|
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: 1227.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGDLDPHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVVDAD 240
Cdd:PRK08978 161 IQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 241 YPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCLLPA 320
Cdd:PRK08978 241 HPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 321 LQQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGL 400
Cdd:PRK08978 321 LQQPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 401 GTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTD 480
Cdd:PRK08978 401 GTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSETDLSD 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513153969 481 NPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS 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: 731.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDP---HFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGV 236
Cdd:COG0028 163 DVQAAEAEEEPappELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 237 VDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNC 316
Cdd:COG0028 243 FPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 317 LLPAL-----QQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRP 391
Cdd:COG0028 323 VLAALlealePRADDRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 392 ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE 471
Cdd:COG0028 403 RRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513153969 472 RYSETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENvwplvPPGASNSEM 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: 703.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYnDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDPHfstvaDEMAFP---------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCT 230
Cdd:TIGR00118 161 DVTTAEIEYPYP-----EKVNLPgyrptvkghPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 231 LKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGL 310
Cdd:TIGR00118 236 LMGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 311 TGD----LNCLLPALQQPLAID--GWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQ 384
Cdd:TIGR00118 316 VGDarnvLEELLKKLFELKERKesAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:TIGR00118 396 FYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQW 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 465 QQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEML 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: 672.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY----DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGAT 76
Cdd:PRK07418 19 ATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 77 NLITGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVD 156
Cdd:PRK07418 99 NLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 157 IPKDIQMAQGDLDPHFSTVADEMAFPQ------AEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCT 230
Cdd:PRK07418 179 IPKDVGQEEFDYVPVEPGSVKPPGYRPtvkgnpRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 231 LKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGL 310
Cdd:PRK07418 259 LMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRPDVPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 311 TGD----LNCLLPALQQPLA---IDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPaDSVVTTDVGQHQMWSA 383
Cdd:PRK07418 339 VGDvrkvLVKLLERSLEPTTpprTQAWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQMWAA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 384 QHMTyTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK07418 418 QFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQ 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 464 WQQLFFQERYSETTLTDN-PDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSE 542
Cdd:PRK07418 497 WQESFYGERYSASNMEPGmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCYPMVPPGKSNAQ 576
|
..
gi 1513153969 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: 663.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 15 GVDTVFGYPGGAIMPVYDALY----DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSI 90
Cdd:CHL00099 24 GVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 91 PIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKDI--------Q 162
Cdd:CHL00099 104 PLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDVglekfdyyP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 163 MAQGDLDPHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVVDADYP 242
Cdd:CHL00099 184 PEPGNTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIFDEDHP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 243 YYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCLLPALQ 322
Cdd:CHL00099 264 LCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIVGDVKKVLQELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 323 QPLAID----------GWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPaDSVVTTDVGQHQMWSAQhMTYTRPE 392
Cdd:CHL00099 344 ELLKNSpnlleseqtqAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDVGQHQMWAAQ-FLKCKPR 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 393 NFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQER 472
Cdd:CHL00099 422 KWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQAFYGER 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513153969 473 YSETTLTDN-PDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:CHL00099 502 YSHSNMEEGaPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENCYPMVAPGKSNSQMI 574
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 659.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYkQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDphfstVADEMAFP---------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCT 230
Cdd:PRK08527 163 DVTATLGEFE-----YPKEISLKtykptykgnSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 231 LKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGL 310
Cdd:PRK08527 238 LMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 311 TGDLNCLLPAL------QQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQ 384
Cdd:PRK08527 318 VGDLKNVLKEMleelkeENPTTYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:PRK08527 398 FYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQW 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 465 QQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK08527 478 QTFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNMI 557
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 649.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08155 13 FTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK08155 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLD--PHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVV 237
Cdd:PRK08155 173 DVQTAVIELEalPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 238 DADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD---- 313
Cdd:PRK08155 253 PKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADvddv 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 LNCLLPALQqPLAIDGWRERSAALRAEHAwrYDHPGEAiyAPL----LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:PRK08155 333 LAQLLPLVE-AQPRAEWHQLVADLQREFP--CPIPKAD--DPLshygLINAVAACVDDNAIITTDVGQHQMWTAQAYPLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK08155 408 RPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFY 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513153969 470 QERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK08155 488 GQRVFAATYPGKINFMQIAAGFGLETCDLNNEADPQAALQEAINRPGPALIHVRIDAEEKVYPMVPPGAANTEMI 562
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-545 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 641.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK06048 8 MTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK06048 88 GIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGDLDphfstVADEMAFP---------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTL 231
Cdd:PRK06048 168 VTTAEIDFD-----YPDKVELRgykptykgnPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 232 KGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK06048 243 MGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPALQ---QPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPaDSVVTTDVGQHQMWSAQHMTY 388
Cdd:PRK06048 323 GDAKQVLKSLIkyvQYCDRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:PRK06048 402 KYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELF 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1513153969 469 FQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEMLE 545
Cdd:PRK06048 482 YDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILD 558
|
|
| 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: 625.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDP-----HFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGV---GMAqAVPALREFLAVTRMPATCTL 231
Cdd:PRK09107 171 DVQFATGTYTPpqkapVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVinsGPE-ASRLLRELVELTGFPITSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 232 KGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK09107 250 MGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPALQQPL----------AIDGWRERSAALRAEHAWRYDHPGEAI---YAPLLLKQLSdrKPADSVVTTDVGQH 378
Cdd:PRK09107 330 GDVGHVLEDMLRLWkargkkpdkeALADWWGQIARWRARNSLAYTPSDDVImpqYAIQRLYELT--KGRDTYITTEVGQH 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 379 QMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRL 458
Cdd:PRK09107 408 QMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYM 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 459 GMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGA 538
Cdd:PRK09107 488 GMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPMIPSGK 567
|
....*.
gi 1513153969 539 SNSEML 544
Cdd:PRK09107 568 AHNEML 573
|
|
| 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: 624.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK07789 31 MTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGD------LD-PHFSTVADemafPQA-EVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTL 231
Cdd:PRK07789 191 DALQAQTTfswpprMDlPGYRPVTK----PHGkQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTTL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 232 KGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK07789 267 MARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPIV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPALQQPLA----------IDGWRERSAALRAEHAWRYDHPGEAIYAP-LLLKQLSDRKPADSVVTTDVGQHQM 380
Cdd:PRK07789 347 GDVKEVIAELIAALRaehaaggkpdLTAWWAYLDGWRETYPLGYDEPSDGSLAPqYVIERLGEIAGPDAIYVAGVGQHQM 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 381 WSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:PRK07789 427 WAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLGM 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 461 VRQWQQLFFQERYSETTLTDN----PDFLTLASAFGIPGQHITRKDQVEAALDTMLS-SQGPYLL--HVSIDELenVWPL 533
Cdd:PRK07789 507 VRQWQTLFYEERYSNTDLHTHshriPDFVKLAEAYGCVGLRCEREEDVDAVIEKARAiNDRPVVIdfVVGKDAM--VWPM 584
|
....*....
gi 1513153969 534 VPPGASNSE 542
Cdd:PRK07789 585 VAAGTSNDE 593
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 617.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQmaQGDLDPHFSTVADEMAFP---------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTL 231
Cdd:PRK06276 161 VQ--EGELDLEKYPIPAKIDLPgykpttfghPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 232 KGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK06276 239 MGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GD----LNCLLPAL--QQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLS----DRKP-ADSVVTTDVGQHQM 380
Cdd:PRK06276 319 GDaknvLRDLLAELmkKEIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMevlrEIDPsKNTIITTDVGQNQM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 381 WSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:PRK06276 399 WMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGM 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 461 VRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVwPLVPPGASN 540
Cdd:PRK06276 479 VYQWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPGGNL 557
|
....
gi 1513153969 541 SEML 544
Cdd:PRK06276 558 TNIL 561
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
1-546 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 599.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQG-----------DLDPHFstVADEMAFpqAEVAQAlqmLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATC 229
Cdd:PRK06725 175 VQNEKVtsfynevveipGYKPEP--RPDSMKL--REVAKA---ISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 230 TLKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIG 309
Cdd:PRK06725 248 TLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 310 LTGDLNCLLPALQQ---PLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHM 386
Cdd:PRK06725 328 VVGDVKKALHMLLHmsiHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 387 TYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQ 466
Cdd:PRK06725 408 KAKNPRTFLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQE 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 467 LFFQERYSETTLtDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEMLEK 546
Cdd:PRK06725 488 MFYENRLSESKI-GSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMIMK 566
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-543 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 599.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK07710 16 MTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGDLDphfstVADEMAFP---------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTL 231
Cdd:PRK07710 176 MVVEEGEFC-----YDVQMDLPgyqpnyepnLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 232 KGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK07710 251 LGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPAL----QQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK07710 331 ADAKQALQVLlqqeGKKENHHEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 388 YTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQL 467
Cdd:PRK07710 411 FKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEE 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513153969 468 FFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEM 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: 597.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITG 81
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 82 LADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKDI 161
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 162 Q--MAQGDLDPHFSTVADEMAFPQ----AEVAQALQMLAQSQQPMLYVGGGVgmAQAVPALREFLAVTRMPATCTLKGLG 235
Cdd:PLN02470 175 QqqLAVPNWNQPMKLPGYLSRLPKppekSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGIPVASTLMGLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 236 VVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLN 315
Cdd:PLN02470 253 AFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADVK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 316 CLLPALQQPLAIDG--------WRERSAALRAEHAWRYDHPGEAI---YAPLLLKQLSDRKpadSVVTTDVGQHQMWSAQ 384
Cdd:PLN02470 333 LALQGLNKLLEERKakrpdfsaWRAELDEQKEKFPLSYPTFGDAIppqYAIQVLDELTDGN---AIISTGVGQHQMWAAQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:PLN02470 410 WYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQW 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 465 QQLFFQERYSETTLTDN-------PDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPG 537
Cdd:PLN02470 490 EDRFYKANRAHTYLGDPdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIPGG 569
|
..
gi 1513153969 538 AS 539
Cdd:PLN02470 570 GT 571
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 532.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 2 NGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNfEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGDL--DP-------HFSTVADEMafpqaEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTL 231
Cdd:PRK07282 171 VSALETDFiyDPevnlpsyQPTLEPNDM-----QIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 232 KGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK07282 246 LGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNcllPALQQPLAID-------GWRERSAALRAEHAWrYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQ 384
Cdd:PRK07282 326 GDAK---KALQMLLAEPtvhnnteKWIEKVTKDKNRVRS-YDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:PRK07282 402 YYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 465 QQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQgPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK07282 482 QESFYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDV-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: 522.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06466 4 LSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDPHFSTVADEMAFPQA------EVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKG 233
Cdd:PRK06466 164 DMTNPAEKFEYEYPKKVKLRSYSPAvrghsgQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 234 LGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD 313
Cdd:PRK06466 244 LGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIVGP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 ----LNCLLPALQQ------PLAIDGWRERSAALRAEHA-WRYDHP-GEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMW 381
Cdd:PRK06466 324 vesvLTEMLAILKEigekpdKEALAAWWKQIDEWRGRHGlFPYDKGdGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQMF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 382 SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMV 461
Cdd:PRK06466 404 AAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGMV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 462 RQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLS-SQGPYLLHVSIDELENVWPLVPPGASN 540
Cdd:PRK06466 484 RQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFIDIYVDRSEHVYPMQIADGSM 563
|
...
gi 1513153969 541 SEM 543
Cdd:PRK06466 564 RDM 566
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
1-544 |
7.92e-179 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 516.66 E-value: 7.92e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIqmaqgdldphfSTVADEMAFPQA---------------EVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTR 224
Cdd:PRK06965 181 DV-----------SKTPCEYEYPKSvemrsynpvtkghsgQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 225 MPATCTLKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHA-KVIHMDIDPAELNKL 303
Cdd:PRK06965 250 YPVTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 304 RQAHIGLTGDLNCLLPAL----------QQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTT 373
Cdd:PRK06965 330 VKVDIPIVGDVKEVLKELieqlqtaehgPDADALAQWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 374 DVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLL 453
Cdd:PRK06965 410 DVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 454 DNQRLGMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQG-PYLLHVSIDELENVWP 532
Cdd:PRK06965 490 NNRYLGMVRQWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDrTVFLDFQTDPTENVWP 569
|
570
....*....|..
gi 1513153969 533 LVPPGASNSEML 544
Cdd:PRK06965 570 MVQAGKGITEML 581
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-543 |
7.81e-170 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 493.18 E-value: 7.81e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08979 4 LSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK08979 84 TGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDPHF-STVADEMAFP-----QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKG 233
Cdd:PRK08979 164 DCLNPAILHPYEYpESIKMRSYNPttsghKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 234 LGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD 313
Cdd:PRK08979 244 LGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 ----LNCLLPALQQ------PLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSA 383
Cdd:PRK08979 324 adkvLDSMLALLDEsgetndEAAIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK08979 404 LYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 464 WQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYL-LHVSIDELENVWPLVPPGASNSE 542
Cdd:PRK08979 484 WQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAMKDRLVfVDINVDETEHVYPMQIRGGAMNE 563
|
.
gi 1513153969 543 M 543
Cdd:PRK08979 564 M 564
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-544 |
3.21e-168 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 489.04 E-value: 3.21e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMAQGDLDPHFSTVADEMAFP------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKG 233
Cdd:PRK06882 164 DMVNPANKFTYEYPEEVSLRSYNptvqghKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 234 LGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD 313
Cdd:PRK06882 244 LGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 ----LNCLLPALQQP------LAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSA 383
Cdd:PRK06882 324 aknvLEEFLSLLEEEnlaksqTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK06882 404 LHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 464 WQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYL-LHVSIDELENVWPLVPPGASNSE 542
Cdd:PRK06882 484 WQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETEHVYPMQIRGGAMNE 563
|
..
gi 1513153969 543 ML 544
Cdd:PRK06882 564 MI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-543 |
5.97e-165 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 480.50 E-value: 5.97e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIqmaqgdLDPHF-------STVADEMAFP-----QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPA 227
Cdd:PRK07979 164 DI------LNPANklpyvwpESVSMRSYNPttqghKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 228 TCTLKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAH 307
Cdd:PRK07979 238 VSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 308 IGLTGDLNCLLPAL----------QQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQ 377
Cdd:PRK07979 318 IPIVGDARQVLEQMlellsqesahQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 378 HQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQR 457
Cdd:PRK07979 398 HQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 458 LGMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTML---SSQGPYLLHVSIDELENVWPLV 534
Cdd:PRK07979 478 LGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALeqvRNNRLVFVDVTVDGSEHVYPMQ 557
|
....*....
gi 1513153969 535 PPGASNSEM 543
Cdd:PRK07979 558 IRGGGMDEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-544 |
9.70e-144 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 426.18 E-value: 9.70e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPGGAIMPVYDA----LYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 79 ITGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIP 158
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 159 KDIQMAQGD--LDPHFSTVADEMAFP----QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLK 232
Cdd:PRK06456 164 RDIFYEKMEeiKWPEKPLVKGYRDFPtridRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVSTFP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 233 GLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFA-PHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK06456 244 GKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVeTRKKFIMVNIDPTDGEKAIKVDVGIY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPALQQPLAIDG-------WRERSAALRAEHAWRYDHPGEAIYAPL-LLKQLSDRKPADSVVTTDVGQHQMWSA 383
Cdd:PRK06456 324 GNAKIILRELIKAITELGqkrdrsaWLKRVKEYKEYYSQFYYTEENGKLKPWkIMKTIRQALPRDAIVTTGVGQHQMWAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK06456 404 VFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLVRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 464 WQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWPLVPPGASNSEM 543
Cdd:PRK06456 484 VQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLKQV 563
|
.
gi 1513153969 544 L 544
Cdd:PRK06456 564 I 564
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-525 |
2.27e-121 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 368.43 E-value: 2.27e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 2 NGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08199 9 TGGQILVDALRANGVERVFCVPGESYLAVLDALHDeTDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVD---VLGlSLActKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDI 157
Cdd:PRK08199 89 GVHTAFQDSTPMILFVGQVARDFREREAFQEIDyrrMFG-PMA--KWVAEIDDAARIPELVSRAFHVATSGRPGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 158 PKDI--QMAQGDLDPHFSTVadeMAFPQAEVAQALQ-MLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGL 234
Cdd:PRK08199 166 PEDVlsETAEVPDAPPYRRV---AAAPGAADLARLAeLLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 235 GVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGK---LNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK08199 243 DLFDNRHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRVYRPDLAIV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPALQ--QPLAIDGWRERSAALRAEH-AWRYDHPGE-AIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK08199 323 ADPAAFAAALAalEPPASPAWAEWTAAAHADYlAWSAPLPGPgAVQLGEVMAWLRERLPADAIITNGAGNYATWLHRFFR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 388 YTRPENFI--TSsglGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQ 465
Cdd:PRK08199 403 FRRYRTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 466 QLFFQERYSETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSID 525
Cdd:PRK08199 480 EREYPGRVSGTDLT-NPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-529 |
1.85e-114 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 350.28 E-value: 1.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAA-MAAIgYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAfMAAT-YGRLTGKAGVCLSTLGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVaapfiGTD-----AFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVL 154
Cdd:PRK08322 80 TGVAYAQLGGMPMVAITGQK-----PIKrskqgSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 155 VDIPKDIQMAQGDLDPH-FSTVADEMAFPQAeVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKG 233
Cdd:PRK08322 155 LELPEDIAAEETDGKPLpRSYSRRPYASPKA-IERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 234 LGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGarFDdrvtgkLNTFAPH-------AKVIHMDIDPAELNKLRQA 306
Cdd:PRK08322 234 KGVIPETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD------VIEKPPFfmnpngdKKVIHINFLPAEVDPVYFP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 307 HIGLTGDLNCLLPALQQPLA-IDGW-----RERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQM 380
Cdd:PRK08322 306 QVEVVGDIANSLWQLKERLAdQPHWdfprfLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 381 WSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:PRK08322 386 WFARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGM 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513153969 461 VRqWQQ--LFFQERYSETTltdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELEN 529
Cdd:PRK08322 466 IR-WKQenMGFEDFGLDFG---NPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSEN 532
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
352-537 |
8.41e-107 |
|
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: 317.52 E-value: 8.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 352 IYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSF 431
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*.
gi 1513153969 512 LSSQGPYLLHVSIDELENVWPLVPPG 537
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-509 |
3.17e-105 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 327.71 E-value: 3.17e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARAT-GKTGVCIATSGPGATNL 78
Cdd:PRK11269 4 MRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 79 ITGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIP 158
Cdd:PRK11269 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 159 KDIQMAQGDLDPHfstvADE---MAFPQAEVAQ---ALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLK 232
Cdd:PRK11269 164 FDVQVAEIEFDPD----TYEplpVYKPAATRAQiekALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 233 GLGVVDADYPYYLGMLGMHGT-KAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLT 311
Cdd:PRK11269 240 GWGAIPDDHPLMAGMVGLQTShRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 312 GDLNCLLPALqqplaIDGWRERSAA--LRAEHAW------------RYDHPGEA-IYAPLLLKQLSDRKPADSVVTTDVG 376
Cdd:PRK11269 320 SDAKAALELL-----VEVAREWKAAgrLPDRSAWvadcqerkrtllRKTHFDNVpIKPQRVYEEMNKAFGRDTCYVSTIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 377 QHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQ 456
Cdd:PRK11269 395 LSQIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNA 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513153969 457 RLGMVRQWQ---------QLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALD 509
Cdd:PRK11269 475 YLGLIRQAQrafdmdycvQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALE 536
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-537 |
2.01e-104 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 324.27 E-value: 2.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGG--VEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK08266 4 MTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 79 ITGLADALLDSIPIVAITGQVAAPFIGTDAFQ--EV-DVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLV 155
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 156 DIPKDIQMAQGDLD--PHFSTVADEMAFPQAeVAQALQMLAQSQQPMLYVGGGVgmAQAVPALREFLAVTRMPATCTLKG 233
Cdd:PRK08266 164 EMPWDVFGQRAPVAaaPPLRPAPPPAPDPDA-IAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPVVAFRSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 234 LGVVDADYPYYLGMLgmhgtkAANLAVQECDLLIAVGARFDDRVTgKLNTFAPHAKVIHMDIDPAELNKLrQAHIGLTGD 313
Cdd:PRK08266 241 RGIVSDRHPLGLNFA------AAYELWPQTDVVIGIGSRLELPTF-RWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 LNCLLPALQQPLAIDGWR--ERSAALRAEHAWRYD-----HPgEAIYapllLKQLSDRKPADSVVTTDVGQHQMWSAQHM 386
Cdd:PRK08266 313 AKAGTAALLDALSKAGSKrpSRRAELRELKAAARQriqavQP-QASY----LRAIREALPDDGIFVDELSQVGFASWFAF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 387 TYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQ 466
Cdd:PRK08266 388 PVYAPRTFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQK 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513153969 467 LFFQERYSETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSI--DELENVWPLVPPG 537
Cdd:PRK08266 468 RRFGGRVVASDLV-NPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVprGSEASPWPFIHPA 539
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
3-530 |
2.93e-99 |
|
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: 310.91 E-value: 2.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGL 82
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 83 ADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKDIq 162
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 163 maqgDLDPHFSTVADEMAFPQAEVA------QALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGV 236
Cdd:TIGR02418 160 ----VDSPVSVKAIPASYAPKLGAApddaidEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 237 VDAD-YPYYLGMLGMHGTKAANLAVQECDLLIAVG---ARFDDRVTGKLNTfaphAKVIHMDIDPAELNKLRQAHIGLTG 312
Cdd:TIGR02418 236 VSRElEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEND----ATIVHIDVEPAQIDNNYQPDLELVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 313 DLNCLLPALQQPL--------AIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQ 384
Cdd:TIGR02418 312 DIASTLDLLAERIpgyelppdALAILEDLKQQREALDRVPATLKQAHLHPLEIIKAMQAIVTDDVTVTVDMGSHYIWMAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP-LKIVLLDNqRLGMVRq 463
Cdd:TIGR02418 392 YFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNiVHIIWNDN-GYNMVE- 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513153969 464 wqqlfFQE--RYSETTLTD--NPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENV 530
Cdd:TIGR02418 470 -----FQEemKYQRSSGVDfgPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNP 535
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
3-537 |
1.26e-95 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 302.31 E-value: 1.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGL--SLACTKHSflVQSLDELPRVIAEAFQVANSGRpGPVLVDIP 158
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMfeDVAVYNHQ--IMSAENLPEIVNQAIRTAYEKK-GVAVLTIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 159 KDIQMAQGDLDPHFS--TVADEMAFPQAE-VAQALQMLAQSQQPMLYVggGVGMAQAVPALREFLAVTRMPATCTLKGLG 235
Cdd:PRK08611 163 DDLPAQKIKDTTNKTvdTFRPTVPSPKPKdIKKAAKLINKAKKPVILA--GLGAKHAKEELLAFAEKAKIPIIHTLPAKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 236 VVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRvtgklnTFAP-HAKVIHMDIDPAELNKLRQAHIGLTGDL 314
Cdd:PRK08611 241 IIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPkKAKAIQIDTDPANIGKRYPVNVGLVGDA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 315 NcllPALQQPLAIDGWRERSAALRA-----EHAWRYDHPGEAIYA-PL----LLKQLSDRKPADSVVTTDVGQHQMWSAQ 384
Cdd:PRK08611 315 K---KALHQLTENIKHVEDRRFLEAcqenmAKWWKWMEEDENNAStPIkperVMAAIQKIADDDAVLSVDVGTVTVWSAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:PRK08611 392 YLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYE 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513153969 465 QQLFFQERYsETTLTDnPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDelENVWPLvpPG 537
Cdd:PRK08611 472 QQAAGELEY-AIDLSD-MDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD--PNAAPL--PG 538
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-531 |
3.67e-95 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 300.62 E-value: 3.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGDLDPHFSTVADEM-AFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVVDA 239
Cdd:PRK08617 165 VVDAPVTSKAIAPLSKPKLgPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVISR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 240 D-YPYYLGMLGMHGTKAANLAVQECDLLIAVG---ARFDDRVTGKLNTfaphAKVIHMDIDPAELNKLRQAHIGLTGD-- 313
Cdd:PRK08617 245 ElEDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSEGD----ATIIHIDVLPAEIDNYYQPERELIGDia 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 --LNCLLPALQQPLAIDGWRE----RSAALRAEHAWRYDHPGEAIYaPL-LLKQLSDRKPADSVVTTDVGQHQMWSAQHM 386
Cdd:PRK08617 321 atLDLLAEKLDGLSLSPQSLEileeLRAQLEELAERPARLEEGAVH-PLrIIRALQDIVTDDTTVTVDVGSHYIWMARYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 387 TYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPL-KIVLLDNqRLGMVRqwq 465
Cdd:PRK08617 400 RSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIvHIIWNDG-HYNMVE--- 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 466 qlfFQE--RYSETTLTD--NPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVW 531
Cdd:PRK08617 476 ---FQEemKYGRSSGVDfgPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIK 542
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-522 |
1.19e-83 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 269.92 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 4 AQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLA 83
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 84 DALLDSIPIVAITGQVAAPFIGTD--AFQEV-DVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK07524 85 QAYADSIPMLVISSVNRRASLGKGrgKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGD-LDPHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGG-VGMAQAVPALREFLAVtrmPATCTLKGLGVVD 238
Cdd:PRK07524 165 VLAAPADhLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAGGGaLAAAAALRALAERLDA---PVALTINAKGLLP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 239 ADYPYYLGmlGMHGTKAANLAVQECDLLIAVG---ARFDDRVTGKlNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLN 315
Cdd:PRK07524 242 AGHPLLLG--ASQSLPAVRALIAEADVVLAVGtelGETDYDVYFD-GGFPLPGELIRIDIDPDQLARNYPPALALVGDAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 316 CLLPAL-----QQPLAIDGWRERSAALRAEHAWRYDhPGEAIYAPlLLKQLSDRKPADSVV--TTdvgqhQMWSAQHMTY 388
Cdd:PRK07524 319 AALEALlarlpGQAAAADWGAARVAALRQALRAEWD-PLTAAQVA-LLDTILAALPDAIFVgdST-----QPVYAGNLYF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 389 TRPEN---FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQwq 465
Cdd:PRK07524 392 DADAPrrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR-- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1513153969 466 qlFFQERYSETTLTD--NPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHV 522
Cdd:PRK07524 470 --YMVARDIEPVGVDpyTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-532 |
4.15e-83 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 269.01 E-value: 4.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 4 AQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLA 83
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 84 DALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRpGPVLVDIPKDIQM 163
Cdd:PRK06457 85 DAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDILR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 164 AQGDLDPHFSTVADEMAFPqAEVAQALQMLAQSQQPMLYVGGGV-GMAQAVPALREFLAVtrmPATCTLKGLGVVDADYP 242
Cdd:PRK06457 164 KSSEYKGSKNTEVGKVKYS-IDFSRAKELIKESEKPVLLIGGGTrGLGKEINRFAEKIGA---PIIYTLNGKGILPDLDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 243 YYLGMLGMHGTKAANLAVQECDLLIAVGARFDdrvtgKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCLL-PAL 321
Cdd:PRK06457 240 KVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLnIDI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 322 QQP-----LAIDGWRERSAALRAEHAWRYDHPgeaIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFIT 396
Cdd:PRK06457 315 EEKsdkfyEELKGKKEDWLDSISKQENSLDKP---MKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASGEQTFIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 397 SSGLGTMGFGLPAAVGAQVARPNDT-VICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSE 475
Cdd:PRK06457 392 SAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMGYPEWGV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513153969 476 TTLtdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWP 532
Cdd:PRK06457 472 DLY--NPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMP 526
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
1-515 |
4.90e-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: 264.42 E-value: 4.90e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:TIGR03457 2 MTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRpGPVLVDIPKD 160
Cdd:TIGR03457 82 AIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 IQMAQGDLDPHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVVDAD 240
Cdd:TIGR03457 161 YFYGEIDVEIPRPVRLDRGAGGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHNDSFPAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 241 YPYYLGMLGMHGTKAANLAVQECDLLIAVGAR---FDDRVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCL 317
Cdd:TIGR03457 241 HPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKVTVGICGDAKAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 318 LPALQQ---PLAIDGWR-ERSAALRAEH-AW-----RYDH----------------PGEAIYAPLLLKQLSDRKPADSVV 371
Cdd:TIGR03457 321 AAEILQrlaGKAGDANRaERKAKIQAERsAWeqelsEMTHerdpfsldmiveqrqeEGNWLHPRQVLRELEKAMPEDAIV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 372 TTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIV 451
Cdd:TIGR03457 401 STDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMTAVRHDIPVTAV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513153969 452 LLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQ 515
Cdd:TIGR03457 481 VFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPALKKAIAAQ 544
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
8-515 |
4.96e-77 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 254.15 E-value: 4.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 8 VHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALL 87
Cdd:PRK07525 13 VETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 88 DSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRpGPVLVDIPKDIQMAQGD 167
Cdd:PRK07525 93 AHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYFYGVID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 168 LD-PHFSTVaDEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVP---ALREFLAVtrmPATCTLKGLGVVDADYPY 243
Cdd:PRK07525 172 VEiPQPVRL-ERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEeckALAERLDA---PVACGYLHNDAFPGSHPL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 244 YLGMLGMHGTKAANLAVQECDLLIAVGARFDdrVTGKL-----NTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDL---- 314
Cdd:PRK07525 248 WVGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLpqygiDYWPKDAKIIQVDINPDRIGLTKKVSVGICGDAkava 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 315 NCLLPALQQPLAIDGWR-ERSAALRAEH-AW---------------------------RYDHPGEAIYAplllkqLSDRK 365
Cdd:PRK07525 326 RELLARLAERLAGDAGReERKALIAAEKsAWeqelsswdhedddpgtdwneeararkpDYMHPRQALRE------IQKAL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 366 PADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQ 445
Cdd:PRK07525 400 PEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVMTAVRHN 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 446 LPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQ 515
Cdd:PRK07525 480 WPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKRAIDAQ 549
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-525 |
8.96e-76 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 250.29 E-value: 8.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06546 3 KTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVrRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVAnSGRPGPVLVDIPK 159
Cdd:PRK06546 83 NGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTLPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQM--AQGDLDPHFSTVADEMAFP-QAEVAQALQMLAQSQQPMLYVGGGVGMAQA-VPALREFLAVtrmPATCTLKGLG 235
Cdd:PRK06546 162 DIADepAPEGFAPSVISPRRPTVVPdPAEVRALADAINEAKKVTLFAGAGVRGAHAeVLALAEKIKA---PVGHSLRGKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 236 VVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFddrvtgKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD-- 313
Cdd:PRK06546 239 WIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDva 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 314 --LNCLLPALQQPlaidgwRERS--AALRAEHAWRYDHPGEAI-------------YAPLLLKQLSDRkpaDSVVTTDVG 376
Cdd:PRK06546 313 etIRALLPLVKEK------TDRRflDRMLKKHARKLEKVVGAYtrkvekhtpihpeYVASILDELAAD---DAVFTVDTG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 377 QHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQ 456
Cdd:PRK06546 384 MCNVWAARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNS 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513153969 457 RLGMVRqwQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSID 525
Cdd:PRK06546 464 TLGMVK--LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-526 |
3.50e-74 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 246.21 E-value: 3.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFG--YPGGAIMpvydALYDGGVEHLLCRHEQ-GAAMAAiGYARATGKTGVCIATSGPGATN 77
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSALFL----AAEAIGIRQIAYRTENaGGAMAD-GYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 78 LITGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKhsfLVQSLDELPRV---IAEAFQVANSGRPGPVL 154
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTK---WVRRVTVAERIddyVDQAFTAATSGRPGPVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 155 VDIPKDIQMAQGDlDPHFSTVADEMAFP-------QAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPA 227
Cdd:PRK06112 166 LLLPADLLTAAAA-APAAPRSNSLGHFPldrtvpaPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 228 TCTLKGLGVVDADYPYYLGMLG-MHGTKAANL----AVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDPAELNK 302
Cdd:PRK06112 245 ATTNMGKGAVDETHPLSLGVVGsLMGPRSPGRhlrdLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 303 LRQAhIGLTGDLNCLLPALQ---QPLAIDGWRERSAAL-----------RAEHAWRYDHPGEAIYAPLLLKQLSDRKPAD 368
Cdd:PRK06112 325 NYEA-LRLVGDARLTLAALTdalRGRDLAARAGRRAALepaiaagreahREDSAPVALSDASPIRPERIMAELQAVLTGD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 369 SVVTTDVGQHQMWSAQHMTYTRP-ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP 447
Cdd:PRK06112 404 TIVVADASYSSIWVANFLTARRAgMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513153969 448 LKIVLLDNQRLGMVRQWQQLFFQErYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDE 526
Cdd:PRK06112 484 VTIVVLNNGILGFQKHAETVKFGT-HTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDP 561
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
7-527 |
1.64e-73 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 243.74 E-value: 1.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 7 VVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADA 85
Cdd:PRK07064 9 IAAFLEQCGVKTAFGVISIHNMPILDAIGRrGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGALVEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 86 LLDSIPIVAITGQVAAPFIGTDA--FQEV-DVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKDIQ 162
Cdd:PRK07064 89 LTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPIDIQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 163 MAQGDLDPHFSTVADEMAFP-QAEVAQALQMLAQSQQPMLYVGGGVgmAQAVPALREfLAVTRMPATCTLKGLGVVDADY 241
Cdd:PRK07064 169 AAEIELPDDLAPVHVAVPEPdAAAVAELAERLAAARRPLLWLGGGA--RHAGAEVKR-LVDLGFGVVTSTQGRGVVPEDH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 242 PYYLGMLgmHGTKAANLAVQECDLLIAVGARFDDRVTGKlNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD----LNCL 317
Cdd:PRK07064 246 PASLGAF--NNSAAVEALYKTCDLLLVVGSRLRGNETLK-YSLALPRPLIRVDADAAADGRGYPNDLFVHGDaarvLARL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 318 LPALQQPLAIDGwrERSAALRAEHAWRYDHPGEAI--YApLLLKQLSDRKPADSVVTTDVG-QHQMWSAQHMTYTRPENF 394
Cdd:PRK07064 323 ADRLEGRLSVDP--AFAADLRAAREAAVADLRKGLgpYA-KLVDALRAALPRDGNWVRDVTiSNSTWGNRLLPIFEPRAN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 395 ITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYS 474
Cdd:PRK07064 400 VHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRRY 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1513153969 475 ETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHV---SIDEL 527
Cdd:PRK07064 479 YVELH-TPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVdmlSIGPF 533
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
7-510 |
3.38e-72 |
|
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: 240.89 E-value: 3.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 7 VVHALRTQGVDTVFGYPGGAIMPVYDALYD--GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLAD 84
Cdd:TIGR02720 5 VLKVLEAWGVDHIYGIPGGSFNSTMDALSAerDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 85 ALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSgRPGPVLVDIPKDIQMA 164
Cdd:TIGR02720 85 AKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVDFGWQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 165 QGDLDPHFSTVADEMAF----PQAE-VAQALQMLAQSQQPMLYVG-GGVGMAQAVPALREFLavtRMPATCTLKGLGVVD 238
Cdd:TIGR02720 164 EIPDNDYYASSVSYQTPllpaPDVEaVTRAVQTLKAAERPVIYYGiGARKAGEELEALSEKL---KIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 239 ADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDdrVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCLL 318
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 319 PALqqpLAIDGWRERSAALRAEHA----WR--YDHPGEAIYAPLLLKQLSD--RKPA--DSVVTTDVGQHQMWSAQHMTY 388
Cdd:TIGR02720 319 AAI---LAQVEPRESTPWWQANVAnvknWRayLASLEDKTEGPLQAYQVYRaiNKIAedDAIYSIDVGDININSNRHLKM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:TIGR02720 396 TPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIKDEQEDT 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1513153969 469 FQErYSETTLTDnPDFLTLASAFGIPGQHITRKDQVEAALDT 510
Cdd:TIGR02720 476 NQP-LIGVDFND-ADFAKIAEGVGAVGFRVNKIEQLPAVFEQ 515
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
4-532 |
2.28e-70 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 236.04 E-value: 2.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 4 AQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGL 82
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRrMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 83 ADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVdIPKDI- 161
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVV-LPGDVa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 162 -QMAQGDLDPHFSTVADEMAFP-QAEVAQALQMLAQSQQPMLYVGGGVGMAQA-VPALREFLAVtrmPATCTLKGLGVVD 238
Cdd:PRK09124 165 lKPAPERATPHWYHAPQPVVTPaEEELRKLAALLNGSSNITLLCGSGCAGAHDeLVALAETLKA---PIVHALRGKEHVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 239 ADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRvtgklNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGD----L 314
Cdd:PRK09124 242 YDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDvkatL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 315 NCLLPALQ---QPLAIDGWRERSAALRAE--HAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:PRK09124 317 AALLPLLEektDRKFLDKALEHYRKARKGldDLAVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQlff 469
Cdd:PRK09124 397 GKRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMK--- 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513153969 470 QERYSET-TLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDELENVWP 532
Cdd:PRK09124 474 AGGYLTDgTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMP 537
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
5-159 |
9.79e-69 |
|
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: 218.17 E-value: 9.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 5 QWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLAD 84
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1513153969 85 ALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-548 |
1.16e-68 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 232.11 E-value: 1.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK08273 3 QTVADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 79 ITGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLsLACTKHSFLVQ--SLDELPRVIAEAFQVANSGRpGPVLVD 156
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSL-FKDVAGAFVQMvtVPEQLRHLVDRAVRTALAER-TVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 157 IPKDIQMAQGDLDPH-FSTVADEMAF-------PQAEVAQALQMLAQSQQPMLYVGGGV-GMAQAVPALREFLA--VTRm 225
Cdd:PRK08273 161 LPNDVQELEYEPPPHaHGTVHSGVGYtrprvvpYDEDLRRAAEVLNAGRKVAILVGAGAlGATDEVIAVAERLGagVAK- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 226 patcTLKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFddrvtgKLNTFAP---HAKVIHMDIDPAELNK 302
Cdd:PRK08273 240 ----ALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFLPkegQARGVQIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 303 LRQAHIGLTGD----LNCLLPALQQPlAIDGWRERSAALRAEhaW------RYDHPGEAIYAPLLLKQLSDRKPADSVVT 372
Cdd:PRK08273 310 RYPMEVNLVGDaaetLRALLPLLERK-KDRSWRERIEKWVAR--WwetleaRAMVPADPVNPQRVFWELSPRLPDNAILT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 373 TDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN-VQELGTVKR-----KQL 446
Cdd:PRK08273 387 ADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKywrqwSDP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 447 PLKIVLLDNQRLGMVrQWQQLFFQ--ERYSET-TLTDNPdFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVS 523
Cdd:PRK08273 467 RLIVLVLNNRDLNQV-TWEQRVMEgdPKFEASqDLPDVP-YARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVK 544
|
570 580
....*....|....*....|....*
gi 1513153969 524 IDelENVwPLVPPGASNSEMLEKLS 548
Cdd:PRK08273 545 TD--PNV-PPLPPHITLEQAKAFAS 566
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
1-532 |
3.81e-67 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 226.53 E-value: 3.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK05858 5 GHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:PRK05858 85 AMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 161 --IQMAQGDLDPHFSTVADEMAFPQ-AEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVV 237
Cdd:PRK05858 165 haFSMADDDGRPGALTELPAGPTPDpDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 238 DADYPYYLgmlgmhgTKAANLAVQECDLLIAVGARFDDRVTgkLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCL 317
Cdd:PRK05858 245 PADHPLAF-------SRARGKALGEADVVLVVGVPMDFRLG--FGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 318 LPAL----QQPLAIDGW----RERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:PRK05858 316 LSALagagGDRTDHQGWieelRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK05858 396 RPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKHPMEALY 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513153969 470 ----------QERYSEttltdnpdfltLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSIDElENVWP 532
Cdd:PRK05858 476 gydvaadlrpGTRYDE-----------VVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDP-SVAYP 536
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
3-169 |
2.19e-63 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 204.78 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITG 81
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 82 LADALLDSIPIVAITGQVAAPFIGTDAFQ-EVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD 160
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*....
gi 1513153969 161 IQMAQGDLD 169
Cdd:pfam02776 161 VLLEEVDED 169
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
374-522 |
1.10e-61 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 199.73 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 374 DVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLL 453
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513153969 454 DNQRLGMVRQWQQLFFQERYSETT--LTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHV 522
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSgkILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
357-524 |
1.40e-53 |
|
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: 178.99 E-value: 1.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 357 LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 437 ELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQG 516
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLS-NPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 1513153969 517 PYLLHVSI 524
Cdd:cd00568 161 PALIEVKT 168
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
186-321 |
1.49e-52 |
|
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: 175.06 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 186 VAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATCTLKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDL 265
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1513153969 266 LIAVGARFDD-RVTGKLNTFAPHAKVIHMDIDPAELNKLRQAHIGLTGDLNCLLPAL 321
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
1-508 |
3.03e-51 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 184.24 E-value: 3.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPggaIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARAT-GKT-GVCIATSGPGATNL 78
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATsGERvGVFAVQYGPGAENA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 79 ITGLADALLDSIPIVAITG-------QVAAPFIGTDAFQEVdvlglslacTKHSFLVQSLDELPRVIAEAFQVANSGRPG 151
Cdd:PRK06154 97 FGGVAQAYGDSVPVLFLPTgyprgstDVAPNFESLRNYRHI---------TKWCEQVTLPDEVPELMRRAFTRLRNGRPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 152 PVLVDIPKDIQMAQGDLDP--HFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATC 229
Cdd:PRK06154 168 PVVLELPVDVLAEELDELPldHRPSRRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 230 TLKGLGVVDADYPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGklnTFAPHAK-VIHMDIDPAELNKLRQAHI 308
Cdd:PRK06154 248 TLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYG---LPMPEGKtIIHSTLDDADLNKDYPIDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 309 GLTGDLNCLLPALQQPLA--IDGWRERSAALRAE-----HAWRydhpgeAIYAPLL---------------LKQLSDrkP 366
Cdd:PRK06154 325 GLVGDAALVLKQMIEELRrrVGPDRGRAQQVAAEieavrAAWL------AKWMPKLtsdstpinpyrvvweLQHAVD--I 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 367 ADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQL 446
Cdd:PRK06154 397 KTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERI 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1513153969 447 PLKIVLLDNQRLGMVRQWQQLfFQERYSETTLTDnpDFLTLASAFGIPGQHITRKDQVEAAL 508
Cdd:PRK06154 477 PILTILLNNFSMGGYDKVMPV-STTKYRATDISG--DYAAIARALGGYGERVEDPEMLVPAL 535
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
2-165 |
5.44e-49 |
|
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: 166.96 E-value: 5.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 2 NGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 81 GLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRpGPVLVDIPKD 160
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....*
gi 1513153969 161 IQMAQ 165
Cdd:cd07039 160 VQDAP 164
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
7-525 |
1.94e-48 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 175.91 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 7 VVHALRTQGVDTVFGYPGGAIMPVYDALYDGgVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADAL 86
Cdd:PRK07092 18 TIDLLRRFGITTVFGNPGSTELPFLRDFPDD-FRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 87 LDSIPIVAITGQVAAPFIGTDAF-QEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPKD--IQM 163
Cdd:PRK07092 97 KNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDdwDQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 164 AQgDLDPHfsTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQA---VPALREFLA----VTRMPATCTLKglgv 236
Cdd:PRK07092 177 AE-PLPAR--TVSSAVRPDPAALARLGDALDAARRPALVVGPAVDRAGAwddAVRLAERHRapvwVAPMSGRCSFP---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 237 vdADYPYYLGMLgmHGTKAA-NLAVQECDLLIAVGAR-FDDRVTGKLNTFAPHAKVIHMDIDPAELNKlrqAHIG--LTG 312
Cdd:PRK07092 250 --EDHPLFAGFL--PASREKiSALLDGHDLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDDPGEAAW---APMGdaIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 313 DLNcllPALQQPLAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQ--MWsaQHMTYTR 390
Cdd:PRK07092 323 DIR---LALRDLLALLPPSARPAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRpaMQ--EHLPMRR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 391 PENFIT--SSGLGtmgFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:PRK07092 398 QGSFYTmaSGGLG---YGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPVF 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1513153969 469 fqeRYSETTLTDNP--DFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSID 525
Cdd:PRK07092 475 ---GVRDVPGLDLPglDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
352-525 |
9.79e-48 |
|
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: 163.86 E-value: 9.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 352 IYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSF 431
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGMVrQWQQLFFQERYSETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFI-KWEQEVMGQPEFGVDLP-NPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....
gi 1513153969 512 LSSQGPYLLHVSID 525
Cdd:cd02014 160 LAADGPVVIDVVTD 173
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
3-526 |
5.85e-46 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 169.78 E-value: 5.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPGgaiMPVYD--ALYDG-GVEHLLCRHEQGA--AMAAIGYAraTGKTGVCIATSGPGATN 77
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAeGIRYIGFRHEQSAgnAAAAAGFL--TQKPGVCLTVSAPGFLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 78 LITGLADALLDSIPIVAITGQVAAPFIGTDA--FQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLV 155
Cdd:PRK09259 87 GLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 156 DIPKDI-------QMAQGDL----DPhfstvADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTR 224
Cdd:PRK09259 167 DLPAKVlaqtmdaDEALTSLvkvvDP-----APAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 225 MPATCTLKGLGVVDADYPyylgmlgmHGTKAA-NLAVQECDLLIAVGARFDDRVT-GKLNTFAPHAKVIHMDIDPAELNK 302
Cdd:PRK09259 242 IPFLPMSMAKGLLPDTHP--------QSAAAArSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQIDIEPQEIDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 303 LRQAHIGLTGDLNCLLPALQQPLAiDGWRERSAALRAEHAWRYDHpGEAIYAPLLLKQLS--DRKPADSVVTTDVGQHQM 380
Cdd:PRK09259 314 NRPIAAPVVGDIGSVMQALLAGLK-QNTFKAPAEWLDALAERKEK-NAAKMAEKLSTDTQpmNFYNALGAIRDVLKENPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 381 WS-----AQHMTYTR-------PENFITSSGLGTMGFGLPAAVGAQVA--RPndtVICISGDGSFMMNVQELGTVKRKQL 446
Cdd:PRK09259 392 IYlvnegANTLDLARniidmykPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGMEVETICRYNL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 447 PLKIVLLDNQrlGMVRQWQQLFFQER-YSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSID 525
Cdd:PRK09259 469 PVTVVIFNNG--GIYRGDDVNLSGAGdPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINVVID 546
|
.
gi 1513153969 526 E 526
Cdd:PRK09259 547 P 547
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-525 |
6.92e-43 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 161.32 E-value: 6.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALYDGGVEH------LLCRHEQGAAMAAIGYARATGKTGVCIATSGPG 74
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpefVICPHEIVAISMAHGYALVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 75 ATNLITGLADALLDSIPIVAITGqvAAPFIGTDAF----------QEV-DVLGLSLACTKHSFLVQSLDELPRVIAEAFQ 143
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFAG--RSPYTEEGELgsrntrihwtQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 144 VANSGRPGPVLVDIPKDIQMAQGD---LDPHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFl 220
Cdd:PRK08327 165 IAMSEPKGPVYLTLPREVLAEEVPevkADAGRQMAPAPPAPDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASLRRL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 221 avtrmpatCTLKGLGVVD---------ADYPYYLGmlgmhGTKAANLAvqECDLLIAVGArfDDRVTGKLNTFAPHAKVI 291
Cdd:PRK08327 244 --------AEELAIPVVEyagevvnypSDHPLHLG-----PDPRADLA--EADLVLVVDS--DVPWIPKKIRPDADARVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 292 HMDIDPA-ELNKLR--QAHIGLTGDLNCLLPALQQPL-------------AIDGWRERSAALRAEH--AWRYDHPGEAIY 353
Cdd:PRK08327 307 QIDVDPLkSRIPLWgfPCDLCIQADTSTALDQLEERLkslasaerrrarrRRAAVRELRIRQEAAKraEIERLKDRGPIT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 354 APLLLKQLSDRKPADSVVTTDVGQHQmwsaQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMM 433
Cdd:PRK08327 387 PAYLSYCLGEVADEYDAIVTEYPFVP----RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 434 NVQE--LGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE-------RYSETTLTDNPDFLTLASAFGIPGQHITRKDQV 504
Cdd:PRK08327 463 GVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEgyaarkgTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEEL 542
|
570 580
....*....|....*....|....*
gi 1513153969 505 EAAL----DTMLSSQGPYLLHVSID 525
Cdd:PRK08327 543 KGALrralAAVRKGRRSAVLDVIVD 567
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
4-526 |
1.45e-42 |
|
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: 159.94 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 4 AQWVVHALRTQGVDTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIaTSGPGATNLITGL 82
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEaHPGIRWVGCCNELNAGYAADGYARVNGLGALVT-TYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 83 ADALLDSIPIVAITGqvaAPfiGTDAFQEVDVLGLSLActKHSFLVQ------------SLD------ELPRVIAEAFQv 144
Cdd:COG3961 87 AGAYAERVPVVHIVG---AP--GTRAQRRGPLLHHTLG--DGDFDHFlrmfeevtvaqaVLTpenaaaEIDRVLAAALR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 145 anSGRPgpVLVDIPKDIQMAQGDLDPHFSTVADEMAFPQAE---VAQALQMLAQSQQPMLYVGGGVGMAQAVPALREFLA 221
Cdd:COG3961 159 --EKRP--VYIELPRDVADAPIEPPEAPLPLPPPASDPAALaaaVAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 222 VTRMPATCTLKGLGVVDADYPYYLGM----LGMHGTKAAnlaVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHMDIDP 297
Cdd:COG3961 235 KTGIPVATTLLGKSVLDESHPQFIGTyagaASSPEVREY---VENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 298 AELNKLRQAHIgltgDLNCLLPALQQplAIDGWRERSAALRAEHAWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQ 377
Cdd:COG3961 312 VRVGGHIYPGV----SLADFLEALAE--LLKKRSAPLPAPAPPPPPPPAAPDAPLTQDRLWQRLQAFLDPGDIVVADTGT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 378 hQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQ- 456
Cdd:COG3961 386 -SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDg 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 457 ----R--LGM------VRQWqqlffqeRYSEttltdnpdfltLASAFGiPGQHITRK----DQVEAALDTMLSSQ-GPYL 519
Cdd:COG3961 465 ytieRaiHGPdgpyndIANW-------DYAK-----------LPEAFG-GGNALGFRvtteGELEEALAAAEANTdRLTL 525
|
....*..
gi 1513153969 520 LHVSIDE 526
Cdd:COG3961 526 IEVVLDK 532
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-159 |
4.37e-36 |
|
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: 131.70 E-value: 4.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 7 VVHALRTQGVDTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARATGKtGVCIATSGPGATNLITGLADA 85
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1513153969 86 LLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGrPGPVLVDIPK 159
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
357-530 |
1.17e-35 |
|
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: 131.26 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 357 LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 437 ELGTVKRKQLPLKIVLLDNQRLGMVRqWQQLFFQERYSETTLTdNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQG 516
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDFG-NPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
170
....*....|....
gi 1513153969 517 PYLLHVSIDELENV 530
Cdd:cd02010 162 VHVIDCPVDYSENI 175
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-524 |
3.67e-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: 118.85 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 357 LLKQLSDRKPADSVV----TTDVGQhqMWsaQHMTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFM 432
Cdd:cd02002 6 LAAALAAALPEDAIIvdeaVTNGLP--LR--DQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 433 MNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQER-----YSETTLTD-NPDFLTLASAFGIPGQHITRKDQVEA 506
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGpgenaPDGLDLLDpGIDFAAIAKAFGVEAERVETPEELDE 160
|
170
....*....|....*...
gi 1513153969 507 ALDTMLSSQGPYLLHVSI 524
Cdd:cd02002 161 ALREALAEGGPALIEVVV 178
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
1-524 |
9.39e-30 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 122.65 E-value: 9.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDALyDG--GVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAAL-DRvpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 79 ITGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGlsLACTKHSFL--VQSLDELPRVIAEAFQVANSGRPGPVLVD 156
Cdd:PRK07586 80 LANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEA--LARPVSGWVrrSESAADVAADAAAAVAAARGAPGQVATLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 157 IPKDIQMAQGDLDPHFSTVADEMAFPQAEVAQALQMLAQSQQPMLYVGGGvgmaqavpALRE--FLAVTRMPATCTLK-- 232
Cdd:PRK07586 158 LPADVAWSEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGR--------ALRErgLAAAARIAAATGARll 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 233 ----------GLGVVDADYPYYLGmlgmhgtKAANLAVQECDLLIAVGARfdDRVT-----GKLNTFAPHAKVIHMDIDP 297
Cdd:PRK07586 230 aetfparmerGAGRPAVERLPYFA-------EQALAQLAGVRHLVLVGAK--APVAffaypGKPSRLVPEGCEVHTLAGP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 298 AE-----LNKLRQAhIGLTGDlnclLPALQQPLAidgWRERSAALRAEHAwrydhpGEAIYAPLllkqlsdrkPADSVVT 372
Cdd:PRK07586 301 GEdaaaaLEALADA-LGAKPA----APPLAAPAR---PPLPTGALTPEAI------AQVIAALL---------PENAIVV 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 373 TDVGQHQMWSAQHMTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVL 452
Cdd:PRK07586 358 DESITSGRGFFPATAGAAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 453 LDN----------QRLGMVRQwqqlffQERYSETTLTDNP--DFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLL 520
Cdd:PRK07586 437 FANrayailrgelARVGAGNP------GPRALDMLDLDDPdlDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLI 510
|
....
gi 1513153969 521 HVSI 524
Cdd:PRK07586 511 EAVV 514
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-524 |
6.77e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 114.20 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 1 MNGAQWVVHALRTQGVDTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALdRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 80 TGLADALLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLDELPRVIAEAFQVANSGRPGPVLVDIPK 159
Cdd:PRK12474 85 ANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 160 DIQMaqgdlDPHFSTVADEMAFPQAEVAQAL-----QMLAQSQQPMLYVGGGVGMAQAVPALREFLAVTRMPATC----- 229
Cdd:PRK12474 165 DVAW-----NEAAYAAQPLRGIGPAPVAAETveriaALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCdtfap 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 230 -TLKGLGVVD-ADYPYYLGMLGMHgtkaanlaVQECDLLIAVGARfddrvtGKLNTFAPHAKVIHMDIDPAELNKLRQAH 307
Cdd:PRK12474 240 rIERGAGRVPiERIPYFHEQITAF--------LKDVEQLVLVGAK------PPVSFFAYPGKPSWGAPPGCEIVYLAQPD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 308 IGLTGDLNCLLPALQQPlaidgwreRSAALRAEHAWRyDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMT 387
Cdd:PRK12474 306 EDLAQALQDLADAVDAP--------AEPAARTPLALP-ALPKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFDMSYD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 388 YTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR-QWQQ 466
Cdd:PRK12474 377 RARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNgELQR 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1513153969 467 LFFQE--RYSETTLT-DNP--DFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSI 524
Cdd:PRK12474 456 VGAQGagRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
357-525 |
1.18e-25 |
|
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: 103.38 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 357 LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 437 ELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQG 516
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGK 163
|
....*....
gi 1513153969 517 PYLLHVSID 525
Cdd:cd02004 164 PALINVIID 172
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
358-508 |
2.72e-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: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 358 LKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQE 437
Cdd:cd02013 10 LRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMME 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1513153969 438 LGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLtDNPDFLTLASAFGIPGQHITRKDQVEAAL 508
Cdd:cd02013 90 IMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTEL-ESESFAKIAEACGAKGITVDKPEDVGPAL 159
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
391-514 |
2.34e-18 |
|
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: 82.97 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 391 PEN--FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQ-----RL--GMV 461
Cdd:cd02005 38 PKGtrFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDgytieRAihGPE 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1513153969 462 RQWQQLffqerysettltDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSS 514
Cdd:cd02005 118 ASYNDI------------ANWNYTKLPEVFGGGGGGLSFRVKTEGELDEALKD 158
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
7-158 |
1.62e-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: 79.85 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 7 VVHALRTQGVDTVFGYPGGAIMP-VYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADA 85
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSRSAPlALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513153969 86 LLDSIPIVAITGQVAAPFIGTDAFQEVDVLGLSLACTKHSFLVQS------LDELPRVIAEAFQVANSGRPGPVLVDIP 158
Cdd:cd07037 83 YYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPpeddddLWYLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
366-525 |
3.83e-15 |
|
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: 74.26 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 366 PADSVVTTDVGQ-----HQMWSAQ-----HMTYtrpenfitssGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNV 435
Cdd:cd02003 13 GDDDVVINAAGSlpgdlHKLWRARtpggyHLEY----------GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 436 QELGTVKRKQLPLKIVLLDNQRLGMVRQWQ-----QLF---FQERYSETTLTDNP----DFLTLASAFGIPGQHITRKDQ 503
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQestgsGSFgteFRDRDQESGQLDGAllpvDFAANARSLGARVEKVKTIEE 162
|
170 180
....*....|....*....|..
gi 1513153969 504 VEAALDTMLSSQGPYLLHVSID 525
Cdd:cd02003 163 LKAALAKAKASDRTTVIVIKTD 184
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
368-530 |
4.04e-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: 74.24 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 368 DSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP 447
Cdd:cd02006 24 DVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 448 LKIVLLDNQRLGMVRQWQQLF---------FQERYSETTLTDNPDFLTLASAFGIPGQHITRKDQVEAALDT----MLSS 514
Cdd:cd02006 104 YIHVLVNNAYLGLIRQAQRAFdmdyqvnlaFENINSSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQakklMAEH 183
|
170
....*....|....*.
gi 1513153969 515 QGPYLLHVSIDELENV 530
Cdd:cd02006 184 RVPVVVEAILERVTNI 199
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
357-526 |
1.96e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 69.09 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 357 LLKQLSDRKPADSVVTTDVG--QHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN 434
Cdd:PRK06163 18 LTCRLVAKLKDEEAVIGGIGntNFDLWAAGQ----RPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 435 VQELGTV-KRKQLPLKIVLLDNQrlgmvrqwqqlFFQERYSETTLT-DNPDFLTLASAFGIPGQHITRKDQ-VEAALDTM 511
Cdd:PRK06163 91 LGALGTIaALAPKNLTIIVMDNG-----------VYQITGGQPTLTsQTVDVVAIARGAGLENSHWAADEAhFEALVDQA 159
|
170
....*....|....*
gi 1513153969 512 LSSQGPYLLHVSIDE 526
Cdd:PRK06163 160 LSGPGPSFIAVRIDD 174
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
5-97 |
6.46e-13 |
|
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: 66.75 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 5 QWVVHALRTQGVDTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGkTGVCIATSGPGATNLITGLA 83
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90
....*....|....
gi 1513153969 84 DALLDSIPIVAITG 97
Cdd:cd07038 80 GAYAEHVPVVHIVG 93
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
15-455 |
6.50e-09 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 58.56 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 15 GVDTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGkTGVCIATSGPGATNLITGLADALLDSIPIV 93
Cdd:PLN02573 30 GVTDVFSVPGDFNLTLLDHLiAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 94 AITGQVAAPFIGTD-----------------AFQEVdvlglslacTKHSFLVQSLDE----LPRVIAEAFQvansgRPGP 152
Cdd:PLN02573 109 CIVGGPNSNDYGTNrilhhtiglpdfsqelrCFQTV---------TCYQAVINNLEDahelIDTAISTALK-----ESKP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 153 V-------LVDIPKdiqmaqgdldPHFS----------TVADEMAFpQAEVAQALQMLAQSQQPMLYVGGGVGMAQAVPA 215
Cdd:PLN02573 175 VyisvscnLAAIPH----------PTFSrepvpffltpRLSNKMSL-EAAVEAAAEFLNKAVKPVLVGGPKLRVAKACKA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 216 LREFL-----AVTRMPATctlKGLgvVDADYPYYLGML-GMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAK 289
Cdd:PLN02573 244 FVELAdasgyPVAVMPSA---KGL--VPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 290 VIHMDIDpaelnklrQAHIGLTGDLNCL-----LPALQQPL-----AIDGWRE----RSAALRAEhawrydhPGEAIYAP 355
Cdd:PLN02573 319 AIIVQPD--------RVTIGNGPAFGCVlmkdfLEALAKRVkknttAYENYKRifvpEGEPLKSE-------PGEPLRVN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 356 LLLKQLSDRKPADSVVTTDVGQHqmW-SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVI-CIsGDGSFMM 433
Cdd:PLN02573 384 VLFKHIQKMLSGDTAVIAETGDS--WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIaCI-GDGSFQV 460
|
490 500
....*....|....*....|..
gi 1513153969 434 NVQELGTVKRKQLPLKIVLLDN 455
Cdd:PLN02573 461 TAQDVSTMIRCGQKSIIFLINN 482
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
390-524 |
1.14e-08 |
|
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: 54.42 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 390 RPENFITssgLGTMGFGLPAAVGAQVARPnDTVICISGDGSFMMNVQELGTV-KRKQLPLKIVLLDNQRlgmvrqwqqlf 468
Cdd:cd02001 34 RDGHFYM---LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAgEFTPLNLILVVLDNRA----------- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 469 fqerYSET----TLTDNPDFLTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSI 524
Cdd:cd02001 99 ----YGSTggqpTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPI 154
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
358-524 |
1.46e-08 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 54.63 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 358 LKQLSDRKPADSVV--TTDVGQHQMWSAQHM-TYTRPENFITssgLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN 434
Cdd:cd03371 5 IEIVLSRAPATAAVvsTTGMTSRELFELRDRpGGGHAQDFLT---VGSMGHASQIALGIALARPDRKVVCIDGDGAALMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 435 VQELGTVKRKQLP-LKIVLLDNQRLGMVRqwqqlffqerySETTLTDNPDFLTLASAFGIPG-QHITRKDQVEAALDTML 512
Cdd:cd03371 82 MGGLATIGGLAPAnLIHIVLNNGAHDSVG-----------GQPTVSFDVSLPAIAKACGYRAvYEVPSLEELVAALAKAL 150
|
170
....*....|..
gi 1513153969 513 SSQGPYLLHVSI 524
Cdd:cd03371 151 AADGPAFIEVKV 162
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
361-525 |
1.56e-07 |
|
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: 51.52 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 361 LSDRKpaDSVVTTDVG--QHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPnDTVICISGDGSFMMNVQEL 438
Cdd:cd03372 9 IADLK--DELVVSNIGfpSKELYAAGD----RPLNFYM---LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 439 GTVKrKQLP--LKIVLLDNqrlgmvRQWQQLFFQERYSettlTDNPDFLTLASAFGIpgQHITRKDQVEAALDTM-LSSQ 515
Cdd:cd03372 79 ATIA-AEKPknLIIVVLDN------GAYGSTGNQPTHA----GKKTDLEAVAKACGL--DNVATVASEEAFEKAVeQALD 145
|
170
....*....|
gi 1513153969 516 GPYLLHVSID 525
Cdd:cd03372 146 GPSFIHVKIK 155
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
410-525 |
6.06e-07 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 49.52 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 410 AVGAQVARpNDTVICISGDGSFM--MNVqeLGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQ---ERYSETTLtdNPDF 484
Cdd:cd02009 60 ALGIALAT-DKPTVLLTGDLSFLhdLNG--LLLGKQEPLNLTIVVINNNGGGIFSLLPQASFEdefERLFGTPQ--GLDF 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1513153969 485 LTLASAFGIPGQHITRKDQVEAALDTMLSSQGPYLLHVSID 525
Cdd:cd02009 135 EHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
401-460 |
2.77e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 42.91 E-value: 2.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513153969 401 GTMGFGLPAAVGAQVARPNDTVICISGDGS--------FMMNVqelgtvkRKQLPLKIVLLDNQRLGM 460
Cdd:PRK11867 69 TIHGRALAIATGLKLANPDLTVIVVTGDGDalaiggnhFIHAL-------RRNIDITYILFNNQIYGL 129
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
42-96 |
1.45e-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: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1513153969 42 LLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSIPIVAIT 96
Cdd:PLN02980 343 IACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLT 397
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
3-156 |
2.26e-03 |
|
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: 39.02 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 3 GAQWVVHALRTQGVDTVFGYPG---GAIMPVYDALYDGGVEHLLCR--HEQGAAMAAIGyARATGKTGVCiATSGPGATN 77
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAKAVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 78 LITGLADALLDSIPIVAITGQ--VAAP-FIGTDAfQEVDvlglSLACTKHSFLV---QSLDELPRVIAEAFQVA-NSGRP 150
Cdd:cd07034 79 MAEALYLAAGAELPLVIVVAQrpGPSTgLPKPDQ-SDLM----AARYGGHPWPVlapSSVQEAFDLALEAFELAeKYRLP 153
|
....*.
gi 1513153969 151 GPVLVD 156
Cdd:cd07034 154 VIVLSD 159
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
394-460 |
2.95e-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: 39.05 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513153969 394 FITSSGL-GTMGFGLPAAVGAQVARPNDTVICISGDG-SFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:cd03375 43 YFNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYGL 111
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
365-460 |
3.75e-03 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 39.35 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513153969 365 KPADSVVTTDVGQHqmwsaqhmtyTRPENFITSSGLGTM-GFGLPAAVGAQVARPNDTVICISGDG-SFMMNVQELGTVK 442
Cdd:PRK11866 32 PPENVVVVSGIGCS----------SNLPEFLNTYGIHGIhGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAA 101
|
90
....*....|....*...
gi 1513153969 443 RKQLPLKIVLLDNQRLGM 460
Cdd:PRK11866 102 RRNVDITYIVSNNQVYGL 119
|
|
| |
