSLIKYVQ----------YCDRKEW------LDKI- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 388 fkreafdpeikNHFSQEVLNEYADALNTELPQTTaLLTINETIPeDSVIICSAGSlpgdlQRLWHSNV-----PNTYHLE 462
Cdd:PRK06048 349 -----------NQWKKEYPLKYKEREDVIKPQYV-IEQIYELCP-DAIIVTEVGQ-----HQMWAAQYfkykyPRTFITS 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 463 YGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEF 542
Cdd:PRK06048 411 GGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELFYDKRYSHTC 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 504294315 543 RTDdnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK06048 491 IKG-----SVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIV 537
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
7-596 |
1.25e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 198.82 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 7 LTTAQALIKFLNQqyihvdgkeepfvEGIFTIFGH--GNVLGIGQAL-EQDAGHLKVyqgKNEQGMAHAAMAYSKQMLRR 83
Cdd:PRK06276 1 MKGAEAIIKALEA-------------EGVKIIFGYpgGALLPFYDALyDSDLIHILT---RHEQAAAHAADGYARASGKV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 84 KIyAVSTSvGPGAANLVAAAGTALANNIPVL---------LIPADTFatrqpdpvlqqmeQEYSA-AITTndalkPVSRY 153
Cdd:PRK06276 65 GV-CVATS-GPGATNLVTGIATAYADSSPVIaltgqvptkLIGNDAF-------------QEIDAlGIFM-----PITKH 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 154 WDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEAYDFDESFFVKRVH---YIDRMQPSERELQGAAELIKSS 230
Cdd:PRK06276 125 NFQIKKPEEIPEIFRAAFEIAKT-GRPGPVHIDLPKDVQEGELDLEKYPIPAKIDlpgYKPTTFGHPLQIKKAAELIAEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 231 KKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDF 310
Cdd:PRK06276 204 ERPVILAGGGVIISGASEELIELSELVKIPVCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 311 ATSSKTAFDFDkAKFLNINVSRMQAYKLDAFQV--VADAKVTLGKLHGLLEGYEsefgttfRELKDEWLAERERLSKVTF 388
Cdd:PRK06276 284 TTGDISSFAPN-AKIIHIDIDPAEIGKNVRVDVpiVGDAKNVLRDLLAELMKKE-------IKNKSEWLERVKKLKKESI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 389 KREAFDPE-IKnhfSQEVLNEYADALNTELPQTtalltinetipeDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSC 467
Cdd:PRK06276 356 PRMDFDDKpIK---PQRVIKELMEVLREIDPSK------------NTIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGT 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 468 MGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHgSGSYYCEFRTDDN 547
Cdd:PRK06276 421 MGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVYQWQNLY-YGKRQSEVHLGET 499
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 504294315 548 QilnvDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:PRK06276 500 P----DFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDP 544
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
22-594 |
5.74e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 196.60 E-value: 5.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 22 IHVDGKEEPFVEGIFTIFGHGNvLGIGQALEQD--AGHLKVYQGKNEQGMAHAAMAYSKQMLRRKIyaVSTSVGPGAANL 99
Cdd:PRK06456 7 ILVDSLKREGVKVIFGIPGLSN-MQIYDAFVEDlaNGELRHVLMRHEQAAAHAADGYARASGVPGV--CTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 100 VAAAGTALANNIPVLLIPADTfatrqPDPVLQQMEQEYSAAITTndaLKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAK 179
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQV-----PRSVMGKMAFQEADAMGV---FENVTKYVIGIKRIDEIPQWIKNAFYIATT-GR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 180 AGPATICISQDVEGEAYD---FDESFFVKRVH----YIDRMqpserELQGAAELIKSSKKPVILVGGGAKYSGARDELVA 252
Cdd:PRK06456 155 PGPVVIDIPRDIFYEKMEeikWPEKPLVKGYRdfptRIDRL-----ALKKAAEILINAERPIILVGTGVVWSNATPEVLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 253 ISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDFDKAKFLNINVSR 332
Cdd:PRK06456 230 LAELLHIPIVSTFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETRKKFIMVNIDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 333 ---MQAYKLDAfQVVADAKVTLGKLHGLLegyeSEFGTTFRelKDEWLaererlskvtfKREAfdpEIKNHFSQEvlneY 409
Cdd:PRK06456 310 tdgEKAIKVDV-GIYGNAKIILRELIKAI----TELGQKRD--RSAWL-----------KRVK---EYKEYYSQF----Y 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 410 ADALNTELPQTTALLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYS 489
Cdd:PRK06456 365 YTEENGKLKPWKIMKTIRQALPRDAIVTTGVGQHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 490 IVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQmDHGSGsyycefrtddNQILNVDYA------KVAEGYGA 563
Cdd:PRK06456 445 LDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVRQVQ-DLFFG----------KRIVGVDYGpspdfvKLAEAFGA 513
|
570 580 590
....*....|....*....|....*....|.
gi 504294315 564 KTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK06456 514 LGFNVTTYEDIEKSLKSAIKEDIPAVIRVPV 544
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
52-596 |
2.12e-53 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 192.52 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 52 EQDAghLKVYQGKNEQGMAHAAMAYSKqmLRRKIyAVSTSV-GPGAANLVAAAGTALANNIPVLLIPADTFATrqpdpvl 130
Cdd:PRK08611 40 EQDK--IKFIQVRHEEVAALAAAAYAK--LTGKI-GVCLSIgGPGAIHLLNGLYDAKMDHVPVLALAGQVTSD------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 131 qQMEQEYSAAITTNDALKPVSRYWDRITRPEQLMSSLLRAfeVMTDPAKAGPATICISQDV----EGEAYDFDESFFVKR 206
Cdd:PRK08611 108 -LLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQA--IRTAYEKKGVAVLTIPDDLpaqkIKDTTNKTVDTFRPT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 207 VhyidrMQPSERELQGAAELIKSSKKPVILVGGGAKysGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITG 286
Cdd:PRK08611 185 V-----PSPKPKDIKKAAKLINKAKKPVILAGLGAK--HAKEELLAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNLGKIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 287 TLAANKAARQADLIIGIGTR--YTDFATssktafdfDKAKFLNINVSRMQA---YKLDAfQVVADAKVTLGKLhgllegy 361
Cdd:PRK08611 258 TKPAYEAMQEADLLIMVGTNypYVDYLP--------KKAKAIQIDTDPANIgkrYPVNV-GLVGDAKKALHQL------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 362 esefgTTFRELKDewlaERERLSKVTFKREAFDPEIKNhfsqevlneyaDALNTELP----QTTAllTINETIPEDSVII 437
Cdd:PRK08611 322 -----TENIKHVE----DRRFLEACQENMAKWWKWMEE-----------DENNASTPikpeRVMA--AIQKIADDDAVLS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 438 CSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLL 517
Cdd:PRK08611 380 VDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVV 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504294315 518 FDNSGFGCINNLQMDHGSGSYYCEFRtddnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:PRK08611 460 LNNQQLAFIKYEQQAAGELEYAIDLS-------DMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDP 531
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
66-594 |
1.74e-52 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 189.27 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 66 EQGMAHAAMAYSKqmLRRKIYAVSTSVGPGAANLVAAAGTALANNIPVLLIpadtfaTRQ-PdpvLQQMEQEYSAAITTN 144
Cdd:PRK08322 47 EQGAAFMAATYGR--LTGKAGVCLSTLGPGATNLVTGVAYAQLGGMPMVAI------TGQkP---IKRSKQGSFQIVDVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 145 DALKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEAYDFDesffVKRVHYIDRMQPSERELQGAA 224
Cdd:PRK08322 116 AMMAPLTKWTRQIVSPDNIPEVVREAFRLAEE-ERPGAVHLELPEDIAAEETDGK----PLPRSYSRRPYASPKAIERAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 225 ELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIG 304
Cdd:PRK08322 191 EAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 305 TRYTDFAtssktafdfdkAKFLN-------INVSRMQA-----YKLDAfQVVADakvtlgklhgllegyeseFGTTFREL 372
Cdd:PRK08322 271 HDVIEKP-----------PFFMNpngdkkvIHINFLPAevdpvYFPQV-EVVGD------------------IANSLWQL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 373 KdewlaerERLSKVTFKREAFDPEIKNHFSQEvLNEYADAlnTELPQTTALL--TINETIPEDSVIICSAGSLPGDLQRL 450
Cdd:PRK08322 321 K-------ERLADQPHWDFPRFLKIREAIEAH-LEEGADD--DRFPMKPQRIvaDLRKVMPDDDIVILDNGAYKIWFARN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 451 WHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ 530
Cdd:PRK08322 391 YRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQ 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504294315 531 MDHGSGSYYCEFRtddnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK08322 471 ENMGFEDFGLDFG-------NPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPV 527
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
440-591 |
3.16e-50 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 171.23 E-value: 3.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 440 AGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFD 519
Cdd:pfam02775 2 IGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504294315 520 NSGFGCINNLQMDHGSGSYYCefrTDDNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIE 591
Cdd:pfam02775 82 NGGYGMTRGQQTPFGGGRYSG---PSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALID 150
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
34-594 |
3.88e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 180.40 E-value: 3.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 34 GIFTIFGH--GNVLGIGQALEQDAGhLKVYQGKNEQGMAHAAMAYSKQMLRRKIyAVSTSvGPGAANLVAAAGTALANNI 111
Cdd:PRK07282 24 GVDTIFGYpgGAVLPLYDAIYNFEG-IRHILARHEQGALHEAEGYAKSTGKLGV-AVVTS-GPGATNAITGIADAMSDSV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 112 PVLL---------IPADTFatRQPDPVlqqmeqeysaAITTndalkPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGP 182
Cdd:PRK07282 101 PLLVftgqvaragIGKDAF--QEADIV----------GITM-----PITKYNYQIRETADIPRIITEAVHIATT-GRPGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 183 ATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLV 262
Cdd:PRK07282 163 VVIDLPKDVSALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 263 ETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDfDKAKFLNINVSRMQAYKL--DA 340
Cdd:PRK07282 243 TTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFA-KNAKVAHIDIDPAEIGKIikTD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 341 FQVVADAKVTLGKlhgLLEgyESEFGTTFRELKDEWLAERERLSKVTFKREAFDPeiknhfsQEVLNeyadalntelpqt 420
Cdd:PRK07282 322 IPVVGDAKKALQM---LLA--EPTVHNNTEKWIEKVTKDKNRVRSYDKKERVVQP-------QAVIE------------- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 421 tallTINETIPEDSVIICSAGSlpgdlQRLWHSNV---PNTYHL--EYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGS 495
Cdd:PRK07282 377 ----RIGELTNGDAIVVTDVGQ-----HQMWAAQYypyQNERQLvtSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 496 FLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMdhgsgSYYCEFRTDDNQILNVDYAKVAEGYGAKTYRANTVEELK 575
Cdd:PRK07282 448 FQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQE-----SFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLA 522
|
570
....*....|....*....
gi 504294315 576 AALEdAKKQNVSTLIEMKV 594
Cdd:PRK07282 523 QDLE-VITEDVPMLIEVDI 540
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
33-581 |
5.96e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 165.91 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALEQDAghLKVYQGKNEQGMAHAAMAYSKqmLRRKIYAVSTSVGPGAANLVAAAGTALANN 110
Cdd:PRK06725 28 LGVTTVFGYpgGAILPVYDALYESG--LKHILTRHEQAAIHAAEGYAR--ASGKVGVVFATSGPGATNLVTGLADAYMDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 111 IPVLLIPADTFATRQPDPVLQQMEqeySAAITTndalkPVSRYWDRITRPEQLMSSLLRAFEVmTDPAKAGPATICISQD 190
Cdd:PRK06725 104 IPLVVITGQVATPLIGKDGFQEAD---VVGITV-----PVTKHNYQVRDVNQLSRIVQEAFYI-AESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 191 VEGE--AYDFDESFFVKrvHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGK 268
Cdd:PRK06725 175 VQNEkvTSFYNEVVEIP--GYKPEPRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 269 STVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFAT---------SSKTAFDFDKAKF-LNINVSrmqaykl 338
Cdd:PRK06725 253 GAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTgklelfsphSKKVHIDIDPSEFhKNVAVE------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 339 daFQVVADAKVTLGK-LHGLLEGYESEFGTTFRELKDEWlaererlsKVTFKREafDPEIKnhfSQEVLNEYADALNTEL 417
Cdd:PRK06725 326 --YPVVGDVKKALHMlLHMSIHTQTDEWLQKVKTWKEEY--------PLSYKQK--ESELK---PQHVINLVSELTNGEA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 418 PQTTALltinetipedsviicsagslpGDLQrLWHSNV-----PNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVG 492
Cdd:PRK06725 391 IVTTEV---------------------GQHQ-MWAAHFykaknPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 493 DGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQmdhgsgSYYCEFRTDDNQILNVDYAKVAEGYGAKTYRANTVE 572
Cdd:PRK06725 449 DASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQ------EMFYENRLSESKIGSPDFVKVAEAYGVKGLRATNST 522
|
....*....
gi 504294315 573 ELKAALEDA 581
Cdd:PRK06725 523 EAKQVMLEA 531
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
33-581 |
5.54e-43 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 163.07 E-value: 5.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALEQDAG--HLKVyqgKNEQGMAHAAMAYSKQMlrRKIYAVSTSVGPGAANLVAAAGTALA 108
Cdd:PRK08979 17 EGVKHIFGYpgGSVLDIYDALHEKSGieHILV---RHEQAAVHMADGYARAT--GKVGVVLVTSGPGATNTITGIATAYM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVLLIPADTfatrqpdpvlqqmeqeySAAITTNDAL---------KPVSRYWDRITRPEQLMSSLLRAFEVMTDpAK 179
Cdd:PRK08979 92 DSIPMVVLSGQV-----------------PSNLIGNDAFqecdmigisRPVVKHSFLVKDAEDIPEIIKKAFYIAST-GR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 180 AGPATICISQDVEGEA----YDFDESffVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISE 255
Cdd:PRK08979 154 PGPVVIDLPKDCLNPAilhpYEYPES--IKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 256 AYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDfatssKTAFDFDK----AKFLNINV- 330
Cdd:PRK08979 232 KLNLPVVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDD-----RTTNNLEKycpnATILHIDId 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 331 --SRMQAYKLDaFQVVADAKVTLGKLHGLLEGYEsefGTTFRELKDEWLAE----RERlskvtfKREAFDPEIKNHFSQE 404
Cdd:PRK08979 307 psSISKTVRVD-IPIVGSADKVLDSMLALLDESG---ETNDEAAIASWWNEievwRSR------NCLAYDKSSERIKPQQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 405 VLneyadalntelpQTTALLTINETIPEDSV---IICSAGSLPGDLQRLWHSNvpntyhleYGYSCMGYEVSGTLGLKLA 481
Cdd:PRK08979 377 VI------------ETLYKLTNGDAYVASDVgqhQMFAALYYPFDKPRRWINS--------GGLGTMGFGLPAAMGVKFA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 482 HPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGsyycefRTDDNQILNV-DYAKVAEG 560
Cdd:PRK08979 437 MPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQWQDMIYQG------RHSHSYMDSVpDFAKIAEA 510
|
570 580
....*....|....*....|.
gi 504294315 561 YGAKTYRANTVEELKAALEDA 581
Cdd:PRK08979 511 YGHVGIRISDPDELESGLEKA 531
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
64-591 |
1.97e-42 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 161.52 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 64 KNEQGMAHAAMAYSKQMLRRKIYAVSTSVGPGAANLVAAAGTALANNIPVLLIPADTfatrqPDPvLQQMEQEYSAAItt 143
Cdd:PRK06154 61 RTERVAVHMADGYARATSGERVGVFAVQYGPGAENAFGGVAQAYGDSVPVLFLPTGY-----PRG-STDVAPNFESLR-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 144 ndALKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEayDFDESFFVKRVHYIDRMQPSERELQGA 223
Cdd:PRK06154 133 --NYRHITKWCEQVTLPDEVPELMRRAFTRLRN-GRPGPVVLELPVDVLAE--ELDELPLDHRPSRRSRPGADPVEVVEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 224 AELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLG--GMGITGTLAanKAARQADLII 301
Cdd:PRK06154 208 AALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKSAFPEDHPLALGsgGRARPATVA--HFLREADVLF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 302 GIGTRYTDFA-----TSSKTAFD--FDKAKfLNINVSRMQAykldafqVVADAKVTLGKL-------HGLLEGYESEFGT 367
Cdd:PRK06154 286 GIGCSLTRSYyglpmPEGKTIIHstLDDAD-LNKDYPIDHG-------LVGDAALVLKQMieelrrrVGPDRGRAQQVAA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 368 TFRELKDEWLAERErlSKVTfkreafdpeiknhfSQEV-LNEYAdaLNTELPQTTAlltinetiPEDSVIICSAGSLPGD 446
Cdd:PRK06154 358 EIEAVRAAWLAKWM--PKLT--------------SDSTpINPYR--VVWELQHAVD--------IKTVIITHDAGSPRDQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 447 LQRLWHSNVPNTYhLEYGYSC-MGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGc 525
Cdd:PRK06154 412 LSPFYVASRPGSY-LGWGKTTqLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILLNNFSMG- 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504294315 526 INNLQMDHGSGSYycefRTDDnqiLNVDYAKVAEGYGAKTYRANTVEELKAALE---DAKKQNVSTLIE 591
Cdd:PRK06154 490 GYDKVMPVSTTKY----RATD---ISGDYAAIARALGGYGERVEDPEMLVPALLralRKVKEGTPALLE 551
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
6-594 |
2.60e-42 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 161.76 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 6 RLTTAQALIKFLNQQyihvdgkeepfveGIFTIFGH--GNVLGIGQAL---EQDaGHLKVYQGKNEQGMAHAAMAYSKQM 80
Cdd:PRK07418 18 RATGAYALMDSLKRH-------------GVKHIFGYpgGAILPIYDELykaEAE-GWLKHILVRHEQGAAHAADGYARAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 81 LRRKIyAVSTSvGPGAANLVAAAGTALANNIPVLLIpadtfaTRQ-PDPvlqqmeqeysaAITTnDALK---------PV 150
Cdd:PRK07418 84 GKVGV-CFGTS-GPGATNLVTGIATAQMDSVPMVVI------TGQvPRP-----------AIGT-DAFQetdifgitlPI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 151 SRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEAYDFD--ESFFVKRVHYIDRMQPSERELQGAAELIK 228
Cdd:PRK07418 144 VKHSYVVRDPSDMARIVAEAFHIASS-GRPGPVLIDIPKDVGQEEFDYVpvEPGSVKPPGYRPTVKGNPRQINAALKLIE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 229 SSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYT 308
Cdd:PRK07418 223 EAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 309 D--------FATSSKTA-FDFDKAKflnINVSRmqaykLDAFQVVADAKVTLGKLHGLLEGYESEFGTTfrelkdEWLAE 379
Cdd:PRK07418 303 DrvtgkldeFASRAKVIhIDIDPAE---VGKNR-----RPDVPIVGDVRKVLVKLLERSLEPTTPPRTQ------AWLER 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 380 RERLskvtfkreafdpeiKNHFSQEVlNEYADALNtelPQTTaLLTINETIPeDSVIICSAGSlpgdlQRLWHS----NV 455
Cdd:PRK07418 369 INRW--------------KQDYPLVV-PPYEGEIY---PQEV-LLAVRDLAP-DAYYTTDVGQ-----HQMWAAqflrNG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 456 PNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMdhgs 535
Cdd:PRK07418 424 PRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQWQE---- 499
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504294315 536 gSYYCEfRTDDNQILN--VDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK07418 500 -SFYGE-RYSASNMEPgmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHV 558
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
220-354 |
2.30e-41 |
|
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: 146.55 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 220 LQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADL 299
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504294315 300 IIGIGTRYTDFATSSKTAFDFDKAKFLNINVSRMQAYKLDA--FQVVADAKVTLGKL 354
Cdd:pfam00205 81 VLAVGARFDDIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPvdVPIVGDAKETLEAL 137
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
34-596 |
6.77e-41 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 157.17 E-value: 6.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 34 GIFTIFGH--GNVLGIGQALE--QDAGHLKVYQGKNEQGMAHAAMAYSKQMLRRKI-YAVStsvGPGAANLVAAAGTALA 108
Cdd:CHL00099 24 GVKHIFGYpgGAILPIYDELYawEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVcFATS---GPGATNLVTGIATAQM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVLLIPAdtfatrqpdpvlqqmeQEYSAAITTnDALKPVSRYwdRITRP----------EQLMSSLLRAFEVMTDPA 178
Cdd:CHL00099 101 DSVPLLVITG----------------QVGRAFIGT-DAFQEVDIF--GITLPivkhsyvvrdARDISRIVAEAFYIAKHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 179 KAGPATICISQDVEGEAYDFDESFFVKRVHYI----DRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAIS 254
Cdd:CHL00099 162 RPGPVLIDIPKDVGLEKFDYYPPEPGNTIIKIlgcrPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 255 EAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDFdKAKFLNINVSRMQ 334
Cdd:CHL00099 242 ELYKIPVTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFAC-NAQVIHIDIDPAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 335 AYKLDAFQV--VADAKVTLGKlhgLLEGYESEFGTTFrelKDEWLAERERLSKVtfkREAFD---PEIKNHFS-QEVLNE 408
Cdd:CHL00099 321 IGKNRIPQVaiVGDVKKVLQE---LLELLKNSPNLLE---SEQTQAWRERINRW---RKEYPlliPKPSTSLSpQEVINE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 409 yadaLNTELPQttALLTIN---ETIPEDSVIICSagslpgdlQRLWHSNVpntyhleyGYSCMGYEVSGTLGLKLAHPDR 485
Cdd:CHL00099 392 ----ISQLAPD--AYFTTDvgqHQMWAAQFLKCK--------PRKWLSSA--------GLGTMGYGLPAAIGAQIAHPNE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 486 EVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMdhgsgSYYCEFRTDDNQILNV-DYAKVAEGYGAK 564
Cdd:CHL00099 450 LVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQ-----AFYGERYSHSNMEEGApDFVKLAEAYGIK 524
|
570 580 590
....*....|....*....|....*....|..
gi 504294315 565 TYRANTVEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:CHL00099 525 GLRIKSRKDLKSSLKEALDYDGPVLIDCQVIE 556
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
6-585 |
1.57e-40 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 156.68 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 6 RLTTAQALIKFLnqqyihvdgkEEPFVEGIFTIFGhGNVLGIGQALEQDAG--HLKVyqgKNEQGMAHAAMAYSkQMLRR 83
Cdd:PRK07789 30 RMTGAQAVVRSL----------EELGVDVVFGIPG-GAILPVYDPLFDSTKvrHVLV---RHEQGAGHAAEGYA-QATGR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 84 KIYAVSTSvGPGAANLVAAAGTALANNIPVLLIPAdtfatrqpdpvlqqmeQEYSAAITTnDALK---------PVSRYW 154
Cdd:PRK07789 95 VGVCMATS-GPGATNLVTPIADANMDSVPVVAITG----------------QVGRGLIGT-DAFQeadivgitmPITKHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 155 DRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPV 234
Cdd:PRK07789 157 FLVTDADDIPRVIAEAFHIAST-GRPGPVLVDIPKDALQAQTTFSWPPRMDLPGYRPVTKPHGKQIREAAKLIAAARRPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 235 ILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSS 314
Cdd:PRK07789 236 LYVGGGVIRAEASAELRELAELTGIPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 315 KTAFDFDkAKFLNINVSRMQAYKLDAFQV--VADAKVTLGKlhgLLEGYESEFGTTFRELKDEWLAERERLSKvTFKReA 392
Cdd:PRK07789 316 LDSFAPD-AKVIHADIDPAEIGKNRHADVpiVGDVKEVIAE---LIAALRAEHAAGGKPDLTAWWAYLDGWRE-TYPL-G 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 393 FDPEIKNHFS-QEVLNeyadalntelpqttallTINETIPEDSVIICSAGSlpgdlQRLWHSNV-----PNTYHLEYGYS 466
Cdd:PRK07789 390 YDEPSDGSLApQYVIE-----------------RLGEIAGPDAIYVAGVGQ-----HQMWAAQFidyekPRTWLNSGGLG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 467 CMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSY-YCEFRTD 545
Cdd:PRK07789 448 TMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVRQWQTLFYEERYsNTDLHTH 527
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 504294315 546 DNQIlnVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQN 585
Cdd:PRK07789 528 SHRI--PDFVKLAEAYGCVGLRCEREEDVDAVIEKARAIN 565
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
425-594 |
6.98e-40 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 143.55 E-value: 6.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 425 TINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELI 504
Cdd:cd00568 5 ALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQELA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 505 TAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCefrtddNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQ 584
Cdd:cd00568 85 TAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSG------TDLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAA 158
|
170
....*....|
gi 504294315 585 NVSTLIEMKV 594
Cdd:cd00568 159 GGPALIEVKT 168
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
93-594 |
1.51e-39 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 152.44 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 93 GPGAANLVAAAGTALANNIPVLLIP----ADTFATRQ------PDpvlQQmeqeysaaittnDALKPVSRYWDRITRPEQ 162
Cdd:PRK07524 73 GPGMTNIATAMGQAYADSIPMLVISsvnrRASLGKGRgklhelPD---QR------------AMVAGVAAFSHTLMSAED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 163 LMSSLLRAFEVMtDPAKAGPATICISQDVEGEAYDFDESFFVKRVhyiDRMQPSERELQGAAELIKSSKKPVILVGGGAK 242
Cdd:PRK07524 138 LPEVLARAFAVF-DSARPRPVHIEIPLDVLAAPADHLLPAPPTRP---ARPGPAPAALAQAAERLAAARRPLILAGGGAL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 243 ysGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGmgiTGTLAANKA-ARQADLIIGIGTRY--TDFATSSKTAFD 319
Cdd:PRK07524 214 --AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLGA---SQSLPAVRAlIAEADVVLAVGTELgeTDYDVYFDGGFP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 320 FDkAKFLNINVSRMQAYK--LDAFQVVADAKVTLGKLHGLLEGyesefgttfRELKDEWLAERerlskVTFKREAFDPEI 397
Cdd:PRK07524 289 LP-GELIRIDIDPDQLARnyPPALALVGDARAALEALLARLPG---------QAAAADWGAAR-----VAALRQALRAEW 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 398 knhfsqevlneyaDALntELPQTTALLTINETIPE-----DSVIICSAGSLPGDL--QRLWhsnvpntYHLEYGYSCMGY 470
Cdd:PRK07524 354 -------------DPL--TAAQVALLDTILAALPDaifvgDSTQPVYAGNLYFDAdaPRRW-------FNASTGYGTLGY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 471 EVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEfrtddnqIL 550
Cdd:PRK07524 412 GLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVARDIEPVGVD-------PY 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 504294315 551 NVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK07524 485 TPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEVDQ 528
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
54-603 |
7.42e-39 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 150.80 E-value: 7.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 54 DAGHLKVYQGKNEQGMAHAAMAYSKQMLRRKIYAVSTsvGPGAANLVAAAGTALANNIPVLLI---PADTFATRQpdpVL 130
Cdd:PRK08199 43 DETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTR--GPGATNASIGVHTAFQDSTPMILFvgqVARDFRERE---AF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 131 QqmEQEYSAAITtndalkPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVegeaydFDESFFV--KRVH 208
Cdd:PRK08199 118 Q--EIDYRRMFG------PMAKWVAEIDDAARIPELVSRAFHVATS-GRPGPVVLALPEDV------LSETAEVpdAPPY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 209 YIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLG--GMGITG 286
Cdd:PRK08199 183 RRVAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDNRHPNYAGdlGLGINP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 287 TLAAnkAARQADLIIGIGTRYTDFATSSKTAFD--FDKAKFLNIN-----VSRMqaYKLDaFQVVADAKVTLGKLHGLLE 359
Cdd:PRK08199 263 ALAA--RIREADLVLAVGTRLGEVTTQGYTLLDipVPRQTLVHVHpdaeeLGRV--YRPD-LAIVADPAAFAAALAALEP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 360 GYESEFGTTFRELKDEWLAERERLskvtFKREAFD-PEIKNHfsqevlneyadalntelpqttalltINETIPEDSVIIC 438
Cdd:PRK08199 338 PASPAWAEWTAAAHADYLAWSAPL----PGPGAVQlGEVMAW-------------------------LRERLPADAIITN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 439 SAGSLPGDLQRLWHSNVPNTYhLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLF 518
Cdd:PRK08199 389 GAGNYATWLHRFFRFRRYRTQ-LAPTSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 519 DNSGFGCINNLQMDHGSGsyycefRTDDNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLPKT 598
Cdd:PRK08199 468 NNGMYGTIRMHQEREYPG------RVSGTDLTNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPEA 541
|
....*
gi 504294315 599 MTDGY 603
Cdd:PRK08199 542 ITPTA 546
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
10-579 |
1.30e-38 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 150.03 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 10 AQALIKFLNQQyihvdgkeepfveGIFTIFGH--GNVLGIGQALeQDAG--HLKVyqgKNEQGMAHAAMAYSKQMLRRKI 85
Cdd:PRK08978 4 AQWVVHALRAQ-------------GVDTVFGYpgGAIMPVYDAL-YDGGveHLLC---RHEQGAAMAAIGYARATGKVGV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 86 yAVSTSvGPGAANLVAAAGTALANNIPVL---------LIPADTFatrqpdpvlqqmeQE-----YSAAITTNDALkpvs 151
Cdd:PRK08978 67 -CIATS-GPGATNLITGLADALLDSVPVVaitgqvsspLIGTDAF-------------QEidvlgLSLACTKHSFL---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 152 rywdrITRPEQLMSSLLRAFEVmtdpAKA---GPATICISQDVEGEAYDFDESFFVKrvhyIDRMQPSERELQGAAELIK 228
Cdd:PRK08978 128 -----VQSLEELPEIMAEAFEI----ASSgrpGPVLVDIPKDIQLAEGELEPHLTTV----ENEPAFPAAELEQARALLA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 229 SSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYT 308
Cdd:PRK08978 195 QAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 309 DFATSSKTAFDfDKAKFLNINVSRMQAYKLDAfqvvadAKVTL-GKLHGLLEGYESEFGTtfrelkDEWLAERERL-SKV 386
Cdd:PRK08978 275 DRVTGKLNTFA-PHAKVIHLDIDPAEINKLRQ------AHVALqGDLNALLPALQQPLNI------DAWRQHCAQLrAEH 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 387 TFKREAFDPEIknhfsqevlneYADALntelpqttaLLTINETIPEDSVIIC--------SAgslpgdlQRLWHSNVPNt 458
Cdd:PRK08978 342 AWRYDHPGEAI-----------YAPAL---------LKQLSDRKPADTVVTTdvgqhqmwVA-------QHMRFTRPEN- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 459 yHL-EYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGS 537
Cdd:PRK08978 394 -FItSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDER 472
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 504294315 538 yYCEFRTDDNQilnvDYAKVAEGYGAKTYRANTVEELKAALE 579
Cdd:PRK08978 473 -YSETDLSDNP----DFVMLASAFGIPGQTITRKDQVEAALD 509
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
33-597 |
2.68e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 149.53 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALeQDAGHLKVYQgKNEQGMAHAAMAYSKqmLRRKIYAVSTSVGPGAANLVAAAGTALANN 110
Cdd:PRK07710 29 EGVEVIFGYpgGAVLPLYDAL-YDCGIPHILT-RHEQGAIHAAEGYAR--ISGKPGVVIATSGPGATNVVTGLADAMIDS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 111 IPVL---------LIPADTFatrQPDPVLqqmeqeysaAITTndalkPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAG 181
Cdd:PRK07710 105 LPLVvftgqvatsVIGSDAF---QEADIM---------GITM-----PVTKHNYQVRKASDLPRIIKEAFHIATT-GRPG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 182 PATICISQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPL 261
Cdd:PRK07710 167 PVLIDIPKDMVVEEGEFCYDVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 262 VETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDfDKAKFLNINVSRMQAYKL--D 339
Cdd:PRK07710 247 VHTLLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFA-KEATVAHIDIDPAEIGKNvpT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 340 AFQVVADAKVTLGKLHgLLEGYESEfgttfrelKDEW---LAERERLSKVTFKREAfdPEIKNHFSQEVLNEYADAlnte 416
Cdd:PRK07710 326 EIPIVADAKQALQVLL-QQEGKKEN--------HHEWlslLKNWKEKYPLSYKRNS--ESIKPQKAIEMLYEITKG---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 417 lpqttalltinetipeDSVIICSAGSlpgdlQRLWHS-----NVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIV 491
Cdd:PRK07710 391 ----------------EAIVTTDVGQ-----HQMWAAqyypfKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 492 GDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQmdhgsgSYYCEFRTDDNQILNV-DYAKVAEGYGAKTYRANT 570
Cdd:PRK07710 450 GDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQ------EEFYNQRYSHSLLSCQpDFVKLAEAYGIKGVRIDD 523
|
570 580
....*....|....*....|....*..
gi 504294315 571 VEELKAALEDAKKQNVSTLIEMKVLPK 597
Cdd:PRK07710 524 ELEAKEQLQHAIELQEPVVIDCRVLQS 550
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
33-581 |
2.05e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 146.98 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALEQDAG--HLKVyqgKNEQGMAHAAMAYSKQMlrRKIYAVSTSVGPGAANLVAAAGTALA 108
Cdd:PRK06882 17 EGVEYVFGYpgGSVLDIYDAIHTLGGieHVLV---RHEQAAVHMADGYARST--GKVGCVLVTSGPGATNAITGIATAYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVLLIPADTFATRQPDPVLQQMEqeySAAITtndalKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICIS 188
Cdd:PRK06882 92 DSVPLVILSGQVPSNLIGTDAFQECD---MLGIS-----RPVVKHSFIVKNAEDIPSTIKKAFYIAST-GRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 189 QDVEGEAYDFDESF--FVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQA 266
Cdd:PRK06882 163 KDMVNPANKFTYEYpeEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 267 GKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFdFDKAKFLNINVSRMQAYK--LDAFQVV 344
Cdd:PRK06882 243 GLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKY-CPNAKVIHIDIDPTSISKnvPAYIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 345 ADAKVTLGKLHGLLEgyESEFGTTFRELKDEWLAERERLSKVTFKREAFDPEIKnhfSQEVLneyadalntelpQTTALL 424
Cdd:PRK06882 322 GSAKNVLEEFLSLLE--EENLAKSQTDLTAWWQQINEWKAKKCLEFDRTSDVIK---PQQVV------------EAIYRL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 425 TINETIPEDSV---IICSAGSLPGDLQRLWHSNvpntyhleYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHS 501
Cdd:PRK06882 385 TNGDAYVASDVgqhQMFAALHYPFDKPRRWINS--------GGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQ 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 502 ELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRtddNQIlnVDYAKVAEGYGAKTYRANTVEELKAALEDA 581
Cdd:PRK06882 457 ELSTAKQYDIPVVIVSLNNRFLGMVKQWQDLIYSGRHSQVYM---NSL--PDFAKLAEAYGHVGIQIDTPDELEEKLTQA 531
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
33-584 |
2.98e-37 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 146.53 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALEQDAG--HLKVyqgKNEQGMAHAAMAYSKQMlrRKIYAVSTSVGPGAANLVAAAGTALA 108
Cdd:PRK07979 17 QGVKQVFGYpgGAVLDIYDALHTVGGidHVLV---RHEQAAVHMADGLARAT--GEVGVVLVTSGPGATNAITGIATAYM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVLLIPAdtfatrqpdpvlqqmeqEYSAAITTNDAL---------KPVSRYWDRITRPEQLMSSLLRAFEVMTDpAK 179
Cdd:PRK07979 92 DSIPLVVLSG-----------------QVATSLIGYDAFqecdmvgisRPVVKHSFLVKQTEDIPQVLKKAFWLAAS-GR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 180 AGPATICISQDVEGEA----YDFDESffVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISE 255
Cdd:PRK07979 154 PGPVVVDLPKDILNPAnklpYVWPES--VSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 256 AYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFdFDKAKFLNINVSRMQA 335
Cdd:PRK07979 232 KLNLPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKY-CPNATVLHIDIDPTSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 336 YKLDA--FQVVADAKVTLGKLHGLLEGYESEfgTTFRELKDEWLAERERLSKVTFKREAFDPEIKNHFSQEVLNeyadal 413
Cdd:PRK07979 311 SKTVTadIPIVGDARQVLEQMLELLSQESAH--QPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLW------ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 414 ntELPQTTALLTINETIPEdsviICSAGSLPGDLQRLWHSNvpntyhleYGYSCMGYEVSGTLGLKLAHPDREVYSIVGD 493
Cdd:PRK07979 383 --RLTKGDAYVTSDVGQHQ----MFAALYYPFDKPRRWINS--------GGLGTMGFGLPAALGVKMALPEETVVCVTGD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 494 GSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ-MDHG---SGSYYCEFRtddnqilnvDYAKVAEGYGAKTYRAN 569
Cdd:PRK07979 449 GSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQWQdMIYSgrhSQSYMQSLP---------DFVRLAEAYGHVGIQIS 519
|
570
....*....|....*
gi 504294315 570 TVEELKAALEDAKKQ 584
Cdd:PRK07979 520 HPDELESKLSEALEQ 534
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
4-591 |
4.14e-37 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 146.30 E-value: 4.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 4 KIRLTTAQALIKFLNQqyihvdgkeepfvEGIFTIFGHgnvlgIGQA------LEQDAGhLKVYQGKNEQGMAHAAMAYS 77
Cdd:PRK07525 3 KMKMTPSEAFVETLQA-------------HGITHAFGI-----IGSAfmdasdLFPPAG-IRFIDVAHEQNAGHMADGYT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 78 KqmLRRKIYAVSTSVGPGAANLVAAAGTALANNIPVLLI-P-ADTFATRQPDpvLQQMEQEysaaittnDALKPVSRYWD 155
Cdd:PRK07525 64 R--VTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVtPqAGTKTIGQGG--FQEAEQM--------PMFEDMTKYQE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 156 RITRPEQLMSSLLRAFevmtDPAKA--GPATICISQDVEGEAYDFDesffVKRVHYIDRMQPSERELQGAAELIKSSKKP 233
Cdd:PRK07525 132 EVRDPSRMAEVLNRVF----DKAKResGPAQINIPRDYFYGVIDVE----IPQPVRLERGAGGEQSLAEAAELLSEAKFP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 234 VILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATS 313
Cdd:PRK07525 204 VILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNPFGTL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 314 SKTAFDF--DKAKFL--NINVSRMQAYKLDAFQVVADAKVT----LGKLHGLLEGYES--EFGTTFRELKDEWLAErerL 383
Cdd:PRK07525 284 PQYGIDYwpKDAKIIqvDINPDRIGLTKKVSVGICGDAKAVarelLARLAERLAGDAGreERKALIAAEKSAWEQE---L 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 384 SKVTFKREAFDPEiknhfsqevLNEYADALNTEL--PQtTALLTINETIPEDSVI------ICSAGslpgdlqrlwhsnv 455
Cdd:PRK07525 361 SSWDHEDDDPGTD---------WNEEARARKPDYmhPR-QALREIQKALPEDAIVstdignNCSIA-------------- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 456 pNTY--------HLEYGY--SCmGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGC 525
Cdd:PRK07525 417 -NSYlrfekgrkYLAPGSfgNC-GYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGA 494
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504294315 526 INNLQMDhgsgsYYcefrtDDNQI-----LNVDYAKVAEGYGAKTYRANTVEELKAALEDA---KKQNVSTLIE 591
Cdd:PRK07525 495 EKKNQVD-----FY-----NNRFVgteldNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAidaQNEGKTTVIE 558
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
58-580 |
1.17e-35 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 141.51 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 58 LKVYQGKNEQGMAHAAMAYSKqmLRRKIYAVSTSVGPGAANLVAAAGTALANNIPVLLIPADTfatrQPDPVLQQMEQEY 137
Cdd:PRK06457 40 VKYVQVRHEEGAALAASVEAK--ITGKPSACMGTSGPGSIHLLNGLYDAKMDHAPVIALTGQV----ESDMIGHDYFQEV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 138 SAAITTNDalkpVSRYWDRITRPEQLMSSLLRAF-EVMTdpaKAGPATICISQDV--EGEAYDFDESFFVKRVHYidrmq 214
Cdd:PRK06457 114 NLTKLFDD----VAVFNQILINPENAEYIIRRAIrEAIS---KRGVAHINLPVDIlrKSSEYKGSKNTEVGKVKY----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 215 psERELQGAAELIKSSKKPVILVGGGAKysGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAA 294
Cdd:PRK06457 182 --SIDFSRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDLDPKVMGGIGLLGTKPSIEAM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 295 RQADLIIGIGTR--YTDFATSS-------------------KTAFDFDKAKFLNINVSRmqayKLDAFqvvadakvtlgk 353
Cdd:PRK06457 258 DKADLLIMLGTSfpYVNFLNKSakviqvdidnsnigkrldvDLSYPIPVAEFLNIDIEE----KSDKF------------ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 354 lhgllegYESEFGTtfrelKDEWLaerERLSKVTFKReafDPEIKnhfsqevlneyadalntelPQTTALLtINETIPED 433
Cdd:PRK06457 322 -------YEELKGK-----KEDWL---DSISKQENSL---DKPMK-------------------PQRVAYI-VSQKCKKD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 434 SVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLA-HPDREVYSIVGDGSFLMLHSELITAIQYNKK 512
Cdd:PRK06457 364 AVIVTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAvENKRQVISFVGDGGFTMTMMELITAKKYDLP 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504294315 513 INVLLFDNSGFGCINNLQMDHGsgsyYCEFRTDdnqILNVDYAKVAEGYGAKTYRANTVEELKAALED 580
Cdd:PRK06457 444 VKIIIYNNSKLGMIKFEQEVMG----YPEWGVD---LYNPDFTKIAESIGFKGFRLEEPKEAEEIIEE 504
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
4-596 |
7.79e-35 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 139.46 E-value: 7.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 4 KIRLTTAQALIKFLNQQyihvdgkeepfveGIFTIFG--HGNVLGIGQAL-------------EQDAGHLKvyqgkneQG 68
Cdd:PRK08155 10 RKRFTGAELIVRLLERQ-------------GIRIVTGipGGAILPLYDALsqstqirhilarhEQGAGFIA-------QG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 69 MAHAA------MAYSkqmlrrkiyavstsvGPGAANLVAAAGTALANNIPVLLIPAdtfatrqpdpvlqqmeQEYSAAIT 142
Cdd:PRK08155 70 MARTTgkpavcMACS---------------GPGATNLVTAIADARLDSIPLVCITG----------------QVPASMIG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 143 TnDALKPVSRYwdRITRP-----------EQLMSSLLRAFEVMTDpAKAGPATICISQDVEGEAYDFDESFFVKRVHYID 211
Cdd:PRK08155 119 T-DAFQEVDTY--GISIPitkhnylvrdiEELPQVISDAFRIAQS-GRPGPVWIDIPKDVQTAVIELEALPAPAEKDAAP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 212 rmQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAAN 291
Cdd:PRK08155 195 --AFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 292 KAARQADLIIGIGTRYTDFATsSKTAFDFDKAKFLNINVSRMQAYKLDAFQVV--ADAKVTLGKLHGLLEgyesefgttf 369
Cdd:PRK08155 273 YILQEADLLIVLGARFDDRAI-GKTEQFCPNAKIIHVDIDRAELGKIKQPHVAiqADVDDVLAQLLPLVE---------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 370 RELKDEWLAERERLskvtfKREaFDPEIKNhfSQEVLNEYAdalnteLPQTTAlltinETIPEDSVIICSAGSlpgdlQR 449
Cdd:PRK08155 342 AQPRAEWHQLVADL-----QRE-FPCPIPK--ADDPLSHYG------LINAVA-----ACVDDNAIITTDVGQ-----HQ 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 450 LWHS-----NVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFG 524
Cdd:PRK08155 398 MWTAqayplNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALG 477
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504294315 525 CINNLQ-MDHGSGSYYCEFRTddnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQ------NVSTLIEMKVLP 596
Cdd:PRK08155 478 LVHQQQsLFYGQRVFAATYPG------KINFMQIAAGFGLETCDLNNEADPQAALQEAINRpgpaliHVRIDAEEKVYP 550
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
33-584 |
8.65e-35 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 139.34 E-value: 8.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGhgnVLGIG-----QALEQdAGHLKVYQGKNEQGMAHAAMAYSKQMLRRKIYAVSTSvGPGAANLVAAAGTAL 107
Cdd:PRK11269 17 EGVTTAFG---VPGAAinpfySAMRK-HGGIRHILARHVEGASHMAEGYTRATAGNIGVCIGTS-GPAGTDMITGLYSAS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 108 ANNIPVLLIpadtfaTRQ-PDPVLQQmeqEYSAAITTNDALKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATIC 186
Cdd:PRK11269 92 ADSIPILCI------TGQaPRARLHK---EDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRS-GRPGPVLID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 187 ISQDVEGEAYDFDESFFVKRVHYidRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQA 266
Cdd:PRK11269 162 LPFDVQVAEIEFDPDTYEPLPVY--KPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 267 GKSTVEADFANNLGGMGI-TGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDFDKaKFLNINVSRMQAYKLDA--FQV 343
Cdd:PRK11269 240 GWGAIPDDHPLMAGMVGLqTSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGR-KFVHVDIEPTQIGRVFGpdLGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 344 VADAKVTLGKLHGLLEGYESEfgttfRELKD--EWLAE-RERlsKVTFKReafdpeiKNHFS------QEVLNEyadaln 414
Cdd:PRK11269 319 VSDAKAALELLVEVAREWKAA-----GRLPDrsAWVADcQER--KRTLLR-------KTHFDnvpikpQRVYEE------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 415 telpqttalltINETIPEDSVIICSAGslpgdLQRLWHSNVPNTYHLEYGYSC-----MGYEVSGTLGLKLAHPDREVYS 489
Cdd:PRK11269 379 -----------MNKAFGRDTCYVSTIG-----LSQIAAAQFLHVYKPRHWINCgqagpLGWTIPAALGVRAADPDRNVVA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 490 IVGDGSFLMLHSELITAIQYN-KKINVLLfDNSGFGCINNLQ----MDhgsgsyYC---EFRTDDNQILN---VDYAKVA 558
Cdd:PRK11269 443 LSGDYDFQFLIEELAVGAQFNlPYIHVLV-NNAYLGLIRQAQrafdMD------YCvqlAFENINSPELNgygVDHVKVA 515
|
570 580
....*....|....*....|....*.
gi 504294315 559 EGYGAKTYRANTVEELKAALEDAKKQ 584
Cdd:PRK11269 516 EGLGCKAIRVFKPEDIAPALEQAKAL 541
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
34-596 |
3.72e-34 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 137.58 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 34 GIFTIFGHGnvlgIGQALEQDAGHLKVYQGKNEQGMAHAAMAYSKQMLRRKIYAVSTSVGPGAANLVAAAGTALANNIPV 113
Cdd:PRK06112 28 GVEQIFGQS----LPSALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLVAPLAEALKASVPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 114 LLIPADTfATRQPDP-VLQQMEQeysAAIttndaLKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICISQDVE 192
Cdd:PRK06112 104 VALVQDV-NRDQTDRnAFQELDH---IAL-----FQSCTKWVRRVTVAERIDDYVDQAFTAATS-GRPGPVVLLLPADLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 193 GEAydfDESFFVKRV----HY-IDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAG 267
Cdd:PRK06112 174 TAA---AAAPAAPRSnslgHFpLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNMG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 268 KSTVeaDFANNLGGmGITGTLAANKA--------ARQADLIIGIGTRYTDFATSSKTAFDFDkAKFLNINVSRMQAYK-L 338
Cdd:PRK06112 251 KGAV--DETHPLSL-GVVGSLMGPRSpgrhlrdlVREADVVLLVGTRTNQNGTDSWSLYPEQ-AQYIHIDVDGEEVGRnY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 339 DAFQVVADAKVTLGKLHGLLEGYesefGTTFRELKDEWLAERERLSkvtfkREAFDPEiknhfSQEVLNEYADALNTE-- 416
Cdd:PRK06112 327 EALRLVGDARLTLAALTDALRGR----DLAARAGRRAALEPAIAAG-----REAHRED-----SAPVALSDASPIRPEri 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 417 LPQTTALLTINETIPEDSviicSAGSlpgdlqrLWHSNV-----PNTYHLE-YGYSCMGYEVSGTLGLKLAHPDREVYSI 490
Cdd:PRK06112 393 MAELQAVLTGDTIVVADA----SYSS-------IWVANFltarrAGMRFLTpRGLAGLGWGVPMAIGAKVARPGAPVICL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 491 VGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGcinnLQMdHGSGSYYCEFrTDDNQILNVDYAKVAEGYGAKTYRANT 570
Cdd:PRK06112 462 VGDGGFAHVWAELETARRMGVPVTIVVLNNGILG----FQK-HAETVKFGTH-TDACHFAAVDHAAIARACGCDGVRVED 535
|
570 580
....*....|....*....|....*.
gi 504294315 571 VEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:PRK06112 536 PAELAQALAAAMAAPGPTLIEVITDP 561
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
426-596 |
1.61e-33 |
|
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: 126.11 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 426 INETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELIT 505
Cdd:cd02014 11 LNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMGDLIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 506 AIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRtddnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQN 585
Cdd:cd02014 91 AVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDLP-------NPDFAKIAEAMGIKGIRVEDPDELEAALDEALAAD 163
|
170
....*....|.
gi 504294315 586 VSTLIEMKVLP 596
Cdd:cd02014 164 GPVVIDVVTDP 174
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
33-580 |
4.09e-33 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 134.45 E-value: 4.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALEQ--DAGHLKVyqgKNEQGMAHAAMAYSKQMLRRKIYAVsTSvGPGAANLVAAAGTALA 108
Cdd:PRK09107 24 QGVEHIFGYpgGAVLPIYDEIFQqdDIQHILV---RHEQGAGHAAEGYARSTGKPGVVLV-TS-GPGATNAVTPLQDALM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVL---------LIPADTFatRQPDPVlqqmeqeysaAITtndalKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAK 179
Cdd:PRK09107 99 DSIPLVcitgqvpthLIGSDAF--QECDTV----------GIT-----RPCTKHNWLVKDVNDLARVIHEAFHVATS-GR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 180 AGPATICISQDVEgeaydFDESFFVK------RVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSG--ARDELV 251
Cdd:PRK09107 161 PGPVVVDIPKDVQ-----FATGTYTPpqkapvHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSGpeASRLLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 252 AISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDfDKAKFLNINV- 330
Cdd:PRK09107 236 ELVELTGFPITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFS-PNSKKIHIDId 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 331 --SRMQAYKLDaFQVVADAKVTLGKlhgLLEGYESEFGTTFRELKDEWLAERERLSKV-TFKREAFDPEIKNHFSQEVLN 407
Cdd:PRK09107 315 psSINKNVRVD-VPIIGDVGHVLED---MLRLWKARGKKPDKEALADWWGQIARWRARnSLAYTPSDDVIMPQYAIQRLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 408 EyadalntelpqttalLTINetipEDSVIICSAGSlpgdlQRLW-----HSNVPNTYHLEYGYSCMGYEVSGTLGLKLAH 482
Cdd:PRK09107 391 E---------------LTKG----RDTYITTEVGQ-----HQMWaaqffGFEEPNRWMTSGGLGTMGYGLPAALGVQIAH 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 483 PDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ-MDHG---SGSYycefrTDDNQilnvDYAKVA 558
Cdd:PRK09107 447 PDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYMGMVRQWQqLLHGnrlSHSY-----TEAMP----DFVKLA 517
|
570 580
....*....|....*....|..
gi 504294315 559 EGYGAKTYRANTVEELKAALED 580
Cdd:PRK09107 518 EAYGAVGIRCEKPGDLDDAIQE 539
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
223-597 |
2.37e-32 |
|
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: 131.82 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 223 AAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGG-MGITGTLAANKAARQADLII 301
Cdd:COG3961 202 AAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyAGAASSPEVREYVENADCVL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 302 GIGTRYTDFATSSKTAfDFDKAKFLNINVSRmqaykldafqvvadakVTLGklhgllegyesefGTTFRE--LKDeWLae 379
Cdd:COG3961 282 CLGVVFTDTNTGGFTA-QLDPERTIDIQPDS----------------VRVG-------------GHIYPGvsLAD-FL-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 380 rERLSKVTFKREAFDPeiknhFSQEVLNEYADALNTELPQTTALLTINETIPEDSVIICSAGS---------LPGDlqrl 450
Cdd:COG3961 329 -EALAELLKKRSAPLP-----APAPPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTslfgaadlrLPEG---- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 451 whsnvpNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGcINnlQ 530
Cdd:COG3961 399 ------ATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGYT-IE--R 469
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504294315 531 MDHGSGSYYcefrtddNQILNVDYAKVAEGYGAK---TYRANTVEELKAALEDAKK-QNVSTLIEMkVLPK 597
Cdd:COG3961 470 AIHGPDGPY-------NDIANWDYAKLPEAFGGGnalGFRVTTEGELEEALAAAEAnTDRLTLIEV-VLDK 532
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
33-581 |
3.02e-32 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 131.79 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQAL--EQDAGHLKVyqgKNEQGMAHAAMAYSKQMLRRKIYAVSTsvGPGAANLVAAAGTALA 108
Cdd:PRK06466 17 EGVEYIYGYpgGAVLHIYDALfkQDKVEHILV---RHEQAATHMADGYARATGKTGVVLVTS--GPGATNAITGIATAYM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVLLIPADTFATRQPDPVLQQMEQeysAAITtndalKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICIS 188
Cdd:PRK06466 92 DSIPMVVLSGQVPSTLIGEDAFQETDM---VGIS-----RPIVKHSFMVKHASEIPEIIKKAFYIAQS-GRPGPVVVDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 189 QDVEGEAYDFdESFFVKRVHyIDRMQPSER----ELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVET 264
Cdd:PRK06466 163 KDMTNPAEKF-EYEYPKKVK-LRSYSPAVRghsgQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 265 QAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFdFDKAKFLNINVSRMQAYKldafQVV 344
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKF-CPNAKIIHIDIDPASISK----TIK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 345 ADAKVtLGKLHGLLegyesefgttfrelkdewlaeRERLSKVTFKREAFDPEIKNHFSQEV--------LNEYADALNTE 416
Cdd:PRK06466 316 ADIPI-VGPVESVL---------------------TEMLAILKEIGEKPDKEALAAWWKQIdewrgrhgLFPYDKGDGGI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 417 LPQTTALLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSF 496
Cdd:PRK06466 374 IKPQQVVETLYEVTNGDAYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 497 LMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ-MDHGS--GSYYCEFRTddnqilnvDYAKVAEGYGAKTYRANTVEE 573
Cdd:PRK06466 454 QMNIQELSTCLQYGLPVKIINLNNGALGMVRQWQdMQYEGrhSHSYMESLP--------DFVKLAEAYGHVGIRITDLKD 525
|
....*...
gi 504294315 574 LKAALEDA 581
Cdd:PRK06466 526 LKPKLEEA 533
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
33-579 |
6.19e-32 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 131.01 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQALEQDAGHLKVYQgKNEQGMAHAAMAYSKQMLRRKIyAVSTSvGPGAANLVAAAGTALANN 110
Cdd:PLN02470 26 EGVDTVFAYpgGASMEIHQALTRSNCIRNVLC-RHEQGEVFAAEGYAKASGKVGV-CIATS-GPGATNLVTGLADALLDS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 111 IPVL---------LIPADTFatrQPDPVLqqmeqEYSAAITTNDALKPVSRYWDRITRpeqlmssllRAFEVMTDpAKAG 181
Cdd:PLN02470 103 VPLVaitgqvprrMIGTDAF---QETPIV-----EVTRSITKHNYLVMDVEDIPRVIR---------EAFFLASS-GRPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 182 PATICISQDVEGEAYDFDESFFVKRVHYIDRMQ--PSERELQGAAELIKSSKKPVILVGGGAkySGARDELVAISEAYNI 259
Cdd:PLN02470 165 PVLVDIPKDIQQQLAVPNWNQPMKLPGYLSRLPkpPEKSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 260 PLVETQAGKSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDfDKAKFLNINV--SRMQAYK 337
Cdd:PLN02470 243 PVASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFA-SRASIVHIDIdpAEIGKNK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 338 LDAFQVVADAKVTLGKLHGLLEGyESEFGTTFRELKDEWLAERErlsKVTFKREAFDPEIKNHFSQEVLNEyadalntel 417
Cdd:PLN02470 322 QPHVSVCADVKLALQGLNKLLEE-RKAKRPDFSAWRAELDEQKE---KFPLSYPTFGDAIPPQYAIQVLDE--------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 418 pqttalltinetIPEDSVIICS---------AGSLPGDLQRLWHSNVpntyhleyGYSCMGYEVSGTLGLKLAHPDREVY 488
Cdd:PLN02470 389 ------------LTDGNAIISTgvgqhqmwaAQWYKYKEPRRWLTSG--------GLGAMGFGLPAAIGAAAANPDAIVV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 489 SIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ---MDHGSGSYYCEFRTDDNQILNvDYAKVAEGYGAKT 565
Cdd:PLN02470 449 DIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWEdrfYKANRAHTYLGDPDAEAEIFP-DFLKFAEGCKIPA 527
|
570
....*....|....
gi 504294315 566 YRANTVEELKAALE 579
Cdd:PLN02470 528 ARVTRKSDLREAIQ 541
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
426-594 |
2.15e-31 |
|
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: 120.47 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 426 INETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELIT 505
Cdd:cd02010 8 LRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELET 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 506 AIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRtddnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQN 585
Cdd:cd02010 88 AVRLKIPLVVLIWNDNGYGLIKWKQEKEYGRDSGVDFG-------NPDFVKYAESFGAKGYRIESADDLLPVLERALAAD 160
|
....*....
gi 504294315 586 VSTLIEMKV 594
Cdd:cd02010 161 GVHVIDCPV 169
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
34-595 |
3.36e-31 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 128.18 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 34 GIFTIFG----HGnvLGIGQALEQDaGHLKVYQGKNEQGMAHAAMAYSKQmlRRKIYAVSTSVGPGAANLVAAAGTALAN 109
Cdd:PRK07064 17 GVKTAFGvisiHN--MPILDAIGRR-GKIRFVPARGEAGAVNMADAHARV--SGGLGVALTSTGTGAGNAAGALVEALTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 110 NIPVLLIPAdtfatrqpdpvlqQMEQEY----SAAI-TTNDA---LKPVSRYWDRITRPEQLMSSLLRAFEV-MTDPAka 180
Cdd:PRK07064 92 GTPLLHITG-------------QIETPYldqdLGYIhEAPDQltmLRAVSKAAFRVRSAETALATIREAVRVaLTAPT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 181 GPATICISQDVEGEAYDFDESFFVKRVhyiDRMQPSERELQGAAELIKSSKKPVILVGGGAKysGARDELVAISEAyNIP 260
Cdd:PRK07064 157 GPVSVEIPIDIQAAEIELPDDLAPVHV---AVPEPDAAAVAELAERLAAARRPLLWLGGGAR--HAGAEVKRLVDL-GFG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 261 LVETQAGKSTVEADFANNLGGMGITGtlAANKAARQADLIIGIGTRYTDFATSSKT--------AFDFDKAKflninVSR 332
Cdd:PRK07064 231 VVTSTQGRGVVPEDHPASLGAFNNSA--AVEALYKTCDLLLVVGSRLRGNETLKYSlalprpliRVDADAAA-----DGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 333 mqAYKLDAFqVVADAKVTLGKLHGLLEGYESefgttfreLKDEWLAE--RERLSKVTFKREAFDPeiknhfsqevlneYA 410
Cdd:PRK07064 304 --GYPNDLF-VHGDAARVLARLADRLEGRLS--------VDPAFAADlrAAREAAVADLRKGLGP-------------YA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 411 DaLNTELPQttalltineTIPEDSVI---ICSAGSLPGDlqRLWHSNVPNT--YHLEYGyscMGYEVSGTLGLKLAHPDR 485
Cdd:PRK07064 360 K-LVDALRA---------ALPRDGNWvrdVTISNSTWGN--RLLPIFEPRAnvHALGGG---IGQGLAMAIGAALAGPGR 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 486 EVYSIVGDGSFlMLH-SELITAIQYNKKINVLLFDNSGFGCINNLQmdhgsgSYYCEFRTDDNQILNVDYAKVAEGYGAK 564
Cdd:PRK07064 425 KTVGLVGDGGL-MLNlGELATAVQENANMVIVLMNDGGYGVIRNIQ------DAQYGGRRYYVELHTPDFALLAASLGLP 497
|
570 580 590
....*....|....*....|....*....|.
gi 504294315 565 TYRANTVEELKAALEDAKKQNVSTLIEMKVL 595
Cdd:PRK07064 498 HWRVTSADDFEAVLREALAKEGPVLVEVDML 528
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
33-583 |
1.41e-30 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 126.84 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 33 EGIFTIFGH--GNVLGIGQAL-EQDA-GHLKVyqgKNEQGMAHAAMAYSKQMLRRKIyAVSTSvGPGAANLVAAAGTALA 108
Cdd:PRK06965 34 EGVEFIWGYpgGAVLYIYDELyKQDKiQHVLV---RHEQAAVHAADGYARATGKVGV-ALVTS-GPGVTNAVTGIATAYM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 109 NNIPVLLIPADTfatrqPDPVL-QQMEQEYSAAITTndalKPVSRYWDRITRPEQLMSSLLRAFEVMTDpAKAGPATICI 187
Cdd:PRK06965 109 DSIPMVVISGQV-----PTAAIgQDAFQECDTVGIT----RPIVKHNFLVKDVRDLAETVKKAFYIART-GRPGPVVVDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 188 SQDVEGEAYDFDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAG 267
Cdd:PRK06965 179 PKDVSKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 268 KSTVEADFANNLGGMGITGTLAANKAARQADLIIGIGTRYTDFATSSKTAFDFDKAKFLNINV---SRMQAYKLDaFQVV 344
Cdd:PRK06965 259 LGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPRKIIHIDIdpsSISKRVKVD-IPIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 345 ADAKVTLGKLHGLLEgyESEFGTTFRELKDEWLAERERLSKVTFKREAFDPEIKNHFSQEVLNEYADAlntelpqttall 424
Cdd:PRK06965 338 GDVKEVLKELIEQLQ--TAEHGPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDG------------ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 425 tinetipeDSVIICSAGSlpgdlQRLWHS-----NVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLML 499
Cdd:PRK06965 404 --------DAFVCSDVGQ-----HQMWAAqfyrfNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMC 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 500 HSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCEFRtddnQILNvDYAKVAEGYGAKTYRANTVEELKAALE 579
Cdd:PRK06965 471 IQELSTCLQYDTPVKIISLNNRYLGMVRQWQEIEYSKRYSHSYM----DALP-DFVKLAEAYGHVGMRIEKTSDVEPALR 545
|
....
gi 504294315 580 DAKK 583
Cdd:PRK06965 546 EALR 549
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
64-592 |
5.82e-29 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 121.63 E-value: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 64 KNEQGMAHAAMAYSKqmLRRKIYAVSTSVGPGAANLV---------AAAGTALANNIPVLLIPADTFATRQPDPVLQQme 134
Cdd:PRK06546 48 RHEEAAAFAAAAEAQ--LTGKLAVCAGSCGPGNLHLInglydahrsGAPVLAIASHIPSAQIGSGFFQETHPDRLFVE-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 135 qeysaaittndalkpVSRYWDRITRPEQlMSSLLRAfEVMTDPAKAGPATICISQDVEGE--AYDFDESFFVKRVhyiDR 212
Cdd:PRK06546 124 ---------------CSGYCEMVSSAEQ-APRVLHS-AIQHAVAGGGVSVVTLPGDIADEpaPEGFAPSVISPRR---PT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 213 MQPSERELQGAAELIKSSKKPVILVGGGAKysGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAANK 292
Cdd:PRK06546 184 VVPDPAEVRALADAINEAKKVTLFAGAGVR--GAHAEVLALAEKIKAPVGHSLRGKEWIQYDNPFDVGMSGLLGYGAAHE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 293 AARQADLIIGIGTR--YTDFATSSKTA-FDFDKAkflniNVSRMQayKLDaFQVVADAKVTLGKLHGLLEGyesefgTTF 369
Cdd:PRK06546 262 AMHEADLLILLGTDfpYDQFLPDVRTAqVDIDPE-----HLGRRT--RVD-LAVHGDVAETIRALLPLVKE------KTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 370 RELKDEWLAERER-LSKVTfkrEAFDPEIKNHfsQEVLNEYADALntelpqttalltINETIPEDSVIICSAGslpgdLQ 448
Cdd:PRK06546 328 RRFLDRMLKKHARkLEKVV---GAYTRKVEKH--TPIHPEYVASI------------LDELAADDAVFTVDTG-----MC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 449 RLWHSN--VPNTYHLEYG---YSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGF 523
Cdd:PRK06546 386 NVWAARyiTPNGRRRVIGsfrHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504294315 524 GCInNLQM------DHGsgsyycefrTDDNqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEM 592
Cdd:PRK06546 466 GMV-KLEMlvdglpDFG---------TDHP---PVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDV 527
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
32-189 |
1.11e-27 |
|
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: 109.16 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 32 VEGIFTIFGHGNvLGIGQALEQDagHLKVYQGKNEQGMAHAAMAYSkqMLRRKIYAVSTSVGPGAANLVAAAGTALANNI 111
Cdd:cd07035 12 VDHVFGVPGGAI-LPLLDALARS--GIRYILVRHEQGAVGMADGYA--RATGKPGVVLVTSGPGLTNAVTGLANAYLDSI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504294315 112 PVLLIPADTFATRQPDPVLQQMEQeysaaittNDALKPVSRYWDRITRPEQLMSSLLRAFEVMTDPAKaGPATICISQ 189
Cdd:cd07035 87 PLLVITGQRPTAGEGRGAFQEIDQ--------VALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRP-GPVALDLPK 155
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
71-594 |
1.07e-26 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 114.71 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 71 HAAMAYSkqMLRRKIYAVSTSVGPGAANLVAAAGTALANNIPVLLIPADTFATRQPD------PVLQQMEQEYSAAITTN 144
Cdd:PRK08327 64 SMAHGYA--LVTGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEGElgsrntRIHWTQEMRDQGGLVRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 145 dALKpvsryWD-RITRPEQLMSSLLRAFEVM-TDPAkaGPATICISQDVEGEAydfdesffVKRVHYIDRMQPSERE--- 219
Cdd:PRK08327 142 -YVK-----WDyEIRRGDQIGEVVARAIQIAmSEPK--GPVYLTLPREVLAEE--------VPEVKADAGRQMAPAPpap 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 220 ----LQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMgITGTLAankaar 295
Cdd:PRK08327 206 dpedIARAAEMLAAAERPVIITWRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPD-PRADLA------ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 296 QADLIIGIGTRYTDFATSSKTAFDfdkAKFLNINV----SRMQAYkldAFQV----VADAKVTLGKLHGLLEGYESEFGT 367
Cdd:PRK08327 279 EADLVLVVDSDVPWIPKKIRPDAD---ARVIQIDVdplkSRIPLW---GFPCdlciQADTSTALDQLEERLKSLASAERR 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 368 TFRELKDEWLAERERLSKVtfKREAfdpeiknhfsqevlneyADALNTELPQTTALLT--INETIPEDSVIICSAGSLPG 445
Cdd:PRK08327 353 RARRRRAAVRELRIRQEAA--KRAE-----------------IERLKDRGPITPAYLSycLGEVADEYDAIVTEYPFVPR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 446 DLQRlwhsNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSE--LITAIQYNKKINVLLFDNSGF 523
Cdd:PRK08327 414 QARL----NKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaHWVAERYGLPVLVVVFNNGGW 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 524 GCI-NNLQMDHGSG-----SYYCEFRTDDnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDA----KKQNVSTLIEMK 593
Cdd:PRK08327 490 LAVkEAVLEVYPEGyaarkGTFPGTDFDP----RPDFAKIAEAFGGYGERVEDPEELKGALRRAlaavRKGRRSAVLDVI 565
|
.
gi 504294315 594 V 594
Cdd:PRK08327 566 V 566
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
421-594 |
1.22e-26 |
|
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: 106.46 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 421 TALLTINETIPEDSvIICSAGSLPGDLQRLWHSNV-PNTYhLEYG-YSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLM 498
Cdd:cd02004 3 RVLHELQEALPDDA-IIVSDGGNTMDWARYILRPRkPRHR-LDAGtFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 499 LHSELITAIQYNKKINVLLFDNSGFGCINNLQ--MDHGSGSYYCEFRtddnqilNVDYAKVAEGYGAKTYRANTVEELKA 576
Cdd:cd02004 81 SGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqlSYGLGLPVTTLLP-------DTRYDLVAEAFGGKGELVTTPEELKP 153
|
170
....*....|....*...
gi 504294315 577 ALEDAKKQNVSTLIEMKV 594
Cdd:cd02004 154 ALKRALASGKPALINVII 171
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
425-594 |
3.47e-25 |
|
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: 102.67 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 425 TINETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYHLEYGYScMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELI 504
Cdd:cd02002 9 ALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRGGG-LGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 505 TAIQYNKKINVLLFDNSGFgciNNLQMDhgSGSYYCEFRTDDNQIL------NVDYAKVAEGYGAKTYRANTVEELKAAL 578
Cdd:cd02002 88 TAARYGLPVTVVILNNRGY---GALRSF--LKRVGPEGPGENAPDGldlldpGIDFAAIAKAFGVEAERVETPEELDEAL 162
|
170
....*....|....*.
gi 504294315 579 EDAKKQNVSTLIEMKV 594
Cdd:cd02002 163 REALAEGGPALIEVVV 178
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
467-599 |
2.03e-23 |
|
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: 97.95 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 467 CMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ-MdhgsgsYYCEFRTD 545
Cdd:cd02015 51 TMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQeL------FYEGRYSH 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504294315 546 DNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLPKTM 599
Cdd:cd02015 125 TTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEALASDGPVLLDVLVDPEEN 178
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
87-594 |
7.24e-23 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 103.01 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 87 AVSTSvGPGAANLVAAAGTALANNIPVLLIpadTFATRQPDpVLQQMEQeysaAITTNDALKPVSRYWDRITRPEQLMSS 166
Cdd:PRK08617 71 VLVTS-GPGVSNLATGLVTATAEGDPVVAI---GGQVKRAD-RLKRTHQ----SMDNVALFRPITKYSAEVQDPDNLSEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 167 LLRAFEVMTDpAKAGPATICISQDV-----EGEAydfdesffVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGA 241
Cdd:PRK08617 142 LANAFRAAES-GRPGAAFVSLPQDVvdapvTSKA--------IAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 242 KYSGARDELVAISEAYNIPLVETQAGKSTV----EADFANNLGgmgitgtLAANKAA----RQADLIIGIGtrytdfats 313
Cdd:PRK08617 213 SSPEVTAAIRRLLERTNLPVVETFQAAGVIsrelEDHFFGRVG-------LFRNQPGdellKKADLVITIG--------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 314 sktafdFD----KAKFLN-------INVSRMQAYKLDAFQ----VVADAKVTLGKLHGLLEGYesEFGTTFRELKDEWLA 378
Cdd:PRK08617 277 ------YDpieyEPRNWNsegdatiIHIDVLPAEIDNYYQpereLIGDIAATLDLLAEKLDGL--SLSPQSLEILEELRA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 379 ERERLSKVTFKREAFdpeiKNHFSQEVlneyadalntelpqttalLTINETIPEDSVIICSAGSLPGDLQRLWHSNVPNT 458
Cdd:PRK08617 349 QLEELAERPARLEEG----AVHPLRII------------------RALQDIVTDDTTVTVDVGSHYIWMARYFRSYEPRH 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 459 YHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQM---DHGS 535
Cdd:PRK08617 407 LLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQEEmkyGRSS 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 504294315 536 GsyyCEFRtddnqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK08617 487 G---VDFG-------PVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPV 535
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
212-581 |
1.06e-22 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 102.37 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 212 RMQPSERELQGAAELIKSSKKPVILVGGGAkySGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGMGITGTLAAN 291
Cdd:PRK09124 183 VVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 292 KAARQADLIIGIGTrytDFATSsktAFDFDKAKFLNINvsrmqaykLDAFQVVADAKVTLGklhglLEGyesEFGTTFRE 371
Cdd:PRK09124 261 HAMMNCDTLLMLGT---DFPYR---QFYPTDAKIIQID--------INPGSLGRRSPVDLG-----LVG---DVKATLAA 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 372 LkdewlaererLSKVTFKREafdpeikNHFSQEVLNEYA------DALNTELPQTTAL----LT--INETIPEDSVIICS 439
Cdd:PRK09124 319 L----------LPLLEEKTD-------RKFLDKALEHYRkarkglDDLAVPSDGGKPIhpqyLArqISEFAADDAIFTCD 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 440 AGSLPGDLQRLWHSNVPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFD 519
Cdd:PRK09124 382 VGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFN 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504294315 520 NSGFGCInNLQMDHGSgsyYCEFRTDdnqILNVDYAKVAEGYGAKTYRANTVEELKAALEDA 581
Cdd:PRK09124 462 NSVLGFV-AMEMKAGG---YLTDGTD---LHNPDFAAIAEACGITGIRVEKASELDGALQRA 516
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
34-596 |
2.08e-22 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 101.53 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 34 GIFTIFGH-GN-VLGIGQALEQDAGHLKVYQGKNEQGMAHAAMAYSKqMLRRKIYAVSTSvGPGAANLVAAAGTALANNI 111
Cdd:PRK08273 17 GVRRVFGYpGDgINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAK-FTGEVGVCLATS-GPGAIHLLNGLYDAKLDHV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 112 PVLLIpadtfatrqpdpVLQQ----MEQEYSAAITTNDALKPV-SRYWDRITRPEQLMSSLLRAFEVMTdpAKAGPATIC 186
Cdd:PRK08273 95 PVVAI------------VGQQaraaLGGHYQQEVDLQSLFKDVaGAFVQMVTVPEQLRHLVDRAVRTAL--AERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 187 ISQDVEGEAYDFDESFFvKRVH-----YIDRMQPSERELQGAAELIKSSKKPVILVGGGAKysGARDELVAISEAYNIPL 261
Cdd:PRK08273 161 LPNDVQELEYEPPPHAH-GTVHsgvgyTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGAL--GATDEVIAVAERLGAGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 262 VETQAGKSTVEADFANNLGGMGITGTLAANKAARQAD--LIIGIGTRYTDFATssktafDFDKAKFLNINV-SRMQA--Y 336
Cdd:PRK08273 238 AKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDtlLMVGSSFPYSEFLP------KEGQARGVQIDIdGRMLGlrY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 337 KLDAfQVVADAKVTLGKLHGLLEGYESefgTTFRELKDEWLAERERlskvTFKREAFDPeiknhfsqevlneyADALNte 416
Cdd:PRK08273 312 PMEV-NLVGDAAETLRALLPLLERKKD---RSWRERIEKWVARWWE----TLEARAMVP--------------ADPVN-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 417 lPQTTALlTINETIPEDSVIICSAGS----------LPGDLQRlwhsnvpntyHLEYGYSCMGYEVSGTLGLKLAHPDRE 486
Cdd:PRK08273 368 -PQRVFW-ELSPRLPDNAILTADSGScanwyardlrMRRGMMA----------SLSGTLATMGPAVPYAIAAKFAHPDRP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 487 VYSIVGDGSFLMLH-SELITAIQY-----NKKINVLLFDNsgfgciNNLQM-------DHGSGsyycefRTDDNQIL-NV 552
Cdd:PRK08273 436 VIALVGDGAMQMNGmAELITVAKYwrqwsDPRLIVLVLNN------RDLNQvtweqrvMEGDP------KFEASQDLpDV 503
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 504294315 553 DYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:PRK08273 504 PYARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDP 547
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
10-191 |
1.37e-21 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 91.91 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 10 AQALIKFLNQQYihvdgkeepfVEGIFTIFGhGNVLGIGQALEQDAGhLKVYQGKNEQGMAHAAMAYSKqmLRRKIYAVS 89
Cdd:pfam02776 2 AEALADVLKALG----------VDTVFGVPG-GHILPLLDALAKSPG-IRYVLTRHEQGAAFAADGYAR--ATGKPGVVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 90 TSVGPGAANLVAAAGTALANNIPVLLIPADTFATRQPDPVLQQMeqeysaaITTNDALKPVSRYWDRITRPEQLMSSLLR 169
Cdd:pfam02776 68 VTSGPGATNALTGLANAYVDSVPLLVISGQRPRSLVGRGALQQE-------LDQLALFRPVTKWAVRVTSADEIPEVLRR 140
|
170 180
....*....|....*....|..
gi 504294315 170 AFEVMTDPaKAGPATICISQDV 191
Cdd:pfam02776 141 AFRAALSG-RPGPVYLEIPLDV 161
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
425-597 |
5.97e-21 |
|
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: 90.67 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 425 TINETIPEDSVIICSAGS---------LPGDL----QRLWHSnvpntyhleygyscMGYEVSGTLGLKLAHPDREVYSIV 491
Cdd:cd02005 10 QVQNFLKPNDILVAETGTswfgaldlkLPKGTrfisQPLWGS--------------IGYSVPAALGAALAAPDRRVILLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 492 GDGSFLMLHSELITAIQYNKKINVLLFDNSGFGcInnLQMDHGSGSYYcefrtddNQILNVDYAKVAE----GYGAKTYR 567
Cdd:cd02005 76 GDGSFQMTVQELSTMIRYGLNPIIFLINNDGYT-I--ERAIHGPEASY-------NDIANWNYTKLPEvfggGGGGLSFR 145
|
170 180 190
....*....|....*....|....*....|.
gi 504294315 568 ANTVEELKAALEDAKKQ-NVSTLIEMkVLPK 597
Cdd:cd02005 146 VKTEGELDEALKDALFNrDKLSLIEV-ILPK 175
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
32-496 |
1.13e-16 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 83.23 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 32 VEGIFTIFGhGNVLGIGQALEQDAghLKVYQGKNEQGMAHAAMAYSKqMLRRKIYAVSTSvGPGAANLVAAAGTALANNI 111
Cdd:PRK05858 20 VDTMFTLSG-GHLFPLYDGAREEG--IRLIDVRHEQTAAFAAEAWAK-LTRVPGVAVLTA-GPGVTNGMSAMAAAQFNQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 112 PVLLIPADTFATRQPDPVLQQMEQEysaaittnDALKPVSRYWDRITRPEQLMSSLLRAFEVMTDPAKaGPATICISQDV 191
Cdd:PRK05858 95 PLVVLGGRAPALRWGMGSLQEIDHV--------PFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHR-GPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 192 ---EGEAYDFDESFFVKRVhyidRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGK 268
Cdd:PRK05858 166 afsMADDDGRPGALTELPA----GPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 269 STVEADFAnnlggmgITGTLAANKAARQADLIIGIGTRyTDFatssKTAF-DF-DKAKFLNINVSRMQaykLDAFQVVAd 346
Cdd:PRK05858 242 GVVPADHP-------LAFSRARGKALGEADVVLVVGVP-MDF----RLGFgVFgGTAQLVHVDDAPPQ---RAHHRPVA- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 347 akvtlGKLHGLLEGYESEFGTTFRELKD--EWLAERERLSKVTFKREAfdpeiknhfsqEVLNEYADALN-----TELpq 419
Cdd:PRK05858 306 -----AGLYGDLSAILSALAGAGGDRTDhqGWIEELRTAETAARARDA-----------AELADDRDPIHpmrvyGEL-- 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504294315 420 ttalltiNETIPEDSVIICSAGSLPGDLQRLWHSNVPNTYhLEYG-YSCMGYEVSGTLGLKLAHPDREVYSIVGDGSF 496
Cdd:PRK05858 368 -------APLLDRDAIVIGDGGDFVSYAGRYIDPYRPGCW-LDPGpFGCLGTGPGYALAARLARPSRQVVLLQGDGAF 437
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
422-596 |
3.55e-15 |
|
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: 74.27 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 422 ALLTINETIPEDSVIICSAGSLPGDLQRLwhSNVPNTYHLE--YGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLML 499
Cdd:cd03371 4 AIEIVLSRAPATAAVVSTTGMTSRELFEL--RDRPGGGHAQdfLTVGSMGHASQIALGIALARPDRKVVCIDGDGAALMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 500 HSELITAIQYNKK--INVlLFDNsgfGCinnlqmdHGS--GSYYCEFRTDDNQIlnvdyAKvAEGYgAKTYRANTVEELK 575
Cdd:cd03371 82 MGGLATIGGLAPAnlIHI-VLNN---GA-------HDSvgGQPTVSFDVSLPAI-----AK-ACGY-RAVYEVPSLEELV 143
|
170 180
....*....|....*....|.
gi 504294315 576 AALEDAKKQNVSTLIEMKVLP 596
Cdd:cd03371 144 AALAKALAADGPAFIEVKVRP 164
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
86-595 |
1.76e-14 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 76.53 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 86 YAVSTSvGPGAANLVAAAG---------TALANNIPvLLIPA--DTFATRQPDPVLqqmeqeysAAITTNDALKPVSRYW 154
Cdd:PRK07092 67 YAQATG-NAAFVNLHSAAGvgnamgnlfTAFKNHTP-LVITAgqQARSILPFEPFL--------AAVQAAELPKPYVKWS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 155 DRITRPEQLMSSLLRAFEVMTDPAKaGPATICISQDvegeayDFD---ESFFVKRVHYidRMQPSERELQGAAELIKSSK 231
Cdd:PRK07092 137 IEPARAEDVPAAIARAYHIAMQPPR-GPVFVSIPYD------DWDqpaEPLPARTVSS--AVRPDPAALARLGDALDAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 232 KPVILVGGGAKYSGARDELVAISEAYNIPL-VETQAGKSTVEAD---FANNLGGM--GITGTLAANkaarqaDLIIGIGT 305
Cdd:PRK07092 208 RPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAPMSGRCSFPEDhplFAGFLPASreKISALLDGH------DLVLVIGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 306 ---RYTDFATSSKtafdFDKAKFLninvsrmqaykldaFQVVADAKVT----LGklhgllegyESEFGTTFRELKDewLA 378
Cdd:PRK07092 282 pvfTYHVEGPGPH----LPEGAEL--------------VQLTDDPGEAawapMG---------DAIVGDIRLALRD--LL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 379 ERERLSKvtfkREAFDPEiknhfsqeVLNEYADALNTELPQTTALLTINETIPEDSVIICSAGSLPGdlqrLWHSNVPNT 458
Cdd:PRK07092 333 ALLPPSA----RPAPPAR--------PMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRP----AMQEHLPMR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 459 YHLEYGYSC---MGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINN----LQM 531
Cdd:PRK07092 397 RQGSFYTMAsggLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWfapvFGV 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504294315 532 DHGSGsyycefrTDdnqILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVL 595
Cdd:PRK07092 477 RDVPG-------LD---LPGLDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
34-591 |
1.16e-13 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 73.87 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 34 GIFTIFGhgnVLGIGQA----LEQDAGhLKVYQGKNEQGMAHAAmAYSKQMLRRKIYAVSTSvGPGAANLVAAAGTALAN 109
Cdd:PRK09259 24 GIDTIYG---VVGIPITdlarLAQAEG-IRYIGFRHEQSAGNAA-AAAGFLTQKPGVCLTVS-APGFLNGLTALANATTN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 110 NIPVLLIPADTfaTRQ-PDpvLQQ-----MEQeYSAAittndalKPVSRYWDRITRPEQLMSSLLRAFE---------VM 174
Cdd:PRK09259 98 CFPMIMISGSS--EREiVD--LQQgdyeeLDQ-LNAA-------KPFCKAAFRVNRAEDIGIGVARAIRtavsgrpggVY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 175 TD-PAKAgpaticISQDVEGEAydfDESFFVKRVHYIDRMQPSERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAI 253
Cdd:PRK09259 166 LDlPAKV------LAQTMDADE---ALTSLVKVVDPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 254 SEAYNIPLVETQAGKSTVEADFANNLGGmgitgtlAANKAARQADLIIGIGTR------YTDFATSSKTafdfdkAKF-- 325
Cdd:PRK09259 237 VEKTGIPFLPMSMAKGLLPDTHPQSAAA-------ARSLALANADVVLLVGARlnwllsHGKGKTWGAD------KKFiq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 326 LNINVSRMQAYKLDAFQVVADAKVTLGKlhgLLEGYESEFGTTFRELKDEWLAERER-LSKVTfKREAFDPEIKNHFSqe 404
Cdd:PRK09259 304 IDIEPQEIDSNRPIAAPVVGDIGSVMQA---LLAGLKQNTFKAPAEWLDALAERKEKnAAKMA-EKLSTDTQPMNFYN-- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 405 vlneyadalntelpqttALLTINETIPED-SVIICSAGSLPGDLQRlwhsNVPNTYHLEYGYSC---------MGYEVSG 474
Cdd:PRK09259 378 -----------------ALGAIRDVLKENpDIYLVNEGANTLDLAR----NIIDMYKPRHRLDCgtwgvmgigMGYAIAA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 475 TLglklaHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFgcinnlqmdhgsgsyyceFRTDDNQILNVD- 553
Cdd:PRK09259 437 AV-----ETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGGI------------------YRGDDVNLSGAGd 493
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 504294315 554 -----------YAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIE 591
Cdd:PRK09259 494 psptvlvhharYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLIN 542
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
422-596 |
1.16e-13 |
|
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: 69.85 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 422 ALLTINETIPEDSVI------ICSAGSlpgdlQRLWHSNvPNTYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGS 495
Cdd:cd02013 9 VLRELEKAMPEDAIVstdignICSVAN-----SYLRFEK-PRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 496 FLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGsyycefRTDDNQILNVDYAKVAEGYGAKTYRANTVEELK 575
Cdd:cd02013 83 WGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNN------RFVGTELESESFAKIAEACGAKGITVDKPEDVG 156
|
170 180
....*....|....*....|....
gi 504294315 576 AALEDA---KKQNVSTLIEMKVLP 596
Cdd:cd02013 157 PALQKAiamMAEGKTTVIEIVCDQ 180
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
468-583 |
1.30e-11 |
|
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: 64.22 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 468 MGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQ----MDHGSGSYYCEFR 543
Cdd:cd02006 59 LGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNNAYLGLIRQAQrafdMDYQVNLAFENIN 138
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 504294315 544 TDDNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKK 583
Cdd:cd02006 139 SSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQAKK 178
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
432-597 |
1.82e-08 |
|
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: 54.60 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 432 EDSVIICSAGSLPGDLQRLWHSNVpNTYHLeygySCMGYEVSGTLGLKLAHPdREVYSIVGDGSFLMLHSELITAIQYN- 510
Cdd:cd03372 13 KDELVVSNIGFPSKELYAAGDRPL-NFYML----GSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATIAAEKp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 511 KKINVLLFDNSGFGCINNlQMDHGSgsyycefrtddnqiLNVDYAKVAEGYG-AKTYRANTVEELKAALEDAKKQnvSTL 589
Cdd:cd03372 87 KNLIIVVLDNGAYGSTGN-QPTHAG--------------KKTDLEAVAKACGlDNVATVASEEAFEKAVEQALDG--PSF 149
|
....*...
gi 504294315 590 IEMKVLPK 597
Cdd:cd03372 150 IHVKIKPG 157
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
217-581 |
3.37e-08 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 56.63 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 217 ERELQGAAELIKSSKKPVILVGGGAKYSGARDELVAISEAYNIPLVETQAGKSTVEADFANNLGGM-GITGTLAANKAAR 295
Cdd:PLN02573 211 EAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 296 QADLIIGIGTRYTDFATSSKTAFdFDKAKFLNINVSRmqaykldafqvvadakVTLGklHGllegyeSEFGTTFreLKDE 375
Cdd:PLN02573 291 SADAYLFAGPIFNDYSSVGYSLL-LKKEKAIIVQPDR----------------VTIG--NG------PAFGCVL--MKDF 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 376 WLAERERLSKVT-----FKReAFDPEiknhfSQEVLNEYADALNTE---------LPQTTALltINETipEDSVIICSAG 441
Cdd:PLN02573 344 LEALAKRVKKNTtayenYKR-IFVPE-----GEPLKSEPGEPLRVNvlfkhiqkmLSGDTAV--IAET--GDSWFNCQKL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 442 SLPGDLQrlwhsnvpntYHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLfdns 521
Cdd:PLN02573 414 KLPEGCG----------YEFQMQYGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFL---- 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504294315 522 gfgcINNlqmdhgsGSYYCEFRTDD---NQILNVDYAKVAE----GYG-AKTYRANTVEELKAALEDA 581
Cdd:PLN02573 480 ----INN-------GGYTIEVEIHDgpyNVIKNWNYTGLVDaihnGEGkCWTAKVRTEEELIEAIATA 536
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
431-591 |
3.09e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 53.34 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 431 PEDSVIICSAGSLPGDLQRLWHSNVPNTyHLEYGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYN 510
Cdd:PRK12474 355 PDQAIYADEALTSGLFFDMSYDRARPHT-HLPLTGGSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMAREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 511 KKINVLLFDNSGFGCIN-NLQMDHGSGSYYCEFRTDDNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTL 589
Cdd:PRK12474 434 LDVTVVIFANRSYAILNgELQRVGAQGAGRNALSMLDLHNPELNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRL 513
|
..
gi 504294315 590 IE 591
Cdd:PRK12474 514 IE 515
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
472-594 |
3.37e-07 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 50.67 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 472 VSGTLGLKLAHPDReVYSIVGD-------GSFLMLHselitaiQYNKKINVLLFDNSGFGCINNL-QMDHGSgsyycEFR 543
Cdd:cd02009 57 LSTALGIALATDKP-TVLLTGDlsflhdlNGLLLGK-------QEPLNLTIVVINNNGGGIFSLLpQASFED-----EFE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504294315 544 TDDNQILNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:cd02009 124 RLFGTPQGLDFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKT 174
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
476-594 |
1.63e-06 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 51.00 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 476 LGLKLAHPDREVYSIVGDGSFLMLHSELITAIQYNKKINVLLFDNSGFGCINNLQMDHGSGSYYCE----FRTDDNQIln 551
Cdd:PRK07586 395 TGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRAYAILRGELARVGAGNPGPRaldmLDLDDPDL-- 472
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 504294315 552 vDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKV 594
Cdd:PRK07586 473 -DWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
467-590 |
7.79e-06 |
|
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: 46.89 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 467 CMGYEVSGTLGLKLAHPDREVYSIVGDGSFlmLHS---ELITAIqYNK-KINVLLFDNS-----GfgcinnlQMDH-GSG 536
Cdd:cd02008 52 CMGASIGVAIGMAKASEDKKVVAVIGDSTF--FHSgilGLINAV-YNKaNITVVILDNRttamtG-------GQPHpGTG 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504294315 537 SYYCEFRTddnqilNVDYAKVAEGYGAK------TYRAN-TVEELKAALEDAKkqnVSTLI 590
Cdd:cd02008 122 KTLTEPTT------VIDIEALVRAIGVKrvvvvdPYDLKaIREELKEALAVPG---VSVII 173
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
468-596 |
1.32e-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: 42.86 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 468 MGYEVSGTLGLKLAHPdREVYSIVGDGSFLMLHSELITAIQYN-KKINVLLFDNSGFGCINNlQMDHGSgsyycefrtdd 546
Cdd:cd02001 44 MGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAGEFTpLNLILVVLDNRAYGSTGG-QPTPSS----------- 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 504294315 547 nqilNVDYAKVAEGYGAKTYRANTVEELKAALEDAKKQNVSTLIEMKVLP 596
Cdd:cd02001 111 ----NVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPIAP 156
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
449-593 |
6.85e-04 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 41.72 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 449 RLWHSNVPNtyHLEYGYScMGYEVS-GTLG------------LKLAHPDREVYSIVGDGSfLMlhsELIT--AIQY--NK 511
Cdd:cd02012 82 RQLGSRLPG--HPEYGLT-PGVEVTtGSLGqglsvavgmalaEKLLGFDYRVYVLLGDGE-LQ---EGSVweAASFagHY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 512 KIN--VLLFDNsgfgciNNLQMDhgsgsyyceFRTDDnQILNVDYAKVAEGYGAKTYRA--NTVEELKAALEDAKKQNVS 587
Cdd:cd02012 155 KLDnlIAIVDS------NRIQID---------GPTDD-ILFTEDLAKKFEAFGWNVIEVdgHDVEEILAALEEAKKSKGK 218
|
....*..
gi 504294315 588 -TLIEMK 593
Cdd:cd02012 219 pTLIIAK 225
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
32-185 |
3.26e-03 |
|
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: 38.48 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504294315 32 VEGIFTIFGHGNVLGIGQALEQDagHLKVYQGKNEQGMAHAAMAYSKQMLRRkiyAVSTSVGPGAANLVAAAGTALANNI 111
Cdd:cd06586 12 VRHVFGYPGDEISSLLDALREGD--KRIIDTVIHELGAAGAAAGYARAGGPP---VVIVTSGTGLLNAINGLADAAAEHL 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504294315 112 PVLlipadtFATRQPDPVLQ--QMEQEysaaITTNDALKPVSRYWDRITRPEQLMSSLLRAFEvmTDPAKAGPATI 185
Cdd:cd06586 87 PVV------FLIGARGISAQakQTFQS----MFDLGMYRSIPEANISSPSPAELPAGIDHAIR--TAYASQGPVVV 150
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
463-520 |
4.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 39.04 E-value: 4.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 504294315 463 YGYSCMGYEVSGTLGLKLAHPDREVYSIVGDGSFLMLHSELIT-AIQYNKKINVLLFDN 520
Cdd:PRK06163 54 YMLGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTiAALAPKNLTIIVMDN 112
|
|
| |
