|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
1-548 |
0e+00 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 1085.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKILPeFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK08978 161 IQLAEGELEPHL-TTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINKIMP 320
Cdd:PRK08978 240 DHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 321 QLELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAG 400
Cdd:PRK08978 320 ALQQPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 401 LGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSETILD 480
Cdd:PRK08978 400 LGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSETDLS 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425475 481 DNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEMLENT 548
Cdd:PRK08978 480 DNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLEKL 547
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-544 |
0e+00 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 678.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESPVKILPEFTPPAIPVVTTD--AIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGT 237
Cdd:COG0028 163 DVQAAEAEEEPAPPELRGYRPRPAPDpeAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 238 IERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINK 317
Cdd:COG0028 243 FPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 318 IMPQL-----ELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDP 392
Cdd:COG0028 323 VLAALlealePRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 393 QNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDG 472
Cdd:COG0028 403 RRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040425475 473 RHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENvwplvPPGASNSEM 544
Cdd:COG0028 483 RYSGTDL-PNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN-----PPGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
1-545 |
0e+00 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 661.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYnDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESPVKILPEFTPPAI-PVVTTD--AIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLG 236
Cdd:TIGR00118 161 DVTTAEIEYPYPEKVNLPGYrPTVKGHplQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 237 TIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDIN 316
Cdd:TIGR00118 241 SFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 KIMPQL------ELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPR 390
Cdd:TIGR00118 321 NVLEELlkklfeLKERKESAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPFR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 391 DPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFF 470
Cdd:TIGR00118 401 KPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELFY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040425475 471 DGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEML 545
Cdd:TIGR00118 481 EERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEMI 555
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 639.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALY----DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGAT 76
Cdd:PRK07418 19 ATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 77 NLVTGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVD 156
Cdd:PRK07418 99 NLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 157 IAKDVQLAE---SPVK----ILPEFTPPAIPvvTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAV 229
Cdd:PRK07418 179 IPKDVGQEEfdyVPVEpgsvKPPGYRPTVKG--NPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 230 STLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANA 309
Cdd:PRK07418 257 TTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 310 PIRGDINKIMPQL-ELSQDISSWVHHSEGLRSSFKWRYDHP------GDLIFAPLLLKQLSDMMPaSAMVSTDVGQHQMW 382
Cdd:PRK07418 337 PIVGDVRKVLVKLlERSLEPTTPPRTQAWLERINRWKQDYPlvvppyEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQMW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 383 AAQHIQpRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMV 462
Cdd:PRK07418 416 AAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 463 RQWQSLFFDGRHSET-ILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASN 541
Cdd:PRK07418 495 RQWQESFYGERYSASnMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCYPMVPPGKSN 574
|
....
gi 1040425475 542 SEML 545
Cdd:PRK07418 575 AQMV 578
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 623.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYkQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLA----ESPVKI-LPEFTPpaipvvTTD----AIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVS 230
Cdd:PRK08527 163 DVTATlgefEYPKEIsLKTYKP------TYKgnsrQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 231 TLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAP 310
Cdd:PRK08527 237 TLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 311 IRGDI----NKIMPQL--ELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAA 384
Cdd:PRK08527 317 IVGDLknvlKEMLEELkeENPTTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 385 QHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQ 464
Cdd:PRK08527 397 QFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 465 WQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEM 544
Cdd:PRK08527 477 WQTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNM 556
|
.
gi 1040425475 545 L 545
Cdd:PRK08527 557 I 557
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-543 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 619.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDG-GVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK07789 31 MTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAES----PVKI-LPEFTPpaipvvTTDA----IEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVS 230
Cdd:PRK07789 191 DALQAQTtfswPPRMdLPGYRP------VTKPhgkqIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 231 TLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAP 310
Cdd:PRK07789 265 TLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 311 IRGDINKIMPQL----------ELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAP-LLLKQLSDMMPASAMVSTDVGQH 379
Cdd:PRK07789 345 IVGDVKEVIAELiaalraehaaGGKPDLTAWWAYLDGWRETYPLGYDEPSDGSLAPqYVIERLGEIAGPDAIYVAGVGQH 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 380 QMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRL 459
Cdd:PRK07789 425 QMWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 460 GMVRQWQSLFFDGRHSETILDDN----PDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAyllHVLID----EEENV 531
Cdd:PRK07789 505 GMVRQWQTLFYEERYSNTDLHTHshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAINDR---PVVIDfvvgKDAMV 581
|
570
....*....|..
gi 1040425475 532 WPLVPPGASNSE 543
Cdd:PRK07789 582 WPMVAAGTSNDE 593
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-546 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 610.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK06048 8 MTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK06048 88 GIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAE----SPVKI-LPEFTPPAipVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGL 235
Cdd:PRK06048 168 VTTAEidfdYPDKVeLRGYKPTY--KGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMGI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 236 GTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDI 315
Cdd:PRK06048 246 GAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIVGDA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 316 NKIMPQLE---LSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPaSAMVSTDVGQHQMWAAQHIQPRDP 392
Cdd:PRK06048 326 KQVLKSLIkyvQYCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKYKYP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 393 QNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDG 472
Cdd:PRK06048 405 RTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELFYDK 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040425475 473 RHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEMLE 546
Cdd:PRK06048 485 RYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILD 558
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
3-545 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 602.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALY----DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNL 78
Cdd:CHL00099 12 GAFALIDSLVRHGVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIA 158
Cdd:CHL00099 92 VTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 159 KDVQLAE----SPVKILPEFTPPAIPVV---TTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVST 231
Cdd:CHL00099 172 KDVGLEKfdyyPPEPGNTIIKILGCRPIykpTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 232 LKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPI 311
Cdd:CHL00099 252 LMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 312 RGDINKIMPQ-LEL---------SQDISSWVHhseglRSSfKWRYDHP------GDLIFAPLLLKQLSDMMPaSAMVSTD 375
Cdd:CHL00099 332 VGDVKKVLQElLELlknspnlleSEQTQAWRE-----RIN-RWRKEYPllipkpSTSLSPQEVINEISQLAP-DAYFTTD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 376 VGQHQMWAAQHIQPRdPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLN 455
Cdd:CHL00099 405 VGQHQMWAAQFLKCK-PRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIIN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 456 NSRLGMVRQWQSLFFDGRHSETILDDN-PDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPL 534
Cdd:CHL00099 484 NKWQGMVRQWQQAFYGERYSHSNMEEGaPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENCYPM 563
|
570
....*....|.
gi 1040425475 535 VPPGASNSEML 545
Cdd:CHL00099 564 VAPGKSNSQMI 574
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 587.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGG-VEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK08155 13 FTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK08155 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESPVKILPE-FTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTI 238
Cdd:PRK08155 173 DVQTAVIELEALPApAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 239 ERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINKI 318
Cdd:PRK08155 253 PKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 319 MPQLE---LSQDISSWVHHSEGLRSSFKWRYDHPGDlifaPL----LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRD 391
Cdd:PRK08155 333 LAQLLplvEAQPRAEWHQLVADLQREFPCPIPKADD----PLshygLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 392 PQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFD 471
Cdd:PRK08155 409 PRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFYG 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040425475 472 GRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEML 545
Cdd:PRK08155 489 QRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTEMI 562
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 566.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLaESPVKILPE--FTPPAIPVVTTDAIE--QAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLG 236
Cdd:PRK06725 175 VQN-EKVTSFYNEvvEIPGYKPEPRPDSMKlrEVAKAISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 237 TIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDIN 316
Cdd:PRK06725 254 AYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 KIMPQL---ELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQ 393
Cdd:PRK06725 334 KALHMLlhmSIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 394 NFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGR 473
Cdd:PRK06725 414 TFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFYENR 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1040425475 474 HSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEML 545
Cdd:PRK06725 494 LSESKI-GSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMI 564
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 555.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAE-------SPVKI-LPEFTPPAI--PVvttdAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVS 230
Cdd:PRK06276 161 VQEGEldlekypIPAKIdLPGYKPTTFghPL----QIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 231 TLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAP 310
Cdd:PRK06276 237 TLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 311 IRGDINKIMPQL--ELS----QDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMM-----PASAMVSTDVGQH 379
Cdd:PRK06276 317 IVGDAKNVLRDLlaELMkkeiKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLreidpSKNTIITTDVGQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 380 QMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRL 459
Cdd:PRK06276 397 QMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 460 GMVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVwPLVPPGA 539
Cdd:PRK06276 477 GMVYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPGG 555
|
....*.
gi 1040425475 540 SNSEML 545
Cdd:PRK06276 556 NLTNIL 561
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
2-540 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 554.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 2 KGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGG-VEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PLN02470 14 KGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PLN02470 94 GLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQ--LA----ESPVKiLPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVqlAKATDAVREFLRLNPMPAVSTLKG 234
Cdd:PLN02470 174 IQqqLAvpnwNQPMK-LPGYLSRLPKPPEKSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGIPVASTLMG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 235 LGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGD 314
Cdd:PLN02470 251 LGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCAD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 315 I-------NKIMPQLELSQ-DISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQH 386
Cdd:PLN02470 331 VklalqglNKLLEERKAKRpDFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 387 IQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQ 466
Cdd:PLN02470 411 YKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 467 SLFFDGRHSETILDDN-------PDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGA 539
Cdd:PLN02470 491 DRFYKANRAHTYLGDPdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIPGGG 570
|
.
gi 1040425475 540 S 540
Cdd:PLN02470 571 T 571
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-545 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 552.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESpvkilpEFTPPAIPVVTT----------DAIEQAQYFLSQATRPVLYVGGGVQLA--KATDAVREFLRLNPMP 227
Cdd:PRK09107 171 DVQFATG------TYTPPQKAPVHVsyqpkvkgdaEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 228 AVSTLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLA 307
Cdd:PRK09107 245 ITSTLMGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 308 NAPIRGDINKIMPQL----------ELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMP-ASAMVSTDV 376
Cdd:PRK09107 325 DVPIIGDVGHVLEDMlrlwkargkkPDKEALADWWGQIARWRARNSLAYTPSDDVIMPQYAIQRLYELTKgRDTYITTEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 377 GQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNN 456
Cdd:PRK09107 405 GQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 457 SRLGMVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVP 536
Cdd:PRK09107 485 QYMGMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPMIP 564
|
....*....
gi 1040425475 537 PGASNSEML 545
Cdd:PRK09107 565 SGKAHNEML 573
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 537.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK07710 16 MTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAE----SPVKI-LPEFTPPAIP-VVTTDAIEQAqyfLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKG 234
Cdd:PRK07710 176 MVVEEgefcYDVQMdLPGYQPNYEPnLLQIRKLVQA---VSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 235 LGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGD 314
Cdd:PRK07710 253 LGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIVAD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 315 INKIMPQLELSQ----DISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPR 390
Cdd:PRK07710 333 AKQALQVLLQQEgkkeNHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 391 DPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFF 470
Cdd:PRK07710 413 TPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEEFY 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1040425475 471 DGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEM 544
Cdd:PRK07710 493 NQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPGKGLHEM 566
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
1-545 |
9.87e-178 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 513.58 E-value: 9.87e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESPvkilpeFTPPAI-------PVVTTDA--IEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVS 230
Cdd:PRK06965 181 DVSKTPCE------YEYPKSvemrsynPVTKGHSgqIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 231 TLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHA-KVIHIDIDAAEFSKLRLANA 309
Cdd:PRK06965 255 TLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 310 PIRGDINKIMPQL-------ELSQD---ISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQH 379
Cdd:PRK06965 335 PIVGDVKEVLKELieqlqtaEHGPDadaLAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 380 QMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRL 459
Cdd:PRK06965 415 QMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYL 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 460 GMVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEM--LESKTAYlLHVLIDEEENVWPLVPP 537
Cdd:PRK06965 495 GMVRQWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREAlrLKDRTVF-LDFQTDPTENVWPMVQA 573
|
....*...
gi 1040425475 538 GASNSEML 545
Cdd:PRK06965 574 GKGITEML 581
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
3-545 |
2.99e-176 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 509.36 E-value: 2.99e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTG 81
Cdd:PRK07282 12 GSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNfEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 82 LADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKDV 161
Cdd:PRK07282 92 IADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 162 QLAE-----SPVKILPEFTPPAIPvvTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLG 236
Cdd:PRK07282 172 SALEtdfiyDPEVNLPSYQPTLEP--NDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 237 TIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDIN 316
Cdd:PRK07282 250 TIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 KIMPQL----ELSQDISSWVHHSEGLRSSFKWrYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDP 392
Cdd:PRK07282 330 KALQMLlaepTVHNNTEKWIEKVTKDKNRVRS-YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPYQNE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 393 QNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDG 472
Cdd:PRK07282 409 RQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESFYEG 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040425475 473 RHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKtAYLLHVLIDEEENVWPLVPPGASNSEML 545
Cdd:PRK07282 489 RTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDV-PMLIEVDISRKEHVLPMVPAGKSNHEML 560
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-544 |
4.84e-170 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 493.49 E-value: 4.84e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK06466 4 LSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLA------ESPVKI-LPEFTPPAIPvvTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTL 232
Cdd:PRK06466 164 DMTNPaekfeyEYPKKVkLRSYSPAVRG--HSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 233 KGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIR 312
Cdd:PRK06466 242 MGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 313 GDINKIMPQL--ELSQD--------ISSWVHHSEGLRSSFK-WRYDHPGDLIFAP-LLLKQLSDMMPASAMVSTDVGQHQ 380
Cdd:PRK06466 322 GPVESVLTEMlaILKEIgekpdkeaLAAWWKQIDEWRGRHGlFPYDKGDGGIIKPqQVVETLYEVTNGDAYVTSDVGQHQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 381 MWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLG 460
Cdd:PRK06466 402 MFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 461 MVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYL-LHVLIDEEENVWPLVPPGA 539
Cdd:PRK06466 482 MVRQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAMKDRLVfIDIYVDRSEHVYPMQIADG 561
|
....*
gi 1040425475 540 SNSEM 544
Cdd:PRK06466 562 SMRDM 566
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-544 |
2.42e-163 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 476.62 E-value: 2.42e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK08979 4 LSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK08979 84 TGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQlaeSPVKILPEFTPPAI------PVVT--TDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFL-RLNpMPAVS 230
Cdd:PRK08979 164 DCL---NPAILHPYEYPESIkmrsynPTTSghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAeKLN-LPVVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 231 TLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAP 310
Cdd:PRK08979 240 TLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 311 IRGDINKIM----PQLELSQD------ISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQ 380
Cdd:PRK08979 320 IVGSADKVLdsmlALLDESGEtndeaaIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 381 MWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLG 460
Cdd:PRK08979 400 MFAALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 461 MVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYL-LHVLIDEEENVWPLVPPGA 539
Cdd:PRK08979 480 MVKQWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVDINVDETEHVYPMQIRGG 559
|
....*
gi 1040425475 540 SNSEM 544
Cdd:PRK08979 560 AMNEM 564
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-545 |
1.84e-162 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 474.40 E-value: 1.84e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQlaeSPVKILPEFTPPAIPVVTTD--------AIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVST 231
Cdd:PRK06882 164 DMV---NPANKFTYEYPEEVSLRSYNptvqghkgQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 232 LKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPI 311
Cdd:PRK06882 241 LMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 312 RGDINKIMPQ---------LELSQ-DISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQM 381
Cdd:PRK06882 321 VGSAKNVLEEflslleeenLAKSQtDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 382 WAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGM 461
Cdd:PRK06882 401 FAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 462 VRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYL-LHVLIDEEENVWPLVPPGAS 540
Cdd:PRK06882 481 VKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETEHVYPMQIRGGA 560
|
....*
gi 1040425475 541 NSEML 545
Cdd:PRK06882 561 MNEMI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-544 |
1.50e-158 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 464.32 E-value: 1.50e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQlaeSPVKILPEFTPPAI------PVVT--TDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVST 231
Cdd:PRK07979 164 DIL---NPANKLPYVWPESVsmrsynPTTQghKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 232 LKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPI 311
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 312 RGDINKI-------MPQLELSQD---ISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQM 381
Cdd:PRK07979 321 VGDARQVleqmlelLSQESAHQPldeIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 382 WAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGM 461
Cdd:PRK07979 401 FAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 462 VRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLL---HVLIDEEENVWPLVPPG 538
Cdd:PRK07979 481 VKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLvfvDVTVDGSEHVYPMQIRG 560
|
....*.
gi 1040425475 539 ASNSEM 544
Cdd:PRK07979 561 GGMDEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-545 |
5.30e-133 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 398.83 E-value: 5.30e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDA----LYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNL 78
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIA 158
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 159 KDVQLAE-----SPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLK 233
Cdd:PRK06456 164 RDIFYEKmeeikWPEKPLVKGYRDFPTRIDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 234 GLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDR-VTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIR 312
Cdd:PRK06456 244 GKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRtFTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVGIY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 313 GDINKIM-------PQLELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPL-LLKQLSDMMPASAMVSTDVGQHQMWAA 384
Cdd:PRK06456 324 GNAKIILrelikaiTELGQKRDRSAWLKRVKEYKEYYSQFYYTEENGKLKPWkIMKTIRQALPRDAIVTTGVGQHQMWAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 385 QHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQ 464
Cdd:PRK06456 404 VFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 465 WQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWPLVPPGASNSEM 544
Cdd:PRK06456 484 VQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLKQV 563
|
.
gi 1040425475 545 L 545
Cdd:PRK06456 564 I 564
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
358-538 |
8.24e-104 |
|
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: 309.81 E-value: 8.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 358 LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQ 437
Cdd:cd02015 6 VIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSFQMNIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 438 ELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKT 517
Cdd:cd02015 86 ELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEALASDG 165
|
170 180
....*....|....*....|.
gi 1040425475 518 AYLLHVLIDEEENVWPLVPPG 538
Cdd:cd02015 166 PVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-528 |
1.38e-97 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 306.80 E-value: 1.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 2 KGAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK08199 9 TGGQILVDALRANGVERVFCVPGESYLAVLDALHDeTDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK08199 89 GVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPED 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKILPEFTPPAiPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK08199 169 VLSETAEVPDAPPYRRVA-AAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGK---LDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINK 317
Cdd:PRK08199 248 RHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRVYRPDLAIVADPAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 318 IMPQLELSQDIS--SWVHHSEGLRSSF-KWRYDH--PGDLIFAPLLLkQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDP 392
Cdd:PRK08199 328 FAAALAALEPPAspAWAEWTAAAHADYlAWSAPLpgPGAVQLGEVMA-WLRERLPADAIITNGAGNYATWLHRFFRFRRY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 393 QNFI--TSaglGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFF 470
Cdd:PRK08199 407 RTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQEREY 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425475 471 DGRHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEE 528
Cdd:PRK08199 484 PGRVSGTDL-TNPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRIDPE 540
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-530 |
6.26e-95 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 299.82 E-value: 6.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVA--SSHIGTdaFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIA 158
Cdd:PRK08322 81 GVAYAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 159 KDVQLAESPVKILPEfTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTI 238
Cdd:PRK08322 159 EDIAAEETDGKPLPR-SYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 239 ERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGarFDdrvtgkLDTFAPH-------AKVIHIDIDAAEFSKLRLANAPI 311
Cdd:PRK08322 238 PETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD------VIEKPPFfmnpngdKKVIHINFLPAEVDPVYFPQVEV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 312 RGDI-NKIMPQLELSQDISSWVH-HSEGLRSSFKWRY-DHPGDLIFAPL---LLKQLSDMMPASAMVSTDVGQHQMWAAQ 385
Cdd:PRK08322 310 VGDIaNSLWQLKERLADQPHWDFpRFLKIREAIEAHLeEGADDDRFPMKpqrIVADLRKVMPDDDIVILDNGAYKIWFAR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 386 HIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQW 465
Cdd:PRK08322 390 NYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1040425475 466 QSLFFdGRHSetILD-DNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEEN 530
Cdd:PRK08322 470 QENMG-FEDF--GLDfGNPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSEN 532
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
3-531 |
5.82e-87 |
|
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. This reaction may be involved in either valine biosynthesis (biosynthetic) or conversion of pyruvate to acetoin and possibly to 2,3-butanediol (catabolic). The biosynthetic type, described by TIGR00118, is also capable of forming acetohydroxybutyrate from pyruvate and 2-oxobutyrate for isoleucine biosynthesis. The family described here, part of the same larger family of thiamine pyrophosphate-dependent enzymes (pfam00205, pfam02776) is the catabolic form, generally found associated with in species with acetolactate decarboxylase and usually found in the same operon. The model may not encompass all catabolic acetolactate synthases, but rather one particular clade in the larger TPP-dependent enzyme family. [Energy metabolism, Fermentation]
Pssm-ID: 131471 [Multi-domain] Cd Length: 539 Bit Score: 278.56 E-value: 5.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGL 82
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 83 ADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKDVQ 162
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 163 LAESPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIERD- 241
Cdd:TIGR02418 161 DSPVSVKAIPASYAPKLGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSREl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 242 DPHYLGMLGMHGTKAANLVVQESDLLIVVG---ARFDDRVTGKldtfAPHAKVIHIDIDAAEFSKLRLANAPIRGDI--- 315
Cdd:TIGR02418 241 EDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNS----ENDATIVHIDVEPAQIDNNYQPDLELVGDIast 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 316 -NKI---MPQLELSQ-------DISSWVHHSEGLRSSFKWRYDHPGDLIfaplllKQLSDMMPASAMVSTDVGQHQMWAA 384
Cdd:TIGR02418 317 lDLLaerIPGYELPPdalaileDLKQQREALDRVPATLKQAHLHPLEII------KAMQAIVTDDVTVTVDMGSHYIWMA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 385 QHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVrQ 464
Cdd:TIGR02418 391 RYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWNDNGYNMV-E 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425475 465 WQSLFFDGRHSEtiLDDNP-DFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENV 531
Cdd:TIGR02418 470 FQEEMKYQRSSG--VDFGPiDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNP 535
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-538 |
2.47e-86 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 277.28 E-value: 2.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGG--VEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNL 78
Cdd:PRK08266 4 MTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQVASSHIGTDAFQ--EM-DVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIV 155
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 156 DIAKDVQLAESPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVqlAKATDAVREFLRLNPMPAVSTLKGL 235
Cdd:PRK08266 164 EMPWDVFGQRAPVAAAPPLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPVVAFRSGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 236 GTIerDDPHYLGMLGMhgtkAANLVVQESDLLIVVGARFDDRVTgKLDTFAPHAKVIHIDIDAAEFSKLRlANAPIRGDI 315
Cdd:PRK08266 242 GIV--SDRHPLGLNFA----AAYELWPQTDVVIGIGSRLELPTF-RWPWRPDGLKVIRIDIDPTEMRRLK-PDVAIVADA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 316 NKIMPqlELSQDISSWVHHSEGLRSSFKWRYDHPGDLIFA--PLL--LKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRD 391
Cdd:PRK08266 314 KAGTA--ALLDALSKAGSKRPSRRAELRELKAAARQRIQAvqPQAsyLRAIREALPDDGIFVDELSQVGFASWFAFPVYA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 392 PQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFD 471
Cdd:PRK08266 392 PRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040425475 472 GRHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLI--DEEENVWPLVPPG 538
Cdd:PRK08266 472 GRVVASDL-VNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVprGSEASPWPFIHPA 539
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-531 |
2.69e-86 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 278.40 E-value: 2.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQ-DVAVCMATSGPGATNL 78
Cdd:PRK11269 4 MRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRATAgNIGVCIGTSGPAGTDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKhsYLVTDIED-LAP-TLAEAFIVAKAGRPGPVIVD 156
Cdd:PRK11269 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTK--WAVTVREPaLVPrVFQQAFHLMRSGRPGPVLID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 157 IAKDVQLAESPVKI-LPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGL 235
Cdd:PRK11269 162 LPFDVQVAEIEFDPdTYEPLPVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMGW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 236 GTIERDDPHYLGMLGMH-GTKAANLVVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDI-----------------D 297
Cdd:PRK11269 242 GAIPDDHPLMAGMVGLQtSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIeptqigrvfgpdlgivsD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 298 AAEFSKLRLANAPIRGDINKImpqlelsQDISSWVHHSEGLRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVSTDVG 377
Cdd:PRK11269 322 AKAALELLVEVAREWKAAGRL-------PDRSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 378 QHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNS 457
Cdd:PRK11269 395 LSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 458 RLGMVRQWQ---------SLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPAL----KEMLESKTAYLLHVL 524
Cdd:PRK11269 475 YLGLIRQAQrafdmdycvQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALeqakALMAEFRVPVVVEVI 554
|
....*..
gi 1040425475 525 IDEEENV 531
Cdd:PRK11269 555 LERVTNI 561
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
2-529 |
3.91e-82 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 267.25 E-value: 3.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 2 KGAELVVSALKQQGIETVFGYPGGAIMPIYDAL--YDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK08611 5 KAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRpGPVIVDIAK 159
Cdd:PRK08611 85 NGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DV---QLAESPVKILPEFTPPaIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKatDAVREFLRLNPMPAVSTLKGLG 236
Cdd:PRK08611 164 DLpaqKIKDTTNKTVDTFRPT-VPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAK--EELLAFAEKAKIPIIHTLPAKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 237 TIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRvtgklDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDIN 316
Cdd:PRK08611 241 IIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV-----DYLPKKAKAIQIDTDPANIGKRYPVNVGLVGDAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 KIMPQL----ELSQDISSWVHHSEGLRSSFKWrYDHPGDLIFAPL----LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQ 388
Cdd:PRK08611 316 KALHQLteniKHVEDRRFLEACQENMAKWWKW-MEEDENNASTPIkperVMAAIQKIADDDAVLSVDVGTVTVWSARYLN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 389 PRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSL 468
Cdd:PRK08611 395 LGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040425475 469 ffDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEE 529
Cdd:PRK08611 475 --AGELEYAIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVDPNA 533
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-532 |
8.34e-81 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 262.87 E-value: 8.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK08617 165 VVDAPVTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVISR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 D-DPHYLGMLGMHGTKAANLVVQESDLLIVVG---ARFDDRVTGKldtfAPHAKVIHIDIDAAEFSKLRLANAPIRGDI- 315
Cdd:PRK08617 245 ElEDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNS----EGDATIIHIDVLPAEIDNYYQPERELIGDIa 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 316 ------NKIMPQLELSQDISSWVhhsEGLRSSFKWRYDHPGDL---IFAPL-LLKQLSDMMPASAMVSTDVGQHQMWAAQ 385
Cdd:PRK08617 321 atldllAEKLDGLSLSPQSLEIL---EELRAQLEELAERPARLeegAVHPLrIIRALQDIVTDDTTVTVDVGSHYIWMAR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 386 HIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQW 465
Cdd:PRK08617 398 YFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIVHIIWNDGHYNMVEFQ 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425475 466 QSLFFdGRHSETILDDnPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVW 532
Cdd:PRK08617 478 EEMKY-GRSSGVDFGP-VDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIK 542
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-533 |
8.13e-78 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 255.14 E-value: 8.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 4 AELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGLA 83
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 84 DAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRpGPVIVDIAKDVQL 163
Cdd:PRK06457 85 DAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDILR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 164 AESPVKilPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQlaKATDAVREFLRLNPMPAVSTLKGLGTIERDDP 243
Cdd:PRK06457 164 KSSEYK--GSKNTEVGKVKYSIDFSRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKIGAPIIYTLNGKGILPDLDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 244 HYLGMLGMHGTKAANLVVQESDLLIVVGARFddrvtgKLDTFAPH-AKVIHIDIDAAEFSKLRLANAPIRGDIN---KIM 319
Cdd:PRK06457 240 KVMGGIGLLGTKPSIEAMDKADLLIMLGTSF------PYVNFLNKsAKVIQVDIDNSNIGKRLDVDLSYPIPVAeflNID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 320 PQ-------LELSQDISSWVHHSEGLRSSfkwrYDHPgdlIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDP 392
Cdd:PRK06457 314 IEeksdkfyEELKGKKEDWLDSISKQENS----LDKP---MKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 393 QNFITSAGLGTMGFGLPAAMGAS-VGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFfd 471
Cdd:PRK06457 387 QTFIFSAWLGSMGIGVPGSVGASfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVM-- 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040425475 472 gRHSETILD-DNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWP 533
Cdd:PRK06457 465 -GYPEWGVDlYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMP 526
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-528 |
3.05e-72 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 241.44 E-value: 3.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:PRK07525 6 MTPSEAFVETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRpGPVIVDIAKD 160
Cdd:PRK07525 86 AVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKILP--EFTPPAIPVvttDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFL-RLNPmPAVSTLKGLGT 237
Cdd:PRK07525 165 YFYGVIDVEIPQpvRLERGAGGE---QSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAeRLDA-PVACGYLHNDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 238 IERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDdrVTGKL-----DTFAPHAKVIHIDIDAAEFSKLRLANAPIR 312
Cdd:PRK07525 241 FPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLpqygiDYWPKDAKIIQVDINPDRIGLTKKVSVGIC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 313 GDINKIMPQL-----------------------ELS---QDISSWVHH--SEGLRSSFKWRYDHPgDLIFAPLLLKQLSD 364
Cdd:PRK07525 319 GDAKAVARELlarlaerlagdagreerkaliaaEKSaweQELSSWDHEddDPGTDWNEEARARKP-DYMHPRQALREIQK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 365 MMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKR 444
Cdd:PRK07525 398 ALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 445 RQIPVKMVLLNNsrlgmvRQW------QSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLES--- 515
Cdd:PRK07525 478 HNWPVTAVVFRN------YQWgaekknQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAqne 551
|
570
....*....|....
gi 1040425475 516 -KTAyLLHVLIDEE 528
Cdd:PRK07525 552 gKTT-VIEIMCNQE 564
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
1-516 |
7.22e-72 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 240.15 E-value: 7.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:TIGR03457 2 MTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRpGPVIVDIAKD 160
Cdd:TIGR03457 82 AIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKIlPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:TIGR03457 161 YFYGEIDVEI-PRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLGMLGMHGTKAANLVVQESDLLIVVGAR---FDDRVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDIN- 316
Cdd:TIGR03457 240 SHPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKVTVGICGDAKa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 ---KIMPQLELS---------------------QDISSWVHhsEGLRSSFKWRYDH---PGDLIFAPLLLKQLSDMMPAS 369
Cdd:TIGR03457 320 aaaEILQRLAGKagdanraerkakiqaersaweQELSEMTH--ERDPFSLDMIVEQrqeEGNWLHPRQVLRELEKAMPED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 370 AMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPV 449
Cdd:TIGR03457 398 AIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIPV 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425475 450 KMVLLNNSRLGMVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESK 516
Cdd:TIGR03457 478 TAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQ 544
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-528 |
5.79e-66 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 224.25 E-value: 5.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFG--YPGGAIMpiydALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNL 78
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSALFL----AAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIA 158
Cdd:PRK06112 90 VAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 159 KDVQLAESPvkilpeftPPAIP-------------VVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNP 225
Cdd:PRK06112 170 ADLLTAAAA--------APAAPrsnslghfpldrtVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 226 MPAVSTLKGLGTIERDDPHYLGMLG-MHGTKAANL----VVQESDLLIVVGARFDDRVTGKLDTFAPHAKVIHIDIDAAE 300
Cdd:PRK06112 242 LPVATTNMGKGAVDETHPLSLGVVGsLMGPRSPGRhlrdLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 301 ----FSKLRLAnapirGDINKIMPQLELS---QDISSWVHHSEGLRSSF-KWRYDHPGDLI------FAPL----LLKQL 362
Cdd:PRK06112 322 vgrnYEALRLV-----GDARLTLAALTDAlrgRDLAARAGRRAALEPAIaAGREAHREDSApvalsdASPIrperIMAEL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 363 SDMMPASAMVSTDVGQHQMWAAQHIQPRDP-QNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGT 441
Cdd:PRK06112 397 QAVLTGDTIVVADASYSSIWVANFLTARRAgMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELET 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 442 LKRRQIPVKMVLLNNSRLGMVRQWQSLFFdGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLL 521
Cdd:PRK06112 477 ARRMGVPVTIVVLNNGILGFQKHAETVKF-GTHTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLI 555
|
....*..
gi 1040425475 522 HVLIDEE 528
Cdd:PRK06112 556 EVITDPS 562
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
375-523 |
2.42e-64 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 206.67 E-value: 2.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 375 DVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLL 454
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040425475 455 NNSRLGMVRQWQSLFFDGRHSET--ILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHV 523
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPsgKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
3-526 |
2.71e-61 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 212.00 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALYD--GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:TIGR02720 1 ASAAVLKVLEAWGVDHIYGIPGGSFNSTMDALSAerDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAgRPGPVIVDIAKD 160
Cdd:TIGR02720 81 GLYDAKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKI-----LPEFTpPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQlaKATDAVREFLRLNPMPAVSTLKGL 235
Cdd:TIGR02720 160 FGWQEIPDNDyyassVSYQT-PLLPAPDVEAVTRAVQTLKAAERPVIYYGIGAR--KAGEELEALSEKLKIPLISTGLAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 236 GTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDdrVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDI 315
Cdd:TIGR02720 237 GIIEDRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 316 NKIMPQ-LELSQDISSWVHHSEGLRSSFKWR--YDHPGDLIFAPLLLKQLSDMM----PASAMVSTDVGQHQMWAAQHIQ 388
Cdd:TIGR02720 315 KKALAAiLAQVEPRESTPWWQANVANVKNWRayLASLEDKTEGPLQAYQVYRAInkiaEDDAIYSIDVGDININSNRHLK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 389 PRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQsl 468
Cdd:TIGR02720 395 MTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQ-- 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 469 ffDGRHSETILDD--NPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYllHVLID 526
Cdd:TIGR02720 473 --EDTNQPLIGVDfnDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAKAIKQGK--PVLID 528
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
4-533 |
3.72e-61 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 211.39 E-value: 3.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 4 AELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGL 82
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRrMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 83 ADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAfIVAKAGRPGPVIVDIAKDVQ 162
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIA-MRKAILNRGVAVVVLPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 163 LAESPVKILPEFTPPAIPVVTTDA--IEQAQYFLSQATRPVLYVGGGVqlAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK09124 165 LKPAPERATPHWYHAPQPVVTPAEeeLRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRvtgklDTFAPHAKVIHIDIDAAEF---SKLRLAnapIRGD--- 314
Cdd:PRK09124 243 DNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLgrrSPVDLG---LVGDvka 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 315 -INKIMPQLELSQDISswvHHSEGLRSSFKWRYD--------HPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQ 385
Cdd:PRK09124 315 tLAALLPLLEEKTDRK---FLDKALEHYRKARKGlddlavpsDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 386 HIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQW 465
Cdd:PRK09124 392 YLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAME 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040425475 466 QSlffdgrhSETILDD-----NPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDEEENVWP 533
Cdd:PRK09124 472 MK-------AGGYLTDgtdlhNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMP 537
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
4-526 |
7.54e-60 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 207.92 E-value: 7.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 4 AELVVSALKQQGIETVFGYPGGAIMPIYDAL-YDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGL 82
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVrRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 83 ADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDlAPTLAEAFIVAKAGRPGPVIVDIAKDVQ 162
Cdd:PRK06546 86 YDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQ-APRVLHSAIQHAVAGGGVSVVTLPGDIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 163 LAESPVKILPEFTPPAIPVVTTDAIEQAQY--FLSQATRPVLYVGGGVqlAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK06546 165 DEPAPEGFAPSVISPRRPTVVPDPAEVRALadAINEAKKVTLFAGAGV--RGAHAEVLALAEKIKAPVGHSLRGKEWIQY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFddrvtgKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGD----IN 316
Cdd:PRK06546 243 DNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDvaetIR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 KIMPQLE------------------LSQDISSWVHHSEglrssfKWRYDHPGdliFAPLLLKQLSDmmpASAMVSTDVGQ 378
Cdd:PRK06546 317 ALLPLVKektdrrfldrmlkkharkLEKVVGAYTRKVE------KHTPIHPE---YVASILDELAA---DDAVFTVDTGM 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 379 HQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSR 458
Cdd:PRK06546 385 CNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNST 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425475 459 LGMVRqwQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLID 526
Cdd:PRK06546 465 LGMVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
3-533 |
6.45e-59 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 204.57 E-value: 6.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGL 82
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 83 ADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKDVQ 162
Cdd:PRK05858 87 AAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 163 LAESPVKILPEFTP--PAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK05858 167 FSMADDDGRPGALTelPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLgmlgmhgTKAANLVVQESDLLIVVGARFDDRVTgkLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINKIMP 320
Cdd:PRK05858 247 DHPLAF-------SRARGKALGEADVVLVVGVPMDFRLG--FGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 321 QL----ELSQDISSWVhhsEGLRSSFKWRYDHPGDLIFA---PL----LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQP 389
Cdd:PRK05858 318 ALagagGDRTDHQGWI---EELRTAETAARARDAAELADdrdPIhpmrVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 390 RDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQ-WQSL 468
Cdd:PRK05858 395 YRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHpMEAL 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425475 469 F-FDgrhseTILDDNPD--FVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLIDeEENVWP 533
Cdd:PRK05858 475 YgYD-----VAADLRPGtrYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTD-PSVAYP 536
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-523 |
1.13e-57 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 200.97 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 4 AELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGLA 83
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 84 DAFMDSIPLVAITGQVASSHIGTD--AFQEM-DVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:PRK07524 85 QAYADSIPMLVISSVNRRASLGKGrgKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 161 VQLAESPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVqlAKATDAVREFLRLNPMPAVSTLKGLGTIER 240
Cdd:PRK07524 165 VLAAPADHLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGA--LAAAAALRALAERLDAPVALTINAKGLLPA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 241 DDPHYLGmlGMHGTKAANLVVQESDLLIVVG---ARFDDRVTGKlDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINK 317
Cdd:PRK07524 243 GHPLLLG--ASQSLPAVRALIAEADVVLAVGtelGETDYDVYFD-GGFPLPGELIRIDIDPDQLARNYPPALALVGDARA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 318 IM-------PQLELSQDISSwvHHSEGLRSSFkwRYDHPGDLIFAPLLLKQLSDMMPASAMV--STDV---GQHqmwAAQ 385
Cdd:PRK07524 320 ALeallarlPGQAAAADWGA--ARVAALRQAL--RAEWDPLTAAQVALLDTILAALPDAIFVgdSTQPvyaGNL---YFD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 386 HIQPRdpQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQw 465
Cdd:PRK07524 393 ADAPR--RWFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR- 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 466 qslFFDGRHSETILDD--NPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHV 523
Cdd:PRK07524 470 ---YMVARDIEPVGVDpyTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
5-159 |
1.55e-57 |
|
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: 188.89 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 5 ELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGLAD 84
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040425475 85 AFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
3-523 |
5.02e-57 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 199.45 E-value: 5.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTG 81
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRrGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 82 LADAFMDSIPLVAITGQVASSHIGTDA--FQEM-DVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIA 158
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 159 KDVQLAESPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGVqlAKATDAVREFLRLNpMPAVSTLKGLGTI 238
Cdd:PRK07064 165 IDIQAAEIELPDDLAPVHVAVPEPDAAAVAELAERLAAARRPLLWLGGGA--RHAGAEVKRLVDLG-FGVVTSTQGRGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 239 ERDDPHYLGMLgmHGTKAANLVVQESDLLIVVGARFDDRVTGK--LDTFAPHakvIHIDIDAAEFSKLRLANAPIRGDIN 316
Cdd:PRK07064 242 PEDHPASLGAF--NNSAAVEALYKTCDLLLVVGSRLRGNETLKysLALPRPL---IRVDADAAADGRGYPNDLFVHGDAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 317 KIMPQLelsqdisswvhhSEGLRSSFKWRYDHPGDLIFA---------------PLLLKQLSDMMPASAMVSTDVG-QHQ 380
Cdd:PRK07064 317 RVLARL------------ADRLEGRLSVDPAFAADLRAAreaavadlrkglgpyAKLVDALRAALPRDGNWVRDVTiSNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 381 MWAAQHIQPRDPQNFITSAGlGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLG 460
Cdd:PRK07064 385 TWGNRLLPIFEPRANVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1040425475 461 MVRQWQSLFFDGRHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHV 523
Cdd:PRK07064 464 VIRNIQDAQYGGRRYYVEL-HTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEV 525
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
358-525 |
4.08e-52 |
|
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: 175.14 E-value: 4.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 358 LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQ 437
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 438 ELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKT 517
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDL-SNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 1040425475 518 AYLLHVLI 525
Cdd:cd00568 161 PALIEVKT 168
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
187-322 |
1.91e-50 |
|
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: 169.67 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 187 IEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVSTLKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDL 266
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1040425475 267 LIVVGARFDD-RVTGKLDTFAPHAKVIHIDIDAAEFSKLRLANAPIRGDINKIMPQL 322
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
3-167 |
4.85e-50 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 169.72 E-value: 4.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTG 81
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 82 LADAFMDSIPLVAITGQVASSHIGTDAFQ-EMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAKD 160
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*..
gi 1040425475 161 VQLAESP 167
Cdd:pfam02776 161 VLLEEVD 167
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
3-527 |
6.14e-47 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 172.48 E-value: 6.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 3 GAELVVSALKQQGIETVFGYPGgaiMPIYD--ALYDG-GVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAeGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGqvaSS--HIgTDA----FQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPV 153
Cdd:PRK09259 89 TALANATTNCFPMIMISG---SSerEI-VDLqqgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 154 IVDI-AK------DVQLAESPVKILPEFTPPAIPvvTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPM 226
Cdd:PRK09259 165 YLDLpAKvlaqtmDADEALTSLVKVVDPAPAQLP--APEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 227 PAV--STLKGLgtIERDDPHYLGmlgmhgtKAANLVVQESDLLIVVGARFDDRVT-GKLDTFAPHAKVIHIDIDAAEFSK 303
Cdd:PRK09259 243 PFLpmSMAKGL--LPDTHPQSAA-------AARSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 304 LRLANAPIRGDINKIMPQLeLSQDISSWVHHSEGLRSSFKWRYDHpGDLIFAPLLLKQLSDMMPASAM-VSTDV------ 376
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQAL-LAGLKQNTFKAPAEWLDALAERKEK-NAAKMAEKLSTDTQPMNFYNALgAIRDVlkenpd 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 377 ------GQHQMWAAQHI----QPRdpqNFITSAGLGTMGFGLPAAMGASV--GRPddqSILISGDGSFMMNVQELGTLKR 444
Cdd:PRK09259 392 iylvneGANTLDLARNIidmyKPR---HRLDCGTWGVMGIGMGYAIAAAVetGKP---VVAIEGDSAFGFSGMEVETICR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 445 RQIPVKMVLLNNSrlGMVR-QWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHV 523
Cdd:PRK09259 466 YNLPVTVVIFNNG--GIYRgDDVNLSGAGDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINV 543
|
....
gi 1040425475 524 LIDE 527
Cdd:PRK09259 544 VIDP 547
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
1-528 |
2.83e-45 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 167.68 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPggaIMPIYDALYDGGVEHILCRHEQGAAMAAIGMARAT--QDVAVCMATSGPGATNL 78
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATsgERVGVFAVQYGPGAENA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQV--ASSHIGTDaFQEMDVIGmslSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVD 156
Cdd:PRK06154 97 FGGVAQAYGDSVPVLFLPTGYprGSTDVAPN-FESLRNYR---HITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 157 IAKDV---QLAESPVkilpEFTPP--AIPVVTTDAIEQAQYFLSQATRPVLYVGGGVQLAKATDAVREFLRLNPMPAVST 231
Cdd:PRK06154 173 LPVDVlaeELDELPL----DHRPSrrSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 232 LKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFDDRVTGkldTFAPHAK-VIHIDIDAAEFSKLRLANAP 310
Cdd:PRK06154 249 LNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYG---LPMPEGKtIIHSTLDDADLNKDYPIDHG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 311 IRGDINKIMPQL---------ELSQDISSWVHHSEGLRSSF--KWrydHP----GDLIFAPllLKQLSDMM----PASAM 371
Cdd:PRK06154 326 LVGDAALVLKQMieelrrrvgPDRGRAQQVAAEIEAVRAAWlaKW---MPkltsDSTPINP--YRVVWELQhavdIKTVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 372 VSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKM 451
Cdd:PRK06154 401 ITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 452 VLLNNSRLGM--------VRQWQSLFFDGrhsetilddnpDFVMLAKAFDIPGKTITRKEEVEPALKEML---ESKTAYL 520
Cdd:PRK06154 481 ILLNNFSMGGydkvmpvsTTKYRATDISG-----------DYAAIARALGGYGERVEDPEMLVPALLRALrkvKEGTPAL 549
|
....*...
gi 1040425475 521 LHVLIDEE 528
Cdd:PRK06154 550 LEVITSEE 557
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
4-546 |
5.07e-44 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 164.70 E-value: 5.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 4 AELVVSALKQQGIETVFGYPGGAIMPIYDAL--YDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTG 81
Cdd:PRK08273 6 ADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 82 LADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMsLSCTKHSYL--VTDIEDLAPTLAEAFIVAKAGRpGPVIVDIAK 159
Cdd:PRK08273 86 LYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSL-FKDVAGAFVqmVTVPEQLRHLVDRAVRTALAER-TVTAVILPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESP--------VKILPEFTPPAIpVVTTDAIEQAQYFLSQATRPVLYVGGGVQlaKATDAVREFLRLNPMPAVST 231
Cdd:PRK08273 164 DVQELEYEppphahgtVHSGVGYTRPRV-VPYDEDLRRAAEVLNAGRKVAILVGAGAL--GATDEVIAVAERLGAGVAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 232 LKGLGTIERDDPHYLGMLGMHGTKAANLVVQESDLLIVVGARFddrvtgKLDTFAP---HAKVIHIDIDAAEFSkLRLan 308
Cdd:PRK08273 241 LLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFLPkegQARGVQIDIDGRMLG-LRY-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 309 aPIR----GD----INKIMPQLELSQD------ISSWVHHSeglRSSFKWRYDHPGDLIFAPLLLKQLSDMMPASAMVST 374
Cdd:PRK08273 312 -PMEvnlvGDaaetLRALLPLLERKKDrswrerIEKWVARW---WETLEARAMVPADPVNPQRVFWELSPRLPDNAILTA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 375 DVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMN-VQELGTLKRR----QIP- 448
Cdd:PRK08273 388 DSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKYwrqwSDPr 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 449 -VKMVlLNNSRLGMVrQWQSLFFDG----RHSETIlddnPDF--VMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLL 521
Cdd:PRK08273 468 lIVLV-LNNRDLNQV-TWEQRVMEGdpkfEASQDL----PDVpyARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVL 541
|
570 580
....*....|....*....|....*
gi 1040425475 522 HVLIDeeENVwPLVPPGASNSEMLE 546
Cdd:PRK08273 542 EVKTD--PNV-PPLPPHITLEQAKA 563
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
358-529 |
5.62e-43 |
|
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: 151.14 E-value: 5.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 358 LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQ 437
Cdd:cd02014 7 VAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGFAMLMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 438 ELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSETIldDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKT 517
Cdd:cd02014 87 DLITAVKYNLPVIVVVFNNSDLGFIKWEQEVMGQPEFGVDL--PNPDFAKIAEAMGIKGIRVEDPDELEAALDEALAADG 164
|
170
....*....|..
gi 1040425475 518 AYLLHVLIDEEE 529
Cdd:cd02014 165 PVVIDVVTDPNE 176
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
2-165 |
2.96e-39 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 140.76 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 2 KGAELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVT 80
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 81 GLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRpGPVIVDIAKD 160
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....*
gi 1040425475 161 VQLAE 165
Cdd:cd07039 160 VQDAP 164
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
358-531 |
5.01e-36 |
|
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: 132.41 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 358 LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQ 437
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 438 ELGTLKRRQIPVKMVLLNNSRLGMVRqWQSLFFDGRHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKT 517
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDF-GNPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
170
....*....|....
gi 1040425475 518 AYLLHVLIDEEENV 531
Cdd:cd02010 162 VHVIDCPVDYSENI 175
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
4-456 |
4.69e-35 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 138.37 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 4 AELVVSALKQQGIETVFGYPGGAIMPIYDALY-DGGVEHILCRHEQGaamaaigmaratqdvAVCMA------------- 69
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEaHPGIRWVGCCNELN---------------AGYAAdgyarvnglgalv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 70 -TSGPGATNLVTGLADAFMDSIPLVAITGQVASS---------H-IGT---DAFQEM--DVigmslscTKHSYLVTdiED 133
Cdd:COG3961 73 tTYGVGELSAINGIAGAYAERVPVVHIVGAPGTRaqrrgpllhHtLGDgdfDHFLRMfeEV-------TVAQAVLT--PE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 134 LAPT-----LAEAFIVAKagrpgPVIVDIAKDV--QLAESPVKILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGG 206
Cdd:COG3961 144 NAAAeidrvLAAALREKR-----PVYIELPRDVadAPIEPPEAPLPLPPPASDPAALAAAVAAAAERLAKAKRPVILAGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 207 GVQLAKATDAVREFLRLNPMPAVSTLKGLGTIERDDPHYLGM----LGMHGTKAAnlvVQESDLLIVVGARFDDRVTG-- 280
Cdd:COG3961 219 EVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQFIGTyagaASSPEVREY---VENADCVLCLGVVFTDTNTGgf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 281 --KLDTfaphAKVIHID-----IDAAEFSKLRLANApIRGdinkimpqleLSQDISSWVHHSEGLRSSFKWRYDHPGDLI 353
Cdd:COG3961 296 taQLDP----ERTIDIQpdsvrVGGHIYPGVSLADF-LEA----------LAELLKKRSAPLPAPAPPPPPPPAAPDAPL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 354 FAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQnFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFM 433
Cdd:COG3961 361 TQDRLWQRLQAFLDPGDIVVADTGTSLFGAADLRLPEGAT-FIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQ 439
|
490 500
....*....|....*....|...
gi 1040425475 434 MNVQELGTLKRRQIPVKMVLLNN 456
Cdd:COG3961 440 LTAQELSTMLRYGLKPIIFVLNN 462
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
11-526 |
2.78e-33 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 133.16 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 11 LKQQGIETVFGYPGGAIMPIYDALYDGgVEHILCRHEQgaamaaigmaratqdVAVCMA------TSGPGATNL------ 78
Cdd:PRK07092 22 LRRFGITTVFGNPGSTELPFLRDFPDD-FRYVLGLQEA---------------VVVGMAdgyaqaTGNAAFVNLhsaagv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 79 ---VTGLADAFMDSIPLVAITGQVASSHIGTDAF-QEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVI 154
Cdd:PRK07092 86 gnaMGNLFTAFKNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 155 VDIAKDvqlaespvkilpEFTPPAIPV----VTT------DAIEQAQYFLSQATRPVLYVGGGVQLAKATD-AVREFLRL 223
Cdd:PRK07092 166 VSIPYD------------DWDQPAEPLpartVSSavrpdpAALARLGDALDAARRPALVVGPAVDRAGAWDdAVRLAERH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 224 NpMPA-VSTLKGLGTIERDDPHYLGML--GMHGTKAAnlvVQESDLLIVVGAR-FDDRVTGKLDTFAPHAKVIHIDIDAA 299
Cdd:PRK07092 234 R-APVwVAPMSGRCSFPEDHPLFAGFLpaSREKISAL---LDGHDLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDDPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 300 EfsklrLANAPIrGD--INKIMPQLELSQDISSwvhhsEGLRSSFKWRYDHP-----GDLIFAPLLLKQLSDMMPASAMV 372
Cdd:PRK07092 310 E-----AAWAPM-GDaiVGDIRLALRDLLALLP-----PSARPAPPARPMPPpapapGEPLSVAFVLQTLAALRPADAIV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 373 STDVGQHQ--MWaaQHIQPRDPQNFITSAGlGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVK 450
Cdd:PRK07092 379 VEEAPSTRpaMQ--EHLPMRRQGSFYTMAS-GGLGYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVT 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1040425475 451 MVLLNNSRLGMVRqWQSLFFDGRHSETIldDNP--DFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLID 526
Cdd:PRK07092 456 FVILNNGRYGALR-WFAPVFGVRDVPGL--DLPglDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-526 |
1.27e-31 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 128.96 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALYDGGVEH------ILCRHEqgaamaaigmaratqDVAVCMA----- 69
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpefVICPHE---------------IVAISMAhgyal 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 70 TSG----------PGATNLVTGLADAFMDSIPLVAITGQ---VASSHIGT-DAF----QEM-DVIGMSLSCTKHSYLVTD 130
Cdd:PRK08327 72 VTGkpqavmvhvdVGTANALGGVHNAARSRIPVLVFAGRspyTEEGELGSrNTRihwtQEMrDQGGLVREYVKWDYEIRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 131 IEDLAPTLAEAFIVAKAGRPGPVIVDIAKDVQLAESPVKILPE--FTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGV 208
Cdd:PRK08327 152 GDQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADAgrQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 209 QLAKATDAVREFLRLNPMPAVSTLKGLGTIERDDPhylgmlgMHGTKAANLVVQESDLLIVVGArfDDRVTGKLDTFAPH 288
Cdd:PRK08327 232 RTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHP-------LHLGPDPRADLAEADLVLVVDS--DVPWIPKKIRPDAD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 289 AKVIHIDIDAAeFSKLRL----ANAPIRGDINKIMPQLE-------------LSQDISSWVHHSEGLRSSFKWRYDHPGD 351
Cdd:PRK08327 303 ARVIQIDVDPL-KSRIPLwgfpCDLCIQADTSTALDQLEerlkslasaerrrARRRRAAVRELRIRQEAAKRAEIERLKD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 352 L--IFAPLLLKQLSDMMPASAMVSTDVGQHQmwaaQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGD 429
Cdd:PRK08327 382 RgpITPAYLSYCLGEVADEYDAIVTEYPFVP----RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 430 GSFMMNVQE--LGTLKRRQIPVKMVLLNNSRLGMVRQ-WQSLFFDG------RHSETILDDNPDFVMLAKAFDIPGKTIT 500
Cdd:PRK08327 458 GSFIFGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEaVLEVYPEGyaarkgTFPGTDFDPRPDFAKIAEAFGGYGERVE 537
|
570 580 590
....*....|....*....|....*....|
gi 1040425475 501 RKEEVEPALKEMLE----SKTAYLLHVLID 526
Cdd:PRK08327 538 DPEELKGALRRALAavrkGRRSAVLDVIVD 567
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
353-525 |
3.46e-31 |
|
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: 119.24 E-value: 3.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 353 IFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGlGTMGFGLPAAMGASVGRPDDQSILISGDGSF 432
Cdd:cd02002 1 LTPEYLAAALAAALPEDAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 433 MMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSE------TILDDNPDFVMLAKAFDIPGKTITRKEEVE 506
Cdd:cd02002 80 MYTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGEnapdglDLLDPGIDFAAIAKAFGVEAERVETPEELD 159
|
170
....*....|....*....
gi 1040425475 507 PALKEMLESKTAYLLHVLI 525
Cdd:cd02002 160 EALREALAEGGPALIEVVV 178
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
6-159 |
1.35e-26 |
|
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: 105.50 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 6 LVVSALKQQGIETVFGYPGGAIMPIYDALYDG-GVEHILCRHEQGAAMAAIGMARATQdVAVCMATSGPGATNLVTGLAD 84
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGG-PPVVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1040425475 85 AFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGrPGPVIVDIAK 159
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
359-528 |
1.97e-26 |
|
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: 106.44 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 359 LKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQE 438
Cdd:cd02013 10 LRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMME 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 439 LGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSETILdDNPDFVMLAKAFDIPGKTITRKEEVEPALKE----MLE 514
Cdd:cd02013 90 IMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTEL-ESESFAKIAEACGAKGITVDKPEDVGPALQKaiamMAE 168
|
170
....*....|....
gi 1040425475 515 SKTAyLLHVLIDEE 528
Cdd:cd02013 169 GKTT-VIEIVCDQE 181
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
358-526 |
1.25e-23 |
|
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: 97.60 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 358 LLKQLSDMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQ 437
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 438 ELGTLKRRQIPVKMVLLNNSRLGMVRQWQSLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKEMLESKT 517
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGK 163
|
....*....
gi 1040425475 518 AYLLHVLID 526
Cdd:cd02004 164 PALINVIID 172
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
1-525 |
5.25e-19 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 90.29 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDALyDG--GVEHILCRHEqgaamaaigmaratqdvAVCM---------- 68
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAAL-DRvpGMRCVLGLFE-----------------GVATgaadgyarma 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 69 ----AT---SGPGATNLVTGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGM--SLSCTKHSylVTDIEDLAPTLA 139
Cdd:PRK07586 63 gkpaATllhLGPGLANGLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEALarPVSGWVRR--SESAADVAADAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 140 EAfIVAKAGRPGPVIVDI-AKDVQLAESPVkILPEFTPPAIPVVTTDAIEQAQYFLSQATRPVLYVGGGV---------- 208
Cdd:PRK07586 141 AA-VAAARGAPGQVATLIlPADVAWSEGGP-PAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRAlrerglaaaa 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 209 QLAKATDAvreflRLNPMPAVSTLK---GLGTIERddPHYLGmlgmhgtKAANLVVQESDLLIVVGARfdDRVT-----G 280
Cdd:PRK07586 219 RIAAATGA-----RLLAETFPARMErgaGRPAVER--LPYFA-------EQALAQLAGVRHLVLVGAK--APVAffaypG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 281 KLDTFAPHAKVIHIDIDAAEFSKLRL-----------ANAPIRGDINKIMPQLELSQDisSWvhhseglrssfkwrydhp 349
Cdd:PRK07586 283 KPSRLVPEGCEVHTLAGPGEDAAAALealadalgakpAAPPLAAPARPPLPTGALTPE--AI------------------ 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 350 GDLIFAplllkqlsdMMPASAMVSTDVGQHQMWAAQHIQPRDPQNFITSAGlGTMGFGLPAAMGASVGRPDDQSILISGD 429
Cdd:PRK07586 343 AQVIAA---------LLPENAIVVDESITSGRGFFPATAGAAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGD 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 430 GSFMMNVQELGTLKRRQIPVKMVLLNN----------SRLGMVRqwqslffDGRHSETILD-DNP--DFVMLAKAFDIPG 496
Cdd:PRK07586 413 GSAMYTIQALWTQARENLDVTTVIFANrayailrgelARVGAGN-------PGPRALDMLDlDDPdlDWVALAEGMGVPA 485
|
570 580
....*....|....*....|....*....
gi 1040425475 497 KTITRKEEVEPALKEMLESKTAYLLHVLI 525
Cdd:PRK07586 486 RRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
374-531 |
1.72e-17 |
|
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: 81.17 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 374 TDVGQHQMWAAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVL 453
Cdd:cd02006 29 TTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIPYIHVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 454 LNNSRLGMVRQWQ---------SLFFDGRHSETILDDNPDFVMLAKAFDIPGKTITRKEEVEPALKE----MLESKTAYL 520
Cdd:cd02006 109 VNNAYLGLIRQAQrafdmdyqvNLAFENINSSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQakklMAEHRVPVV 188
|
170
....*....|.
gi 1040425475 521 LHVLIDEEENV 531
Cdd:cd02006 189 VEAILERVTNI 199
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
390-529 |
3.70e-17 |
|
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: 79.50 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 390 RDPQN--FITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSRLGMVRQ--- 464
Cdd:cd02005 36 KLPKGtrFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAihg 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 465 WQSLFFDgrhsetIldDNPDFVMLAKAF----DIPGKTITRKEEVEPALKEMLE-SKTAYLLHVLIDEEE 529
Cdd:cd02005 116 PEASYND------I--ANWNYTKLPEVFggggGGLSFRVKTEGELDEALKDALFnRDKLSLIEVILPKDD 177
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-525 |
2.11e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 75.68 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 1 MKGAELVVSALKQQGIETVFGYPGGAIMPIYDAL-YDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLV 79
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALdRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 80 TGLADAFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLVTDIEDLAPTLAEAFIVAKAGRPGPVIVDIAK 159
Cdd:PRK12474 85 ANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 160 DVQLAESPVKILPEFTPPAIPVVtTDAIEQAQYFLSQATRPVLYVGGGVQLA---KATDAVR-----EFLRLNPMPAVST 231
Cdd:PRK12474 165 DVAWNEAAYAAQPLRGIGPAPVA-AETVERIAALLRNGKKSALLLRGSALRGaplEAAGRIQaktgvRLYCDTFAPRIER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 232 LKGLGTIERddphyLGMLGMHGTKaanlVVQESDLLIVVGARfddrvtGKLDTFAPHAKVIHIDIDAAEFSKLrlanapi 311
Cdd:PRK12474 244 GAGRVPIER-----IPYFHEQITA----FLKDVEQLVLVGAK------PPVSFFAYPGKPSWGAPPGCEIVYL------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 312 rgdinkIMPQLELSQDIsSWVHHSEGLRSSFKWRY-----DHPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHQMWAAQH 386
Cdd:PRK12474 302 ------AQPDEDLAQAL-QDLADAVDAPAEPAARTplalpALPKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFDMS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 387 IQPRDPQNFITSAGlGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNsrlgmvRQWQ 466
Cdd:PRK12474 375 YDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFAN------RSYA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1040425475 467 SLFFD---------GRHSETILD-DNP--DFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLI 525
Cdd:PRK12474 448 ILNGElqrvgaqgaGRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
379-526 |
5.75e-12 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 65.02 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 379 HQMWaaqhiQPRDPQNFITSAGLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSR 458
Cdd:cd02003 30 HKLW-----RARTPGGYHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 459 LGMVRQWQ---------SLFFDGRHSETILDDNP---DFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLID 526
Cdd:cd02003 105 FGCINNLQestgsgsfgTEFRDRDQESGQLDGALlpvDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
64-517 |
2.33e-09 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 60.10 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 64 VAVCMATSGPGATNLVTGLADAFMDSIPLVAITGQVASSHIGTD-----------------AFQEmdvigmslsCTKHSY 126
Cdd:PLN02573 79 VGACVVTFTVGGLSVLNAIAGAYSENLPVICIVGGPNSNDYGTNrilhhtiglpdfsqelrCFQT---------VTCYQA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 127 LVTDIEDlAPTLAEAFIVAKAGRPGPVIVDIAkdVQLAESPvkiLPEFTPPAIPVVTTD----------AIEQAQYFLSQ 196
Cdd:PLN02573 150 VINNLED-AHELIDTAISTALKESKPVYISVS--CNLAAIP---HPTFSREPVPFFLTPrlsnkmsleaAVEAAAEFLNK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 197 ATRPVLYVGGGVQLAKATDAVREFLR-----LNPMPAVstlKGLgtIERDDPHYLGML-GMHGTKAANLVVQESDLLIVV 270
Cdd:PLN02573 224 AVKPVLVGGPKLRVAKACKAFVELADasgypVAVMPSA---KGL--VPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 271 GARFDDRVTGKLDTFAPHAKVIHIDIDaaefsKLRLANAPIRGDInkIMPQL--ELSQDISS-----------WVHHSEG 337
Cdd:PLN02573 299 GPIFNDYSSVGYSLLLKKEKAIIVQPD-----RVTIGNGPAFGCV--LMKDFleALAKRVKKnttayenykriFVPEGEP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 338 LRSSfkwrydhPGDLIFAPLLLKQLSDMMPASAMVSTDVGQHqmW-AAQHIQPRDPQNFITSAGLGTMGFGLPAAMGASV 416
Cdd:PLN02573 372 LKSE-------PGEPLRVNVLFKHIQKMLSGDTAVIAETGDS--WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQ 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 417 GRPDDQSILISGDGSFMMNVQELGTLKRRQIPVKMVLLNNSrlgmvrqwqslffdGRHSETILDDNP-------DFVMLA 489
Cdd:PLN02573 443 AAPDKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNG--------------GYTIEVEIHDGPynviknwNYTGLV 508
|
490 500
....*....|....*....|....*....
gi 1040425475 490 KAFDI-PGKTITRKEEVEPALKEMLESKT 517
Cdd:PLN02573 509 DAIHNgEGKCWTAKVRTEEELIEAIATAT 537
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
379-456 |
4.15e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 53.68 E-value: 4.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1040425475 379 HQMWAAQHiqprDPQNFITsagLGTMGFGLPAAMGASVGRPDDQSILISGDGSFMMNVQELGTL-KRRQIPVKMVLLNN 456
Cdd:PRK06163 41 FDLWAAGQ----RPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIaALAPKNLTIIVMDN 112
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
6-158 |
1.62e-06 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 48.26 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 6 LVVSALKQQGIETVFGYPGGAIMP-IYDALYDGGVEHILCRHEQGAAMAAIGMARATQDVAVCMATSGPGATNLVTGLAD 84
Cdd:cd07037 2 ALVEELKRLGVRDVVISPGSRSAPlALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 85 AFMDSIPLVAITGQVASSHIGTDAFQEMDVIGMSLSCTKHSYLV------TDIEDLAPTLAEAFIVAKAGRPGPVIVDIA 158
Cdd:cd07037 82 AYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLpppeddDDLWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
11-108 |
8.14e-05 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 43.25 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 11 LKQQGIETVFGYPGGAIMPIYDALYD-GGVEHILCRHE-----------QgaamaaigmaraTQDVAVCMATSGPGATNL 78
Cdd:cd07038 7 LKQLGVKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNElnagyaadgyaR------------VKGLGALVTTYGVGELSA 74
|
90 100 110
....*....|....*....|....*....|
gi 1040425475 79 VTGLADAFMDSIPLVAITGQVASSHIGTDA 108
Cdd:cd07038 75 LNGIAGAYAEHVPVVHIVGAPSTKAQASGL 104
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
411-526 |
2.95e-03 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 38.73 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040425475 411 AMGASVGRpDDQSILISGDGSFM--MNVqeLGTLKRRQIPVKMVLLNNS-----RLGMVRQWQSlFFDgRHSETILddNP 483
Cdd:cd02009 60 ALGIALAT-DKPTVLLTGDLSFLhdLNG--LLLGKQEPLNLTIVVINNNgggifSLLPQASFED-EFE-RLFGTPQ--GL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1040425475 484 DFVMLAKAFDIPGKTITRKEEVEPALKEMLESKTAYLLHVLID 526
Cdd:cd02009 133 DFEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| |
