|
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: 1233.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IQLASGELEPWFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAVEAD 240
Cdd:PRK08978 161 IQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 241 YPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPA 320
Cdd:PRK08978 241 HPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 321 LQQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGL 400
Cdd:PRK08978 321 LQQPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 401 GTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTD 480
Cdd:PRK08978 401 GTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSETDLSD 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 813120958 481 NPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS 548
Cdd:PRK08978 481 NPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS 548
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-543 |
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: 745.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEP---WFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGA 236
Cdd:COG0028 163 DVQAAEAEEEPappELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 237 VEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:COG0028 243 FPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 317 LLPAL-----QQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRP 391
Cdd:COG0028 323 VLAALlealePRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 392 ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE 471
Cdd:COG0028 403 RRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 813120958 472 RYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENvwplvPPGASNSEM 543
Cdd:COG0028 483 RYSGTDLP-NPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN-----PPGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
1-544 |
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: 718.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYnDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEPwfttvDNEATFP---------QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCT 230
Cdd:TIGR00118 161 DVTTAEIEYPY-----PEKVNLPgyrptvkghPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 231 LKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVAL 310
Cdd:TIGR00118 236 LMGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 311 QGD----LNSLLPAL--QQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQ 384
Cdd:TIGR00118 316 VGDarnvLEELLKKLfeLKERKESAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:TIGR00118 396 FYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQW 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 465 QQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:TIGR00118 476 QELFYEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEMI 555
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 686.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY----DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGAT 76
Cdd:PRK07418 19 ATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 77 NLITGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVD 156
Cdd:PRK07418 99 NLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 157 IPKDIQLASGELEPWFTTVDNEATFPQ------ADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCT 230
Cdd:PRK07418 179 IPKDVGQEEFDYVPVEPGSVKPPGYRPtvkgnpRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 231 LKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVAL 310
Cdd:PRK07418 259 LMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 311 QGDL-NSLLPALQQPLKIDAWRQSCAELRAEHAWRYDHP------GETIYAPLLLKQLSERKPaDSVVTTDVGQHQMWSA 383
Cdd:PRK07418 339 VGDVrKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPlvvppyEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQMWAA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 384 QHMTyTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK07418 418 QFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQ 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 464 WQQLFFQERYSETTLTDN-PDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSE 542
Cdd:PRK07418 497 WQESFYGERYSASNMEPGmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCYPMVPPGKSNAQ 576
|
..
gi 813120958 543 ML 544
Cdd:PRK07418 577 MV 578
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
15-544 |
0e+00 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 678.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 15 GVKTVFGYPGGAIMPVYDALY----DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLADALLDSV 90
Cdd:CHL00099 24 GVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 91 PVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKDIQLasgELEP 170
Cdd:CHL00099 104 PLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVGL---EKFD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 171 WFTTVDNEATFP-----------QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAVEA 239
Cdd:CHL00099 181 YYPPEPGNTIIKilgcrpiykptIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIFDE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 240 DYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLP 319
Cdd:CHL00099 261 DHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIVGDVKKVLQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 320 ALQQPLKID----------AWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPaDSVVTTDVGQHQMWSAQhMTYT 389
Cdd:CHL00099 341 ELLELLKNSpnlleseqtqAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDVGQHQMWAAQ-FLKC 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:CHL00099 419 KPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQAFY 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 813120958 470 QERYSETTLTDN-PDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:CHL00099 499 GERYSHSNMEEGaPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENCYPMVAPGKSNSQMI 574
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 655.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK08155 13 FTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK08155 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEPWFTTVDNEA--TFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAV 237
Cdd:PRK08155 173 DVQTAVIELEALPAPAEKDAapAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 238 EADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD---- 313
Cdd:PRK08155 253 PKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADvddv 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 LNSLLPALQQPLKiDAWRQSCAELRAEHAwrYDHPGETiyAPL----LLKQLSERKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:PRK08155 333 LAQLLPLVEAQPR-AEWHQLVADLQREFP--CPIPKAD--DPLshygLINAVAACVDDNAIITTDVGQHQMWTAQAYPLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK08155 408 RPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFY 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813120958 470 QERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK08155 488 GQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTEMI 562
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 655.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYkQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEpWFTTVDNEATFP-----QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGL 234
Cdd:PRK08527 163 DVTATLGEFE-YPKEISLKTYKPtykgnSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 235 GAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDL 314
Cdd:PRK08527 242 GVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIVGDL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 315 NSLLPAL------QQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTY 388
Cdd:PRK08527 322 KNVLKEMleelkeENPTTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQFYPF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:PRK08527 402 NYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQTFF 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 813120958 469 FQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK08527 482 YEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNMI 557
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 644.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK06048 8 MTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK06048 88 GIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IQLASGELEpWFTTVDNEATFP-----QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLG 235
Cdd:PRK06048 168 VTTAEIDFD-YPDKVELRGYKPtykgnPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMGIG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 236 AVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD-- 313
Cdd:PRK06048 247 AIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIVGDak 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 --LNSLLPALQQpLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPaDSVVTTDVGQHQMWSAQHMTYTRP 391
Cdd:PRK06048 327 qvLKSLIKYVQY-CDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKYKYP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 392 ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE 471
Cdd:PRK06048 405 RTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELFYDK 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 813120958 472 RYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEMLE 545
Cdd:PRK06048 485 RYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILD 558
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-542 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 635.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK07789 31 MTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEpWFTTVD----NEATFPQA-DVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGL 234
Cdd:PRK07789 191 DALQAQTTFS-WPPRMDlpgyRPVTKPHGkQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTLMAR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 235 GAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDL 314
Cdd:PRK07789 270 GAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPIVGDV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 315 NSLLPALQQPLK----------IDAWRQSCAELRAEHAWRYDHPGETIYAP-LLLKQLSERKPADSVVTTDVGQHQMWSA 383
Cdd:PRK07789 350 KEVIAELIAALRaehaaggkpdLTAWWAYLDGWRETYPLGYDEPSDGSLAPqYVIERLGEIAGPDAIYVAGVGQHQMWAA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK07789 430 QFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGMVRQ 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 464 WQQLFFQERYSETTLTDN----PDFLMLASAFGIPGQHITRKDQVEAALDTMLA-SEGPYLL--HVSIDELenVWPLVPP 536
Cdd:PRK07789 510 WQTLFYEERYSNTDLHTHshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAiNDRPVVIdfVVGKDAM--VWPMVAA 587
|
....*.
gi 813120958 537 GASNSE 542
Cdd:PRK07789 588 GTSNDE 593
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-544 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 630.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEPWFTTVDNEATFP--QADVEQARQ---MLEQAKKPMLYVGGGV---GMaKAVPALRKFIAVTQMPVTCTL 231
Cdd:PRK09107 171 DVQFATGTYTPPQKAPVHVSYQPkvKGDAEAITEaveLLANAKRPVIYSGGGVinsGP-EASRLLRELVELTGFPITSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK09107 250 MGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 312 GDLNSLLPALQQPLK----------IDAWRQSCAELRAEHAWRYDHPGETI---YAPLLLKQLSerKPADSVVTTDVGQH 378
Cdd:PRK09107 330 GDVGHVLEDMLRLWKargkkpdkeaLADWWGQIARWRARNSLAYTPSDDVImpqYAIQRLYELT--KGRDTYITTEVGQH 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 379 QMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRL 458
Cdd:PRK09107 408 QMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYM 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 459 GMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGA 538
Cdd:PRK09107 488 GMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPMIPSGK 567
|
....*.
gi 813120958 539 SNSEML 544
Cdd:PRK09107 568 AHNEML 573
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 622.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IQLASGELE--PWFTTVDNEATFPQA-----DVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKG 233
Cdd:PRK06276 161 VQEGELDLEkyPIPAKIDLPGYKPTTfghplQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 234 LGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK06276 241 KGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 ----LNSLLPAL--QQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSE-----RKPADSVVTTDVGQHQMWS 382
Cdd:PRK06276 321 aknvLRDLLAELmkKEIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMEvlreiDPSKNTIITTDVGQNQMWM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:PRK06276 401 AHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 463 QWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVwPLVPPGASNSE 542
Cdd:PRK06276 481 QWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPGGNLTN 559
|
..
gi 813120958 543 ML 544
Cdd:PRK06276 560 IL 561
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-543 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 606.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK07710 16 MTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IQLASGELEpwfttVDNEATFP------QADVEQARQMLE---QAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTL 231
Cdd:PRK07710 176 MVVEEGEFC-----YDVQMDLPgyqpnyEPNLLQIRKLVQavsVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 312 GD----LNSLLPALQQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK07710 331 ADakqaLQVLLQQEGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 388 YTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQL 467
Cdd:PRK07710 411 FKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEE 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 813120958 468 FFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEM 543
Cdd:PRK07710 491 FYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPGKGLHEM 566
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
3-539 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 596.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITG 81
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 82 LADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKDI 161
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 162 Q--LASGELEPWFTTVDNEATFPQ----ADVEQARQMLEQAKKPMLYVGGGVgmAKAVPALRKFIAVTQMPVTCTLKGLG 235
Cdd:PLN02470 175 QqqLAVPNWNQPMKLPGYLSRLPKppekSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGIPVASTLMGLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 236 AVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD-- 313
Cdd:PLN02470 253 AFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADvk 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 -----LNSLLPALQ-QPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PLN02470 333 lalqgLNKLLEERKaKRPDFSAWRAELDEQKEKFPLSYPTFGDAIPPQYAIQVLDELTDGNAIISTGVGQHQMWAAQWYK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 388 YTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQL 467
Cdd:PLN02470 413 YKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQWEDR 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 813120958 468 FFQERYSETTLTDN-------PDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGAS 539
Cdd:PLN02470 493 FYKANRAHTYLGDPdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIPGGGT 571
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
1-546 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 596.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IQLASgelepwFTTVDNEATF-------PQADVEQARQMLE---QAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCT 230
Cdd:PRK06725 175 VQNEK------VTSFYNEVVEipgykpePRPDSMKLREVAKaisKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVST 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 231 LKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVAL 310
Cdd:PRK06725 249 LMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 311 QGDLNSLLPALQQ---PLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK06725 329 VGDVKKALHMLLHmsiHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 388 YTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQL 467
Cdd:PRK06725 409 AKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEM 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 813120958 468 FFQERYSETTLtDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEMLEK 546
Cdd:PRK06725 489 FYENRLSESKI-GSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMIMK 566
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 546.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 2 NGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNfEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IQlasgELEPWFTTvDNEATFP------QADVEQARQMLEQ---AKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTL 231
Cdd:PRK07282 171 VS----ALETDFIY-DPEVNLPsyqptlEPNDMQIKKILKQlskAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK07282 246 LGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 312 GDLNSLLPALQQPLKIDA----WRQSCAELRAEHAWrYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK07282 326 GDAKKALQMLLAEPTVHNntekWIEKVTKDKNRVRS-YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 388 YTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQL 467
Cdd:PRK07282 405 YQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQES 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 813120958 468 FFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEgPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK07282 485 FYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDV-PMLIEVDISRKEHVLPMVPAGKSNHEML 560
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-543 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 532.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK06466 4 LSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEPWF-TTVDNEATFPQA-----DVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKG 233
Cdd:PRK06466 164 DMTNPAEKFEYEYpKKVKLRSYSPAVrghsgQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 234 LGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK06466 244 LGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIVGP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 LNSLLPALQQPLK----------IDAWRQSCAELRAEHA-WRYDHP-GETIYAPLLLKQLSERKPADSVVTTDVGQHQMW 381
Cdd:PRK06466 324 VESVLTEMLAILKeigekpdkeaLAAWWKQIDEWRGRHGlFPYDKGdGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQMF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 382 SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMV 461
Cdd:PRK06466 404 AAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGMV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 462 RQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLA-SEGPYLLHVSIDELENVWPLVPPGASN 540
Cdd:PRK06466 484 RQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIADGSM 563
|
...
gi 813120958 541 SEM 543
Cdd:PRK06466 564 RDM 566
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
1-544 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 527.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEpWFTTVDNEATFP-----QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGL 234
Cdd:PRK06965 181 DVSKTPCEYE-YPKSVEMRSYNPvtkghSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 235 GAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNA-SVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK06965 260 GAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIVGD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 LNSLLPALQQPLK----------IDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSA 383
Cdd:PRK06965 340 VKEVLKELIEQLQtaehgpdadaLAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQMWAA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK06965 420 QFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGMVRQ 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 464 WQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAAL-DTMLASEGPYLLHVSIDELENVWPLVPPGASNSE 542
Cdd:PRK06965 500 WQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALrEALRLKDRTVFLDFQTDPTENVWPMVQAGKGITE 579
|
..
gi 813120958 543 ML 544
Cdd:PRK06965 580 ML 581
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-543 |
1.40e-171 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 497.42 E-value: 1.40e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK08979 4 LSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK08979 84 TGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIqLASGELEPWF--TTVDNEATFP-----QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLK 232
Cdd:PRK08979 164 DC-LNPAILHPYEypESIKMRSYNPttsghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 233 GLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQG 312
Cdd:PRK08979 243 GLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 313 DLNSLLPALQQPLK----------IDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWS 382
Cdd:PRK08979 323 SADKVLDSMLALLDesgetndeaaIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMFA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:PRK08979 403 ALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 463 QWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYL-LHVSIDELENVWPLVPPGASNS 541
Cdd:PRK08979 483 QWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVDINVDETEHVYPMQIRGGAMN 562
|
..
gi 813120958 542 EM 543
Cdd:PRK08979 563 EM 564
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-544 |
1.03e-170 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 495.20 E-value: 1.03e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASG----------ELEPWFTTVDNEatfpQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTC 229
Cdd:PRK06882 164 DMVNPANkftyeypeevSLRSYNPTVQGH----KGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 230 TLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVA 309
Cdd:PRK06882 240 SLMGLGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 310 LQGD----LNSLLPALQQP------LKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQ 379
Cdd:PRK06882 320 IVGSaknvLEEFLSLLEEEnlaksqTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 380 MWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLG 459
Cdd:PRK06882 400 MFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 460 MVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYL-LHVSIDELENVWPLVPPGA 538
Cdd:PRK06882 480 MVKQWQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETEHVYPMQIRGG 559
|
....*.
gi 813120958 539 SNSEML 544
Cdd:PRK06882 560 AMNEMI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-543 |
5.13e-169 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 490.90 E-value: 5.13e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELE-PWFTTVDNEATFP-----QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKG 233
Cdd:PRK07979 164 DILNPANKLPyVWPESVSMRSYNPttqghKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 234 LGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK07979 244 LGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 LNSLLPAL----------QQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSA 383
Cdd:PRK07979 324 ARQVLEQMlellsqesahQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK07979 404 LYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 464 WQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLL---HVSIDELENVWPLVPPGASN 540
Cdd:PRK07979 484 WQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALEQVRNNRLvfvDVTVDGSEHVYPMQIRGGGM 563
|
...
gi 813120958 541 SEM 543
Cdd:PRK07979 564 DEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-544 |
1.21e-145 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 431.18 E-value: 1.21e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPGGAIMPVYDA----LYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNL 78
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 79 ITGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIP 158
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 159 KDIQLASGELEPWFTT--VDNEATFP----QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLK 232
Cdd:PRK06456 164 RDIFYEKMEEIKWPEKplVKGYRDFPtridRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 233 GLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPN-ASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK06456 244 GKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKVDVGIY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 312 GDLNSLL-------PALQQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPL-LLKQLSERKPADSVVTTDVGQHQMWSA 383
Cdd:PRK06456 324 GNAKIILrelikaiTELGQKRDRSAWLKRVKEYKEYYSQFYYTEENGKLKPWkIMKTIRQALPRDAIVTTGVGQHQMWAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK06456 404 VFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 464 WQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWPLVPPGASNSEM 543
Cdd:PRK06456 484 VQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLKQV 563
|
.
gi 813120958 544 L 544
Cdd:PRK06456 564 I 564
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-525 |
1.20e-119 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 363.81 E-value: 1.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 2 NGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK08199 9 TGGQILVDALRANGVERVFCVPGESYLAVLDALHDeTDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVD---VLGlSLActKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDI 157
Cdd:PRK08199 89 GVHTAFQDSTPMILFVGQVARDFREREAFQEIDyrrMFG-PMA--KWVAEIDDAARIPELVSRAFHVATSGRPGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 158 PKDIQLASGElEPWFTTVDNEATFP-QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGA 236
Cdd:PRK08199 166 PEDVLSETAE-VPDAPPYRRVAAAPgAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 237 VEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGK---LNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK08199 245 FDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRVYRPDLAIVAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 LNSLLPALQ--QPLKIDAWRQSCAELRAEH-AWRYDH--PGETIYAPLLLkQLSERKPADSVVTTDVGQHQMWSAQHMTY 388
Cdd:PRK08199 325 PAAFAAALAalEPPASPAWAEWTAAAHADYlAWSAPLpgPGAVQLGEVMA-WLRERLPADAIITNGAGNYATWLHRFFRF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 389 TRPENFI--TSsglGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQ 466
Cdd:PRK08199 404 RRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 813120958 467 LFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSID 525
Cdd:PRK08199 481 REYPGRVSGTDLT-NPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-529 |
1.30e-116 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 355.67 E-value: 1.30e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAA-MAAIgYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAfMAAT-YGRLTGKAGVCLSTLGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVsapfiGTD-----AFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVL 154
Cdd:PRK08322 80 TGVAYAQLGGMPMVAITGQK-----PIKrskqgSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 155 VDIPKDIQLASGELEPwfTTVDNEATfPQAD---VEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTL 231
Cdd:PRK08322 155 LELPEDIAAEETDGKP--LPRSYSRR-PYASpkaIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGarFDdrvtgkLNTFAP-------NASVIHMDIDPAEMNKLR 304
Cdd:PRK08322 232 MGKGVIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD------VIEKPPffmnpngDKKVIHINFLPAEVDPVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 305 QAHVALQGDLNSLLPAL------QQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQH 378
Cdd:PRK08322 304 FPQVEVVGDIANSLWQLkerladQPHWDFPRFLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 379 QMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRL 458
Cdd:PRK08322 384 KIWFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAY 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 459 GMVRqWQQ--LFFQERYSETTltdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELEN 529
Cdd:PRK08322 464 GMIR-WKQenMGFEDFGLDFG---NPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSEN 532
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
352-537 |
1.88e-108 |
|
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: 321.75 E-value: 1.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 352 IYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSF 431
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*.
gi 813120958 512 LASEGPYLLHVSIDELENVWPLVPPG 537
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-537 |
5.49e-105 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 325.81 E-value: 5.49e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGG--VEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNL 78
Cdd:PRK08266 4 MTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 79 ITGLADALLDSVPVVAITGQVSAPFIGTDAFQ--EV-DVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLV 155
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 156 DIPKDIQLASGELEPwfTTVDNEATFPQAD---VEQARQMLEQAKKPMLYVGGGVgmAKAVPALRKFIAVTQMPVTCTLK 232
Cdd:PRK08266 164 EMPWDVFGQRAPVAA--APPLRPAPPPAPDpdaIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPVVAFRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 233 GLGAVEADYPYYLGMLgmhgtkAANFAVQECDLLIAVGARFDDRVTgKLNTFAPNASVIHMDIDPAEMNKLrQAHVALQG 312
Cdd:PRK08266 240 GRGIVSDRHPLGLNFA------AAYELWPQTDVVIGIGSRLELPTF-RWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 313 DLNSLLPALQQPL-KIDAWRQS-CAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTR 390
Cdd:PRK08266 312 DAKAGTAALLDALsKAGSKRPSrRAELRELKAAARQRIQAVQPQASYLRAIREALPDDGIFVDELSQVGFASWFAFPVYA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 391 PENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQ 470
Cdd:PRK08266 392 PRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 813120958 471 ERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSI--DELENVWPLVPPG 537
Cdd:PRK08266 472 GRVVASDLV-NPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVprGSEASPWPFIHPA 539
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-509 |
4.23e-101 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 316.92 E-value: 4.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARST-GKTGVCIATSGPGATNL 78
Cdd:PRK11269 4 MRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 79 ITGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIP 158
Cdd:PRK11269 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 159 KDIQLASGELEPwfttvDNEATFP-------QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTL 231
Cdd:PRK11269 164 FDVQVAEIEFDP-----DTYEPLPvykpaatRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 232 KGLGAVEADYPYYLGMLGMHGT-KAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKL------- 303
Cdd:PRK11269 239 MGWGAIPDDHPLMAGMVGLQTShRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVfgpdlgi 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 304 -RQAHVALQgdlnsLLPALQQPLKI-------DAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDV 375
Cdd:PRK11269 319 vSDAKAALE-----LLVEVAREWKAagrlpdrSAWVADCQERKRTLLRKTHFDNVPIKPQRVYEEMNKAFGRDTCYVSTI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 376 GQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDN 455
Cdd:PRK11269 394 GLSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNN 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 456 QRLGMVRQWQ---------QLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALD 509
Cdd:PRK11269 474 AYLGLIRQAQrafdmdycvQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALE 536
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
3-530 |
7.23e-100 |
|
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: 312.45 E-value: 7.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGL 82
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 83 ADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKDI- 161
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 162 -QLASGELEPWFTTVDNEATfPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAVEAD 240
Cdd:TIGR02418 161 dSPVSVKAIPASYAPKLGAA-PDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 241 -YPYYLGMLGMHGTKAANFAVQECDLLIAVG---ARFDDRVTGKLNtfapNASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:TIGR02418 240 lEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQPDLELVGDIAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 317 LLPALQQPL--------------KIDAWRQSCAELRAEHAWRYDHPGETIyaplllKQLSERKPADSVVTTDVGQHQMWS 382
Cdd:TIGR02418 316 TLDLLAERIpgyelppdalaileDLKQQREALDRVPATLKQAHLHPLEII------KAMQAIVTDDVTVTVDMGSHYIWM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP-LKIVLLDNqRLGMV 461
Cdd:TIGR02418 390 ARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNiVHIIWNDN-GYNMV 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 462 RqwqqlfFQE--RYSETTLTD--NPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENV 530
Cdd:TIGR02418 469 E------FQEemKYQRSSGVDfgPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNP 535
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-531 |
1.69e-98 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 309.09 E-value: 1.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 I--QLASGELEPWFTTVdNEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAVE 238
Cdd:PRK08617 165 VvdAPVTSKAIAPLSKP-KLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVIS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 239 AD-YPYYLGMLGMHGTKAANFAVQECDLLIAVG---ARFDDRVTGKLNtfapNASVIHMDIDPAEMNKLRQAHVALQGD- 313
Cdd:PRK08617 244 RElEDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSEG----DATIIHIDVLPAEIDNYYQPERELIGDi 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 ---LNSLLPALQQPLKIDAWRQSCAELRAEHAWRYDHP---GETIYAPL-LLKQLSERKPADSVVTTDVGQHQMWSAQHM 386
Cdd:PRK08617 320 aatLDLLAEKLDGLSLSPQSLEILEELRAQLEELAERParlEEGAVHPLrIIRALQDIVTDDTTVTVDVGSHYIWMARYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 387 TYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPL-KIVLLDNqRLGMVRqwq 465
Cdd:PRK08617 400 RSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIvHIIWNDG-HYNMVE--- 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 466 qlfFQE--RYSETTLTD--NPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVW 531
Cdd:PRK08617 476 ---FQEemKYGRSSGVDfgPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIK 542
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
3-537 |
1.79e-98 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 309.62 E-value: 1.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGL--SLACTKHSflVQSLAELPRIMAEAFEVANAGRpGPVLVDIP 158
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMfeDVAVYNHQ--IMSAENLPEIVNQAIRTAYEKK-GVAVLTIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 159 KDI---QLASGELEPWFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGggVGMAKAVPALRKFIAVTQMPVTCTLKGLG 235
Cdd:PRK08611 163 DDLpaqKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAG--LGAKHAKEELLAFAEKAKIPIIHTLPAKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 236 AVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRvtgklnTFAPN-ASVIHMDIDPAEMNKLRQAHVALQGDL 314
Cdd:PRK08611 241 IIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNVGLVGDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 315 NSLLPALQQPLKIDAWR---QSCAElRAEHAWRYDHPGETIYA-PL----LLKQLSERKPADSVVTTDVGQHQMWSAQHM 386
Cdd:PRK08611 315 KKALHQLTENIKHVEDRrflEACQE-NMAKWWKWMEEDENNAStPIkperVMAAIQKIADDDAVLSVDVGTVTVWSARYL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 387 TYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQ 466
Cdd:PRK08611 394 NLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQ 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 813120958 467 LFFQERYsETTLTDnPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDelENVWPLvpPG 537
Cdd:PRK08611 474 AAGELEY-AIDLSD-MDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD--PNAAPL--PG 538
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-532 |
1.72e-87 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 280.56 E-value: 1.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 4 AQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLA 83
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 84 DALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGL--SLACTKHSFLVQSLAELprIMAEAFEVANAGRpGPVLVDIPKDI 161
Cdd:PRK06457 85 DAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLfdDVAVFNQILINPENAEY--IIRRAIREAISKR-GVAHINLPVDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 162 QLASGELEPWFTTVDNEATFPqADVEQARQMLEQAKKPMLYVGGGV-GMAKAVpalRKFIAVTQMPVTCTLKGLGAVEAD 240
Cdd:PRK06457 162 LRKSSEYKGSKNTEVGKVKYS-IDFSRAKELIKESEKPVLLIGGGTrGLGKEI---NRFAEKIGAPIIYTLNGKGILPDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 241 YPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDdrvtgKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPA 320
Cdd:PRK06457 238 DPKVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 321 ----------LQQPLKIDAWRQSCAELRAEHawryDHPgetIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTR 390
Cdd:PRK06457 313 dieeksdkfyEELKGKKEDWLDSISKQENSL----DKP---MKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 391 PENFITSSGLGTMGFGLPAAVGAQVARPNDT-VICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK06457 386 EQTFIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMG 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 470 QERYSETTLtdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWP 532
Cdd:PRK06457 466 YPEWGVDLY--NPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMP 526
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
1-515 |
3.46e-81 |
|
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: 264.80 E-value: 3.46e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:TIGR03457 2 MTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRpGPVLVDIPKD 160
Cdd:TIGR03457 82 AIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 IqlasgelepWFTTVDNEATFPQ---------ADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTL 231
Cdd:TIGR03457 161 Y---------FYGEIDVEIPRPVrldrgaggaTSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGAR---FDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHV 308
Cdd:TIGR03457 232 LHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKVTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 309 ALQGDLNSLLPALQQPLKI------------------DAWRQSCAELRAEH--------AWRYDHPGETIYAPLLLKQLS 362
Cdd:TIGR03457 312 GICGDAKAAAAEILQRLAGkagdanraerkakiqaerSAWEQELSEMTHERdpfsldmiVEQRQEEGNWLHPRQVLRELE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 363 ERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVK 442
Cdd:TIGR03457 392 KAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 443 RKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASE 515
Cdd:TIGR03457 472 RHDIPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQ 544
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
8-515 |
5.64e-79 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 259.16 E-value: 5.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 8 VHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLADALL 87
Cdd:PRK07525 13 VETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 88 DSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRpGPVLVDIPKDiqLASGE 167
Cdd:PRK07525 93 AHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD--YFYGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 168 LE---PWFTTVDNEATFPQAdVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAVEADYPYY 244
Cdd:PRK07525 170 IDveiPQPVRLERGAGGEQS-LAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAFPGSHPLW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 245 LGMLGMHGTKAANFAVQECDLLIAVGARFDdrVTGKL-----NTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLP 319
Cdd:PRK07525 249 VGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLpqygiDYWPKDAKIIQVDINPDRIGLTKKVSVGICGDAKAVAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 320 ALQQPLKID-------------------AWRQSCAELRAEHawryDHPGETIYAPLLLKQ---LSERK---------PAD 368
Cdd:PRK07525 327 ELLARLAERlagdagreerkaliaaeksAWEQELSSWDHED----DDPGTDWNEEARARKpdyMHPRQalreiqkalPED 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 369 SVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPL 448
Cdd:PRK07525 403 AIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHNWPV 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 813120958 449 KIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASE 515
Cdd:PRK07525 483 TAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQ 549
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-522 |
9.37e-79 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 257.21 E-value: 9.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 4 AQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLA 83
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 84 DALLDSVPVVAITGQVSAPFIGTD--AFQEV-DVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK07524 85 QAYADSIPMLVISSVNRRASLGKGrgKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 I--QLASGELEPWFTTVDNEATFPqADVEQARQMLEQAKKPMLYVGGG-VGMAkavPALRKFIAVTQMPVTCTLKGLGAV 237
Cdd:PRK07524 165 VlaAPADHLLPAPPTRPARPGPAP-AALAQAAERLAAARRPLILAGGGaLAAA---AALRALAERLDAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 238 EADYPYYLGmlGMHGTKAANFAVQECDLLIAVG---ARFDDRVTGKlNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDL 314
Cdd:PRK07524 241 PAGHPLLLG--ASQSLPAVRALIAEADVVLAVGtelGETDYDVYFD-GGFPLPGELIRIDIDPDQLARNYPPALALVGDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 315 NSLLPALQQPLKIDAWRQSCAELRAE---HAWRYDHPGETIYAPLLLKQLSERKPADSVV--TTdvgqhQMWSAQHMTYT 389
Cdd:PRK07524 318 RAALEALLARLPGQAAAADWGAARVAalrQALRAEWDPLTAAQVALLDTILAALPDAIFVgdST-----QPVYAGNLYFD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 390 RPEN---FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQwqq 466
Cdd:PRK07524 393 ADAPrrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR--- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 813120958 467 lFFQERYSETTLTD--NPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHV 522
Cdd:PRK07524 470 -YMVARDIEPVGVDpyTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-525 |
3.01e-77 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 254.14 E-value: 3.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK06546 3 KTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVrRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVAnAGRPGPVLVDIPK 159
Cdd:PRK06546 83 NGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTLPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DI--QLASGELEPWFTTVDNEATFP-QADVEQARQMLEQAKKPMLYVGGGVGMAKA-VPALRKFIAVtqmPVTCTLKGLG 235
Cdd:PRK06546 162 DIadEPAPEGFAPSVISPRRPTVVPdPAEVRALADAINEAKKVTLFAGAGVRGAHAeVLALAEKIKA---PVGHSLRGKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 236 AVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFddrvtgKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD-- 313
Cdd:PRK06546 239 WIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDva 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 314 --LNSLLPALQQplKIDawRQSCAELRAEHAWRYDHPGETI-------------YAPLLLKQLSERkpaDSVVTTDVGQH 378
Cdd:PRK06546 313 etIRALLPLVKE--KTD--RRFLDRMLKKHARKLEKVVGAYtrkvekhtpihpeYVASILDELAAD---DAVFTVDTGMC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 379 QMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRL 458
Cdd:PRK06546 386 NVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTL 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 813120958 459 GMVRqwQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSID 525
Cdd:PRK06546 466 GMVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
4-532 |
2.09e-76 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 251.83 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 4 AQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGL 82
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRrMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 83 ADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVdIPKDIQ 162
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVV-LPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 163 LASGELEP---WFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGGGVgmAKAVPALRKFIAVTQMPVTCTLKGLGAVEA 239
Cdd:PRK09124 165 LKPAPERAtphWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 240 DYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRvtgklNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLP 319
Cdd:PRK09124 243 DNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 320 ALQQPLK-------IDAWRQSCAELRAE--HAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTR 390
Cdd:PRK09124 318 ALLPLLEektdrkfLDKALEHYRKARKGldDLAVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 391 PENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQlffQ 470
Cdd:PRK09124 398 KRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMK---A 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 471 ERYSET-TLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDELENVWP 532
Cdd:PRK09124 475 GGYLTDgTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMP 537
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-526 |
4.04e-75 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 248.91 E-value: 4.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFG--YPGGAIMpvydALYDGGVEHLLCRHEQ-GAAMAAiGYARSTGKTGVCIATSGPGATN 77
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSALFL----AAEAIGIRQIAYRTENaGGAMAD-GYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 78 LITGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKhsfLVQSLAELPRI---MAEAFEVANAGRPGPVL 154
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTK---WVRRVTVAERIddyVDQAFTAATSGRPGPVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 155 VDIPKDIqLASGELEPWFTTVDNEATFP-------QADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPV 227
Cdd:PRK06112 166 LLLPADL-LTAAAAAPAAPRSNSLGHFPldrtvpaPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 228 TCTLKGLGAVEADYPYYLGMLG-MHGTKAANF----AVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNK 302
Cdd:PRK06112 245 ATTNMGKGAVDETHPLSLGVVGsLMGPRSPGRhlrdLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 303 LRQAhVALQGDLNSLLPALQ---QPLKIDAWRQSCAEL-----------RAEHAWRYDHPGETIYAPLLLKQLSERKPAD 368
Cdd:PRK06112 325 NYEA-LRLVGDARLTLAALTdalRGRDLAARAGRRAALepaiaagreahREDSAPVALSDASPIRPERIMAELQAVLTGD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 369 SVVTTDVGQHQMWSAQHMTYTRP-ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP 447
Cdd:PRK06112 404 TIVVADASYSSIWVANFLTARRAgMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 813120958 448 LKIVLLDNQRLGMVRQWQQLFFQErYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDE 526
Cdd:PRK06112 484 VTIVVLNNGILGFQKHAETVKFGT-HTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDP 561
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
7-524 |
6.88e-74 |
|
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: 245.52 E-value: 6.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 7 VVHALRAQGVKTVFGYPGGAIMPVYDALYD--GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLAD 84
Cdd:TIGR02720 5 VLKVLEAWGVDHIYGIPGGSFNSTMDALSAerDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 85 ALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAgRPGPVLVDIPKDIQLA 164
Cdd:TIGR02720 85 AKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVDFGWQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 165 SGELEPWFTTVDNEATF--PQADVEQ---ARQMLEQAKKPMLYVG-GGVGMAKAVPALRKFIavtQMPVTCTLKGLGAVE 238
Cdd:TIGR02720 164 EIPDNDYYASSVSYQTPllPAPDVEAvtrAVQTLKAAERPVIYYGiGARKAGEELEALSEKL---KIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 239 ADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDdrVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLL 318
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 319 PA---LQQPLKIDAWRQscAELRAEHAWR--YDHPGETIYAPLLLKQ----LSERKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:TIGR02720 319 AAilaQVEPRESTPWWQ--ANVANVKNWRayLASLEDKTEGPLQAYQvyraINKIAEDDAIYSIDVGDININSNRHLKMT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:TIGR02720 397 PKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDTN 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 813120958 470 QErYSETTLTDnPDFLMLASAFGIPGQHITRKDQVEAALDT--MLASEGPYLLHVSI 524
Cdd:TIGR02720 477 QP-LIGVDFND-ADFAKIAEGVGAVGFRVNKIEQLPAVFEQakAIKQGKPVLIDAKI 531
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-548 |
1.05e-73 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 245.59 E-value: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNL 78
Cdd:PRK08273 3 QTVADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 79 ITGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLsLACTKHSFLVQ--SLAELPRIMAEAFEVANAGRpGPVLVD 156
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSL-FKDVAGAFVQMvtVPEQLRHLVDRAVRTALAER-TVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 157 IPKDIQ-LASGELEPWFTTVDNEATF-------PQADVEQARQMLEQAKKPMLYVGGGvgmakAVPALRKFIAVTQM--- 225
Cdd:PRK08273 161 LPNDVQeLEYEPPPHAHGTVHSGVGYtrprvvpYDEDLRRAAEVLNAGRKVAILVGAG-----ALGATDEVIAVAERlga 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 226 PVTCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFddrvtgKLNTFAP---NASVIHMDIDPAEMNK 302
Cdd:PRK08273 236 GVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFLPkegQARGVQIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 303 LRQAHVALQGD----LNSLLPALQQplKID-AWRQSCAELRAEhaW------RYDHPGETIYAPLLLKQLSERKPADSVV 371
Cdd:PRK08273 310 RYPMEVNLVGDaaetLRALLPLLER--KKDrSWRERIEKWVAR--WwetleaRAMVPADPVNPQRVFWELSPRLPDNAIL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 372 TTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN-VQELGTVKR-----KQ 445
Cdd:PRK08273 386 TADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKywrqwSD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 446 LPLKIVLLDNQRLGMVrQWQQLFFQ--ERYSET-TLTDNPdFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHV 522
Cdd:PRK08273 466 PRLIVLVLNNRDLNQV-TWEQRVMEgdPKFEASqDLPDVP-YARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEV 543
|
570 580
....*....|....*....|....*.
gi 813120958 523 SIDelENVwPLVPPGASNSEMLEKLS 548
Cdd:PRK08273 544 KTD--PNV-PPLPPHITLEQAKAFAS 566
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
7-527 |
4.92e-71 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 237.20 E-value: 4.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 7 VVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLADA 85
Cdd:PRK07064 9 IAAFLEQCGVKTAFGVISIHNMPILDAIGRrGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGALVEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 86 LLDSVPVVAITGQVSAPFIGTDA--FQEV-DVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKDIQ 162
Cdd:PRK07064 89 LTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPIDIQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 163 LASGELEPWFTTVDNEATFPQAD-VEQARQMLEQAKKPMLYVGGGV-GMAKAVPALRKFiavtQMPVTCTLKGLGAVEAD 240
Cdd:PRK07064 169 AAEIELPDDLAPVHVAVPEPDAAaVAELAERLAAARRPLLWLGGGArHAGAEVKRLVDL----GFGVVTSTQGRGVVPED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 241 YPYYLGMLgmHGTKAANFAVQECDLLIAVGARFDDRVTGKlNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD----LNS 316
Cdd:PRK07064 245 HPASLGAF--NNSAAVEALYKTCDLLLVVGSRLRGNETLK-YSLALPRPLIRVDADAAADGRGYPNDLFVHGDaarvLAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 317 LLPALQQPLKIDAwrQSCAELRAEHAWRYDHPGETI--YApLLLKQLSERKPADSVVTTDVG-QHQMWSAQHMTYTRPEN 393
Cdd:PRK07064 322 LADRLEGRLSVDP--AFAADLRAAREAAVADLRKGLgpYA-KLVDALRAALPRDGNWVRDVTiSNSTWGNRLLPIFEPRA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 394 FITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERY 473
Cdd:PRK07064 399 NVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRR 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 813120958 474 SETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHV---SIDEL 527
Cdd:PRK07064 478 YYVELH-TPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVdmlSIGPF 533
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
5-159 |
2.64e-68 |
|
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: 217.01 E-value: 2.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 5 QWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLAD 84
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 813120958 85 ALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
1-532 |
1.75e-64 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 219.59 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:PRK05858 5 GHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:PRK05858 85 AMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 161 --IQLASGELEPWFTTVDNEATFPQAD-VEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAV 237
Cdd:PRK05858 165 haFSMADDDGRPGALTELPAGPTPDPDaLARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 238 EADYPYYLgmlgmhgTKAANFAVQECDLLIAVGARFDDRVTgkLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSL 317
Cdd:PRK05858 245 PADHPLAF-------SRARGKALGEADVVLVVGVPMDFRLG--FGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 318 LPAL----QQPLKIDAW----RQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:PRK05858 316 LSALagagGDRTDHQGWieelRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK05858 396 RPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPMEALY 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 470 ----------QERYSEttltdnpdflmLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSIDElENVWP 532
Cdd:PRK05858 476 gydvaadlrpGTRYDE-----------VVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDP-SVAYP 536
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
374-522 |
1.57e-63 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 204.74 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 374 DVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLL 453
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 813120958 454 DNQRLGMVRQWQQLFFQERYSETT--LTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHV 522
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSgkILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
3-169 |
6.33e-63 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 203.62 E-value: 6.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITG 81
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 82 LADALLDSVPVVAITGQVSAPFIGTDAFQ-EVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKD 160
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*....
gi 813120958 161 IQLASGELE 169
Cdd:pfam02776 161 VLLEEVDED 169
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
1-522 |
1.70e-56 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 198.50 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPggaIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARST-GKT-GVCIATSGPGATNL 78
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATsGERvGVFAVQYGPGAENA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 79 ITGLADALLDSVPVVAITGQVSAP-------FIGTDAFQEVdvlglslacTKHSFLVQSLAELPRIMAEAFEVANAGRPG 151
Cdd:PRK06154 97 FGGVAQAYGDSVPVLFLPTGYPRGstdvapnFESLRNYRHI---------TKWCEQVTLPDEVPELMRRAFTRLRNGRPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 152 PVLVDIPKDI-QLASGELEPWFTTVdnEATFPQAD---VEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPV 227
Cdd:PRK06154 168 PVVLELPVDVlAEELDELPLDHRPS--RRSRPGADpveVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 228 TCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKlnTFAPNASVIHMDIDPAEMNKLRQAH 307
Cdd:PRK06154 246 MTTLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGL--PMPEGKTIIHSTLDDADLNKDYPID 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 308 VALQGD----LNSLLPALQQPLKIDAWR--QSCAELRAEH-AW-RYDHPGETI-YAPL----LLKQLSER-KPADSVVTT 373
Cdd:PRK06154 324 HGLVGDaalvLKQMIEELRRRVGPDRGRaqQVAAEIEAVRaAWlAKWMPKLTSdSTPInpyrVVWELQHAvDIKTVIITH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 374 DVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLL 453
Cdd:PRK06154 404 DAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIPILTILL 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 813120958 454 DNQRLGMVRQWQQLfFQERYSETTLTDnpDFLMLASAFGIPGQHITRKDQVEAALDTML--ASEG-PYLLHV 522
Cdd:PRK06154 484 NNFSMGGYDKVMPV-STTKYRATDISG--DYAAIARALGGYGERVEDPEMLVPALLRALrkVKEGtPALLEV 552
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
186-321 |
1.20e-55 |
|
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: 183.53 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 186 VEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDL 265
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 813120958 266 LIAVGARFDD-RVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPAL 321
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
357-524 |
5.69e-55 |
|
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: 182.84 E-value: 5.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 357 LLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 437 ELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEG 516
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLS-NPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 813120958 517 PYLLHVSI 524
Cdd:cd00568 161 PALIEVKT 168
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
2-165 |
1.13e-50 |
|
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: 171.19 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 2 NGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLIT 80
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 81 GLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRpGPVLVDIPKD 160
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....*
gi 813120958 161 IQLAS 165
Cdd:cd07039 160 VQDAP 164
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
352-525 |
4.43e-49 |
|
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: 167.71 E-value: 4.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 352 IYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSF 431
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGMVrQWQQLFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFI-KWEQEVMGQPEFGVDLP-NPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....
gi 813120958 512 LASEGPYLLHVSID 525
Cdd:cd02014 160 LAADGPVVIDVVTD 173
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
3-526 |
3.09e-46 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 170.55 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPGgaiMPVYD--ALYDG-GVEHLLCRHEQGA--AMAAIGYArsTGKTGVCIATSGPGATN 77
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAeGIRYIGFRHEQSAgnAAAAAGFL--TQKPGVCLTVSAPGFLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 78 LITGLADALLDSVPVVAITGQVSAPFIGTDA--FQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLV 155
Cdd:PRK09259 87 GLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 156 DIPKDI-------QLASGELepwFTTVDNEATFPQAD--VEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMP 226
Cdd:PRK09259 167 DLPAKVlaqtmdaDEALTSL---VKVVDPAPAQLPAPeaVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 227 VTCTLKGLGAVEADYPyylgmlgmHGTKAA-NFAVQECDLLIAVGARFDDRVT-GKLNTFAPNASVIHMDIDPAEMNKLR 304
Cdd:PRK09259 244 FLPMSMAKGLLPDTHP--------QSAAAArSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQIDIEPQEIDSNR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 305 QAHVALQGDLNSLLPAL-----QQPLKIDA-WRQSCAELRAEHAWRY------DHPGETIYAPL--LLKQLSERKpaDSV 370
Cdd:PRK09259 316 PIAAPVVGDIGSVMQALlaglkQNTFKAPAeWLDALAERKEKNAAKMaeklstDTQPMNFYNALgaIRDVLKENP--DIY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 371 VTTDvgqhqmwSAQHMTYTR-------PENFITSSGLGTMGFGLPAAVGAQVA--RPndtVICISGDGSFMMNVQELGTV 441
Cdd:PRK09259 394 LVNE-------GANTLDLARniidmykPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGMEVETI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 442 KRKQLPLKIVLLDNQrlGMVRQWQQLFFQER-YSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLL 520
Cdd:PRK09259 464 CRYNLPVTVVIFNNG--GIYRGDDVNLSGAGdPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLI 541
|
....*.
gi 813120958 521 HVSIDE 526
Cdd:PRK09259 542 NVVIDP 547
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
7-525 |
3.07e-44 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 164.36 E-value: 3.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 7 VVHALRAQGVKTVFGYPGGAIMPVYDALYDGgVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLADAL 86
Cdd:PRK07092 18 TIDLLRRFGITTVFGNPGSTELPFLRDFPDD-FRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 87 LDSVPVVAITGQVSAPFIGTDAF-QEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPKDIQLAS 165
Cdd:PRK07092 97 KNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDDWDQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 166 GELEPwFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPV-TCTLKGLGAVEADYPYY 244
Cdd:PRK07092 177 AEPLP-ARTVSSAVRPDPAALARLGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAPMSGRCSFPEDHPLF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 245 LGML--GMHGTKAAnfaVQECDLLIAVGAR-FDDRVTGKLNTFAPNASVIHMDIDPAEmnklrqAHVALQGD--LNSLLP 319
Cdd:PRK07092 256 AGFLpaSREKISAL---LDGHDLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDDPGE------AAWAPMGDaiVGDIRL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 320 ALQQPLKIDAWRQSCAELRAEHAWRYDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQ--MWsaQHMTYTRPENFIT- 396
Cdd:PRK07092 327 ALRDLLALLPPSARPAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRpaMQ--EHLPMRRQGSFYTm 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 397 -SSGLGtmgFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFfqeRYSE 475
Cdd:PRK07092 405 aSGGLG---YGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPVF---GVRD 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 813120958 476 TTLTDNP--DFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSID 525
Cdd:PRK07092 479 VPGLDLPglDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-513 |
3.67e-41 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 156.31 E-value: 3.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALYDGGVEH------LLCRHEQGAAMAAIGYARSTGKTGVCIATSGPG 74
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpefVICPHEIVAISMAHGYALVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 75 ATNLITGLADALLDSVPVVAITGQvsAPFIGTDAF----------QEV-DVLGLSLACTKHSFLVQSLAELPRIMAEAFE 143
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFAGR--SPYTEEGELgsrntrihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 144 VANAGRPGPVLVDIPKDIQLASGE-----LEPWFTTVdnEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRK 218
Cdd:PRK08327 165 IAMSEPKGPVYLTLPREVLAEEVPevkadAGRQMAPA--PPAPDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASLRR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 219 FIAVTQMPVTCTLKGLGAVEADYPYYLGMLgmhgtkaANFAVQECDLLIAVGArfDDRVTGKLNTFAPNASVIHMDIDPA 298
Cdd:PRK08327 243 LAEELAIPVVEYAGEVVNYPSDHPLHLGPD-------PRADLAEADLVLVVDS--DVPWIPKKIRPDADARVIQIDVDPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 299 -EMNKLR--QAHVALQGDLNSLLPALQQPLK-------------IDAWRQSCAELRAEH--AWRYDHPGETIYAPLLLKQ 360
Cdd:PRK08327 314 kSRIPLWgfPCDLCIQADTSTALDQLEERLKslasaerrrarrrRAAVRELRIRQEAAKraEIERLKDRGPITPAYLSYC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 361 LSERKPADSVVTTDVGQHQmwsaQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQE--L 438
Cdd:PRK08327 394 LGEVADEYDAIVTEYPFVP----RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 439 GTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE-------RYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:PRK08327 470 WVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEgyaarkgTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEELKGALRRA 549
|
..
gi 813120958 512 LA 513
Cdd:PRK08327 550 LA 551
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
4-526 |
9.37e-41 |
|
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: 154.93 E-value: 9.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 4 AQWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIaTSGPGATNLITGL 82
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAhPGIRWVGCCNELNAGYAADGYARVNGLGALVT-TYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 83 ADALLDSVPVVAITGqvsAPfiGTDAFQEVDVLGLSLActKHSFLVQ------------SL------AELPRIMAEAFEv 144
Cdd:COG3961 87 AGAYAERVPVVHIVG---AP--GTRAQRRGPLLHHTLG--DGDFDHFlrmfeevtvaqaVLtpenaaAEIDRVLAAALR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 145 anAGRPgpVLVDIPKD-----IQLASGELEPWFTTVDNEATfpQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKF 219
Cdd:COG3961 159 --EKRP--VYIELPRDvadapIEPPEAPLPLPPPASDPAAL--AAAVAAAAERLAKAKRPVILAGVEVHRFGLQEELLAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 220 IAVTQMPVTCTLKGLGAVEADYPYYLGM----LGMHGTKAAnfaVQECDLLIAVGARFDDRVTGkLNTFAPNASVIhMDI 295
Cdd:COG3961 233 AEKTGIPVATTLLGKSVLDESHPQFIGTyagaASSPEVREY---VENADCVLCLGVVFTDTNTG-GFTAQLDPERT-IDI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 296 DPaemNKLRQAHVALQG-DLNSLLPALQQPLKIDAWRQSCAELRAEHAwrYDHPGETIYAPLLLKQLSERKPADSVVTTD 374
Cdd:COG3961 308 QP---DSVRVGGHIYPGvSLADFLEALAELLKKRSAPLPAPAPPPPPP--PAAPDAPLTQDRLWQRLQAFLDPGDIVVAD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 375 VGQhQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLD 454
Cdd:COG3961 383 TGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 455 NQ-----R--LGM------VRQWqqlffqeRYSEttltdnpdflmLASAFGiPGQHITRK----DQVEAALDTMLA-SEG 516
Cdd:COG3961 462 NDgytieRaiHGPdgpyndIANW-------DYAK-----------LPEAFG-GGNALGFRvtteGELEEALAAAEAnTDR 522
|
570
....*....|
gi 813120958 517 PYLLHVSIDE 526
Cdd:COG3961 523 LTLIEVVLDK 532
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
357-530 |
6.70e-37 |
|
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: 134.72 E-value: 6.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 357 LLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 437 ELGTVKRKQLPLKIVLLDNQRLGMVRqWQQLFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEG 516
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDFG-NPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
170
....*....|....
gi 813120958 517 PYLLHVSIDELENV 530
Cdd:cd02010 162 VHVIDCPVDYSENI 175
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-159 |
7.37e-37 |
|
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: 134.01 E-value: 7.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 7 VVHALRAQGVKTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARSTGKtGVCIATSGPGATNLITGLADA 85
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 813120958 86 LLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGrPGPVLVDIPK 159
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-524 |
5.59e-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: 118.47 E-value: 5.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 357 LLKQLSERKPADSVV----TTDVGQhqMWsaQHMTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFM 432
Cdd:cd02002 6 LAAALAAALPEDAIIvdeaVTNGLP--LR--DQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 433 MNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQER-----YSETTLTD-NPDFLMLASAFGIPGQHITRKDQVEA 506
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGpgenaPDGLDLLDpGIDFAAIAKAFGVEAERVETPEELDE 160
|
170
....*....|....*...
gi 813120958 507 ALDTMLASEGPYLLHVSI 524
Cdd:cd02002 161 ALREALAEGGPALIEVVV 178
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
1-524 |
3.84e-30 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 123.80 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDALyDG--GVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNL 78
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAAL-DRvpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 79 ITGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGlsLACTKHSFL--VQSLAELPRIMAEAFEVANAGRPGPVLVD 156
Cdd:PRK07586 80 LANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEA--LARPVSGWVrrSESAADVAADAAAAVAAARGAPGQVATLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 157 IPKDIQLASGELEPWFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVT------QMPVTCT 230
Cdd:PRK07586 158 LPADVAWSEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATgarllaETFPARM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 231 LKGLGAVEADYPYYLGmlgmhgtKAANFAVQECDLLIAVGARfdDRVT-----GKLNTFAPNASVIHMDIDPAEmnklrQ 305
Cdd:PRK07586 238 ERGAGRPAVERLPYFA-------EQALAQLAGVRHLVLVGAK--APVAffaypGKPSRLVPEGCEVHTLAGPGE-----D 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 306 AHVALQG--DLNSLLPALQQPLKIDAWRQSCAELRAEHAwrydhpGETIYAPLllkqlserkPADSVVTTDVGQHQMWSA 383
Cdd:PRK07586 304 AAAALEAlaDALGAKPAAPPLAAPARPPLPTGALTPEAI------AQVIAALL---------PENAIVVDESITSGRGFF 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 384 QHMTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDN-------- 455
Cdd:PRK07586 369 PATAGAAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANrayailrg 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 456 --QRLGMVRQwqqlffQERYSETTLTDNP--DFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSI 524
Cdd:PRK07586 448 elARVGAGNP------GPRALDMLDLDDPdlDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
357-525 |
2.30e-27 |
|
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: 108.39 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 357 LLKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 437 ELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEG 516
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGK 163
|
....*....
gi 813120958 517 PYLLHVSID 525
Cdd:cd02004 164 PALINVIID 172
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-524 |
7.16e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 104.95 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 1 MNGAQWVVHALRAQGVKTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLI 79
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALdRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 80 TGLADALLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLAELPRIMAEAFEVANAGRPGPVLVDIPK 159
Cdd:PRK12474 85 ANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 160 DIQLASGELEPWFTTVDNEATFPQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPVTC------TLKG 233
Cdd:PRK12474 165 DVAWNEAAYAAQPLRGIGPAPVAAETVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCdtfaprIERG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 234 LGAVE-ADYPYYLGMLGMHgtkaanfaVQECDLLIAVGARfdDRVT-----GKLNTFAPnasvihmdiDPAEMNKLRQAH 307
Cdd:PRK12474 245 AGRVPiERIPYFHEQITAF--------LKDVEQLVLVGAK--PPVSffaypGKPSWGAP---------PGCEIVYLAQPD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 308 VALQGDLNSLLPALQQPLKIDAWRQSCAElraehawryDHPGETIYAPLLLKQLSERKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK12474 306 EDLAQALQDLADAVDAPAEPAARTPLALP---------ALPKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFDMSYD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 388 YTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR-QWQQ 466
Cdd:PRK12474 377 RARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNgELQR 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813120958 467 LFFQE--RYSETTLT-DNP--DFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSI 524
Cdd:PRK12474 456 VGAQGagRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
358-513 |
2.69e-23 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 97.58 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 358 LKQLSERKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQE 437
Cdd:cd02013 10 LRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMME 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 813120958 438 LGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLtDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLA 513
Cdd:cd02013 90 IMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTEL-ESESFAKIAEACGAKGITVDKPEDVGPALQKAIA 164
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
391-528 |
7.50e-19 |
|
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: 84.51 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 391 PEN--FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQ-----RL--GMV 461
Cdd:cd02005 38 PKGtrFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDgytieRAihGPE 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 813120958 462 RQWQQLffqerysettltDNPDFLMLASAFGIPGQHITRK----DQVEAALDTMLA-SEGPYLLHVSIDELE 528
Cdd:cd02005 118 ASYNDI------------ANWNYTKLPEVFGGGGGGLSFRvkteGELDEALKDALFnRDKLSLIEVILPKDD 177
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
7-158 |
6.51e-17 |
|
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: 78.31 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 7 VVHALRAQGVKTVFGYPGGAIMP-VYDALYDGGVEHLLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLADA 85
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSRSAPlALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 813120958 86 LLDSVPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQS------LAELPRIMAEAFEVANAGRPGPVLVDIP 158
Cdd:cd07037 83 YYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPpeddddLWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
361-525 |
2.25e-16 |
|
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: 77.73 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 361 LSERKPADSVVTTDVGQ-----HQMWSAQ-----HMTYtrpenfitssGLGTMGFGLPAAVGAQVARPNDTVICISGDGS 430
Cdd:cd02003 8 LNEAIGDDDVVINAAGSlpgdlHKLWRARtpggyHLEY----------GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 431 FMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQ-----QLF---FQERYSETTLTDNP----DFLMLASAFGIPGQHI 498
Cdd:cd02003 78 YLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNLQestgsGSFgteFRDRDQESGQLDGAllpvDFAANARSLGARVEKV 157
|
170 180
....*....|....*....|....*..
gi 813120958 499 TRKDQVEAALDTMLASEGPYLLHVSID 525
Cdd:cd02003 158 KTIEELKAALAKAKASDRTTVIVIKTD 184
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
368-530 |
8.11e-15 |
|
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: 73.47 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 368 DSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP 447
Cdd:cd02006 24 DVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 448 LKIVLLDNQRLGMVRQWQQLF---------FQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTM--LASEG 516
Cdd:cd02006 104 YIHVLVNNAYLGLIRQAQRAFdmdyqvnlaFENINSSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQAkkLMAEH 183
|
170
....*....|....*.
gi 813120958 517 --PYLLHVSIDELENV 530
Cdd:cd02006 184 rvPVVVEAILERVTNI 199
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
5-108 |
1.62e-14 |
|
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: 71.37 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 5 QWVVHALRAQGVKTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARSTGkTGVCIATSGPGATNLITGLA 83
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90 100
....*....|....*....|....*
gi 813120958 84 DALLDSVPVVAITGQVSAPFIGTDA 108
Cdd:cd07038 80 GAYAEHVPVVHIVGAPSTKAQASGL 104
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
357-526 |
6.88e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 70.63 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 357 LLKQLSERKPADSVVTTDVG--QHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN 434
Cdd:PRK06163 18 LTCRLVAKLKDEEAVIGGIGntNFDLWAAGQ----RPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 435 VQELGTV-KRKQLPLKIVLLDNQrlgmvrqwqqlFFQERYSETTLT-DNPDFLMLASAFGIPGQHITRKDQ-VEAALDTM 511
Cdd:PRK06163 91 LGALGTIaALAPKNLTIIVMDNG-----------VYQITGGQPTLTsQTVDVVAIARGAGLENSHWAADEAhFEALVDQA 159
|
170
....*....|....*
gi 813120958 512 LASEGPYLLHVSIDE 526
Cdd:PRK06163 160 LSGPGPSFIAVRIDD 174
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
15-455 |
8.73e-10 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 61.25 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 15 GVKTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARSTGkTGVCIATSGPGATNLITGLADALLDSVPVV 93
Cdd:PLN02573 30 GVTDVFSVPGDFNLTLLDHLiAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 94 AITGQVSAPFIGTD-----------------AFQEVdvlglslacTKHSFLVQSLAELPRIMAEAFEVAnAGRPGPV--- 153
Cdd:PLN02573 109 CIVGGPNSNDYGTNrilhhtiglpdfsqelrCFQTV---------TCYQAVINNLEDAHELIDTAISTA-LKESKPVyis 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 154 ----LVDIPKDIqlASGELEPWFTT--VDNEATFpQADVEQARQMLEQAKKPMLYVGGGVGMAKAVPALRKFIAVTQMPV 227
Cdd:PLN02573 179 vscnLAAIPHPT--FSREPVPFFLTprLSNKMSL-EAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 228 TCTLKGLGAVEADYPYYLGML-GMHGTKAANFAVQECDLLIAVGARFDD---------------------RVT-GKLNTF 284
Cdd:PLN02573 256 AVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDyssvgyslllkkekaiivqpdRVTiGNGPAF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 285 apnASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPAlQQPLKIDawrqscaelraehawrydhPGETIYAPLLLKQLSER 364
Cdd:PLN02573 336 ---GCVLMKDFLEALAKRVKKNTTAYENYKRIFVPE-GEPLKSE-------------------PGEPLRVNVLFKHIQKM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 365 KPADSVVTTDVGQHqmW-SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVI-CIsGDGSFMMNVQELGTVK 442
Cdd:PLN02573 393 LSGDTAVIAETGDS--WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIaCI-GDGSFQVTAQDVSTMI 469
|
490
....*....|...
gi 813120958 443 RKQLPLKIVLLDN 455
Cdd:PLN02573 470 RCGQKSIIFLINN 482
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
370-524 |
1.32e-09 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 57.11 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 370 VVTTDVGQHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPnDTVICISGDGSFMMNVQELGTV-KRKQLPL 448
Cdd:cd02001 18 VSTTGYASRELYDVQD----RDGHFYM---LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAgEFTPLNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 449 KIVLLDNQRlgmvrqwqqlffqerYSET----TLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSI 524
Cdd:cd02001 90 ILVVLDNRA---------------YGSTggqpTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPI 154
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
358-524 |
8.66e-09 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 55.40 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 358 LKQLSERKPADSVV--TTDVGQHQMWSAQHM-TYTRPENFITssgLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN 434
Cdd:cd03371 5 IEIVLSRAPATAAVvsTTGMTSRELFELRDRpGGGHAQDFLT---VGSMGHASQIALGIALARPDRKVVCIDGDGAALMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 435 VQELGTVKRKQLP-LKIVLLDNQRLGMVRqwqqlffqerySETTLTDNPDFLMLASAFGIPG-QHITRKDQVEAALDTML 512
Cdd:cd03371 82 MGGLATIGGLAPAnLIHIVLNNGAHDSVG-----------GQPTVSFDVSLPAIAKACGYRAvYEVPSLEELVAALAKAL 150
|
170
....*....|..
gi 813120958 513 ASEGPYLLHVSI 524
Cdd:cd03371 151 AADGPAFIEVKV 162
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
368-525 |
1.39e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 54.60 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 368 DSVVTTDVG--QHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPnDTVICISGDGSFMMNVQELGTVKrKQ 445
Cdd:cd03372 14 DELVVSNIGfpSKELYAAGD----RPLNFYM---LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGALATIA-AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 446 LP--LKIVLLDNqrlgmvRQWQQLFFQERYSettlTDNPDFLMLASAFGIpgQHITRKDQVEAALDTM-LASEGPYLLHV 522
Cdd:cd03372 85 KPknLIIVVLDN------GAYGSTGNQPTHA----GKKTDLEAVAKACGL--DNVATVASEEAFEKAVeQALDGPSFIHV 152
|
...
gi 813120958 523 SID 525
Cdd:cd03372 153 KIK 155
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
410-525 |
3.91e-06 |
|
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: 47.20 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 410 AVGAQVARpNDTVICISGDGSFM--MNVqeLGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQ---ERYSETTLtdNPDF 484
Cdd:cd02009 60 ALGIALAT-DKPTVLLTGDLSFLhdLNG--LLLGKQEPLNLTIVVINNNGGGIFSLLPQASFEdefERLFGTPQ--GLDF 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 813120958 485 LMLASAFGIPGQHITRKDQVEAALDTMLASEGPYLLHVSID 525
Cdd:cd02009 135 EHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
401-460 |
2.79e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 42.91 E-value: 2.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 813120958 401 GTMGFGLPAAVGAQVARPNDTVICISGDGS--------FMMNVqelgtvkRKQLPLKIVLLDNQRLGM 460
Cdd:PRK11867 69 TIHGRALAIATGLKLANPDLTVIVVTGDGDalaiggnhFIHAL-------RRNIDITYILFNNQIYGL 129
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
3-156 |
4.53e-04 |
|
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, 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. 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 of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.
Pssm-ID: 132917 [Multi-domain] Cd Length: 160 Bit Score: 40.95 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 3 GAQWVVHALRAQGVKTVFGYPG---GAIMPVYDALYDGGVEHLLCR--HEQGAAMAAIGyARSTGKTGVCiATSGPGATN 77
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAKAVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 78 LITGLADALLDSVPVVAITGQ--VSAP-FIGTDAfQEVDvlglSLACTKHSFLV---QSLAELPRIMAEAFEVA-NAGRP 150
Cdd:cd07034 79 MAEALYLAAGAELPLVIVVAQrpGPSTgLPKPDQ-SDLM----AARYGGHPWPVlapSSVQEAFDLALEAFELAeKYRLP 153
|
....*.
gi 813120958 151 GPVLVD 156
Cdd:cd07034 154 VIVLSD 159
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
42-96 |
1.47e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 41.77 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 813120958 42 LLCRHEQGAAMAAIGYARSTGKTGVCIATSGPGATNLITGLADALLDSVPVVAIT 96
Cdd:PLN02980 343 IACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLT 397
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
356-460 |
1.98e-03 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 39.43 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 356 LLLKQLSER--KPADSVVTTDVGQHqmwsaqhmtyTRPENFITSSGL-GTMGFGLPAAVGAQVARPNDTVICISGDG-SF 431
Cdd:cd03375 13 ALAKALAELgiDPEKVVVVSGIGCS----------SRLPYYFNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdLA 82
|
90 100
....*....|....*....|....*....
gi 813120958 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:cd03375 83 AIGGNHFIHAARRNIDITVIVHNNQIYGL 111
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
348-460 |
2.56e-03 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 40.12 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813120958 348 PGETIYAPL--LLKQLSER--KPADSVVTTDVGQHqmwsaqhmtyTRPENFITSSGLGTM-GFGLPAAVGAQVARPNDTV 422
Cdd:PRK11866 11 PGCGNYGILeaLRKALAELgiPPENVVVVSGIGCS----------SNLPEFLNTYGIHGIhGRVLPIATGVKWANPKLTV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 813120958 423 ICISGDG-SFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:PRK11866 81 IGYGGDGdGYGIGLGHLPHAARRNVDITYIVSNNQVYGL 119
|
|
| |
