|
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: 1237.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08978 1 MNGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK08978 81 GLADALLDSVPVVAITGQVSSPLIGTDAFQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVDIPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IQLASGTLEPYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAVEAD 240
Cdd:PRK08978 161 IQLAEGELEPHLTTVENEPAFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLKGLGAVEAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 241 YPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPA 320
Cdd:PRK08978 241 HPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDRVTGKLNTFAPHAKVIHLDIDPAEINKLRQAHVALQGDLNALLPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 321 LQQSLKIDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGL 400
Cdd:PRK08978 321 LQQPLNIDAWRQHCAQLRAEHAWRYDHPGEAIYAPALLKQLSDRKPADTVVTTDVGQHQMWVAQHMRFTRPENFITSSGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 401 GTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTD 480
Cdd:PRK08978 401 GTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLGMVRQWQQLFFDERYSETDLSD 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489937867 481 NPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS 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: 748.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:COG0028 3 MTGADALVEALEAEGVETVFGVPGGAILPLYDALRRqSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:COG0028 83 TGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGTLEPYFTTVKNVEVFPHAD---VEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGA 236
Cdd:COG0028 163 DVQAAEAEEEPAPPELRGYRPRPAPDpeaIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGKGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 237 VEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:COG0028 243 FPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGDAKA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPALQQSLK-----IDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRP 391
Cdd:COG0028 323 VLAALLEALEpraddRAAWLARIAAWRAEYLAAYAADDGPIKPQRVIAALREALPDDAIVVTDVGQHQMWAARYLRFRRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 392 ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE 471
Cdd:COG0028 403 RRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQELFYGG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489937867 472 RYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENvwplvPPGASNSEM 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: 716.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYnDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGTlEPYFTTVK----NVEVFPH-ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGL 234
Cdd:TIGR00118 161 DVTTAEIE-YPYPEKVNlpgyRPTVKGHpLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 235 GAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD- 313
Cdd:TIGR00118 240 GSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDRVTGNLAKFAPNAKIIHIDIDPAEIGKNVRVDIPIVGDa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 314 ---LNSLLPALQQSLKID--AWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTY 388
Cdd:TIGR00118 320 rnvLEELLKKLFELKERKesAWLEQINKWKKEYPLKMDYTEEGIKPQQVIEELSRVTKDEAIVTTDVGQHQMWAAQFYPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:TIGR00118 400 RKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIPVKILILNNRYLGMVRQWQELF 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489937867 469 FQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:TIGR00118 480 YEERYSHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDVVVDKPENVLPMVAPGGGLDEMI 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: 685.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY----DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGAT 76
Cdd:PRK07418 19 ATGAYALMDSLKRHGVKHIFGYPGGAILPIYDELYkaeaEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 77 NLITGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVD 156
Cdd:PRK07418 99 NLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 157 IPKDIqlasGTLEPYFTTVKNVEVFP----------HADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMP 226
Cdd:PRK07418 179 IPKDV----GQEEFDYVPVEPGSVKPpgyrptvkgnPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 227 VACTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQA 306
Cdd:PRK07418 255 VTTTLMGKGAFDEHHPLSVGMLGMHGTAYANFAVTECDLLIAVGARFDDRVTGKLDEFASRAKVIHIDIDPAEVGKNRRP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 307 HVALQGDL-NSLLPALQQSLKIDAWRQHSAELRTEHTWRYDHP------GEAIYAPLLLKQLSDRKPaDSVVTTDVGQHQ 379
Cdd:PRK07418 335 DVPIVGDVrKVLVKLLERSLEPTTPPRTQAWLERINRWKQDYPlvvppyEGEIYPQEVLLAVRDLAP-DAYYTTDVGQHQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 380 MWSAQHMTyTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLG 459
Cdd:PRK07418 414 MWAAQFLR-NGPRRWISSAGLGTMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQG 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 460 MVRQWQQLFFQERYSETTLTDN-PDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGA 538
Cdd:PRK07418 493 MVRQWQESFYGERYSASNMEPGmPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDVHVRRDENCYPMVPPGK 572
|
....*.
gi 489937867 539 SNSEML 544
Cdd:PRK07418 573 SNAQMV 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: 679.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 15 GVQTVFGYPGGAIMPVYDALY----DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSV 90
Cdd:CHL00099 24 GVKHIFGYPGGAILPIYDELYawekKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATAQMDSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 91 PVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKDIqlasgTLE- 169
Cdd:CHL00099 104 PLLVITGQVGRAFIGTDAFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDIPKDV-----GLEk 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 170 -PYFTTVKNVEVFPHAD-----------VEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAV 237
Cdd:CHL00099 179 fDYYPPEPGNTIIKILGcrpiykptikrIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIPVTTTLMGKGIF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSL 317
Cdd:CHL00099 259 DEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAEIGKNRIPQVAIVGDVKKV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 318 LPALQQSLKID----------AWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPaDSVVTTDVGQHQMWSAQhMT 387
Cdd:CHL00099 339 LQELLELLKNSpnlleseqtqAWRERINRWRKEYPLLIPKPSTSLSPQEVINEISQLAP-DAYFTTDVGQHQMWAAQ-FL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 388 YTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQL 467
Cdd:CHL00099 417 KCKPRKWLSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNKWQGMVRQWQQA 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489937867 468 FFQERYSETTLTDN-PDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:CHL00099 497 FYGERYSHSNMEEGaPDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLIDCQVIEDENCYPMVAPGKSNSQMI 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: 662.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08527 3 LSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYkQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK08527 83 TGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASG--------TLEPYFTTVKnvevFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTL 231
Cdd:PRK08527 163 DVTATLGefeypkeiSLKTYKPTYK----GNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK08527 239 MARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNADYPIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 312 GDLNSLLPALQQSLK------IDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQH 385
Cdd:PRK08527 319 GDLKNVLKEMLEELKeenpttYKEWREILKRYNELHPLSYEDSDEVLKPQWVIERVGELLGDDAIISTDVGQHQMWVAQF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 386 MTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQ 465
Cdd:PRK08527 399 YPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYKIPVINIILNNNFLGMVRQWQ 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 466 QLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK08527 479 TFFYEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDVKIDRFENVLPMVPAGGALYNMI 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: 657.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08155 13 FTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTqIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK08155 93 TAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWIDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGTLE--PYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAV 237
Cdd:PRK08155 173 DVQTAVIELEalPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTLMALGML 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD---- 313
Cdd:PRK08155 253 PKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADvddv 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 314 LNSLLPALQQSLKiDAWRQHSAELRTEHTwrYDHPGEAiyAPL----LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYT 389
Cdd:PRK08155 333 LAQLLPLVEAQPR-AEWHQLVADLQREFP--CPIPKAD--DPLshygLINAVAACVDDNAIITTDVGQHQMWTAQAYPLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 390 RPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK08155 408 RPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQSLFY 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489937867 470 QERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEML 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: 645.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK06048 8 MTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNLVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK06048 88 GIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDLPKD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IQlasgTLEPYFTTVKNVEVFPHA--------DVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLK 232
Cdd:PRK06048 168 VT----TAEIDFDYPDKVELRGYKptykgnpqQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 233 GLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQG 312
Cdd:PRK06048 244 GIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEISKNVKVDVPIVG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 313 D----LNSLLPALQQSlKIDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPaDSVVTTDVGQHQMWSAQHMTY 388
Cdd:PRK06048 324 DakqvLKSLIKYVQYC-DRKEWLDKINQWKKEYPLKYKEREDVIKPQYVIEQIYELCP-DAIIVTEVGQHQMWAAQYFKY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:PRK06048 402 KYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELATAVQNDIPVIVAILNNGYLGMVRQWQELF 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 469 FQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLE 545
Cdd:PRK06048 482 YDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVIDFIVECEENVSPMVPAGAAINEILD 558
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
1-542 |
0e+00 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 640.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK07789 31 MTGAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK07789 111 TPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGT--------LEPYFTTVKnvevfPHA-DVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACT 230
Cdd:PRK07789 191 DALQAQTTfswpprmdLPGYRPVTK-----PHGkQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVTT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 231 LKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVAL 310
Cdd:PRK07789 266 LMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIGKNRHADVPI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 311 QGDLNSLLPALQQSLK----------IDAWRQHSAELRTEHTWRYDHPGEAIYAP-LLLKQLSDRKPADSVVTTDVGQHQ 379
Cdd:PRK07789 346 VGDVKEVIAELIAALRaehaaggkpdLTAWWAYLDGWRETYPLGYDEPSDGSLAPqYVIERLGEIAGPDAIYVAGVGQHQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 380 MWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLG 459
Cdd:PRK07789 426 MWAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATCAIEGIPIKVALINNGNLG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 460 MVRQWQQLFFQERYSETTLTDN----PDFLMLASAFGIPGQHITRKDQVEAALD-TMLNSEGPYLL--HVSIDELenVWP 532
Cdd:PRK07789 506 MVRQWQTLFYEERYSNTDLHTHshriPDFVKLAEAYGCVGLRCEREEDVDAVIEkARAINDRPVVIdfVVGKDAM--VWP 583
|
570
....*....|
gi 489937867 533 LVPPGASNSE 542
Cdd:PRK07789 584 MVAAGTSNDE 593
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
1-544 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 632.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK09107 11 MTGAEMVVQALKDQGVEHIFGYPGGAVLPIYDEIFqQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGTLEPYFTTVKNVEVFP--HADVEQARK---MLAQAQKPILYVGGGV---GMAqAVPALREFIAVTQMPVACTL 231
Cdd:PRK09107 171 DVQFATGTYTPPQKAPVHVSYQPkvKGDAEAITEaveLLANAKRPVIYSGGGVinsGPE-ASRLLRELVELTGFPITSTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK09107 250 MGLGAYPASGKNWLGMLGMHGTYEANMAMHDCDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVRVDVPII 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 312 GDLNSLLPALQQSLK----------IDAWRQHSAELRTEHTWRYDHPGEAI---YAPLLLKQLSdrKPADSVVTTDVGQH 378
Cdd:PRK09107 330 GDVGHVLEDMLRLWKargkkpdkeaLADWWGQIARWRARNSLAYTPSDDVImpqYAIQRLYELT--KGRDTYITTEVGQH 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 379 QMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRL 458
Cdd:PRK09107 408 QMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNNQYM 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 459 GMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGA 538
Cdd:PRK09107 488 GMVRQWQQLLHGNRLSHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIFDCRVANLENCFPMIPSGK 567
|
....*.
gi 489937867 539 SNSEML 544
Cdd:PRK09107 568 AHNEML 573
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
1-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 627.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK06276 81 GIATAYADSSPVIALTGQVPTKLIGNDAFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLPKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IQLASGTLEPYFTTVK------NVEVFPHA-DVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKG 233
Cdd:PRK06276 161 VQEGELDLEKYPIPAKidlpgyKPTTFGHPlQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTLMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 234 LGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK06276 241 KGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVDVPIVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 314 ----LNSLLPAL--QQSLKIDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLS----DRKP-ADSVVTTDVGQHQMWS 382
Cdd:PRK06276 321 aknvLRDLLAELmkKEIKNKSEWLERVKKLKKESIPRMDFDDKPIKPQRVIKELMevlrEIDPsKNTIITTDVGQNQMWM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:PRK06276 401 AHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIAEYDIPVVICIFDNRTLGMVY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 463 QWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVwPLVPPGASNSE 542
Cdd:PRK06276 481 QWQNLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPAEAL-PMVPPGGNLTN 559
|
..
gi 489937867 543 ML 544
Cdd:PRK06276 560 IL 561
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
3-539 |
0e+00 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 607.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGG-VEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITG 81
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQALTRSNcIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 82 LADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKDI 161
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 162 Q--LASGTLEPYFTTVKNVEVFP----HADVEQARKMLAQAQKPILYVGGGVgmAQAVPALREFIAVTQMPVACTLKGLG 235
Cdd:PLN02470 175 QqqLAVPNWNQPMKLPGYLSRLPkppeKSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGIPVASTLMGLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 236 AVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD-- 313
Cdd:PLN02470 253 AFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIGKNKQPHVSVCADvk 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 314 -----LNSLLPALQ-QSLKIDAWRQHSAELRTEHTWRYDHPGEAI---YAPLLLKQLSDRKpadSVVTTDVGQHQMWSAQ 384
Cdd:PLN02470 333 lalqgLNKLLEERKaKRPDFSAWRAELDEQKEKFPLSYPTFGDAIppqYAIQVLDELTDGN---AIISTGVGQHQMWAAQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 385 HMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQW 464
Cdd:PLN02470 410 WYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATIHVENLPVKIMVLNNQHLGMVVQW 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 465 QQLFFQERYSETTLTDN-------PDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPG 537
Cdd:PLN02470 490 EDRFYKANRAHTYLGDPdaeaeifPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDTPGPYLLDVIVPHQEHVLPMIPGG 569
|
..
gi 489937867 538 AS 539
Cdd:PLN02470 570 GT 571
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-543 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 602.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK07710 16 MTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IQLASGTLEpyfttvKNVEV-FP------HADVEQARKML---AQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACT 230
Cdd:PRK07710 176 MVVEEGEFC------YDVQMdLPgyqpnyEPNLLQIRKLVqavSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 231 LKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVAL 310
Cdd:PRK07710 250 LLGLGGFPADHPLFLGMAGMHGTYTANMALYECDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEIPI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 311 QGDLNSLLPAL--QQSLKID--AWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHM 386
Cdd:PRK07710 330 VADAKQALQVLlqQEGKKENhhEWLSLLKNWKEKYPLSYKRNSESIKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYY 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 387 TYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQ 466
Cdd:PRK07710 410 PFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 467 LFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEM 543
Cdd:PRK07710 490 EFYNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMPMVAPGKGLHEM 566
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
1-546 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 595.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK06725 15 VTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNLVT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK06725 95 GLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIPKD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IQLASGTLE-PYFTTVKNVEVFPHADVEQARKM---LAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGA 236
Cdd:PRK06725 175 VQNEKVTSFyNEVVEIPGYKPEPRPDSMKLREVakaISKAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVSTLMGLGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 237 VEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:PRK06725 255 YPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEFHKNVAVEYPVVGDVKK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPALQQS---LKIDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPEN 393
Cdd:PRK06725 335 ALHMLLHMsihTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGEAIVTTEVGQHQMWAAHFYKAKNPRT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 394 FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERY 473
Cdd:PRK06725 415 FLTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQTIAENNIPVKVFIINNKFLGMVRQWQEMFYENRL 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489937867 474 SETTLtDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNSEMLEK 546
Cdd:PRK06725 495 SESKI-GSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVDFCVEEGENVFPMVPPNKGNNEMIMK 566
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
2-544 |
0e+00 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 543.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 2 NGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNfEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IQlASGTLEPYFTTVKnvevFPH------ADVEQARKMLAQ---AQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTL 231
Cdd:PRK07282 171 VS-ALETDFIYDPEVN----LPSyqptlePNDMQIKKILKQlskAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK07282 246 LGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 312 GDLNSLLPALQQSLKIDAWRQHSAELRTEHTWR---YDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTY 388
Cdd:PRK07282 326 GDAKKALQMLLAEPTVHNNTEKWIEKVTKDKNRvrsYDKKERVVQPQAVIERIGELTNGDAIVVTDVGQHQMWAAQYYPY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:PRK07282 406 QNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNNHSLGMVRQWQESF 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489937867 469 FQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEgPYLLHVSIDELENVWPLVPPGASNSEML 544
Cdd:PRK07282 486 YEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDLEVITEDV-PMLIEVDISRKEHVLPMVPAGKSNHEML 560
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-543 |
0e+00 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 532.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06466 4 LSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFkQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK06466 84 TGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGTLE-PYFTTVKNVEVFP----HA-DVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKG 233
Cdd:PRK06466 164 DMTNPAEKFEyEYPKKVKLRSYSPavrgHSgQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 234 LGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK06466 244 LGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIKADIPIVGP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 314 LNSLLPALQQSLK----------IDAWRQHSAELRTEH-TWRYDHP-GEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMW 381
Cdd:PRK06466 324 VESVLTEMLAILKeigekpdkeaLAAWWKQIDEWRGRHgLFPYDKGdGGIIKPQQVVETLYEVTNGDAYVTSDVGQHQMF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 382 SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMV 461
Cdd:PRK06466 404 AAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVKIINLNNGALGMV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 462 RQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALD-TMLNSEGPYLLHVSIDELENVWPLVPPGASN 540
Cdd:PRK06466 484 RQWQDMQYEGRHSHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEeAFAMKDRLVFIDIYVDRSEHVYPMQIADGSM 563
|
...
gi 489937867 541 SEM 543
Cdd:PRK06466 564 RDM 566
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
1-544 |
0e+00 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 522.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06965 21 SIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYkQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK06965 101 TGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLASGTlepyFTTVKNVEVFPHADVE-----QARK---MLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTL 231
Cdd:PRK06965 181 DVSKTPCE----YEYPKSVEMRSYNPVTkghsgQIRKavsLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 232 KGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNA-SVIHMDIDPAEMNKLRQAHVAL 310
Cdd:PRK06965 257 MGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 311 QGD----LNSLLPALQQS-LKIDA-----WRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQM 380
Cdd:PRK06965 337 VGDvkevLKELIEQLQTAeHGPDAdalaqWWKQIEGWRSRDCLKYDRESEIIKPQYVVEKLWELTDGDAFVCSDVGQHQM 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 381 WSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:PRK06965 417 WAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVKIISLNNRYLGM 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 461 VRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLN-SEGPYLLHVSIDELENVWPLVPPGAS 539
Cdd:PRK06965 497 VRQWQEIEYSKRYSHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDFQTDPTENVWPMVQAGKG 576
|
....*
gi 489937867 540 NSEML 544
Cdd:PRK06965 577 ITEML 581
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-543 |
8.87e-173 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 500.50 E-value: 8.87e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08979 4 LSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK08979 84 TGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIqLASGTLEPYF--TTVK----NVEVFPH-ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLK 232
Cdd:PRK08979 164 DC-LNPAILHPYEypESIKmrsyNPTTSGHkGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 233 GLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQG 312
Cdd:PRK08979 243 GLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVDIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 313 D----LNSLLPALQQSLK------IDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWS 382
Cdd:PRK08979 323 SadkvLDSMLALLDESGEtndeaaIASWWNEIEVWRSRNCLAYDKSSERIKPQQVIETLYKLTNGDAYVASDVGQHQMFA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:PRK08979 403 ALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNRFLGMVK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 463 QWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLN-SEGPYLLHVSIDELENVWPLVPPGASNS 541
Cdd:PRK08979 483 QWQDMIYQGRHSHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKALAmKDRLVFVDINVDETEHVYPMQIRGGAMN 562
|
..
gi 489937867 542 EM 543
Cdd:PRK08979 563 EM 564
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-544 |
3.17e-170 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 494.05 E-value: 3.17e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06882 4 LSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK06882 84 TGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 D-IQLASGTLEPYFTTVK----NVEVFPH-ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKG 233
Cdd:PRK06882 164 DmVNPANKFTYEYPEEVSlrsyNPTVQGHkGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 234 LGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD 313
Cdd:PRK06882 244 LGAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 314 ----LNSLLPALQQ------SLKIDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSA 383
Cdd:PRK06882 324 aknvLEEFLSLLEEenlaksQTDLTAWWQQINEWKAKKCLEFDRTSDVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK06882 404 LHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 464 WQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYL-LHVSIDELENVWPLVPPGASNSE 542
Cdd:PRK06882 484 WQDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKDKLVfVDVNVDETEHVYPMQIRGGAMNE 563
|
..
gi 489937867 543 ML 544
Cdd:PRK06882 564 MI 565
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-543 |
8.09e-170 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 493.21 E-value: 8.09e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK07979 4 LSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK07979 84 TGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIqLASGTLEPYFTTVK------NVEVFPH-ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLK 232
Cdd:PRK07979 164 DI-LNPANKLPYVWPESvsmrsyNPTTQGHkGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 233 GLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQG 312
Cdd:PRK07979 243 GLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 313 D-------LNSLLPALQQSLKIDA---WRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWS 382
Cdd:PRK07979 323 DarqvleqMLELLSQESAHQPLDEirdWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:PRK07979 403 ALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNRYLGMVK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 463 QWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTML---NSEGPYLLHVSIDELENVWPLVPPGAS 539
Cdd:PRK07979 483 QWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALeqvRNNRLVFVDVTVDGSEHVYPMQIRGGG 562
|
....
gi 489937867 540 NSEM 543
Cdd:PRK07979 563 MDEM 566
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
3-544 |
9.36e-148 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 436.58 E-value: 9.36e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPGGAIMPVYDA----LYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 79 ITGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIP 158
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 159 KDIQLASgtLE----PYFTTVKNVEVFPH----ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACT 230
Cdd:PRK06456 164 RDIFYEK--MEeikwPEKPLVKGYRDFPTridrLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIPIVST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 231 LKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPN-ASVIHMDIDPAEMNKLRQAHVA 309
Cdd:PRK06456 242 FPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETrKKFIMVNIDPTDGEKAIKVDVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 310 LQGDLNSLL-------PALQQSLKIDAWRQHSAELRTEHTWRYDHPGEAIYAPL-LLKQLSDRKPADSVVTTDVGQHQMW 381
Cdd:PRK06456 322 IYGNAKIILrelikaiTELGQKRDRSAWLKRVKEYKEYYSQFYYTEENGKLKPWkIMKTIRQALPRDAIVTTGVGQHQMW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 382 SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMV 461
Cdd:PRK06456 402 AEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNRTLGLV 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 462 RQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWPLVPPGASNS 541
Cdd:PRK06456 482 RQVQDLFFGKRIVGVDYGPSPDFVKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVDKEELALPTLPPGGRLK 561
|
...
gi 489937867 542 EML 544
Cdd:PRK06456 562 QVI 564
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
2-525 |
4.08e-123 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 372.67 E-value: 4.08e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 2 NGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08199 9 TGGQILVDALRANGVERVFCVPGESYLAVLDALHDeTDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK08199 89 GVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPED 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IqLASGTLEPYFTTVKNVEVFPHA-DVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAVEA 239
Cdd:PRK08199 169 V-LSETAEVPDAPPYRRVAAAPGAaDLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQDLFDN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 240 DYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGK---LNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:PRK08199 248 RHPNYAGDLGLGINPALAARIREADLVLAVGTRLGEVTTQGytlLDIPVPRQTLVHVHPDAEELGRVYRPDLAIVADPAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPALQQsLKIDA---WRQHSAELRTEH-TWRYDHPGE-AIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRP 391
Cdd:PRK08199 328 FAAALAA-LEPPAspaWAEWTAAAHADYlAWSAPLPGPgAVQLGEVMAWLRERLPADAIITNGAGNYATWLHRFFRFRRY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 392 ENFI--TSsglGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK08199 407 RTQLapTS---GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMYGTIRMHQEREY 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489937867 470 QERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSID 525
Cdd:PRK08199 484 PGRVSGTDLT-NPDFAALARAYGGHGETVERTEDFAPAFERALASGKPALIEIRID 538
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
1-529 |
4.81e-120 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 364.53 E-value: 4.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAA-MAAIgYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAfMAAT-YGRLTGKAGVCLSTLGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVA--SSFIGTdaFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDI 157
Cdd:PRK08322 80 TGVAYAQLGGMPMVAITGQKPikRSKQGS--FQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 158 PKDIQLASGTLEPYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAV 237
Cdd:PRK08322 158 PEDIAAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLGMLGMHGTKAANFAVQECDLLIAVGarFDdrvtgkLNTFAP-------NASVIHMDIDPAEMNKLRQAHVAL 310
Cdd:PRK08322 238 PETHPLSLGTAGLSQGDYVHCAIEHADLIINVG--HD------VIEKPPffmnpngDKKVIHINFLPAEVDPVYFPQVEV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 311 QGDLNsllPALQQSLKIDAWRQH---------SAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMW 381
Cdd:PRK08322 310 VGDIA---NSLWQLKERLADQPHwdfprflkiREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDDDIVILDNGAYKIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 382 SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMV 461
Cdd:PRK08322 387 FARNYRAYEPNTCLLDNALATMGAGLPSAIAAKLVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMI 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 462 RqWQQ--LFFQERYSETTltdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELEN 529
Cdd:PRK08322 467 R-WKQenMGFEDFGLDFG---NPDFVKYAESYGAKGYRVESADDLLPTLEEALAQPGVHVIDCPVDYSEN 532
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
352-537 |
1.35e-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: 319.44 E-value: 1.35e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 352 IYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSF 431
Cdd:cd02015 1 IKPQEVIKELSELTPGDAIVTTDVGQHQMWAAQYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEA 160
|
170 180
....*....|....*....|....*.
gi 489937867 512 LNSEGPYLLHVSIDELENVWPLVPPG 537
Cdd:cd02015 161 LASDGPVLLDVLVDPEENVLPMVPPG 186
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-537 |
1.76e-104 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 324.27 E-value: 1.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGG--VEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK08266 4 MTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGdrIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 79 ITGLADALLDSVPVVAITGQVASSFIGTDAFQ--EV-DVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLV 155
Cdd:PRK08266 84 GAALLTAYGCNSPVLCLTGQIPSALIGKGRGHlhEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPVAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 156 DIPKDIQLASGTLEPYFTTVKNVEVFPHAD-VEQARKMLAQAQKPILYVGGGVgmAQAVPALREFIAVTQMPVACTLKGL 234
Cdd:PRK08266 164 EMPWDVFGQRAPVAAAPPLRPAPPPAPDPDaIAAAAALIAAAKNPMIFVGGGA--AGAGEEIRELAEMLQAPVVAFRSGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 235 GAVEADYPYYLGMLgmhgtkAANFAVQECDLLIAVGARFDDRVTgKLNTFAPNASVIHMDIDPAEMNKLrQAHVALQGDL 314
Cdd:PRK08266 242 GIVSDRHPLGLNFA------AAYELWPQTDVVIGIGSRLELPTF-RWPWRPDGLKVIRIDIDPTEMRRL-KPDVAIVADA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 315 NSLLPALQQSL-KIDAWRQHSAELRTEHTWRYDHPGEAIYAPL-LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPE 392
Cdd:PRK08266 314 KAGTAALLDALsKAGSKRPSRRAELRELKAAARQRIQAVQPQAsYLRAIREALPDDGIFVDELSQVGFASWFAFPVYAPR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 393 NFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQER 472
Cdd:PRK08266 394 TFVTCGYQGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGR 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 473 YSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSI--DELENVWPLVPPG 537
Cdd:PRK08266 474 VVASDLV-NPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEVPVprGSEASPWPFIHPA 539
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
3-530 |
3.59e-103 |
|
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: 320.93 E-value: 3.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGL 82
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 83 ADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKDI- 161
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRADLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQDVv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 162 -QLASGTLEPYFTTVKnVEVFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAVEAD 240
Cdd:TIGR02418 161 dSPVSVKAIPASYAPK-LGAAPDDAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQGAGAVSRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 241 -YPYYLGMLGMHGTKAANFAVQECDLLIAVG---ARFDDRVTGKLNtfapNASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:TIGR02418 240 lEDHFFGRVGLFRNQPGDRLLKQADLVITIGydpIEYEPRNWNSEN----DATIVHIDVEPAQIDNNYQPDLELVGDIAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPAL----------QQSLKIDAWRQHSAELRTEHTWRYD----HPGEaiyaplLLKQLSDRKPADSVVTTDVGQHQMWS 382
Cdd:TIGR02418 316 TLDLLaeripgyelpPDALAILEDLKQQREALDRVPATLKqahlHPLE------IIKAMQAIVTDDVTVTVDMGSHYIWM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP-LKIVLLDNqRLGMV 461
Cdd:TIGR02418 390 ARYFRSYRARHLLISNGMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNiVHIIWNDN-GYNMV 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489937867 462 RqwqqlfFQE--RYSETTLTD--NPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENV 530
Cdd:TIGR02418 469 E------FQEemKYQRSSGVDfgPIDFVKYAESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYSDNP 535
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
3-537 |
3.75e-101 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 316.94 E-value: 3.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08611 6 AGEALVKLLQDWGIDHVYGIPGDSIDAVVDALrkEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRpGPVLVDIPKD 160
Cdd:PRK08611 86 GLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 I---QLASGTLEPYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGggVGMAQAVPALREFIAVTQMPVACTLKGLGAV 237
Cdd:PRK08611 165 LpaqKIKDTTNKTVDTFRPTVPSPKPKDIKKAAKLINKAKKPVILAG--LGAKHAKEELLAFAEKAKIPIIHTLPAKGII 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRvtgklnTFAPN-ASVIHMDIDPAEMNKLRQAHVALQGDLNS 316
Cdd:PRK08611 243 PDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVGTNYPYV------DYLPKkAKAIQIDTDPANIGKRYPVNVGLVGDAKK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPALQQSLKIDAWR---QHSAElRTEHTWRYDHPGEAIYA-PL----LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTY 388
Cdd:PRK08611 317 ALHQLTENIKHVEDRrflEACQE-NMAKWWKWMEEDENNAStPIkperVMAAIQKIADDDAVLSVDVGTVTVWSARYLNL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 389 TRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLF 468
Cdd:PRK08611 396 GTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKYEQQAA 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 469 FQERYsETTLTDnPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDelENVWPLvpPG 537
Cdd:PRK08611 476 GELEY-AIDLSD-MDYAKFAEACGGKGYRVEKAEELDPAFEEALAQDKPVIIDVYVD--PNAAPL--PG 538
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-531 |
1.51e-99 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 311.79 E-value: 1.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK08617 5 KYGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK08617 85 GLVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 IqlasgTLEPyfTTVKNVE--------VFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLK 232
Cdd:PRK08617 165 V-----VDAP--VTSKAIAplskpklgPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 233 GLGAVEAD-YPYYLGMLGMHGTKAANFAVQECDLLIAVG---ARFDDRVTGKLNtfapNASVIHMDIDPAEMNKLRQAHV 308
Cdd:PRK08617 238 AAGVISRElEDHFFGRVGLFRNQPGDELLKKADLVITIGydpIEYEPRNWNSEG----DATIIHIDVLPAEIDNYYQPER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 309 ALQGD----LNSLLPAL------QQSLKIDAWRQHSAELRTEHTWRYDhpGEAIYaPL-LLKQLSDRKPADSVVTTDVGQ 377
Cdd:PRK08617 314 ELIGDiaatLDLLAEKLdglslsPQSLEILEELRAQLEELAERPARLE--EGAVH-PLrIIRALQDIVTDDTTVTVDVGS 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 378 HQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPL-KIVLLDNq 456
Cdd:PRK08617 391 HYIWMARYFRSYEPRHLLFSNGMQTLGVALPWAIAAALVRPGKKVVSVSGDGGFLFSAMELETAVRLKLNIvHIIWNDG- 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 457 RLGMVRqwqqlfFQE--RYSETTLTD--NPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVW 531
Cdd:PRK08617 470 HYNMVE------FQEemKYGRSSGVDfgPVDFVKYAESFGAKGLRVTSPDELEPVLREALATDGPVVIDIPVDYSDNIK 542
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-509 |
2.36e-99 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 312.68 E-value: 2.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARAT-GKTGVCIATSGPGATNL 78
Cdd:PRK11269 4 MRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKhGGIRHILARHVEGASHMAEGYTRATaGNIGVCIGTSGPAGTDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 79 ITGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIP 158
Cdd:PRK11269 84 ITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 159 KDIQLA-----SGTLEPYftTVKNVEvfPH-ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLK 232
Cdd:PRK11269 164 FDVQVAeiefdPDTYEPL--PVYKPA--ATrAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 233 GLGAVEADYPYYLGMLGMH-GTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQ 311
Cdd:PRK11269 240 GWGAIPDDHPLMAGMVGLQtSHRYGNATLLASDFVLGIGNRWANRHTGSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 312 GDLNSllpALQQSLKIDAWRQHSAELRTEHTW------------RYDHPGEA-IYAPLLLKQLSDRKPADSVVTTDVGQH 378
Cdd:PRK11269 320 SDAKA---ALELLVEVAREWKAAGRLPDRSAWvadcqerkrtllRKTHFDNVpIKPQRVYEEMNKAFGRDTCYVSTIGLS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 379 QMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRL 458
Cdd:PRK11269 397 QIAAAQFLHVYKPRHWINCGQAGPLGWTIPAALGVRAADPDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNNAYL 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 459 GMVRQWQ---------QLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALD 509
Cdd:PRK11269 477 GLIRQAQrafdmdycvQLAFENINSPELNGYGVDHVKVAEGLGCKAIRVFKPEDIAPALE 536
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
4-532 |
4.81e-88 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 281.72 E-value: 4.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 4 AQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLA 83
Cdd:PRK06457 5 AEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 84 DALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRpGPVLVDIPKDIQL 163
Cdd:PRK06457 85 DAKMDHAPVIALTGQVESDMIGHDYFQEVNLTKLFDDVAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLPVDILR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 164 ASGTLEPYFTTVKNVEVFPhADVEQARKMLAQAQKPILYVGGGV-GMAQAVPALREFIAVtqmPVACTLKGLGAVEADYP 242
Cdd:PRK06457 164 KSSEYKGSKNTEVGKVKYS-IDFSRAKELIKESEKPVLLIGGGTrGLGKEINRFAEKIGA---PIIYTLNGKGILPDLDP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 243 YYLGMLGMHGTKAANFAVQECDLLIAVGARFDdrvtgKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPA-- 320
Cdd:PRK06457 240 KVMGGIGLLGTKPSIEAMDKADLLIMLGTSFP-----YVNFLNKSAKVIQVDIDNSNIGKRLDVDLSYPIPVAEFLNIdi 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 321 --------LQQSLKIDAW--RQHSAELRTehtwryDHPgeaIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTR 390
Cdd:PRK06457 315 eeksdkfyEELKGKKEDWldSISKQENSL------DKP---MKPQRVAYIVSQKCKKDAVIVTDTGNVTMWTARHFRASG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 391 PENFITSSGLGTMGFGLPAAVGAQVARPNDT-VICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFF 469
Cdd:PRK06457 386 EQTFIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSKLGMIKFEQEVMG 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489937867 470 QERYSETTLtdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWP 532
Cdd:PRK06457 466 YPEWGVDLY--NPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDPNERPMP 526
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
8-510 |
5.42e-83 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 269.56 E-value: 5.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 8 VHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALL 87
Cdd:PRK07525 13 VETLQAHGITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYW 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 88 DSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRpGPVLVDIPKDiqlasgt 167
Cdd:PRK07525 93 AHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRD------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 168 lepYFTTVKNVEVFPHADVE----------QARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAV 237
Cdd:PRK07525 165 ---YFYGVIDVEIPQPVRLErgaggeqslaEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDdrVTGKL-----NTFAPNASVIHMDIDPAEMNKLRQAHVALQG 312
Cdd:PRK07525 242 PGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLN--PFGTLpqygiDYWPKDAKIIQVDINPDRIGLTKKVSVGICG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 313 DLNSLLPALQQSLKID-------------------AWRQHSAELRTE-----HTWR---------YDHPGEAIYAplllk 359
Cdd:PRK07525 320 DAKAVARELLARLAERlagdagreerkaliaaeksAWEQELSSWDHEdddpgTDWNeeararkpdYMHPRQALRE----- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 360 qLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELG 439
Cdd:PRK07525 395 -IQKALPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDGAWGISMNEVM 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489937867 440 TVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDT 510
Cdd:PRK07525 474 TAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYAGIAEAMGAEGVVVDTQEELGPALKR 544
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
4-522 |
6.34e-83 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 268.00 E-value: 6.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 4 AQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLA 83
Cdd:PRK07524 5 GEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 84 DALLDSVPVVAITG--QVASSFIGTDAFQEV-DVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK07524 85 QAYADSIPMLVISSvnRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 I--QLASGTLEPYFTTVKNVEVFPhADVEQARKMLAQAQKP-ILYVGGGVGMAQAVPALREFIavtQMPVACTLKGLGAV 237
Cdd:PRK07524 165 VlaAPADHLLPAPPTRPARPGPAP-AALAQAAERLAAARRPlILAGGGALAAAAALRALAERL---DAPVALTINAKGLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLGmlGMHGTKAANFAVQECDLLIAVG---ARFDDRVTGKlNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDL 314
Cdd:PRK07524 241 PAGHPLLLG--ASQSLPAVRALIAEADVVLAVGtelGETDYDVYFD-GGFPLPGELIRIDIDPDQLARNYPPALALVGDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 315 NSLLPALQQSLKIDAWRQHSAELRTEHTW---RYDH-PGEAIYAPlLLKQLSDRKPADSVV--TTdvgqhQMWSAQHMTY 388
Cdd:PRK07524 318 RAALEALLARLPGQAAAADWGAARVAALRqalRAEWdPLTAAQVA-LLDTILAALPDAIFVgdST-----QPVYAGNLYF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 389 TRPEN---FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQwq 465
Cdd:PRK07524 392 DADAPrrwFNASTGYGTLGYGLPAAIGAALGAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRR-- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 466 qlFFQERYSETTLTD--NPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHV 522
Cdd:PRK07524 470 --YMVARDIEPVGVDpyTPDFIALARAFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
1-508 |
1.59e-82 |
|
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: 268.27 E-value: 1.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:TIGR03457 2 MTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRpGPVLVDIPKD 160
Cdd:TIGR03457 82 AIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 iqlasgtlepYFTTVKNVEVfPH-----------ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVAC 229
Cdd:TIGR03457 161 ----------YFYGEIDVEI-PRpvrldrgaggaTSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 230 TLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGAR---FDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQA 306
Cdd:TIGR03457 230 SYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRlgpFGTLPQYGIDYWPKNAKIIQVDANAKMIGLVKKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 307 HVALQGDLNSLLPALQQSLKI------------------DAWRQHSAELRTEH-----TWRYDH---PGEAIYAPLLLKQ 360
Cdd:TIGR03457 310 TVGICGDAKAAAAEILQRLAGkagdanraerkakiqaerSAWEQELSEMTHERdpfslDMIVEQrqeEGNWLHPRQVLRE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 361 LSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGT 440
Cdd:TIGR03457 390 LEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSMNEIMT 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489937867 441 VKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAAL 508
Cdd:TIGR03457 470 AVRHDIPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFAGIADAMGAKGVVVDKPEDVGPAL 537
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-526 |
5.07e-79 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 258.92 E-value: 5.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFG--YPGGAIMpvydALYDGGVEHLLCRHEQ-GAAMAAiGYARATGKTGVCIATSGPGATN 77
Cdd:PRK06112 14 GTVAHAIARALKRHGVEQIFGqsLPSALFL----AAEAIGIRQIAYRTENaGGAMAD-GYARVSGKVAVVTAQNGPAATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 78 LITGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDI 157
Cdd:PRK06112 89 LVAPLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 158 PKDIqLASGTLEPYFTTVKNVEVFP-------HADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACT 230
Cdd:PRK06112 169 PADL-LTAAAAAPAAPRSNSLGHFPldrtvpaPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 231 LKGLGAVEADYPYYLGMLG-MHGTKAANF----AVQECDLLIAVGARFDDRVTGKLNTFAPNASVIHMDIDPAEMNKLRQ 305
Cdd:PRK06112 248 NMGKGAVDETHPLSLGVVGsLMGPRSPGRhlrdLVREADVVLLVGTRTNQNGTDSWSLYPEQAQYIHIDVDGEEVGRNYE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 306 AhVALQGDLNSLLPALQQSLKI------------------DAWRQHSAELRTehtwRYDHPGEAIYAPLLLKQLSDRKPA 367
Cdd:PRK06112 328 A-LRLVGDARLTLAALTDALRGrdlaaragrraalepaiaAGREAHREDSAP----VALSDASPIRPERIMAELQAVLTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 368 DSVVTTDVGQHQMWSAQHMTYTRP-ENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQL 446
Cdd:PRK06112 403 DTIVVADASYSSIWVANFLTARRAgMRFLTPRGLAGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 447 PLKIVLLDNQRLGMVRQWQQLFFQErYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDE 526
Cdd:PRK06112 483 PVTIVVLNNGILGFQKHAETVKFGT-HTDACHFAAVDHAAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDP 561
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-525 |
6.85e-78 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 256.07 E-value: 6.85e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK06546 3 KTVAEQLVEQLVAAGVKRIYGIVGDSLNPIVDAVrRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVAnSGRPGPVLVDIPK 159
Cdd:PRK06546 83 NGLYDAHRSGAPVLAIASHIPSAQIGSGFFQETHPDRLFVECSGYCEMVSSAEQAPRVLHSAIQHA-VAGGGVSVVTLPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DI--QLASGTLEPYFTTVKNVEVFP-HADVEQARKMLAQAQKPILYVGGGVGMAQA-VPALREFIAVtqmPVACTLKGLG 235
Cdd:PRK06546 162 DIadEPAPEGFAPSVISPRRPTVVPdPAEVRALADAINEAKKVTLFAGAGVRGAHAeVLALAEKIKA---PVGHSLRGKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 236 AVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFddrvtgKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLN 315
Cdd:PRK06546 239 WIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLGTDF------PYDQFLPDVRTAQVDIDPEHLGRRTRVDLAVHGDVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 316 SLLPALQQSLKIDAWRQHSAELRTEHTWRYDHPGEAI-------------YAPLLLKQLSDRkpaDSVVTTDVGQHQMWS 382
Cdd:PRK06546 313 ETIRALLPLVKEKTDRRFLDRMLKKHARKLEKVVGAYtrkvekhtpihpeYVASILDELAAD---DAVFTVDTGMCNVWA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:PRK06546 390 ARYITPNGRRRVIGSFRHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489937867 463 qwQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSID 525
Cdd:PRK06546 470 --LEMLVDGLPDFGTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTD 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
4-532 |
1.27e-75 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 249.91 E-value: 1.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 4 AQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGL 82
Cdd:PRK09124 6 ADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRrMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 83 ADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVdIPKDIQ 162
Cdd:PRK09124 86 FDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSNPEQLPRVLAIAMRKAILNRGVAVVV-LPGDVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 163 LA---SGTLEPYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGGGVgmAQAVPALREFIAVTQMPVACTLKGLGAVEA 239
Cdd:PRK09124 165 LKpapERATPHWYHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGC--AGAHDELVALAETLKAPIVHALRGKEHVEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 240 DYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRvtgklNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLP 319
Cdd:PRK09124 243 DNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYR-----QFYPTDAKIIQIDINPGSLGRRSPVDLGLVGDVKATLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 320 ALQQSLK-------IDAWRQHSAELRTE--HTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTR 390
Cdd:PRK09124 318 ALLPLLEektdrkfLDKALEHYRKARKGldDLAVPSDGGKPIHPQYLARQISEFAADDAIFTCDVGTPTVWAARYLKMNG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 391 PENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQlffQ 470
Cdd:PRK09124 398 KRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVAMEMK---A 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489937867 471 ERYSET-TLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDELENVWP 532
Cdd:PRK09124 475 GGYLTDgTDLHNPDFAAIAEACGITGIRVEKASELDGALQRAFAHDGPALVDVVTAKQELAMP 537
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-548 |
1.99e-73 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 244.82 E-value: 1.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDAL--YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK08273 3 QTVADFILERLREWGVRRVFGYPGDGINGLLGALgrADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 79 ITGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMsLSCTKHSFLVQ--SLEELPRIMAEAFAVANSGRpGPVLVD 156
Cdd:PRK08273 83 LNGLYDAKLDHVPVVAIVGQQARAALGGHYQQEVDLQSL-FKDVAGAFVQMvtVPEQLRHLVDRAVRTALAER-TVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 157 IPKDIQ--------LASGTLEPYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGGGvgmaqAVPALREFIAVTQM--- 225
Cdd:PRK08273 161 LPNDVQeleyepppHAHGTVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAG-----ALGATDEVIAVAERlga 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 226 PVACTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFddrvtgKLNTFAP---NASVIHMDIDPAEMNK 302
Cdd:PRK08273 236 GVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGSSF------PYSEFLPkegQARGVQIDIDGRMLGL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 303 LRQAHVALQGD----LNSLLPALQQSlKIDAWRQHSAELRteHTW------RYDHPGEAIYAPLLLKQLSDRKPADSVVT 372
Cdd:PRK08273 310 RYPMEVNLVGDaaetLRALLPLLERK-KDRSWRERIEKWV--ARWwetleaRAMVPADPVNPQRVFWELSPRLPDNAILT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 373 TDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN-VQELGTVKR-----KQL 446
Cdd:PRK08273 387 ADSGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAHPDRPVIALVGDGAMQMNgMAELITVAKywrqwSDP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 447 PLKIVLLDNQRLGMVrQWQQLFFQ--ERYSET-TLTDNPdFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVS 523
Cdd:PRK08273 467 RLIVLVLNNRDLNQV-TWEQRVMEgdPKFEASqDLPDVP-YARFAELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVK 544
|
570 580
....*....|....*....|....*
gi 489937867 524 IDelENVwPLVPPGASNSEMLEKLS 548
Cdd:PRK08273 545 TD--PNV-PPLPPHITLEQAKAFAS 566
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
7-524 |
1.30e-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: 242.05 E-value: 1.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 7 VVHALRAQGVQTVFGYPGGAIMPVYDALYD--GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLAD 84
Cdd:TIGR02720 5 VLKVLEAWGVDHIYGIPGGSFNSTMDALSAerDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 85 ALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSgRPGPVLVDIPKDIQLA 164
Cdd:TIGR02720 85 AKEDHVPVLALVGQVPTTGMNMDTFQEMNENPIYADVAVYNRTAMTAESLPHVIDEAIRRAYA-HNGVAVVTIPVDFGWQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 165 SGTLEPYFTTVKNVEVF--PHADVEQ---ARKMLAQAQKPILYVG-GGVGMAQAVPALREFIavtQMPVACTLKGLGAVE 238
Cdd:TIGR02720 164 EIPDNDYYASSVSYQTPllPAPDVEAvtrAVQTLKAAERPVIYYGiGARKAGEELEALSEKL---KIPLISTGLAKGIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 239 ADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDdrVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLL 318
Cdd:TIGR02720 241 DRYPAYLGSAYRVAQKPANEALFQADLVLFVGNNYP--FAEVSKAFKNTKYFIQIDIDPAKLGKRHHTDIAVLADAKKAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 319 PA-LQQSLKIDA-------------WRQHSAEL--RTEHTWRYdhpgEAIYaplllKQLSDRKPADSVVTTDVGQHQMWS 382
Cdd:TIGR02720 319 AAiLAQVEPREStpwwqanvanvknWRAYLASLedKTEGPLQA----YQVY-----RAINKIAEDDAIYSIDVGDININS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 383 AQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR 462
Cdd:TIGR02720 390 NRHLKMTPKNKWITSNLFATMGVGVPGAIAAKLNYPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNCTYGFIK 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489937867 463 QWQQLFFQErYSETTLTDnPDFLMLASAFGIPGQHITRKDQVEAALDT-MLNSEG-PYLLHVSI 524
Cdd:TIGR02720 470 DEQEDTNQP-LIGVDFND-ADFAKIAEGVGAVGFRVNKIEQLPAVFEQaKAIKQGkPVLIDAKI 531
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
7-527 |
1.25e-71 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 238.74 E-value: 1.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 7 VVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADA 85
Cdd:PRK07064 9 IAAFLEQCGVKTAFGVISIHNMPILDAIGRrGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGALVEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 86 LLDSVPVVAITGQVASSFIGTDA--FQEV-DVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKDIQ 162
Cdd:PRK07064 89 LTAGTPLLHITGQIETPYLDQDLgyIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIPIDIQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 163 LASGTLePYFTTVKNVEVFPH--ADVEQARKMLAQAQKPILYVGGGVgmAQAVPALREFIAVTqMPVACTLKGLGAVEAD 240
Cdd:PRK07064 169 AAEIEL-PDDLAPVHVAVPEPdaAAVAELAERLAAARRPLLWLGGGA--RHAGAEVKRLVDLG-FGVVTSTQGRGVVPED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 241 YPYYLGMLgmHGTKAANFAVQECDLLIAVGARFDDRVTGKlNTFAPNASVIHMDIDPAEMNKLRQAHVALQGD----LNS 316
Cdd:PRK07064 245 HPASLGAF--NNSAAVEALYKTCDLLLVVGSRLRGNETLK-YSLALPRPLIRVDADAAADGRGYPNDLFVHGDaarvLAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPALQQSLKIDAwrQHSAELRTEHTWRYDHPGEAI--YApLLLKQLSDRKPADSVVTTDVG-QHQMWSAQHMTYTRPEN 393
Cdd:PRK07064 322 LADRLEGRLSVDP--AFAADLRAAREAAVADLRKGLgpYA-KLVDALRAALPRDGNWVRDVTiSNSTWGNRLLPIFEPRA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 394 FITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERY 473
Cdd:PRK07064 399 NVHALG-GGIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRR 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 474 SETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHV---SIDEL 527
Cdd:PRK07064 478 YYVELH-TPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVEVdmlSIGPF 533
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
5-159 |
4.88e-70 |
|
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: 221.64 E-value: 4.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 5 QWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLAD 84
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489937867 85 ALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
1-532 |
5.15e-67 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 226.14 E-value: 5.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:PRK05858 5 GHAGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:PRK05858 85 AMAAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 161 --IQLASGTLEPYFTTVKNVEVFPHAD-VEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAV 237
Cdd:PRK05858 165 haFSMADDDGRPGALTELPAGPTPDPDaLARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 238 EADYPYYLgmlgmhgTKAANFAVQECDLLIAVGARFDDRVTgkLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSL 317
Cdd:PRK05858 245 PADHPLAF-------SRARGKALGEADVVLVVGVPMDFRLG--FGVFGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 318 LPALQQSLKIDA-WRQHSAELRTEHTWRYD-------------HPGEaIYAPlLLKQLSDrkpaDSVVTTDVGQHQMWSA 383
Cdd:PRK05858 316 LSALAGAGGDRTdHQGWIEELRTAETAARArdaaeladdrdpiHPMR-VYGE-LAPLLDR----DAIVIGDGGDFVSYAG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 384 QHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQ 463
Cdd:PRK05858 390 RYIDPYRPGCWLDPGPFGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKH 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 464 WQQLFF----------QERYSEttltdnpdflmLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSIDElENVWP 532
Cdd:PRK05858 470 PMEALYgydvaadlrpGTRYDE-----------VVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDP-SVAYP 536
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
3-164 |
1.91e-63 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 205.16 E-value: 1.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITG 81
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKsPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 82 LADALLDSVPVVAITGQVASSFIGTDAFQ-EVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD 160
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....
gi 489937867 161 IQLA 164
Cdd:pfam02776 161 VLLE 164
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
374-522 |
2.85e-63 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 203.97 E-value: 2.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 374 DVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLL 453
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489937867 454 DNQRLGMVRQWQQLFFQERYSETT--LTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHV 522
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSGPSgkILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
1-508 |
1.45e-58 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 204.28 E-value: 1.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPggaIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARAT-GKT-GVCIATSGPGATNL 78
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLFGFP---VNELFDAAAAAGIRPVIARTERVAVHMADGYARATsGERvGVFAVQYGPGAENA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 79 ITGLADALLDSVPVVAITG-------QVASSFIGTDAFQEVdvlgmslscTKHSFLVQSLEELPRIMAEAFAVANSGRPG 151
Cdd:PRK06154 97 FGGVAQAYGDSVPVLFLPTgyprgstDVAPNFESLRNYRHI---------TKWCEQVTLPDEVPELMRRAFTRLRNGRPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 152 PVLVDIPKDI-QLASGTLEPYFTTVKNVEVFPH-ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVAC 229
Cdd:PRK06154 168 PVVLELPVDVlAEELDELPLDHRPSRRSRPGADpVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 230 TLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKlnTFAPNASVIHMDIDPAEMNKLRQAHVA 309
Cdd:PRK06154 248 TLNGKSAFPEDHPLALGSGGRARPATVAHFLREADVLFGIGCSLTRSYYGL--PMPEGKTIIHSTLDDADLNKDYPIDHG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 310 LQGDLNSLLPALQQSLKIDAWRQH------SAELRTEHtwrydhpgEAIYAPLLLKQLSDRKP----------------A 367
Cdd:PRK06154 326 LVGDAALVLKQMIEELRRRVGPDRgraqqvAAEIEAVR--------AAWLAKWMPKLTSDSTPinpyrvvwelqhavdiK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 368 DSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP 447
Cdd:PRK06154 398 TVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALVINLWGDAAFGMTGMDFETAVRERIP 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489937867 448 LKIVLLDNQRLGMVRQWQQLfFQERYSETTLTDnpDFLMLASAFGIPGQHITRKDQVEAAL 508
Cdd:PRK06154 478 ILTILLNNFSMGGYDKVMPV-STTKYRATDISG--DYAAIARALGGYGERVEDPEMLVPAL 535
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
186-321 |
9.16e-56 |
|
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a 2-fold Rossman fold.
Pssm-ID: 425523 [Multi-domain] Cd Length: 137 Bit Score: 183.53 E-value: 9.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 186 VEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVACTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDL 265
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 266 LIAVGARFDD-RVTGKLNTFAPNASVIHMDIDPAEMNKLRQAHVALQGDLNSLLPAL 321
Cdd:pfam00205 81 VLAVGARFDDiRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
357-524 |
1.68e-54 |
|
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: 181.68 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 357 LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 437 ELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEG 516
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLS-NPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGG 160
|
....*...
gi 489937867 517 PYLLHVSI 524
Cdd:cd00568 161 PALIEVKT 168
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
2-165 |
1.80e-51 |
|
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: 173.51 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 2 NGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALY-DGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLIT 80
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 81 GLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRpGPVLVDIPKD 160
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR-GVAVLILPGD 159
|
....*
gi 489937867 161 IQLAS 165
Cdd:cd07039 160 VQDAP 164
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
352-525 |
1.58e-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: 166.17 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 352 IYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSF 431
Cdd:cd02014 2 IHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 432 MMNVQELGTVKRKQLPLKIVLLDNQRLGMVrQWQQLFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTM 511
Cdd:cd02014 82 AMLMGDLITAVKYNLPVIVVVFNNSDLGFI-KWEQEVMGQPEFGVDLP-NPDFAKIAEAMGIKGIRVEDPDELEAALDEA 159
|
170
....*....|....
gi 489937867 512 LNSEGPYLLHVSID 525
Cdd:cd02014 160 LAADGPVVIDVVTD 173
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
3-526 |
2.11e-48 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 176.71 E-value: 2.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPGgaiMPVYD--ALYDG-GVEHLLCRHEQGA--AMAAIGYAraTGKTGVCIATSGPGATN 77
Cdd:PRK09259 12 GFHLVIDALKLNGIDTIYGVVG---IPITDlaRLAQAeGIRYIGFRHEQSAgnAAAAAGFL--TQKPGVCLTVSAPGFLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 78 LITGLADALLDSVPVVAITGQVASSFIGTDA--FQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLV 155
Cdd:PRK09259 87 GLTALANATTNCFPMIMISGSSEREIVDLQQgdYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 156 DIPKDI-------QLASGTLepyfttVKNVEVFPH-----ADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVT 223
Cdd:PRK09259 167 DLPAKVlaqtmdaDEALTSL------VKVVDPAPAqlpapEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 224 QMP-----VActlKGLgaVEADYPyylgmlgmHGTKAA-NFAVQECDLLIAVGARFDDRVT-GKLNTFAPNASVIHMDID 296
Cdd:PRK09259 241 GIPflpmsMA---KGL--LPDTHP--------QSAAAArSLALANADVVLLVGARLNWLLShGKGKTWGADKKFIQIDIE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 297 PAEMNKLRQAHVALQGDLNSLLPALQQSLKiDAWRQHSAELRTEHTWRYDHpGEAIYAPLLLKQLS--DRKPADSVVTTD 374
Cdd:PRK09259 308 PQEIDSNRPIAAPVVGDIGSVMQALLAGLK-QNTFKAPAEWLDALAERKEK-NAAKMAEKLSTDTQpmNFYNALGAIRDV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 375 VGQHQMWS-----AQHMTYTR-------PENFITSSGLGTMGFGLPAAVGAQVA--RPndtVICISGDGSFMMNVQELGT 440
Cdd:PRK09259 386 LKENPDIYlvnegANTLDLARniidmykPRHRLDCGTWGVMGIGMGYAIAAAVEtgKP---VVAIEGDSAFGFSGMEVET 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 441 VKRKQLPLKIVLLDNQrlGMVRQWQQLFFQER-YSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYL 519
Cdd:PRK09259 463 ICRYNLPVTVVIFNNG--GIYRGDDVNLSGAGdPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTL 540
|
....*..
gi 489937867 520 LHVSIDE 526
Cdd:PRK09259 541 INVVIDP 547
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
7-525 |
5.66e-47 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 171.68 E-value: 5.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 7 VVHALRAQGVQTVFGYPGGAIMPVYDALYDGgVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADAL 86
Cdd:PRK07092 18 TIDLLRRFGITTVFGNPGSTELPFLRDFPDD-FRYVLGLQEAVVVGMADGYAQATGNAAFVNLHSAAGVGNAMGNLFTAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 87 LDSVPVVAITGQVASSFIGTDAF-QEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPKD--IQL 163
Cdd:PRK07092 97 KNHTPLVITAGQQARSILPFEPFlAAVQAAELPKPYVKWSIEPARAEDVPAAIARAYHIAMQPPRGPVFVSIPYDdwDQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 164 AsgtlEPYFTTVKNVEVFPHADVEQA-RKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPV-ACTLKGLGAVEADY 241
Cdd:PRK07092 177 A----EPLPARTVSSAVRPDPAALARlGDALDAARRPALVVGPAVDRAGAWDDAVRLAERHRAPVwVAPMSGRCSFPEDH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 242 PYYLGML--GMHGTKAanfAVQECDLLIAVGAR-FDDRVTGKLNTFAPNASVIHMDIDPAEmnklrqAHVALQGD--LNS 316
Cdd:PRK07092 253 PLFAGFLpaSREKISA---LLDGHDLVLVIGAPvFTYHVEGPGPHLPEGAELVQLTDDPGE------AAWAPMGDaiVGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 317 LLPALQQSLKIDAWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQ--MWsaQHMTYTRPENF 394
Cdd:PRK07092 324 IRLALRDLLALLPPSARPAPPARPMPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPSTRpaMQ--EHLPMRRQGSF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 395 IT--SSGLgtmGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFfqeR 472
Cdd:PRK07092 402 YTmaSGGL---GYGLPAAVGVALAQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRWFAPVF---G 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489937867 473 YSETTLTDNP--DFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSID 525
Cdd:PRK07092 476 VRDVPGLDLPglDFVALARGYGCEAVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-509 |
7.14e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 164.02 E-value: 7.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALYDGGVEH------LLCRHEQGAAMAAIGYARATGKTGVCIATSGPG 74
Cdd:PRK08327 7 YTAAELFLELLKELGVDYIFINSGTDYPPIIEAKARARAAGrplpefVICPHEIVAISMAHGYALVTGKPQAVMVHVDVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 75 ATNLITGLADALLDSVPVVAI--------TGQVAS--SFIGTdaFQEV-DVLGMSLSCTKHSFLVQSLEELPRIMAEAFA 143
Cdd:PRK08327 87 TANALGGVHNAARSRIPVLVFagrspyteEGELGSrnTRIHW--TQEMrDQGGLVREYVKWDYEIRRGDQIGEVVARAIQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 144 VANSGRPGPVLVDIPKDIqLASGTLEPYFTTVKNVEVFPHA----DVEQARKMLAQAQKPILYVGGGVGMAQAVPALREF 219
Cdd:PRK08327 165 IAMSEPKGPVYLTLPREV-LAEEVPEVKADAGRQMAPAPPApdpeDIARAAEMLAAAERPVIITWRAGRTAEGFASLRRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 220 IAVTQMPVACTLKGLGAVEADYPYYLGMLgmhgtkaANFAVQECDLLIAVGArfDDRVTGKLNTFAPNASVIHMDIDPA- 298
Cdd:PRK08327 244 AEELAIPVVEYAGEVVNYPSDHPLHLGPD-------PRADLAEADLVLVVDS--DVPWIPKKIRPDADARVIQIDVDPLk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 299 EMNKLR--QAHVALQGDLNSLLPALQQSLK-------------IDAWRQHSAELRTEHTWRYDHPGEA--IYAPLLLKQL 361
Cdd:PRK08327 315 SRIPLWgfPCDLCIQADTSTALDQLEERLKslasaerrrarrrRAAVRELRIRQEAAKRAEIERLKDRgpITPAYLSYCL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 362 SDRKPADSVVTTDVGQHQmwsaQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQE--LG 439
Cdd:PRK08327 395 GEVADEYDAIVTEYPFVP----RQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDRLVIATVGDGSFIFGVPEaaHW 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 440 TVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQE-------RYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALD 509
Cdd:PRK08327 471 VAERYGLPVLVVVFNNGGWLAVKEAVLEVYPEgyaarkgTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEELKGALR 547
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
4-526 |
8.17e-41 |
|
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 443161 [Multi-domain] Cd Length: 545 Bit Score: 154.93 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 4 AQWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGKTGVCIaTSGPGATNLITGL 82
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAhPGIRWVGCCNELNAGYAADGYARVNGLGALVT-TYGVGELSAINGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 83 ADALLDSVPVVAITGQVASSFIGTD-----------------AFQEVDVLGMSLS---CTkhsflvqslEELPRIMAEAF 142
Cdd:COG3961 87 AGAYAERVPVVHIVGAPGTRAQRRGpllhhtlgdgdfdhflrMFEEVTVAQAVLTpenAA---------AEIDRVLAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 143 AvanSGRPgpVLVDIPKDI-------QLASGTLEPYFTTVKNVEVFphadVEQARKMLAQAQKPILYVGGGVGMAQAVPA 215
Cdd:COG3961 158 R---EKRP--VYIELPRDVadapiepPEAPLPLPPPASDPAALAAA----VAAAAERLAKAKRPVILAGVEVHRFGLQEE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 216 LREFIAVTQMPVACTLKGLGAVEADYPYYLGM----LGMHGTKAAnfaVQECDLLIAVGARFDDRVTGkLNTFAPNASVI 291
Cdd:COG3961 229 LLALAEKTGIPVATTLLGKSVLDESHPQFIGTyagaASSPEVREY---VENADCVLCLGVVFTDTNTG-GFTAQLDPERT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 292 hMDIDPaemNKLRQAHVALQG-DLNSLLPAL-QQSLKIDAWRQHSAELRTehtWRYDHPGEAIYAPLLLKQLSDRKPADS 369
Cdd:COG3961 305 -IDIQP---DSVRVGGHIYPGvSLADFLEALaELLKKRSAPLPAPAPPPP---PPPAAPDAPLTQDRLWQRLQAFLDPGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 370 VVTTDVGQhQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLK 449
Cdd:COG3961 378 IVVADTGT-SLFGAADLRLPEGATFIAQPLWGSIGYTLPAALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 450 IVLLDNQ-----R--LGM------VRQWqqlffqeRYSEttltdnpdflmLASAFGiPGQHITRK----DQVEAALDTML 512
Cdd:COG3961 457 IFVLNNDgytieRaiHGPdgpyndIANW-------DYAK-----------LPEAFG-GGNALGFRvtteGELEEALAAAE 517
|
570
....*....|....*
gi 489937867 513 -NSEGPYLLHVSIDE 526
Cdd:COG3961 518 aNTDRLTLIEVVLDK 532
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-159 |
7.78e-39 |
|
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: 139.40 E-value: 7.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 7 VVHALRAQGVQTVFGYPGGAIMPVYDALYDG-GVEHLLCRHEQGAAMAAIGYARATGKtGVCIATSGPGATNLITGLADA 85
Cdd:cd06586 3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGdKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489937867 86 LLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGrPGPVLVDIPK 159
Cdd:cd06586 82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
357-530 |
2.20e-36 |
|
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.
Pssm-ID: 238968 [Multi-domain] Cd Length: 177 Bit Score: 133.18 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 357 LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd02010 4 IVHDLRAVMGDDDIVLLDVGAHKIWMARYYRTYAPNTCLISNGLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 437 ELGTVKRKQLPLKIVLLDNQRLGMVRqWQQLFFQERYSETTLTdNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEG 516
Cdd:cd02010 84 ELETAVRLKIPLVVLIWNDNGYGLIK-WKQEKEYGRDSGVDFG-NPDFVKYAESFGAKGYRIESADDLLPVLERALAADG 161
|
170
....*....|....
gi 489937867 517 PYLLHVSIDELENV 530
Cdd:cd02010 162 VHVIDCPVDYSENI 175
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
1-524 |
1.71e-31 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 127.65 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDALyDG--GVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNL 78
Cdd:PRK07586 1 MNGAESLVRTLVDGGVDVCFANPGTSEMHFVAAL-DRvpGMRCVLGLFEGVATGAADGYARMAGKPAATLLHLGPGLANG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 79 ITGLADALLDSVPVVAITGQVASSFIGTDAFQEVDV--LGMSLSCTKHSflVQSLEELPRIMAEAFAVANSGRPGPVLVD 156
Cdd:PRK07586 80 LANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIeaLARPVSGWVRR--SESAADVAADAAAAVAAARGAPGQVATLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 157 IPKDIQLASGTLEPYFTTVKNVEVFPHADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVT------QMPVACT 230
Cdd:PRK07586 158 LPADVAWSEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRERGLAAAARIAAATgarllaETFPARM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 231 LKGLGAVEADYPYYLGmlgmhgtKAANFAVQECDLLIAVGARfdDRVT-----GKLNTFAPNASVIHMDIDPAEmnklrQ 305
Cdd:PRK07586 238 ERGAGRPAVERLPYFA-------EQALAQLAGVRHLVLVGAK--APVAffaypGKPSRLVPEGCEVHTLAGPGE-----D 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 306 AHVALQgdlnsllpALQQSLKIDAWRQHSAELRtehtwRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSAQH 385
Cdd:PRK07586 304 AAAALE--------ALADALGAKPAAPPLAAPA-----RPPLPTGALTPEAIAQVIAALLPENAIVVDESITSGRGFFPA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 386 MTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDN---------- 455
Cdd:PRK07586 371 TAGAAPHDWLTLTG-GAIGQGLPLATGAAVACPDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANrayailrgel 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489937867 456 QRLGMVRQwqqlffQERYSETTLTDNP--DFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSI 524
Cdd:PRK07586 450 ARVGAGNP------GPRALDMLDLDDPdlDWVALAEGMGVPARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
357-524 |
1.83e-30 |
|
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: 116.93 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 357 LLKQLSDRKPADSVV----TTDVGQhqMWsaQHMTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFM 432
Cdd:cd02002 6 LAAALAAALPEDAIIvdeaVTNGLP--LR--DQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 433 MNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQER-----YSETTLTD-NPDFLMLASAFGIPGQHITRKDQVEA 506
Cdd:cd02002 81 YTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGpgenaPDGLDLLDpGIDFAAIAKAFGVEAERVETPEELDE 160
|
170
....*....|....*...
gi 489937867 507 ALDTMLNSEGPYLLHVSI 524
Cdd:cd02002 161 ALREALAEGGPALIEVVV 178
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
357-525 |
2.10e-26 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 105.69 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 357 LLKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQ 436
Cdd:cd02004 4 VLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 437 ELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEG 516
Cdd:cd02004 84 ELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGK 163
|
....*....
gi 489937867 517 PYLLHVSID 525
Cdd:cd02004 164 PALINVIID 172
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-524 |
1.70e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 106.88 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 1 MNGAQWVVHALRAQGVQTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLI 79
Cdd:PRK12474 5 MNGADSVVDTLLNCGVEVCFANPGTSEMHFVAALdRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 80 TGLADALLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELPRIMAEAFAVANSGRPGPVLVDIPK 159
Cdd:PRK12474 85 ANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 160 DIQLAsgtlEPYFTTVKNVEVFP---HAD-VEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMPVAC------ 229
Cdd:PRK12474 165 DVAWN----EAAYAAQPLRGIGPapvAAEtVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCdtfapr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 230 TLKGLGAVE-ADYPYYLGMLGMHgtkaanfaVQECDLLIAVGARfdDRVT-----GKLNTFAPnasvihmdiDPAEMNKL 303
Cdd:PRK12474 241 IERGAGRVPiERIPYFHEQITAF--------LKDVEQLVLVGAK--PPVSffaypGKPSWGAP---------PGCEIVYL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 304 RQAHVALQGDLNSLLPALqqslkiDAWRQHSAelRTEHTWRyDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHQMWSA 383
Cdd:PRK12474 302 AQPDEDLAQALQDLADAV------DAPAEPAA--RTPLALP-ALPKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 384 QHMTYTRPENFITSSGlGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVR- 462
Cdd:PRK12474 373 MSYDRARPHTHLPLTG-GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRSYAILNg 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 463 QWQQLFFQE--RYSETTLT-DNP--DFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSI 524
Cdd:PRK12474 452 ELQRVGAQGagRNALSMLDlHNPelNWMKIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
358-508 |
2.91e-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: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 358 LKQLSDRKPADSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQE 437
Cdd:cd02013 10 LRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDGAWGMSMME 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489937867 438 LGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLtDNPDFLMLASAFGIPGQHITRKDQVEAAL 508
Cdd:cd02013 90 IMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTEL-ESESFAKIAEACGAKGITVDKPEDVGPAL 159
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
391-528 |
2.64e-19 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 85.66 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 391 PEN--FITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQ-----RL--GMV 461
Cdd:cd02005 38 PKGtrFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDgytieRAihGPE 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489937867 462 RQWQQLffqerysettltDNPDFLMLASAFGIPGQHITRKDQVEAALDTML-----NSEGPYLLHVSIDELE 528
Cdd:cd02005 118 ASYNDI------------ANWNYTKLPEVFGGGGGGLSFRVKTEGELDEALkdalfNRDKLSLIEVILPKDD 177
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
7-158 |
4.62e-19 |
|
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: 84.47 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 7 VVHALRAQGVQTVFGYPGGAIMP-VYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADA 85
Cdd:cd07037 3 LVEELKRLGVRDVVISPGSRSAPlALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVVEA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 86 LLDSVPVVAITGQVASSFIGTDAFQEVDVLGMSLSCTKHSFLVQSLEELP------RIMAEAFAVANSGRPGPVLVDIP 158
Cdd:cd07037 83 YYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDdlwyllRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
366-525 |
1.14e-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: 75.80 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 366 PADSVVTTDVGQ-----HQMWSAQ-----HMTYtrpenfitssGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNV 435
Cdd:cd02003 13 GDDDVVINAAGSlpgdlHKLWRARtpggyHLEY----------GYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 436 QELGTVKRKQLPLKIVLLDNQRLGMVRQWQ-----QLF---FQERYSETTLTDNP----DFLMLASAFGIPGQHITRKDQ 503
Cdd:cd02003 83 SEIVTAVQEGLKIIIVLFDNHGFGCINNLQestgsGSFgteFRDRDQESGQLDGAllpvDFAANARSLGARVEKVKTIEE 162
|
170 180
....*....|....*....|..
gi 489937867 504 VEAALDTMLNSEGPYLLHVSID 525
Cdd:cd02003 163 LKAALAKAKASDRTTVIVIKTD 184
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
368-530 |
7.80e-15 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 73.47 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 368 DSVVTTDVGQHQMWSAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMNVQELGTVKRKQLP 447
Cdd:cd02006 24 DVRYVTTIGLSQIAGAQMLHVYKPRHWINCGQAGPLGWTVPAALGVAAADPDRQVVALSGDYDFQFMIEELAVGAQHRIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 448 LKIVLLDNQRLGMVRQWQQLF---------FQERYSETTLTDNPDFLMLASAFGIPGQHITRKDQVEAALDT----MLNS 514
Cdd:cd02006 104 YIHVLVNNAYLGLIRQAQRAFdmdyqvnlaFENINSSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQakklMAEH 183
|
170
....*....|....*.
gi 489937867 515 EGPYLLHVSIDELENV 530
Cdd:cd02006 184 RVPVVVEAILERVTNI 199
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
5-97 |
4.72e-14 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 69.83 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 5 QWVVHALRAQGVQTVFGYPGGAIMPVYDALYD-GGVEHLLCRHEQGAAMAAIGYARATGkTGVCIATSGPGATNLITGLA 83
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEEnPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90
....*....|....
gi 489937867 84 DALLDSVPVVAITG 97
Cdd:cd07038 80 GAYAEHVPVVHIVG 93
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
357-526 |
2.16e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 69.09 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 357 LLKQLSDRKPADSVVTTDVG--QHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN 434
Cdd:PRK06163 18 LTCRLVAKLKDEEAVIGGIGntNFDLWAAGQ----RPQNFYM---LGSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 435 VQELGTV-KRKQLPLKIVLLDNQrlgmvrqwqqlFFQERYSETTLT-DNPDFLMLASAFGIPGQHITRKDQ-VEAALDTM 511
Cdd:PRK06163 91 LGALGTIaALAPKNLTIIVMDNG-----------VYQITGGQPTLTsQTVDVVAIARGAGLENSHWAADEAhFEALVDQA 159
|
170
....*....|....*
gi 489937867 512 LNSEGPYLLHVSIDE 526
Cdd:PRK06163 160 LSGPGPSFIAVRIDD 174
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
15-455 |
2.33e-12 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 69.34 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 15 GVQTVFGYPGGAIMPVYDAL-YDGGVEHLLCRHEQGAAMAAIGYARATGkTGVCIATSGPGATNLITGLADALLDSVPVV 93
Cdd:PLN02573 30 GVTDVFSVPGDFNLTLLDHLiAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAGAYSENLPVI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 94 AITGQVASSFIGTD-----------------AFQEVdvlgmslscTKHSFLVQSLEELPRIMAEAFAVAnSGRPGPVLVD 156
Cdd:PLN02573 109 CIVGGPNSNDYGTNrilhhtiglpdfsqelrCFQTV---------TCYQAVINNLEDAHELIDTAISTA-LKESKPVYIS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 157 IP---KDIQLASGTLE--PYFTTVK-----NVEvfphADVEQARKMLAQAQKPILYVGGGVGMAQAVPALREFIAVTQMP 226
Cdd:PLN02573 179 VScnlAAIPHPTFSREpvPFFLTPRlsnkmSLE----AAVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 227 VACTLKGLGAVEADYPYYLGML-GMHGTKAANFAVQECDLLIAVGARFDDRVT-GKLNTFAPNASVIhmdIDPaemNKLR 304
Cdd:PLN02573 255 VAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYSSvGYSLLLKKEKAII---VQP---DRVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 305 QAHVALQGD--LNSLLPALQQSLKID--AWRQHSAELRTEHTWRYDHPGEAIYAPLLLKQLSDRKPADSVVTTDVGQHqm 380
Cdd:PLN02573 329 IGNGPAFGCvlMKDFLEALAKRVKKNttAYENYKRIFVPEGEPLKSEPGEPLRVNVLFKHIQKMLSGDTAVIAETGDS-- 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489937867 381 W-SAQHMTYTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVI-CIsGDGSFMMNVQELGTVKRKQLPLKIVLLDN 455
Cdd:PLN02573 407 WfNCQKLKLPEGCGYEFQMQYGSIGWSVGATLGYAQAAPDKRVIaCI-GDGSFQVTAQDVSTMIRCGQKSIIFLINN 482
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
390-524 |
1.60e-09 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 56.73 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 390 RPENFITssgLGTMGFGLPAAVGAQVARPnDTVICISGDGSFMMNVQELGTV-KRKQLPLKIVLLDNQRlgmvrqwqqlf 468
Cdd:cd02001 34 RDGHFYM---LGSMGLAGSIGLGLALGLS-RKVIVVDGDGSLLMNPGVLLTAgEFTPLNLILVVLDNRA----------- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 469 fqerYSET----TLTDNPDFLMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSI 524
Cdd:cd02001 99 ----YGSTggqpTPSSNVNLEAWAAACGYLVLSAPLLGGLGSEFAGLLATTGPTLLHAPI 154
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
358-524 |
5.76e-09 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 55.78 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 358 LKQLSDRKPADSVV--TTDVGQHQMWSAQHM-TYTRPENFITssgLGTMGFGLPAAVGAQVARPNDTVICISGDGSFMMN 434
Cdd:cd03371 5 IEIVLSRAPATAAVvsTTGMTSRELFELRDRpGGGHAQDFLT---VGSMGHASQIALGIALARPDRKVVCIDGDGAALMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 435 VQELGTVKRKQLP-LKIVLLDNQRLGMVRqwqqlffqerySETTLTDNPDFLMLASAFGIPG-QHITRKDQVEAALDTML 512
Cdd:cd03371 82 MGGLATIGGLAPAnLIHIVLNNGAHDSVG-----------GQPTVSFDVSLPAIAKACGYRAvYEVPSLEELVAALAKAL 150
|
170
....*....|..
gi 489937867 513 NSEGPYLLHVSI 524
Cdd:cd03371 151 AADGPAFIEVKV 162
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
361-525 |
5.56e-08 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 52.68 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 361 LSDRKpaDSVVTTDVG--QHQMWSAQHmtytRPENFITssgLGTMGFGLPAAVGAQVARPnDTVICISGDGSFMMNVQEL 438
Cdd:cd03372 9 IADLK--DELVVSNIGfpSKELYAAGD----RPLNFYM---LGSMGLASSIGLGLALAQP-RKVIVIDGDGSLLMNLGAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 439 GTVKrKQLP--LKIVLLDNqrlgmvRQWQQLFFQERYSettlTDNPDFLMLASAFGIpgQHITRKDQVEAALDTM-LNSE 515
Cdd:cd03372 79 ATIA-AEKPknLIIVVLDN------GAYGSTGNQPTHA----GKKTDLEAVAKACGL--DNVATVASEEAFEKAVeQALD 145
|
170
....*....|
gi 489937867 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 |
6.76e-06 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 46.43 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 410 AVGAQVARpNDTVICISGDGSFM--MNVqeLGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQ---ERYSETTLtdNPDF 484
Cdd:cd02009 60 ALGIALAT-DKPTVLLTGDLSFLhdLNG--LLLGKQEPLNLTIVVINNNGGGIFSLLPQASFEdefERLFGTPQ--GLDF 134
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489937867 485 LMLASAFGIPGQHITRKDQVEAALDTMLNSEGPYLLHVSID 525
Cdd:cd02009 135 EHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| TPP_PYR_PFOR_IOR-alpha_like |
cd07034 |
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ... |
3-156 |
1.91e-05 |
|
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: 44.80 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 3 GAQWVVHALRAQGVQTVFGYPG---GAIMPVYDALYDGGVEHLLCR--HEQGAAMAAIGyARATGKTGVCiATSGPGATN 77
Cdd:cd07034 1 GNEAVARGALAAGVDVVAAYPItpsTEIAETLAKAVLGELGGVVVQaeSEHAAAEAAIG-ASAAGARAMT-ATSGPGLNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 78 LITGLADALLDSVPVVAITGQ---VASSFIGTDAfQEVdvlgMSLSCTKHSFLV---QSLEELPRIMAEAFAVA-NSGRP 150
Cdd:cd07034 79 MAEALYLAAGAELPLVIVVAQrpgPSTGLPKPDQ-SDL----MAARYGGHPWPVlapSSVQEAFDLALEAFELAeKYRLP 153
|
....*.
gi 489937867 151 GPVLVD 156
Cdd:cd07034 154 VIVLSD 159
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
401-460 |
2.79e-04 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 42.91 E-value: 2.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489937867 401 GTMGFGLPAAVGAQVARPNDTVICISGDGS--------FMMNVqelgtvkRKQLPLKIVLLDNQRLGM 460
Cdd:PRK11867 69 TIHGRALAIATGLKLANPDLTVIVVTGDGDalaiggnhFIHAL-------RRNIDITYILFNNQIYGL 129
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
42-96 |
1.35e-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: 1.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489937867 42 LLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSVPVVAIT 96
Cdd:PLN02980 343 IACFDERSLAFHALGYARGSLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLT 397
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
394-460 |
2.72e-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: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489937867 394 FITSSGL-GTMGFGLPAAVGAQVARPNDTVICISGDG-SFMMNVQELGTVKRKQLPLKIVLLDNQRLGM 460
Cdd:cd03375 43 YFNTYGFhTLHGRALAVATGVKLANPDLTVIVVSGDGdLAAIGGNHFIHAARRNIDITVIVHNNQIYGL 111
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
365-460 |
3.49e-03 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 39.35 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489937867 365 KPADSVVTTDVGQHqmwsaqhmtyTRPENFITSSGLGTM-GFGLPAAVGAQVARPNDTVICISGDG-SFMMNVQELGTVK 442
Cdd:PRK11866 32 PPENVVVVSGIGCS----------SNLPEFLNTYGIHGIhGRVLPIATGVKWANPKLTVIGYGGDGdGYGIGLGHLPHAA 101
|
90
....*....|....*...
gi 489937867 443 RKQLPLKIVLLDNQRLGM 460
Cdd:PRK11866 102 RRNVDITYIVSNNQVYGL 119
|
|
| |
