|
Name |
Accession |
Description |
Interval |
E-value |
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
1-569 |
1.24e-147 |
|
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: 437.28 E-value: 1.24e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNH--PELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGG 78
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDALRRQsgIRHILV--RHEQGAAFMADGYARATGKPGVCLVTSGPGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 79 TNAITGVMGGWVDSIPMFVISGQVkfsttiastnvPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFL 155
Cdd:COG0028 79 TNLVTGLADAYMDSVPVLAITGQV-----------PTSLIGRgafQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 156 AGHGRPGPVWLDIPLNVQGALIETDAlqhYDPSEDAVQVVAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQ 235
Cdd:COG0028 148 ATSGRPGPVVLDIPKDVQAAEAEEEP---APPELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 236 LLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQiSYNWENFAKDAYLVAVDIDA 315
Cdd:COG0028 225 LAERLGAPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALAEADLVLAVGARFDDRV-TGNWDEFAPDAKIIHIDIDP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 316 GELKKpTLTVDMPIHADLGDFLPGLLGAMQAdHKLGNIEWLEWCRKINQKYPAVQPhhyTPHSPVNPYVFMDRLSQYLDE 395
Cdd:COG0028 304 AEIGK-NYPVDLPIVGDAKAVLAALLEALEP-RADDRAAWLARIAAWRAEYLAAYA---ADDGPIKPQRVIAALREALPD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 396 GDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLN 475
Cdd:COG0028 379 DAIVVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLARPDRPVVAITGDGGFQMNLQELATAVRYGLP 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 476 LKIFWLNNDGYHSIRQTQTNIFNARFcgvnetSGISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEV 553
Cdd:COG0028 459 VKVVVLNNGGLGMVRQWQELFYGGRY------SGTDLPNPDfaKLAEAFGAKGERVETPEELEAALEEALASDGPALIDV 532
|
570
....*....|....*.
gi 501445419 554 ILNPAQGFEPKLSSRI 569
Cdd:COG0028 533 RVDPEENPPGATLDEM 548
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
3-553 |
1.05e-84 |
|
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: 275.06 E-value: 1.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 3 MKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAI 82
Cdd:TIGR00118 1 MSGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDSGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 83 TGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHG 159
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQ-----------VPTSLIGSdafQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 160 RPGPVWLDIPLNVQGALIEtdalqhYDPSED-AVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSHDVFIQ 235
Cdd:TIGR00118 150 RPGPVLVDLPKDVTTAEIE------YPYPEKvNLPGYRPTVKGHPLQIkkaAELINLAKKPVILVGGGVIIAGASEELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 236 LLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDA 315
Cdd:TIGR00118 224 LAERIQIPVTTTLMGLGSFPEDHPLSLGMLGMHGTKTANLAVHECDLIIAVGARFDDR-VTGNLAKFAPNAKIIHIDIDP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 316 GELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGNIEWLEWCRKINQKYPAVQPHHytpHSPVNPYVFMDRLSQYLDE 395
Cdd:TIGR00118 303 AEIGK-NVRVDIPIVGDARNVLEELLKKLFELKERKESAWLEQINKWKKEYPLKMDYT---EEGIKPQQVIEELSRVTKD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 396 GDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLN 475
Cdd:TIGR00118 379 EAIVTTDVGQHQMWAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPESTVICITGDGSFQMNLQELSTAVQYDIP 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501445419 476 LKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEV 553
Cdd:TIGR00118 459 VKILILNNRYLGMVRQWQELFYEERY---SHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALSSNEPVLLDV 533
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
2-555 |
3.83e-76 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 252.39 E-value: 3.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 2 EMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNhPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNA 81
Cdd:PRK06048 7 KMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 82 ITGVMGGWVDSIPMFVISGQVkfsttiastnvPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGH 158
Cdd:PRK06048 86 VTGIATAYMDSVPIVALTGQV-----------PRSMIGNdafQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 159 GRPGPVWLDIPLNVQGALIETD-----ALQHYDPSE--DAVQVvappsndvySQLIEKICNARKPVILAGSGIRLSGSHD 231
Cdd:PRK06048 155 GRPGPVLIDLPKDVTTAEIDFDypdkvELRGYKPTYkgNPQQI---------KRAAELIMKAERPIIYAGGGVISSNASE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 232 VFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAV 311
Cdd:PRK06048 226 ELVELAETIPAPVTTTLMGIGAIPTEHPLSLGMLGMHGTKYANYAIQESDLIIAVGARFDDR-VTGKLASFAPNAKIIHI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 312 DIDAGELKKpTLTVDMPIHADLGDFLPGLLGAMQADhklgniEWLEWCRKINQ---KYPAvqphHYTPHSPV-NPYVFMD 387
Cdd:PRK06048 305 DIDPAEISK-NVKVDVPIVGDAKQVLKSLIKYVQYC------DRKEWLDKINQwkkEYPL----KYKEREDViKPQYVIE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 388 RLSQYLDEGdVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQ 467
Cdd:PRK06048 374 QIYELCPDA-IIVTEVGQHQMWAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKVGKPDKTVIDIAGDGSFQMNSQELA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 468 TIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSGISFpsaDKIARAYGFEFIKIDAVEDMDEKIKKVLLSDT 547
Cdd:PRK06048 453 TAVQNDIPVIVAILNNGYLGMVRQWQELFYDKRYSHTCIKGSVDF---VKLAEAYGALGLRVEKPSEVRPAIEEAVASDR 529
|
....*...
gi 501445419 548 SIVCEVIL 555
Cdd:PRK06048 530 PVVIDFIV 537
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-534 |
1.19e-75 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 251.17 E-value: 1.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTN 80
Cdd:PRK08155 11 KRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDALSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGATN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 81 AITGVMGGWVDSIPMFVISGQVkfsttiastnvPLRQLGDQEFNIVD----SVRcMTKYAVMLTEPESIAYHLERALFLA 156
Cdd:PRK08155 91 LVTAIADARLDSIPLVCITGQV-----------PASMIGTDAFQEVDtygiSIP-ITKHNYLVRDIEELPQVISDAFRIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 157 GHGRPGPVWLDIPLNVQGALIETDALqhydPSEDAVQVVAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQL 236
Cdd:PRK08155 159 QSGRPGPVWIDIPKDVQTAVIELEAL----PAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARAREL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 237 LEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKDAYLVAVDIDAG 316
Cdd:PRK08155 235 AEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGARSTNYILQEADLLIVLGARFDDRAIG-KTEQFCPNAKIIHVDIDRA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 317 ELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLgniEWLEWCRKINQKYPAVQPhhyTPHSPVNPYVFMDRLSQYLDEG 396
Cdd:PRK08155 314 ELGK-IKQPHVAIQADVDDVLAQLLPLVEAQPRA---EWHQLVADLQREFPCPIP---KADDPLSHYGLINAVAACVDDN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 397 DVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNL 476
Cdd:PRK08155 387 AIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPERKVLCFSGDGSLMMNIQEMATAAENQLDV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 501445419 477 KIFWLNNDGYHSIRQTQTNIFNARFCGVNETSGISFPsadKIARAYGFEFIKIDAVED 534
Cdd:PRK08155 467 KIILMNNEALGLVHQQQSLFYGQRVFAATYPGKINFM---QIAAGFGLETCDLNNEAD 521
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
6-556 |
1.55e-73 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 245.50 E-value: 1.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 6 SDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGV 85
Cdd:PRK07282 13 SDLVLETLRDLGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAITGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 86 MGGWVDSIPMFVISGQVKFSTtiastnvplrqLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPG 162
Cdd:PRK07282 93 ADAMSDSVPLLVFTGQVARAG-----------IGKdafQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 163 PVWLDIPLNVQGalIETDA-------LQHYDPSEDavqvvapPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQ 235
Cdd:PRK07282 162 PVVIDLPKDVSA--LETDFiydpevnLPSYQPTLE-------PNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 236 LLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKDAYLVAVDIDA 315
Cdd:PRK07282 233 FAERYQIPVVTTLLGQGTIATSHPLFLGMGGMHGSYAANIAMTEADFMINIGSRFDDRLTG-NPKTFAKNAKVAHIDIDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 316 GELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGniEWLEWCRKINQKYPAVQPhhytPHSPVNPYVFMDRLSQYLDE 395
Cdd:PRK07282 312 AEIGK-IIKTDIPVVGDAKKALQMLLAEPTVHNNTE--KWIEKVTKDKNRVRSYDK----KERVVQPQAVIERIGELTNG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 396 GDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLN 475
Cdd:PRK07282 385 DAIVVTDVGQHQMWAAQYYPYQNERQLVTSGGLGTMGFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 476 LKIFWLNNDGYHSIRQTQTNIFNARfcgVNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIkKVLLSDTSIVCEVIL 555
Cdd:PRK07282 465 IKVVMLNNHSLGMVRQWQESFYEGR---TSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDL-EVITEDVPMLIEVDI 540
|
.
gi 501445419 556 N 556
Cdd:PRK07282 541 S 541
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
13-554 |
5.12e-70 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 236.90 E-value: 5.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 13 MVENGITDLFTVTGGGAMHLNDSLgNHPELVSTYNH----HEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGG 88
Cdd:CHL00099 20 LVRHGVKHIFGYPGGAILPIYDEL-YAWEKKGLIKHilvrHEQGAAHAADGYARSTGKVGVCFATSGPGATNLVTGIATA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 89 WVDSIPMFVISGQVkfSTTIASTNvplrqlGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDI 168
Cdd:CHL00099 99 QMDSVPLLVITGQV--GRAFIGTD------AFQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPVLIDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 169 PLNVQgalIETDALQHYDPSEDAVQV-----VAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIP 243
Cdd:CHL00099 171 PKDVG---LEKFDYYPPEPGNTIIKIlgcrpIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELAELYKIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 244 VVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAGELKKpTL 323
Cdd:CHL00099 248 VTTTLMGKGIFDEDHPLCLGMLGMHGTAYANFAVSECDLLIALGARFDDR-VTGKLDEFACNAQVIHIDIDPAEIGK-NR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 324 TVDMPIHADLGDFLPGLLGAMQ-ADHKLGNIEWLEWCRKIN---QKYPAVQPHHYTPHSPVNPYVFMDRLSQyldegDVT 399
Cdd:CHL00099 326 IPQVAIVGDVKKVLQELLELLKnSPNLLESEQTQAWRERINrwrKEYPLLIPKPSTSLSPQEVINEISQLAP-----DAY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 400 VTGNgsacVCSFQ---AMVIKKNQRLF-TNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLN 475
Cdd:CHL00099 401 FTTD----VGQHQmwaAQFLKCKPRKWlSSAGLGTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 476 LKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSGIsfPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIV--CEV 553
Cdd:CHL00099 477 IKIIIINNKWQGMVRQWQQAFYGERYSHSNMEEGA--PDFVKLAEAYGIKGLRIKSRKDLKSSLKEALDYDGPVLidCQV 554
|
.
gi 501445419 554 I 554
Cdd:CHL00099 555 I 555
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
3-559 |
7.78e-69 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 233.49 E-value: 7.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 3 MKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLgNHPELVSTYNHHEQACAIAAEAYARLTGRIAlVCV-TSGPGGTNA 81
Cdd:PRK06276 1 MKGAEAIIKALEAEGVKIIFGYPGGALLPFYDAL-YDSDLIHILTRHEQAAAHAADGYARASGKVG-VCVaTSGPGATNL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 82 ITGVMGGWVDSIPMFVISGQVkfsttiastnvPLRQLGDQEFNIVDSVRC---MTKYAVMLTEPESIAYHLERALFLAGH 158
Cdd:PRK06276 79 VTGIATAYADSSPVIALTGQV-----------PTKLIGNDAFQEIDALGIfmpITKHNFQIKKPEEIPEIFRAAFEIAKT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 159 GRPGPVWLDIPLNVQGAliETDALQHYDPSEDAVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSHDVFIQ 235
Cdd:PRK06276 148 GRPGPVHIDLPKDVQEG--ELDLEKYPIPAKIDLPGYKPTTFGHPLQIkkaAELIAEAERPVILAGGGVIISGASEELIE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 236 LLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDA 315
Cdd:PRK06276 226 LSELVKIPVCTTLMGKGAFPEDHPLALGMVGMHGTKAANYSVTESDVLIAIGCRFSDR-TTGDISSFAPNAKIIHIDIDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 316 GELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGNIEWLEwcrKINQKYPAVQPHHYTPHSPVNPYVFMDRLSQYLDE 395
Cdd:PRK06276 305 AEIGK-NVRVDVPIVGDAKNVLRDLLAELMKKEIKNKSEWLE---RVKKLKKESIPRMDFDDKPIKPQRVIKELMEVLRE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 396 GD-----VTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTII 470
Cdd:PRK06276 381 IDpskntIITTDVGQNQMWMAHFFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKPDANVIAITGDGGFLMNSQELATIA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 471 HNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVN--ETsgisfPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTS 548
Cdd:PRK06276 461 EYDIPVVICIFDNRTLGMVYQWQNLYYGKRQSEVHlgET-----PDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEP 535
|
570
....*....|.
gi 501445419 549 IVCEVILNPAQ 559
Cdd:PRK06276 536 YLLDIIIDPAE 546
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
1-556 |
3.78e-67 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 228.45 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTN 80
Cdd:PRK08527 1 KKLSGSQMVCEALKEEGVKVVFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 81 AITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGDQEFNIVDSV---RCMTKYAVMLTEPESIAYHLERALFLAG 157
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQ-----------VPNSLIGTDAFQEIDAVgisRPCVKHNYLVKSIEELPRILKEAFYIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 158 HGRPGPVWLDIPLNVQGALIETdalqHYdPSEDAVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSHDVFI 234
Cdd:PRK08527 150 SGRPGPVHIDIPKDVTATLGEF----EY-PKEISLKTYKPTYKGNSRQIkkaAEAIKEAKKPLFYLGGGAILSNASEEIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 235 QLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDID 314
Cdd:PRK08527 225 ELVKKTGIPAVETLMARGVLRSDDPLLLGMLGMHGSYAANMAMSECDLLISLGARFDDR-VTGKLSEFAKHAKIIHVDID 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 315 AGELKKpTLTVDMPIHADLGDFLPGLLGAMQaDHKLGNIEwlEWcRKINQKYPAVQPHHYTPHSPV-NPYVFMDRLSQYL 393
Cdd:PRK08527 304 PSSISK-IVNADYPIVGDLKNVLKEMLEELK-EENPTTYK--EW-REILKRYNELHPLSYEDSDEVlKPQWVIERVGELL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 394 DEGDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNK 473
Cdd:PRK08527 379 GDDAIISTDVGQHQMWVAQFYPFNYPRQLATSGGLGTMGYGLPAALGAKLAVPDKVVINFTGDGSILMNIQELMTAVEYK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 474 LNLKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEV 553
Cdd:PRK08527 459 IPVINIILNNNFLGMVRQWQTFFYEERY---SETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESDKVALIDV 535
|
...
gi 501445419 554 ILN 556
Cdd:PRK08527 536 KID 538
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-591 |
6.67e-65 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 222.70 E-value: 6.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEM-KVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGT 79
Cdd:PRK06466 1 MELlSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 80 NAITGVMGGWVDSIPMFVISGQVkfsttiASTNVplrqlGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLA 156
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQV------PSTLI-----GEdafQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 157 GHGRPGPVWLDIPLNVqgalieTDALQHYD---PSEDAVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSH 230
Cdd:PRK06466 150 QSGRPGPVVVDIPKDM------TNPAEKFEyeyPKKVKLRSYSPAVRGHSGQIrkaVEMLLAAKRPVIYSGGGVVLGNAS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 231 DVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKDAYLVA 310
Cdd:PRK06466 224 ALLTELAHLLNLPVTNTLMGLGGFPGTDRQFLGMLGMHGTYEANMAMHHADVILAVGARFDDRVTN-GPAKFCPNAKIIH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 311 VDIDAGELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGNIEWLE-WCRKINQ--KYPAVQPHHYTPHSPVNPyvfmD 387
Cdd:PRK06466 303 IDIDPASISK-TIKADIPIVGPVESVLTEMLAILKEIGEKPDKEALAaWWKQIDEwrGRHGLFPYDKGDGGIIKP----Q 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 388 RLSQYLDEgdVTvtgNGSACVCS-------FQAMVIKKNQ-RLFTNS-GCASMGYGLPAALGAAVALGGKRVICLDGDGS 458
Cdd:PRK06466 378 QVVETLYE--VT---NGDAYVTSdvgqhqmFAAQYYKFNKpNRWINSgGLGTMGFGLPAAMGVKLAFPDQDVACVTGEGS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 459 IQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEK 538
Cdd:PRK06466 453 IQMNIQELSTCLQYGLPVKIINLNNGALGMVRQWQDMQYEGRH---SHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPK 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 501445419 539 IKKVL-LSDTSIVCEVILNPAQGFEPKLssriLQDGTMvspslEDMfpFLSAEE 591
Cdd:PRK06466 530 LEEAFaMKDRLVFIDIYVDRSEHVYPMQ----IADGSM-----RDM--WLSKTE 572
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-543 |
1.52e-64 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 221.62 E-value: 1.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEM-KVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGT 79
Cdd:PRK08979 1 MEMlSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 80 NAITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLA 156
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQ-----------VPSNLIGNdafQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 157 GHGRPGPVWLDIPLNVQGALIEtdaLQHYDPSEDAVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSHDVF 233
Cdd:PRK08979 150 STGRPGPVVIDLPKDCLNPAIL---HPYEYPESIKMRSYNPTTSGHKGQIkrgLQALLAAKKPVLYVGGGAIISGADKQI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 234 IQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKDAYLVAVDI 313
Cdd:PRK08979 227 LQLAEKLNLPVVSTLMGLGAFPGTHKNSLGMLGMHGRYEANMAMHNADLIFGIGVRFDDRTTN-NLEKYCPNATILHIDI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 314 DAGELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGNIEWLE-WCRKINQkYPAVQPHHYTPHSpvnpyvfmDRLS-Q 391
Cdd:PRK08979 306 DPSSISK-TVRVDIPIVGSADKVLDSMLALLDESGETNDEAAIAsWWNEIEV-WRSRNCLAYDKSS--------ERIKpQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 392 YLDEGDVTVTgNGSACVCS-------FQAMV--IKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMN 462
Cdd:PRK08979 376 QVIETLYKLT-NGDAYVASdvgqhqmFAALYypFDKPRRWINSGGLGTMGFGLPAAMGVKFAMPDETVVCVTGDGSIQMN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 463 LQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKV 542
Cdd:PRK08979 455 IQELSTALQYDIPVKIINLNNRFLGMVKQWQDMIYQGRH---SHSYMDSVPDFAKIAEAYGHVGIRISDPDELESGLEKA 531
|
.
gi 501445419 543 L 543
Cdd:PRK08979 532 L 532
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-563 |
2.16e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 221.38 E-value: 2.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 2 EMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSL-GNHPELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGGTN 80
Cdd:PRK06725 14 EVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALyESGLKHILT--RHEQAAIHAAEGYARASGKVGVVFATSGPGATN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 81 AITGVMGGWVDSIPMFVISGQVkfSTTIASTNvplrqlGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGR 160
Cdd:PRK06725 92 LVTGLADAYMDSIPLVVITGQV--ATPLIGKD------GFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 161 PGPVWLDIPLNVQGALI-----ETDALQHYDPSedavqvvAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQ 235
Cdd:PRK06725 164 PGPVLIDIPKDVQNEKVtsfynEVVEIPGYKPE-------PRPDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 236 LLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDA 315
Cdd:PRK06725 237 FARENRIPVVSTLMGLGAYPPGDPLFLGMLGMHGTYAANMAVTECDLLLALGVRFDDR-VTGKLELFSPHSKKVHIDIDP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 316 GELKKpTLTVDMPIHADLGDFLPGLL---GAMQADhklgniEWLEWCRKINQKYPAvqpHHYTPHSPVNPYVFMDRLSQy 392
Cdd:PRK06725 316 SEFHK-NVAVEYPVVGDVKKALHMLLhmsIHTQTD------EWLQKVKTWKEEYPL---SYKQKESELKPQHVINLVSE- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 393 LDEGDVTVT---GNGSACVCSFQAMvikKNQRLF-TNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQT 468
Cdd:PRK06725 385 LTNGEAIVTtevGQHQMWAAHFYKA---KNPRTFlTSGGLGTMGFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 469 IIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFcgvnETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTS 548
Cdd:PRK06725 462 IAENNIPVKVFIINNKFLGMVRQWQEMFYENRL----SESKIGSPDFVKVAEAYGVKGLRATNSTEAKQVMLEAFAHEGP 537
|
570
....*....|....*
gi 501445419 549 IVCEVILNPAQGFEP 563
Cdd:PRK06725 538 VVVDFCVEEGENVFP 552
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
49-553 |
7.27e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 221.08 E-value: 7.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 49 HEQACAIAAEAYARLTGRIAlVCV-TSGPGGTNAITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGD---QEFN 124
Cdd:PRK07418 68 HEQGAAHAADGYARATGKVG-VCFgTSGPGATNLVTGIATAQMDSVPMVVITGQ-----------VPRPAIGTdafQETD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 125 IVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNVqgALIETDalqhYDPSEDAvQVVAP------P 198
Cdd:PRK07418 136 IFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLIDIPKDV--GQEEFD----YVPVEPG-SVKPPgyrptvK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 199 SNDV-YSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAW---NAHDnlwDDHPLYCGRPGTIGTRGGN 274
Cdd:PRK07418 209 GNPRqINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQIPVTTTLmgkGAFD---EHHPLSVGMLGMHGTAYAN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 275 FVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAGELKKpTLTVDMPIHADLGDFLPGLLG-AMQADHKLGNI 353
Cdd:PRK07418 286 FAVTECDLLIAVGARFDDR-VTGKLDEFASRAKVIHIDIDPAEVGK-NRRPDVPIVGDVRKVLVKLLErSLEPTTPPRTQ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 354 EWLEWCRKINQKYPAVQPHHYTPHSPVNPYVFMDRLSQyldegDVTVTGNgsacVCSFQ---AMVIKKNQRLFTNS-GCA 429
Cdd:PRK07418 364 AWLERINRWKQDYPLVVPPYEGEIYPQEVLLAVRDLAP-----DAYYTTD----VGQHQmwaAQFLRNGPRRWISSaGLG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 430 SMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSG 509
Cdd:PRK07418 435 TMGFGMPAAMGVKVALPDEEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNGWQGMVRQWQESFYGERYSASNMEPG 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 501445419 510 IsfPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEV 553
Cdd:PRK07418 515 M--PDFVKLAEAFGVKGMVISERDQLKDAIAEALAHDGPVLIDV 556
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
17-558 |
3.64e-63 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 217.44 E-value: 3.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 17 GITDLFTVTGGGAMHLNDSLGNhpelvSTYNH----HEQACAIAAEAYARLTGRIAlVCV-TSGPGGTNAITGVMGGWVD 91
Cdd:PRK08978 15 GVDTVFGYPGGAIMPVYDALYD-----GGVEHllcrHEQGAAMAAIGYARATGKVG-VCIaTSGPGATNLITGLADALLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 92 SIPMFVISGQVkfsttiaSTNVplrqLGDQEFNIVD----SVRCmTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLD 167
Cdd:PRK08978 89 SVPVVAITGQV-------SSPL----IGTDAFQEIDvlglSLAC-TKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 168 IPLNVQGALIETDALQHYDPSEdavqvVAPPSNDVySQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTA 247
Cdd:PRK08978 157 IPKDIQLAEGELEPHLTTVENE-----PAFPAAEL-EQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVAT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 248 WNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAGELKKPTLtVDM 327
Cdd:PRK08978 231 LKGLGAVEADHPYYLGMLGMHGTKAANLAVQECDLLIAVGARFDDR-VTGKLNTFAPHAKVIHLDIDPAEINKLRQ-AHV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 328 PIHADLGDFLPGLLGAMQADhklgniEWLEWCRKINQKYPAVQPHhytPHSPVNPYVFMDRLSQYLDEGDVTVTGNGSAC 407
Cdd:PRK08978 309 ALQGDLNALLPALQQPLNID------AWRQHCAQLRAEHAWRYDH---PGEAIYAPALLKQLSDRKPADTVVTTDVGQHQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 408 VCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYH 487
Cdd:PRK08978 380 MWVAQHMRFTRPENFITSSGLGTMGFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQELGTIKRKQLPVKIVLLDNQRLG 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501445419 488 SIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILNPA 558
Cdd:PRK08978 460 MVRQWQQLFFDERY---SETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVSIDEL 527
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
13-553 |
1.49e-61 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 214.19 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 13 MVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWVDS 92
Cdd:PRK09107 21 LKDQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAVTPLQDALMDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 93 IPMFVISGQVkfSTTIASTNvplrqlGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNV 172
Cdd:PRK09107 101 IPLVCITGQV--PTHLIGSD------AFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVDIPKDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 173 QGAlietdALQHYDPSEDAVQVVAPPSND----VYSQLIEKICNARKPVILAGSGIRLSGSHDVfiQLLEKL----NIPV 244
Cdd:PRK09107 173 QFA-----TGTYTPPQKAPVHVSYQPKVKgdaeAITEAVELLANAKRPVIYSGGGVINSGPEAS--RLLRELveltGFPI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 245 VT------AWNAHDNLWddhplyCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAGEL 318
Cdd:PRK09107 246 TStlmglgAYPASGKNW------LGMLGMHGTYEANMAMHDCDVMLCVGARFDDR-ITGRLDAFSPNSKKIHIDIDPSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 319 KKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGNIEWL-EWCRKINQkYPAVQPHHYTPHSPV-NPYVFMDRLSQYLDEG 396
Cdd:PRK09107 319 NK-NVRVDVPIIGDVGHVLEDMLRLWKARGKKPDKEALaDWWGQIAR-WRARNSLAYTPSDDViMPQYAIQRLYELTKGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 397 DVTVTGN-GSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLN 475
Cdd:PRK09107 397 DTYITTEvGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTAVQYNLP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 476 LKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIV--CEV 553
Cdd:PRK09107 477 VKIFILNNQYMGMVRQWQQLLHGNRL---SHSYTEAMPDFVKLAEAYGAVGIRCEKPGDLDDAIQEMIDVDKPVIfdCRV 553
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
15-541 |
2.99e-60 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 210.99 E-value: 2.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 15 ENGITDLFTVTGGGAMHLNDSLGNHPELvstyNH----HEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWV 90
Cdd:PRK07789 43 ELGVDVVFGIPGGAILPVYDPLFDSTKV----RHvlvrHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTPIADANM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 91 DSIPMFVISGQVkFSTTIAStnvplrqlgD--QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDI 168
Cdd:PRK07789 119 DSVPVVAITGQV-GRGLIGT---------DafQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 169 PLNVQGAliETD-------ALQHYDPsedavqvVAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLN 241
Cdd:PRK07789 189 PKDALQA--QTTfswpprmDLPGYRP-------VTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 242 IPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAGELKKp 321
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQHLGMPGMHGTVAAVAALQRSDLLIALGARFDDR-VTGKLDSFAPDAKVIHADIDPAEIGK- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 322 TLTVDMPIHADLGDFLPGLLGAMQADHKLGNI----EWLEWCRKINQKYPAVqphhYTPHS--PVNPYVFMDRLSQYLDE 395
Cdd:PRK07789 338 NRHADVPIVGDVKEVIAELIAALRAEHAAGGKpdltAWWAYLDGWRETYPLG----YDEPSdgSLAPQYVIERLGEIAGP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 396 GDVTVTGNG-----SACVCSFQamvikkNQRLFTNSGCA-SMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTI 469
Cdd:PRK07789 414 DAIYVAGVGqhqmwAAQFIDYE------KPRTWLNSGGLgTMGYAVPAAMGAKVGRPDKEVWAIDGDGCFQMTNQELATC 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501445419 470 IHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVN-ETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKK 541
Cdd:PRK07789 488 AIEGIPIKVALINNGNLGMVRQWQTLFYEERYSNTDlHTHSHRIPDFVKLAEAYGCVGLRCEREEDVDAVIEK 560
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
21-578 |
2.11e-59 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 207.69 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 21 LFTVTGGGAMHLNDSLGNhPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWVDSIPMFVISG 100
Cdd:PRK07710 34 IFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 101 QVKfSTTIASTNVplrqlgdQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNVQGALIETD 180
Cdd:PRK07710 113 QVA-TSVIGSDAF-------QEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKDMVVEEGEFC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 181 alqhYDPSED--AVQVVAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDH 258
Cdd:PRK07710 185 ----YDVQMDlpGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGLGGFPADH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 259 PLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAGELKKPTLTvDMPIHADLGDFLP 338
Cdd:PRK07710 261 PLFLGMAGMHGTYTANMALYECDLLINIGARFDDR-VTGNLAYFAKEATVAHIDIDPAEIGKNVPT-EIPIVADAKQALQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 339 GLLgaMQADHKLGNIEWLEWCRKINQKYPAvqphHYTPHSPV-NPYVFMDRLSQYLDEGDVTVTGNGSACVCSFQAMVIK 417
Cdd:PRK07710 339 VLL--QQEGKKENHHEWLSLLKNWKEKYPL----SYKRNSESiKPQKAIEMLYEITKGEAIVTTDVGQHQMWAAQYYPFK 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 418 KNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIF 497
Cdd:PRK07710 413 TPDKWVTSGGLGTMGFGLPAAIGAQLAKPDETVVAIVGDGGFQMTLQELSVIKELSLPVKVVILNNEALGMVRQWQEEFY 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 498 NARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILNPAQGFEPklssrilqdgtMVS 577
Cdd:PRK07710 493 NQRY---SHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQLQHAIELQEPVVIDCRVLQSEKVMP-----------MVA 558
|
.
gi 501445419 578 P 578
Cdd:PRK07710 559 P 559
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-543 |
2.66e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 202.39 E-value: 2.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEM-KVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGT 79
Cdd:PRK07979 1 MEMlSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 80 NAITGVMGGWVDSIPMFVISGQVKfSTTIASTNVplrqlgdQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHG 159
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVA-TSLIGYDAF-------QECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 160 RPGPVWLDIPLNVQGALIEtdaLQHYDPSEDAVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSHDVFIQL 236
Cdd:PRK07979 153 RPGPVVVDLPKDILNPANK---LPYVWPESVSMRSYNPTTQGHKGQIkraLQTLVAAKKPVVYVGGGAINAACHQQLKEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 237 LEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKDAYLVAVDIDAG 316
Cdd:PRK07979 230 VEKLNLPVVSSLMGLGAFPATHRQSLGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTN-NLAKYCPNATVLHIDIDPT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 317 ELKKpTLTVDMPIHAD----LGDFLpGLLGAMQADHKLGNIEwlEWCRKINQkYPAVQPHHYTPHS-PVNPYVFMDRLSQ 391
Cdd:PRK07979 309 SISK-TVTADIPIVGDarqvLEQML-ELLSQESAHQPLDEIR--DWWQQIEQ-WRARQCLKYDTHSeKIKPQAVIETLWR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 392 yLDEGDVTVTGNgsacVCSFQAMV-----IKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQEL 466
Cdd:PRK07979 384 -LTKGDAYVTSD----VGQHQMFAalyypFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQEL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501445419 467 QTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVL 543
Cdd:PRK07979 459 STALQYELPVLVLNLNNRYLGMVKQWQDMIYSGRH---SQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEAL 532
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
4-559 |
5.40e-57 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 201.50 E-value: 5.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 4 KVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAIT 83
Cdd:PLN02470 14 KGADILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 84 GVMGGWVDSIPMFVISGQVkfsttiastnvPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGR 160
Cdd:PLN02470 94 GLADALLDSVPLVAITGQV-----------PRRMIGTdafQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 161 PGPVWLDIPLNVQGALietdALQHYDPSED----AVQVVAPPSNDVYSQLIEKICNARKPVILAGSGIrlSGSHDVFIQL 236
Cdd:PLN02470 163 PGPVLVDIPKDIQQQL----AVPNWNQPMKlpgyLSRLPKPPEKSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 237 LEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRqISYNWENFAKDAYLVAVDIDAG 316
Cdd:PLN02470 237 VELTGIPVASTLMGLGAFPASDELSLQMLGMHGTVYANYAVDSADLLLAFGVRFDDR-VTGKLEAFASRASIVHIDIDPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 317 EL---KKPTLtvdmPIHADLGDFLPGLLGAMQADhKLGNIEWLEWCRKIN---QKYPAvqphHYTPHSPVNPYVFMDRLS 390
Cdd:PLN02470 316 EIgknKQPHV----SVCADVKLALQGLNKLLEER-KAKRPDFSAWRAELDeqkEKFPL----SYPTFGDAIPPQYAIQVL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 391 QYLDEGDVTV-TGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTI 469
Cdd:PLN02470 387 DELTDGNAIIsTGVGQHQMWAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANPDAIVVDIDGDGSFIMNIQELATI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 470 IHNKLNLKIFWLNNDGYHSIRQTQTNIFNAR----FCGVNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLS 545
Cdd:PLN02470 467 HVENLPVKIMVLNNQHLGMVVQWEDRFYKANrahtYLGDPDAEAEIFPDFLKFAEGCKIPAARVTRKSDLREAIQKMLDT 546
|
570
....*....|....
gi 501445419 546 DTSIVCEVILnPAQ 559
Cdd:PLN02470 547 PGPYLLDVIV-PHQ 559
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
15-541 |
7.80e-57 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 200.91 E-value: 7.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 15 ENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWVDSIP 94
Cdd:PRK06882 16 DEGVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITGIATAYTDSVP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 95 MFVISGQVKfSTTIASTNVplrqlgdQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNVQG 174
Cdd:PRK06882 96 LVILSGQVP-SNLIGTDAF-------QECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIPKDMVN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 175 AlieTDALQHYDPSEDAVQVVAPPSNDVYSQL---IEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAH 251
Cdd:PRK06882 168 P---ANKFTYEYPEEVSLRSYNPTVQGHKGQIkkaLKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLMGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 252 DNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKDAYLVAVDIDAGELKKpTLTVDMPIHA 331
Cdd:PRK06882 245 GAYPSTDKQFLGMLGMHGTYEANNAMHESDLILGIGVRFDDRTTN-NLAKYCPNAKVIHIDIDPTSISK-NVPAYIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 332 DLGDFLPGLLGAMQADHKL-GNIEWLEWCRKINQkYPAVQPHHYTPHSPV-NPYVFMDRLSQyLDEGDVTVTGN-GSACV 408
Cdd:PRK06882 323 SAKNVLEEFLSLLEEENLAkSQTDLTAWWQQINE-WKAKKCLEFDRTSDViKPQQVVEAIYR-LTNGDAYVASDvGQHQM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 409 CSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHS 488
Cdd:PRK06882 401 FAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNRFLGM 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 501445419 489 IRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKK 541
Cdd:PRK06882 481 VKQWQDLIYSGRH---SQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQ 530
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
2-563 |
4.62e-50 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 182.70 E-value: 4.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 2 EMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNA 81
Cdd:PRK06965 20 DSIGAEILMKALAAEGVEFIWGYPGGAVLYIYDELYKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 82 ITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGDQEFNIVDSV---RCMTKYAVMLTEPESIAYHLERALFLAGH 158
Cdd:PRK06965 100 VTGIATAYMDSIPMVVISGQ-----------VPTAAIGQDAFQECDTVgitRPIVKHNFLVKDVRDLAETVKKAFYIART 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 159 GRPGPVWLDIPLNVqgalieTDALQHYDPSEDAVQVVAPPSNDVYSQLIEK----ICNARKPVILAGSGIRLSGSHDVFI 234
Cdd:PRK06965 169 GRPGPVVVDIPKDV------SKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKavslLLSAKRPYIYTGGGVILANASRELR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 235 QLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAK-DAYLVAVDI 313
Cdd:PRK06965 243 QLADLLGYPVTNTLMGLGAYPASDKKFLGMLGMHGTYEANMAMQHCDVLIAIGARFDDRVIG-NPAHFASrPRKIIHIDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 314 DAGELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGNIEWL-EWCRKINQkYPAVQPHHYTPHSPV-NPYVFMDRLSQ 391
Cdd:PRK06965 322 DPSSISK-RVKVDIPIVGDVKEVLKELIEQLQTAEHGPDADALaQWWKQIEG-WRSRDCLKYDRESEIiKPQYVVEKLWE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 392 yLDEGDVTVTGN-GSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTII 470
Cdd:PRK06965 400 -LTDGDAFVCSDvGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHPDDDVVCITGEGSIQMCIQELSTCL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 471 HNKLNLKIFWLNNDGYHSIRQTQTNIFNARFcgvNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVL-LSDTSI 549
Cdd:PRK06965 479 QYDTPVKIISLNNRYLGMVRQWQEIEYSKRY---SHSYMDALPDFVKLAEAYGHVGMRIEKTSDVEPALREALrLKDRTV 555
|
570
....*....|....
gi 501445419 550 VCEVILNPAQGFEP 563
Cdd:PRK06965 556 FLDFQTDPTENVWP 569
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
17-556 |
4.55e-45 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 168.48 E-value: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 17 GITDLFTVTGGGAMHLNDSL---GNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWVDSI 93
Cdd:PRK06456 16 GVKVIFGIPGLSNMQIYDAFvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNLVTGLITAYWDSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 94 PMFVISGQvkfsttiastnVPLRQLGDQEFNIVDSVRCM---TKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPL 170
Cdd:PRK06456 96 PVIAITGQ-----------VPRSVMGKMAFQEADAMGVFenvTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDIPR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 171 NVQGALIETDALqhydPSEDAVQVVAPPSNDVYSQLIEK----ICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVT 246
Cdd:PRK06456 165 DIFYEKMEEIKW----PEKPLVKGYRDFPTRIDRLALKKaaeiLINAERPIILVGTGVVWSNATPEVLELAELLHIPIVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 247 AWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQI-SYNwENFAKDAYLVAVDIDAGELKKpTLTV 325
Cdd:PRK06456 241 TFPGKTAIPHDHPLYFGPMGYYGRAEASMAALESDAMLVVGARFSDRTFtSYD-EMVETRKKFIMVNIDPTDGEK-AIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 326 DMPIHADLGDFLPGLLGAM-QADHKLGNIEWLEWCRKINQKYPavQPHHYTPHSPVNPYVFMDRLSQYLDEGDVTVTGNG 404
Cdd:PRK06456 319 DVGIYGNAKIILRELIKAItELGQKRDRSAWLKRVKEYKEYYS--QFYYTEENGKLKPWKIMKTIRQALPRDAIVTTGVG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 405 SACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNND 484
Cdd:PRK06456 397 QHQMWAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKLARPDKVVVDLDGDGSFLMTGTNLATAVDEHIPVISVIFDNR 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501445419 485 GYHSIRQTQTNIFNARFCGVNETsgisfPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILN 556
Cdd:PRK06456 477 TLGLVRQVQDLFFGKRIVGVDYG-----PSPDfvKLAEAFGALGFNVTTYEDIEKSLKSAIKEDIPAVIRVPVD 545
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
5-180 |
2.66e-44 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 155.09 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 5 VSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHP--ELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAI 82
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSPgiRYVLT--RHEQGAAFAADGYARATGKPGVVLVTSGPGATNAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 83 TGVMGGWVDSIPMFVISGQVkfSTTIASTNVPlrqlgDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPG 162
Cdd:pfam02776 79 TGLANAYVDSVPLLVISGQR--PRSLVGRGAL-----QQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPG 151
|
170
....*....|....*...
gi 501445419 163 PVWLDIPLNVQGALIETD 180
Cdd:pfam02776 152 PVYLEIPLDVLLEEVDED 169
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
16-523 |
1.39e-43 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 163.89 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 16 NGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWVDSIPM 95
Cdd:PRK08199 21 NGVERVFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASIGVHTAFQDSTPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 96 FVISGQVKfsttiastnvpLRQLGDQEFNIVDSVRC---MTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNV 172
Cdd:PRK08199 101 ILFVGQVA-----------RDFREREAFQEIDYRRMfgpMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPEDV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 173 qgaLIETDALqhydPSEDAVQVVAP-PSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAH 251
Cdd:PRK08199 170 ---LSETAEV----PDAPPYRRVAAaPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFRRQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 252 DNLWDDHPLYCGRPG-----TIGTRggnfvVQNCDLLLSLGCRMN-IRQISYNW-ENFAKDAYLVAVDIDAGELKKpTLT 324
Cdd:PRK08199 243 DLFDNRHPNYAGDLGlginpALAAR-----IREADLVLAVGTRLGeVTTQGYTLlDIPVPRQTLVHVHPDAEELGR-VYR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 325 VDMPIHADLGDFLpgllgAMQADHK-LGNIEWLEWCRKINQKYPAVQPHHYTPhSPVNpyvfMDRLSQYLDE---GDVTV 400
Cdd:PRK08199 317 PDLAIVADPAAFA-----AALAALEpPASPAWAEWTAAAHADYLAWSAPLPGP-GAVQ----LGEVMAWLRErlpADAII 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 401 T---GNGSACVCSFQAMvikknQRLFTNSG--CASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLN 475
Cdd:PRK08199 387 TngaGNYATWLHRFFRF-----RRYRTQLAptSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLP 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501445419 476 LKIFWLNNDGYHSIRQTQTNIFNARfcgvneTSGISF--PSADKIARAYG 523
Cdd:PRK08199 462 IIVIVVNNGMYGTIRMHQEREYPGR------VSGTDLtnPDFAALARAYG 505
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-553 |
1.30e-39 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 152.47 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPE---LVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPG 77
Cdd:PRK08266 2 TTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLFDALYKAGDrirVIHT--RHEQAAGYMAFGYARSTGRPGVCSVVPGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 78 GTNAITGVMGGWVDSIPMFVISGQVKfSTTIASTNVPLRQLGDQefniVDSVRCMTKYAVMLTEPESIAYHLERALFLAG 157
Cdd:PRK08266 80 VLNAGAALLTAYGCNSPVLCLTGQIP-SALIGKGRGHLHEMPDQ----LATLRSFTKWAERIEHPSEAPALVAEAFQQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 158 HGRPGPVWLDIPLNVQGALIETDALQHYDPsedavqvVAPPSNDvySQLIEK----ICNARKPVILAGSGIRlsGSHDVF 233
Cdd:PRK08266 155 SGRPRPVALEMPWDVFGQRAPVAAAPPLRP-------APPPAPD--PDAIAAaaalIAAAKNPMIFVGGGAA--GAGEEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 234 IQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPgtigtrGGNFVVQNCDLLLSLGCRMniRQISYNWENFAKDAYLVAVDI 313
Cdd:PRK08266 224 RELAEMLQAPVVAFRSGRGIVSDRHPLGLNFA------AAYELWPQTDVVIGIGSRL--ELPTFRWPWRPDGLKVIRIDI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 314 DAGELKKptLTVDMPIHADLGDFLPGLLGAMQA--DHKLGNIEWL----EWCRkinQKYPAVQPHHytphspvnpyVFMD 387
Cdd:PRK08266 296 DPTEMRR--LKPDVAIVADAKAGTAALLDALSKagSKRPSRRAELrelkAAAR---QRIQAVQPQA----------SYLR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 388 RLSQYL-DEGDVT--VTGNGSACVCSFQAMvikkNQRLFTNSGC-ASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNL 463
Cdd:PRK08266 361 AIREALpDDGIFVdeLSQVGFASWFAFPVY----APRTFVTCGYqGTLGYGFPTALGAKVANPDRPVVSITGDGGFMFGV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 464 QELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSgisfPSADKIARAYGFEFIKIDAVEDMDEKIKKVL 543
Cdd:PRK08266 437 QELATAVQHNIGVVTVVFNNNAYGNVRRDQKRRFGGRVVASDLVN----PDFVKLAESFGVAAFRVDSPEELRAALEAAL 512
|
570
....*....|
gi 501445419 544 LSDTSIVCEV 553
Cdd:PRK08266 513 AHGGPVLIEV 522
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
205-340 |
1.46e-39 |
|
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: 141.16 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 205 QLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLL 284
Cdd:pfam00205 3 KAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAANEALEEADLVL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 501445419 285 SLGCRMNIRQISYNWENFAKDAYLVAVDIDAGELKKpTLTVDMPIHADLGDFLPGL 340
Cdd:pfam00205 83 AVGARFDDIRTTGKLPEFAPDAKIIHIDIDPAEIGK-NYPVDVPIVGDAKETLEAL 137
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
7-169 |
2.48e-38 |
|
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: 138.43 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 7 DYIASFMVENGITDLFTVTGGGAMHLNDSLGNH-PELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGV 85
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSgIRYILV--RHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 86 MGGWVDSIPMFVISGQVKFSTtiastnvpLRQLGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVW 165
Cdd:cd07035 79 ANAYLDSIPLLVITGQRPTAG--------EGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVA 150
|
....
gi 501445419 166 LDIP 169
Cdd:cd07035 151 LDLP 154
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
2-556 |
4.62e-37 |
|
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: 145.39 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 2 EMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHP-ELVSTYnhHEQACAIAAEAYARLTGRIALVCVTSGPGGTN 80
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGiRFIPVV--HEQGAGHMADGFARVTGRMSMVIGQNGPGVTN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 81 AITGVMGGWVDSIPMFVISGQVKfSTTIAstnvplrQLGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGR 160
Cdd:TIGR03457 79 CVTAIAAAYWAHTPVVIVTPEAG-TKTIG-------LGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 161 pGPVWLDIPLNVQGALIETDALQhydpsedAVQVVAPPSNDV-YSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEK 239
Cdd:TIGR03457 151 -GPAQLNIPRDYFYGEIDVEIPR-------PVRLDRGAGGATsLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 240 LNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQI--SYNWENFAKDAYLVAVDIDA-- 315
Cdd:TIGR03457 223 LGAPVVNSYLHNDSFPASHPLWVGPLGYQGSKAAMKLISDADVVLALGTRLGPFGTlpQYGIDYWPKNAKIIQVDANAkm 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 316 -GELKKPTLTV---DMPIHADLGDFLPGLLGAMQADHKLGNIE-----WL----EWCRKINQ-KYPAVQPHHYTPHSPVN 381
Cdd:TIGR03457 303 iGLVKKVTVGIcgdAKAAAAEILQRLAGKAGDANRAERKAKIQaersaWEqelsEMTHERDPfSLDMIVEQRQEEGNWLH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 382 PYVFMDRLSQYLDEGDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQM 461
Cdd:TIGR03457 383 PRQVLRELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNCGYAFPTIIGAKIAAPDRPVVAYAGDGAWGM 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 462 NLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSGISFPsadKIARAYGFEFIKIDAVEDMDEKIKK 541
Cdd:TIGR03457 463 SMNEIMTAVRHDIPVTAVVFRNRQWGAEKKNQVDFYNNRFVGTELESELSFA---GIADAMGAKGVVVDKPEDVGPALKK 539
|
570
....*....|....*...
gi 501445419 542 VLLSDT---SIVCEVILN 556
Cdd:TIGR03457 540 AIAAQAegkTTVIEIVCT 557
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
1-486 |
2.17e-36 |
|
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: 142.99 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQacaiaaeayaRLTGrIALVCVTSGPGGTN 80
Cdd:COG3961 3 MTYTVGDYLLDRLAELGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELnagyaadgyaRVNG-LGALVTTYGVGELS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 81 AITGVMGGWVDSIPMFVISGqvkfsttIASTNVplRQ--------LGDQEF-NIVDSVRCMTKYAVMLTePESIAYHLER 151
Cdd:COG3961 82 AINGIAGAYAERVPVVHIVG-------APGTRA--QRrgpllhhtLGDGDFdHFLRMFEEVTVAQAVLT-PENAAAEIDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 152 ALFLA-GHGRPgpVWLDIPLNVQGALIEtdalqhydPSEDAVQVVAPPSNDvySQL-------IEKICNARKPVILAGSG 223
Cdd:COG3961 152 VLAAAlREKRP--VYIELPRDVADAPIE--------PPEAPLPLPPPASDP--AALaaavaaaAERLAKAKRPVILAGVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 224 IRLSGSHDVFIQLLEKLNIPVVTAwnahdnLWD------DHPLYcgrpgtIGTRGGNF-------VVQNCDLLLSLGCRM 290
Cdd:COG3961 220 VHRFGLQEELLALAEKTGIPVATT------LLGksvldeSHPQF------IGTYAGAAsspevreYVENADCVLCLGVVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 291 NirqiSYN------WENFAK--DAYLVAVDIDAgelkkptlTVDMPIHadLGDFLPGLLGAmqadhklgniewlewCRKI 362
Cdd:COG3961 288 T----DTNtggftaQLDPERtiDIQPDSVRVGG--------HIYPGVS--LADFLEALAEL---------------LKKR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 363 NQKYPAvqPHHYTPHSPVNPY------VFMDRLSQYLDEGDVTVTGNGSACVCSfQAMVIKKNQRLFTNSGCASMGYGLP 436
Cdd:COG3961 339 SAPLPA--PAPPPPPPPAAPDapltqdRLWQRLQAFLDPGDIVVADTGTSLFGA-ADLRLPEGATFIAQPLWGSIGYTLP 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 501445419 437 AALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGY 486
Cdd:COG3961 416 AALGAALAAPDRRVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDGY 465
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-361 |
3.14e-36 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 143.20 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLT-GRIAlVCV-TSGPGG 78
Cdd:PRK11269 2 AKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATaGNIG-VCIgTSGPAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 79 TNAITGVMGGWVDSIPMFVISGQVkfsttiastnvPLRQLGDQEFNIVDSVRC---MTKYAVMLTEPESIAYHLERALFL 155
Cdd:PRK11269 81 TDMITGLYSASADSIPILCITGQA-----------PRARLHKEDFQAVDIESIakpVTKWAVTVREPALVPRVFQQAFHL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 156 AGHGRPGPVWLDIPLNVQGALIETDA-----LQHYDPSEDAVQVVappsndvysQLIEKICNARKPVILAGSGIRLSGSH 230
Cdd:PRK11269 150 MRSGRPGPVLIDLPFDVQVAEIEFDPdtyepLPVYKPAATRAQIE---------KALEMLNAAERPLIVAGGGVINADAS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 231 DVFIQLLEKLNIPVVT---AWNAhdnLWDDHPLYCGRPGtIGT--RGGNFVVQNCDLLLSLGCRMNIRQISyNWENFAKD 305
Cdd:PRK11269 221 DLLVEFAELTGVPVIPtlmGWGA---IPDDHPLMAGMVG-LQTshRYGNATLLASDFVLGIGNRWANRHTG-SVEVYTKG 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 306 AYLVAVDIDAGELKKpTLTVDMPIHADLGDFLPGLLGA---MQADHKLGNI-EWLEWCRK 361
Cdd:PRK11269 296 RKFVHVDIEPTQIGR-VFGPDLGIVSDAKAALELLVEVareWKAAGRLPDRsAWVADCQE 354
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
385-554 |
5.77e-35 |
|
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: 129.68 E-value: 5.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 385 FMDRLSQYLDEGDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQ 464
Cdd:cd00568 2 VLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 465 ELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVnetsGISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLL 544
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGT----DLSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALA 157
|
170
....*....|
gi 501445419 545 SDTSIVCEVI 554
Cdd:cd00568 158 AGGPALIEVK 167
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
6-567 |
7.15e-34 |
|
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: 135.65 E-value: 7.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 6 SDYIASFMVENGITDLFTVTGGGAMHLNDSLGNH-PELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITG 84
Cdd:TIGR02418 2 ADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKgIELIVV--RHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 85 VMGGWVDSIPMFVISGQVKFSTtiastnvpLRQLGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPV 164
Cdd:TIGR02418 80 LATANSEGDPVVAIGGQVKRAD--------LLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 165 WLDIPLNVQGALIETDALqhydPSEDAVQVVAPPSNDVySQLIEKICNARKPVILAGsgirLSGSHDVFIQ----LLEKL 240
Cdd:TIGR02418 152 FVSLPQDVVDSPVSVKAI----PASYAPKLGAAPDDAI-DEVAEAIQNAKLPVLLLG----LRASSPETTEavrrLLKKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 241 NIPVVTAWNAHDNL-WDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGcrmnIRQISY---NWeNFAKDAYLVAVDIDAG 316
Cdd:TIGR02418 223 QLPVVETFQGAGAVsRELEDHFFGRVGLFRNQPGDRLLKQADLVITIG----YDPIEYeprNW-NSENDATIVHIDVEPA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 317 ELKKpTLTVDMPIHADLGDFLPGLlgAMQADHKLGNIEWLEWCRKINQKYPAVQPHHYTPHSP-VNPYVFMDRLSQYLDE 395
Cdd:TIGR02418 298 QIDN-NYQPDLELVGDIASTLDLL--AERIPGYELPPDALAILEDLKQQREALDRVPATLKQAhLHPLEIIKAMQAIVTD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 396 gDVTVTGN-GSACVC------SFQAMvikknQRLFTNsGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQT 468
Cdd:TIGR02418 375 -DVTVTVDmGSHYIWmaryfrSYRAR-----HLLISN-GMQTLGVALPWAIGAALVRPNTKVVSVSGDGGFLFSSMELET 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 469 IIHNKLN-LKIFWlnNDGYHSIRQTQTNIFNARfcgvneTSGISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLS 545
Cdd:TIGR02418 448 AVRLKLNiVHIIW--NDNGYNMVEFQEEMKYQR------SSGVDFGPIDfvKYAESFGAKGLRVESPDQLEPTLRQAMEV 519
|
570 580
....*....|....*....|..
gi 501445419 546 DTSIVCEVILNPAQgfEPKLSS 567
Cdd:TIGR02418 520 EGPVVVDIPVDYSD--NPKLMS 539
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
3-553 |
1.64e-33 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 134.57 E-value: 1.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 3 MKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHP-ELVSTynHHEQACAIAAEAYARLTGRiALVCV-TSGPGGTN 80
Cdd:PRK08322 1 MKAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSiKLILT--RHEQGAAFMAATYGRLTGK-AGVCLsTLGPGATN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 81 AITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGDQEFNIVDSVRCM---TKYAVMLTEPESIAYHLERALFLAG 157
Cdd:PRK08322 78 LVTGVAYAQLGGMPMVAITGQ-----------KPIKRSKQGSFQIVDVVAMMaplTKWTRQIVSPDNIPEVVREAFRLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 158 HGRPGPVWLDIPLNVQGALIETDALQHyDPSEDAVqvvapPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLL 237
Cdd:PRK08322 147 EERPGAVHLELPEDIAAEETDGKPLPR-SYSRRPY-----ASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 238 EKLNIPVVTAWNAHDNLWDDHPLYCgrpGTIGTRGGNFV---VQNCDLLLSLG--------CRMN------IRQISYnwe 300
Cdd:PRK08322 221 DKTGIPFFTTQMGKGVIPETHPLSL---GTAGLSQGDYVhcaIEHADLIINVGhdviekppFFMNpngdkkVIHINF--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 301 nfakdaylVAVDIDagelkkPTLTVDMPIHADLGDFLPGLLGAMQADHKLGNiewlEWCRKINQKYPAvqphHYTPHS-- 378
Cdd:PRK08322 295 --------LPAEVD------PVYFPQVEVVGDIANSLWQLKERLADQPHWDF----PRFLKIREAIEA----HLEEGAdd 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 379 ---PVNPYVFMDRLSQYLDEGDVTVTGNGSacvcsfQAMVIKKNQR-------LFTNsGCASMGYGLPAALGAAVALGGK 448
Cdd:PRK08322 353 drfPMKPQRIVADLRKVMPDDDIVILDNGA------YKIWFARNYRayepntcLLDN-ALATMGAGLPSAIAAKLVHPDR 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 449 RVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFnarfcgvNETSGISFPSAD--KIARAYGFEF 526
Cdd:PRK08322 426 KVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDNAYGMIRWKQENMG-------FEDFGLDFGNPDfvKYAESYGAKG 498
|
570 580
....*....|....*....|....*....
gi 501445419 527 IKIDAVEDMDEKIKKVLLSD--TSIVCEV 553
Cdd:PRK08322 499 YRVESADDLLPTLEEALAQPgvHVIDCPV 527
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
62-560 |
1.79e-33 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 134.33 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 62 RLTGRIALVCVTSGPGGTNAITGVMGGWVDSIPMFVISGqVKFSTTIASTNVPLRQLGDQEfNIVDSVrcmTKYAVMLTE 141
Cdd:PRK07524 60 RVSGKPGVCFIITGPGMTNIATAMGQAYADSIPMLVISS-VNRRASLGKGRGKLHELPDQR-AMVAGV---AAFSHTLMS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 142 PESIAYHLERALFLAGHGRPGPVWLDIPLNVQGALIEtdalqHYDPSEDAVQVVAPPSNDVYSQLIEKICNARKPVILAG 221
Cdd:PRK07524 135 AEDLPEVLARAFAVFDSARPRPVHIEIPLDVLAAPAD-----HLLPAPPTRPARPGPAPAALAQAAERLAAARRPLILAG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 222 SGIRlsGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGrpGTIGTRGGNFVVQNCDLLLSLGCRMNirQISYNW-- 299
Cdd:PRK07524 210 GGAL--AAAAALRALAERLDAPVALTINAKGLLPAGHPLLLG--ASQSLPAVRALIAEADVVLAVGTELG--ETDYDVyf 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 300 -ENFAKDAYLVAVDIDAGELKKPTLTvDMPIHADLGDFLPGLLGAMQ---ADHKLGniewLEWCRKINQkypAVQPHHyT 375
Cdd:PRK07524 284 dGGFPLPGELIRIDIDPDQLARNYPP-ALALVGDARAALEALLARLPgqaAAADWG----AARVAALRQ---ALRAEW-D 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 376 PhsPVNPYV-FMDRLSQYLDE----GDVT---VTGNgsacvCSFQAmvikKNQRLFTNS--GCASMGYGLPAALGAAVAL 445
Cdd:PRK07524 355 P--LTAAQVaLLDTILAALPDaifvGDSTqpvYAGN-----LYFDA----DAPRRWFNAstGYGTLGYGLPAAIGAALGA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 446 GGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIfNARFCGVNetsgISFPSADKIARAYGFE 525
Cdd:PRK07524 424 PERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGYGEIRRYMVAR-DIEPVGVD----PYTPDFIALARAFGCA 498
|
490 500 510
....*....|....*....|....*....|....*
gi 501445419 526 FIKIDAVEDMDEKIKKVLLSDTSIVCEVILNPAQG 560
Cdd:PRK07524 499 AERVADLEQLQAALRAAFARPGPTLIEVDQACWFA 533
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
1-556 |
1.13e-32 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 132.81 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLgnhP----ELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGP 76
Cdd:PRK07525 4 MKMTPSEAFVETLQAHGITHAFGIIGSAFMDASDLF---PpagiRFIDV--AHEQNAGHMADGYTRVTGRMGMVIGQNGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 77 GGTNAITGVMGGWVDSIPMFVISGQvkfsttiaSTNVPLRQLGDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLA 156
Cdd:PRK07525 79 GITNFVTAVATAYWAHTPVVLVTPQ--------AGTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 157 GHGRpGPVWLDIPLNVQGALIETDALQ--HYDPSEDAVQVVAppsndvysQLIEKICNARKPVILAGSGIRLSGSHDVFI 234
Cdd:PRK07525 151 KRES-GPAQINIPRDYFYGVIDVEIPQpvRLERGAGGEQSLA--------EAAELLSEAKFPVILSGAGVVLSDAIEECK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 235 QLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMN----IRQisYNWENFAKDAYLVA 310
Cdd:PRK07525 222 ALAERLDAPVACGYLHNDAFPGSHPLWVGPLGYNGSKAAMELIAKADVVLALGTRLNpfgtLPQ--YGIDYWPKDAKIIQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 311 VDIDAGELKKpTLTVDMPIHADLGDFLPGLLGAMQA--------DHKLGNI--EWLEWCRKI--------------NQKY 366
Cdd:PRK07525 300 VDINPDRIGL-TKKVSVGICGDAKAVARELLARLAErlagdagrEERKALIaaEKSAWEQELsswdhedddpgtdwNEEA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 367 PAVQPHhytphsPVNPYVFMDRLSQYLDEGDVTVT--GNGSACVCSFQAMviKKNQRLFTNSGCASMGYGLPAALGAAVA 444
Cdd:PRK07525 379 RARKPD------YMHPRQALREIQKALPEDAIVSTdiGNNCSIANSYLRF--EKGRKYLAPGSFGNCGYAFPAIIGAKIA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 445 LGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSGISFPsadKIARAYGF 524
Cdd:PRK07525 451 CPDRPVVGFAGDGAWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVGTELDNNVSYA---GIAEAMGA 527
|
570 580 590
....*....|....*....|....*....|....*
gi 501445419 525 EFIKIDAVEDMDEKIKKVLLSDTS---IVCEVILN 556
Cdd:PRK07525 528 EGVVVDTQEELGPALKRAIDAQNEgktTVIEIMCN 562
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
5-568 |
2.59e-31 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 128.41 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 5 VSDYIASFMVENGITDLFTVTGGGAMHLNDSL-GNHPELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAIT 83
Cdd:PRK06457 4 VAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIrKSKVKYVQV--RHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 84 GVMGGWVDSIPMFVISGQVKFSTtiastnvplrqLGDQEFNIVDSVRCMTKYAV---MLTEPESIAYHLERALFLAGHGR 160
Cdd:PRK06457 82 GLYDAKMDHAPVIALTGQVESDM-----------IGHDYFQEVNLTKLFDDVAVfnqILINPENAEYIIRRAIREAISKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 161 pGPVWLDIPLNVQGALIETDALQHYdpsedavQVVAPPSNDVYSQLIEKICNARKPVILAGSGIRlsGSHDVFIQLLEKL 240
Cdd:PRK06457 151 -GVAHINLPVDILRKSSEYKGSKNT-------EVGKVKYSIDFSRAKELIKESEKPVLLIGGGTR--GLGKEINRFAEKI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 241 NIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCrmnirqiSYNWENFA-KDAYLVAVDIDAGELK 319
Cdd:PRK06457 221 GAPIIYTLNGKGILPDLDPKVMGGIGLLGTKPSIEAMDKADLLIMLGT-------SFPYVNFLnKSAKVIQVDIDNSNIG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 320 KpTLTVDMPIHADLGDFLPglLGAMQADHKLgnieWLEWCRKINQKYPAVQPHHYTPHSPVNPYVFMDRLSQYLDEGDVT 399
Cdd:PRK06457 294 K-RLDVDLSYPIPVAEFLN--IDIEEKSDKF----YEELKGKKEDWLDSISKQENSLDKPMKPQRVAYIVSQKCKKDAVI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 400 VTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKR-VICLDGDGSIQMNLQELQTIIHNKLNLKI 478
Cdd:PRK06457 367 VTDTGNVTMWTARHFRASGEQTFIFSAWLGSMGIGVPGSVGASFAVENKRqVISFVGDGGFTMTMMELITAKKYDLPVKI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 479 FWLNNDGYHSIRqtqtniFNARFCGVNETsGISF--PSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILN 556
Cdd:PRK06457 447 IIYNNSKLGMIK------FEQEVMGYPEW-GVDLynPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVD 519
|
570
....*....|...
gi 501445419 557 PAQ-GFEPKLSSR 568
Cdd:PRK06457 520 PNErPMPPKLTFK 532
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
62-566 |
6.40e-31 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 127.57 E-value: 6.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 62 RLTGRIALVCVTSGPGGTNAITGVMGGWVDSIPMFVISgqvkfsttiasTNVPLRQLGDQEFNIVDSV---RCMTKYAVM 138
Cdd:PRK06112 70 RVSGKVAVVTAQNGPAATLLVAPLAEALKASVPIVALV-----------QDVNRDQTDRNAFQELDHIalfQSCTKWVRR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 139 LTEPESIAYHLERALFLAGHGRPGPVWLDIPLNV------QGALIETDALQHYdPSEDAVqvvapPSNDVYSQLIEKICN 212
Cdd:PRK06112 139 VTVAERIDDYVDQAFTAATSGRPGPVVLLLPADLltaaaaAPAAPRSNSLGHF-PLDRTV-----PAPQRLAEAASLLAQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 213 ARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGT-IGTRG-GNF---VVQNCDLLLSLG 287
Cdd:PRK06112 213 AQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNMGKGAVDETHPLSLGVVGSlMGPRSpGRHlrdLVREADVVLLVG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 288 CRMNiRQISYNWENFAKDAYLVAVDIDAGEL------------KKPTLtvdmpihADLGDFLPGLLGAMQADHKLGNIEW 355
Cdd:PRK06112 293 TRTN-QNGTDSWSLYPEQAQYIHIDVDGEEVgrnyealrlvgdARLTL-------AALTDALRGRDLAARAGRRAALEPA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 356 LEWCRKINQKYPAvqPHHYTPHSPVNPYVFMDRLSQYLDeGDVTVTGNGsacvcSFQAMVI-------KKNQRLFTNSGC 428
Cdd:PRK06112 365 IAAGREAHREDSA--PVALSDASPIRPERIMAELQAVLT-GDTIVVADA-----SYSSIWVanfltarRAGMRFLTPRGL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 429 ASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNND--GYhsirqtQTNIFNARFCgvNE 506
Cdd:PRK06112 437 AGLGWGVPMAIGAKVARPGAPVICLVGDGGFAHVWAELETARRMGVPVTIVVLNNGilGF------QKHAETVKFG--TH 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501445419 507 TSGISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILNPA-----QGFEPKLS 566
Cdd:PRK06112 509 TDACHFAAVDhaAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITDPSafppiSFFEPMDR 575
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
5-553 |
4.25e-30 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 124.72 E-value: 4.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 5 VSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIAlVCVTS-GPGGTNAIt 83
Cdd:PRK07064 5 VGELIAAFLEQCGVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGLG-VALTStGTGAGNAA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 84 gvmGGWVDSI----PMFVISGQVKfSTTIASTNVPLRQLGDQefniVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHG 159
Cdd:PRK07064 83 ---GALVEALtagtPLLHITGQIE-TPYLDQDLGYIHEAPDQ----LTMLRAVSKAAFRVRSAETALATIREAVRVALTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 160 RPGPVWLDIPLNVQGALIETDALQhydpseDAVQVVAP-PSNDVYSQLIEKICNARKPVILAGSGIRLSGSHdvfIQLLE 238
Cdd:PRK07064 155 PTGPVSVEIPIDIQAAEIELPDDL------APVHVAVPePDAAAVAELAERLAAARRPLLWLGGGARHAGAE---VKRLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 239 KLNIPVVTAWNAHDNLWDDHPLycgrpgTIGTRGGNFVV----QNCDLLLSLGCRMNIRQiSYNWEnFAKDAYLVAVDID 314
Cdd:PRK07064 226 DLGFGVVTSTQGRGVVPEDHPA------SLGAFNNSAAVealyKTCDLLLVVGSRLRGNE-TLKYS-LALPRPLIRVDAD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 315 AGELKKpTLTVDMPIHADLGDFLPGLLGAMQAdHKLGNIEWLEWCRKINQKYPAVQPHHYTPHSpvnpyVFMDRLSQYLD 394
Cdd:PRK07064 298 AAADGR-GYPNDLFVHGDAARVLARLADRLEG-RLSVDPAFAADLRAAREAAVADLRKGLGPYA-----KLVDALRAALP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 395 EG-----DVTVTGN--GSACVCSFQAmvikkNQRLFTNSGcaSMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQ 467
Cdd:PRK07064 371 RDgnwvrDVTISNStwGNRLLPIFEP-----RANVHALGG--GIGQGLAMAIGAALAGPGRKTVGLVGDGGLMLNLGELA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 468 TIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNetsgISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDT 547
Cdd:PRK07064 444 TAVQENANMVIVLMNDGGYGVIRNIQDAQYGGRRYYVE----LHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEG 519
|
....*.
gi 501445419 548 SIVCEV 553
Cdd:PRK07064 520 PVLVEV 525
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-572 |
6.87e-30 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 124.34 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYN-HHEQACAIAAEAYARLTGRIAlVCVT-SGPGG 78
Cdd:PRK08611 2 AKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVVDALRKEQDKIKFIQvRHEEVAALAAAAYAKLTGKIG-VCLSiGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 79 TNAITGVMGGWVDSIPMFVISGQVkfsttiASTNvplrqLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFL 155
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQV------TSDL-----LGTdffQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 156 AgHGRPGPVWLDIPLNVQGALIETDAlqHYDPSEDAVQVVAPPSNDVY--SQLIEKicnARKPVILAGSGIRLSGshDVF 233
Cdd:PRK08611 150 A-YEKKGVAVLTIPDDLPAQKIKDTT--NKTVDTFRPTVPSPKPKDIKkaAKLINK---AKKPVILAGLGAKHAK--EEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 234 IQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGcrmnirqISYNWENF-AKDAYLVAVD 312
Cdd:PRK08611 222 LAFAEKAKIPIIHTLPAKGIIPDDHPYSLGNLGKIGTKPAYEAMQEADLLIMVG-------TNYPYVDYlPKKAKAIQID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 313 IDAGELKKpTLTVDMPIHADLGDFLPGLL--GAMQADHKlgnieWLEWCRKINQKYPA-VQPHHYTPHSPVNPYVFMDRL 389
Cdd:PRK08611 295 TDPANIGK-RYPVNVGLVGDAKKALHQLTenIKHVEDRR-----FLEACQENMAKWWKwMEEDENNASTPIKPERVMAAI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 390 SQYLDEGDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTI 469
Cdd:PRK08611 369 QKIADDDAVLSVDVGTVTVWSARYLNLGTNQKFIISSWLGTMGCGLPGAIAAKIAFPDRQAIAICGDGGFSMVMQDFVTA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 470 IHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFcgvnetsGISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDT 547
Cdd:PRK08611 449 VKYKLPIVVVVLNNQQLAFIKYEQQAAGELEY-------AIDLSDMDyaKFAEACGGKGYRVEKAEELDPAFEEALAQDK 521
|
570 580
....*....|....*....|....*
gi 501445419 548 SIVCEVILNPAqgfEPKLSSRILQD 572
Cdd:PRK08611 522 PVIIDVYVDPN---AAPLPGKIVND 543
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
3-523 |
3.11e-29 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 122.23 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 3 MKVSDYIASFMVENGITDLFtvtGGGAMHLNDS---LGNHPELVSTynhhEQACAIAAEAYARLTG--RIALVCVTSGPG 77
Cdd:PRK06154 20 MKVAEAVAEILKEEGVELLF---GFPVNELFDAaaaAGIRPVIART----ERVAVHMADGYARATSgeRVGVFAVQYGPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 78 GTNAITGVMGGWVDSIPMFVISGQVKfsttIASTNVPlrqlgdQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAG 157
Cdd:PRK06154 93 AENAFGGVAQAYGDSVPVLFLPTGYP----RGSTDVA------PNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 158 HGRPGPVWLDIPLNVQGALIETDALQHYDPSedavQVVAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLL 237
Cdd:PRK06154 163 NGRPGPVVLELPVDVLAEELDELPLDHRPSR----RSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 238 EKLNIPVVTAWNAHDNLWDDHPLYCG-----RPGTIgtrgGNFvVQNCDLLLSLGCrmnirqiSYNWENFA----KDAYL 308
Cdd:PRK06154 239 ELLEIPVMTTLNGKSAFPEDHPLALGsggraRPATV----AHF-LREADVLFGIGC-------SLTRSYYGlpmpEGKTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 309 VAVDIDAGELKKptltvDMPI-HADLGD---FLPGLLGAMQADHK---------LGNIEWL--EWCRKINQKYPAVQphh 373
Cdd:PRK06154 307 IHSTLDDADLNK-----DYPIdHGLVGDaalVLKQMIEELRRRVGpdrgraqqvAAEIEAVraAWLAKWMPKLTSDS--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 374 ytphSPVNPYVFMDRLSQYLDEGDVTVT---GNGSACVCSFqaMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRV 450
Cdd:PRK06154 379 ----TPINPYRVVWELQHAVDIKTVIIThdaGSPRDQLSPF--YVASRPGSYLGWGKTTQLGYGLGLAMGAKLARPDALV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501445419 451 ICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNND---GYHSIRQTQTNIFNARFcgvnetsgISFPSADkIARAYG 523
Cdd:PRK06154 453 INLWGDAAFGMTGMDFETAVRERIPILTILLNNFsmgGYDKVMPVSTTKYRATD--------ISGDYAA-IARALG 519
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
402-553 |
1.47e-26 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 105.36 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 402 GNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWL 481
Cdd:pfam02775 1 DIGCHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501445419 482 NNDGYHSIRQTQTNIFNARFCGvneTSGISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEV 553
Cdd:pfam02775 81 NNGGYGMTRGQQTPFGGGRYSG---PSGKILPPVDfaKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
382-554 |
5.81e-26 |
|
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: 104.89 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 382 PYVFMDRLSQYLDEGDVTVTGNGS----ACvcsfQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDG 457
Cdd:cd02015 3 PQEVIKELSELTPGDAIVTTDVGQhqmwAA----QYYRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARPDKTVICIDGDG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 458 SIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCgvnETSGISFPSADKIARAYGFEFIKIDAVEDMDE 537
Cdd:cd02015 79 SFQMNIQELATAAQYNLPVKIVILNNGSLGMVRQWQELFYEGRYS---HTTLDSNPDFVKLAEAYGIKGLRVEKPEELEA 155
|
170
....*....|....*..
gi 501445419 538 KIKKVLLSDTSIVCEVI 554
Cdd:cd02015 156 ALKEALASDGPVLLDVL 172
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
1-541 |
1.60e-23 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 104.55 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVS--DYIASFMVENGITDLFTVTGGGAMHLNDSLGNH-PELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPG 77
Cdd:PRK08617 1 TDKKKYgaDLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSgPELIVT--RHEQNAAFMAAAIGRLTGKPGVVLVTSGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 78 GTNAITGVMGGWVDSIPMFVISGQVKfsttiasTNVPLRQLgDQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAG 157
Cdd:PRK08617 79 VSNLATGLVTATAEGDPVVAIGGQVK-------RADRLKRT-HQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 158 HGRPGPVWLDIPLNVQGALIETDALQhydPSEDAVQVVAPPSnDVySQLIEKICNARKPVILAGsgirLSGSHDVFI--- 234
Cdd:PRK08617 151 SGRPGAAFVSLPQDVVDAPVTSKAIA---PLSKPKLGPASPE-DI-NYLAELIKNAKLPVLLLG----MRASSPEVTaai 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 235 -QLLEKLNIPVVTAWNAHDNLWDDH-PLYCGRPGTIGTRGGNFVVQNCDLLLSLGcrmnIRQISY---NWeNFAKDAYLV 309
Cdd:PRK08617 222 rRLLERTNLPVVETFQAAGVISRELeDHFFGRVGLFRNQPGDELLKKADLVITIG----YDPIEYeprNW-NSEGDATII 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 310 AVDIDAGELKK---PTL--------TVDMpihadLGDFLPGLlgAMQADHKlgniEWLEWCRKinQKYPAVQPHHYTPHS 378
Cdd:PRK08617 297 HIDVLPAEIDNyyqPEReligdiaaTLDL-----LAEKLDGL--SLSPQSL----EILEELRA--QLEELAERPARLEEG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 379 PVNPYVFMDRLSQYLDEgDVTVTGN-GS------ACVCSFQAmvikkNQRLFTNsGCASMGYGLPAALGAAVALGGKRVI 451
Cdd:PRK08617 364 AVHPLRIIRALQDIVTD-DTTVTVDvGShyiwmaRYFRSYEP-----RHLLFSN-GMQTLGVALPWAIAAALVRPGKKVV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 452 CLDGDGSIQMNLQELQTIIHNKLNL-KIFWlnNDGYHSIRQTQTNIFNARfcgvneTSGISFPSAD--KIARAYGFEFIK 528
Cdd:PRK08617 437 SVSGDGGFLFSAMELETAVRLKLNIvHIIW--NDGHYNMVEFQEEMKYGR------SSGVDFGPVDfvKYAESFGAKGLR 508
|
570
....*....|...
gi 501445419 529 IDAVEDMDEKIKK 541
Cdd:PRK08617 509 VTSPDELEPVLRE 521
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
17-483 |
1.12e-22 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 102.11 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 17 GITDLFTVTGGGAMHLNDslGNHPELVSTYN-HHEQACAIAAEAYARLTGRIALVCVTSGPGGTNAITGVMGGWVDSIPM 95
Cdd:PRK05858 19 GVDTMFTLSGGHLFPLYD--GAREEGIRLIDvRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAAQFNQSPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 96 FVISGQvkfsttiastnVPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNV 172
Cdd:PRK05858 97 VVLGGR-----------APALRWGMgslQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 173 QGALIETDALQHYDPsedAVQVVAPPSNDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHD 252
Cdd:PRK05858 166 AFSMADDDGRPGALT---ELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 253 NLWDDHPLYCGRpgtigTRGGNFvvQNCDLLLSLGCRMNIRqISYNWenFAKDAYLVAVDIDAGELKKPtLTVDMPIHAD 332
Cdd:PRK05858 243 VVPADHPLAFSR-----ARGKAL--GEADVVLVVGVPMDFR-LGFGV--FGGTAQLVHVDDAPPQRAHH-RPVAAGLYGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 333 LGDFLPGLLGAM--QADHKlgniEWLEWCRKINQKYPAVQPHHYTPHS-PVNPYVFMDRLSQYLDEgDVTVTGNGSACVc 409
Cdd:PRK05858 312 LSAILSALAGAGgdRTDHQ----GWIEELRTAETAARARDAAELADDRdPIHPMRVYGELAPLLDR-DAIVIGDGGDFV- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 410 SFQAMVIKKNQrlftnSGC-------ASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLN 482
Cdd:PRK05858 386 SYAGRYIDPYR-----PGCwldpgpfGCLGTGPGYALAARLARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGN 460
|
.
gi 501445419 483 N 483
Cdd:PRK05858 461 N 461
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
1-554 |
3.84e-22 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 100.45 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIAlVCVTS-GPGGT 79
Cdd:PRK09124 1 MKQTVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGTIEWMHTRHEEVAAFAAGAEAQLTGELA-VCAGScGPGNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 80 NAITGVMGGWVDSIPMFVISGQVKfSTTIASTNVplrqlgdQEFNIVDSVRCMTKYAVMLTEPESIAYHLERALfLAGHG 159
Cdd:PRK09124 80 HLINGLFDCHRNHVPVLAIAAHIP-SSEIGSGYF-------QETHPQELFRECSHYCELVSNPEQLPRVLAIAM-RKAIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 160 RPGPVWLDIPLNVqgALIETDALQHYDPSEDAVQVVAPPSNDVySQLIEKICNARKPVILAGSGIrlSGSHDVFIQLLEK 239
Cdd:PRK09124 151 NRGVAVVVLPGDV--ALKPAPERATPHWYHAPQPVVTPAEEEL-RKLAALLNGSSNITLLCGSGC--AGAHDELVALAET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 240 LNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCRMNIRQIsynwenFAKDAYLVAVDIDAGELK 319
Cdd:PRK09124 226 LKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGYHAMMNCDTLLMLGTDFPYRQF------YPTDAKIIQIDINPGSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 320 KPTlTVDMPIHADLGDFLPGLLGAMQADHKLGnieWLEWCRKinqkypavqphHYT--------------PHSPVNPYVF 385
Cdd:PRK09124 300 RRS-PVDLGLVGDVKATLAALLPLLEEKTDRK---FLDKALE-----------HYRkarkglddlavpsdGGKPIHPQYL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 386 MDRLSQYLDEGDVTVTGNGSACVcsFQAMVIKKN--QRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNL 463
Cdd:PRK09124 365 ARQISEFAADDAIFTCDVGTPTV--WAARYLKMNgkRRLLGSFNHGSMANAMPQALGAQAAHPGRQVVALSGDGGFSMLM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 464 QELQTIIHNKLNLKIFWLNND--GYHSIRQTQTNIfnarfcgVNETSGISFPSADKIARAYGFEFIKIDAVEDMDEKIKK 541
Cdd:PRK09124 443 GDFLSLVQLKLPVKIVVFNNSvlGFVAMEMKAGGY-------LTDGTDLHNPDFAAIAEACGITGIRVEKASELDGALQR 515
|
570
....*....|...
gi 501445419 542 VLLSDTSIVCEVI 554
Cdd:PRK09124 516 AFAHDGPALVDVV 528
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
49-569 |
8.05e-22 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 99.29 E-value: 8.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 49 HEQACAIAAEAYARLTGRIAlVCVT-SGPGGTNAITGVMGGWVDSIPMFVISGqvkfsttiASTN--VPLRQlGD-QEFN 124
Cdd:PRK09259 55 HEQSAGNAAAAAGFLTQKPG-VCLTvSAPGFLNGLTALANATTNCFPMIMISG--------SSEReiVDLQQ-GDyEELD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 125 IVDSVRCMTKYAVMLTEPESIAYHLERALFLAGHGRPGPVWLDIPLNVQGALIETDALQhydpsEDAVQVVAP-----PS 199
Cdd:PRK09259 125 QLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDLPAKVLAQTMDADEAL-----TSLVKVVDPapaqlPA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 200 NDVYSQLIEKICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGrpgtiGTRGgnFVVQN 279
Cdd:PRK09259 200 PEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMSMAKGLLPDTHPQSAA-----AARS--LALAN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 280 CDLLLSLGCRMnirqisyNW-------ENFAKDAYLVAVDIDAGELKKpTLTVDMPIHADLGDFLPGLLGAMQADHKLGN 352
Cdd:PRK09259 273 ADVVLLVGARL-------NWllshgkgKTWGADKKFIQIDIEPQEIDS-NRPIAAPVVGDIGSVMQALLAGLKQNTFKAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 353 IEWLEWCRKINQKYPA-VQPHHYTPHSPVNPYVFMDRLSQYLDEG-DVTVTGNGsACVCSFQAMVI---KKNQRLFTNS- 426
Cdd:PRK09259 345 AEWLDALAERKEKNAAkMAEKLSTDTQPMNFYNALGAIRDVLKENpDIYLVNEG-ANTLDLARNIIdmyKPRHRLDCGTw 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 427 ---GCAsMGYGlpaalGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHsiRQTQTNIFNARfcg 503
Cdd:PRK09259 424 gvmGIG-MGYA-----IAAAVETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGGIY--RGDDVNLSGAG--- 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501445419 504 vnETSGISF-PSA--DKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILNPAQGFEpklSSRI 569
Cdd:PRK09259 493 --DPSPTVLvHHAryDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINVVIDPAAGTE---SGHI 556
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
64-543 |
1.85e-20 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 95.07 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 64 TGRIALVCVTSGPGGTNAITGVMGGWVDSIPMFVISGQVKFSTT--IASTNVPLRQLGDQeFNIVDSVRCMTKYAVMLTE 141
Cdd:PRK08327 73 TGKPQAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEEgeLGSRNTRIHWTQEM-RDQGGLVREYVKWDYEIRR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 142 PESIAYHLERALFLAGHGRPGPVWLDIPLNVqgaLIETDALQHYDPSEdAVQVVAP-PSNDVYSQLIEKICNARKPVILA 220
Cdd:PRK08327 152 GDQIGEVVARAIQIAMSEPKGPVYLTLPREV---LAEEVPEVKADAGR-QMAPAPPaPDPEDIARAAEMLAAAERPVIIT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 221 GSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPgtigtrgGNFVVQNCDLLLSLGCrmnirQISY--- 297
Cdd:PRK08327 228 WRAGRTAEGFASLRRLAEELAIPVVEYAGEVVNYPSDHPLHLGPD-------PRADLAEADLVLVVDS-----DVPWipk 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 298 -NWENFakDAYLVAVDIDAGELKKP--TLTVDMPIHADLGDFLP----GLLGAMQADHKLGNIEWLEW--CRKINQKYPA 368
Cdd:PRK08327 296 kIRPDA--DARVIQIDVDPLKSRIPlwGFPCDLCIQADTSTALDqleeRLKSLASAERRRARRRRAAVreLRIRQEAAKR 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 369 VQPHHYTPHSPVNPYVFMDRLSQYLDEGDVTVTGNGSacvcSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGK 448
Cdd:PRK08327 374 AEIERLKDRGPITPAYLSYCLGEVADEYDAIVTEYPF----VPRQARLNKPGSYFGDGSAGGLGWALGAALGAKLATPDR 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 449 RVICLDGDGSIQMNLQELQTIIHNKLNLKIFW--LNNDGYHSIRQTQTNIFNArfcGV----NETSGISF-PSAD--KIA 519
Cdd:PRK08327 450 LVIATVGDGSFIFGVPEAAHWVAERYGLPVLVvvFNNGGWLAVKEAVLEVYPE---GYaarkGTFPGTDFdPRPDfaKIA 526
|
490 500
....*....|....*....|....
gi 501445419 520 RAYGFEFIKIDAVEDMDEKIKKVL 543
Cdd:PRK08327 527 EAFGGYGERVEDPEELKGALRRAL 550
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
385-486 |
1.71e-18 |
|
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.
Pssm-ID: 238963 [Multi-domain] Cd Length: 183 Bit Score: 83.35 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 385 FMDRLSQYLDEGDVTVTGNGSACVCSFQAMvIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQ 464
Cdd:cd02005 7 LWQQVQNFLKPNDILVAETGTSWFGALDLK-LPKGTRFISQPLWGSIGYSVPAALGAALAAPDRRVILLVGDGSFQMTVQ 85
|
90 100
....*....|....*....|..
gi 501445419 465 ELQTIIHNKLNLKIFWLNNDGY 486
Cdd:cd02005 86 ELSTMIRYGLNPIIFLINNDGY 107
|
|
| IolD |
COG3962 |
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism ... |
68-550 |
9.99e-17 |
|
TPP-dependent trihydroxycyclohexane-1,2-dione (THcHDO) dehydratase, myo-inositol metabolism [Carbohydrate transport and metabolism];
Pssm-ID: 443162 [Multi-domain] Cd Length: 622 Bit Score: 83.64 E-value: 9.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 68 ALVCVTS-GPGGTNAITGVMGGWVDSIPMFVISGQVkFSTTIAStnvP-LRQL---GDQEFNIVDSVRCMTKYAVMLTEP 142
Cdd:COG3962 85 IMACTSSiGPGATNMVTAAALATANRLPVLLLPGDT-FATRQPD---PvLQQLehfHDPTISVNDAFRPVSRYWDRITRP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 143 ESIAYHLERALflaghgR----P---GPVWLDIPLNVQGalietdalQHYD-PSE---DAVQVVA--PPSNDVYSQLIEK 209
Cdd:COG3962 161 EQLMSALPRAM------RvltdPaetGAVTLALPQDVQA--------EAYDyPESffaKRVHRIRrpPPDPAELARAVEL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 210 ICNARKPVILAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCR 289
Cdd:COG3962 227 IRAAKRPLIIAGGGVRYSEATEALRAFAEATGIPVAETQAGKGALPWDHPLNLGGIGVTGTLAANALAAEADLVIGVGTR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 290 mnirqisYN------WENFA-KDAYLVAVDI---DAGELKKptltvdMPIHADLGDFLPGLLGAMqADHKLGNiEWLEWC 359
Cdd:COG3962 307 -------LQdfttgsKTLFAnPDVRFVNINVarfDAYKHDA------LPVVADAREGLEALTEAL-AGWRYPA-AWTDEA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 360 RKINQKYPAVQPHHYTPHSPVNPY---VF--MDRLSqylDEGDVTVTGNGS--ACVcsfqamvikknQRLFTNSG----- 427
Cdd:COG3962 372 AELKAEWDAEVDRLYAPTNGGLPTqaqVIgaVNEAA---GPDDIVVCAAGSlpGDL-----------HKLWRTRDpgtyh 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 428 ------CasMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARF 501
Cdd:COG3962 438 veygysC--MGYEIAGGLGVKLAEPDREVYVMVGDGSYLMLNSELVTSVQEGKKIIVVLLDNHGFGCINRLQMSTGSQSF 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 501445419 502 C----GVNETSGI---SFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIV 550
Cdd:COG3962 516 GtelrDRDTETGRldgGLLPVDfaANAASLGAKAYRVTTIAELRAALERAKAADRTTV 573
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
379-557 |
1.54e-16 |
|
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: 77.57 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 379 PVNPYVFMDRLSQYLDEGDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGS 458
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDVGNVTVWAARHLRMNGKQRFILSGLLATMGNGLPGAIAAKLAYPDRQVIALSGDGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 459 IQMNLQELQTIIHNKLNLKIFWLNND--GYHSIRQTQTNifnarfcgvNETSGISFPSAD--KIARAYGFEFIKIDAVED 534
Cdd:cd02014 81 FAMLMGDLITAVKYNLPVIVVVFNNSdlGFIKWEQEVMG---------QPEFGVDLPNPDfaKIAEAMGIKGIRVEDPDE 151
|
170 180
....*....|....*....|...
gi 501445419 535 MDEKIKKVLLSDTSIVCEVILNP 557
Cdd:cd02014 152 LEAALDEALAADGPVVIDVVTDP 174
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
64-555 |
1.59e-16 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 82.70 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 64 TGRIALVCVTSGPGGTNAITGVMGGWVDSIPMFVISGQVKFSTtiastnvplrqLGDQEF-NIVDSV---RCMTKYAVML 139
Cdd:PRK07092 71 TGNAAFVNLHSAAGVGNAMGNLFTAFKNHTPLVITAGQQARSI-----------LPFEPFlAAVQAAelpKPYVKWSIEP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 140 TEPESIAYHLERALFLAGHGRPGPVWLDIPLNvqgalietDALQHYDP-SEDAVQVVAPPSNDVYSQLIEKICNARKPVI 218
Cdd:PRK07092 140 ARAEDVPAAIARAYHIAMQPPRGPVFVSIPYD--------DWDQPAEPlPARTVSSAVRPDPAALARLGDALDAARRPAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 219 LAGSGIRLSGSHDVFIQLLEKLNIPVVTAWNAHDNLW-DDHPLYCG-----RPGTIGTRGGNfvvqncDLLLSLGCRMNi 292
Cdd:PRK07092 212 VVGPAVDRAGAWDDAVRLAERHRAPVWVAPMSGRCSFpEDHPLFAGflpasREKISALLDGH------DLVLVIGAPVF- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 293 rqiSYNWENFAK----DAYLVAVDIDAGELKKPTltVDMPIHADLGDFLPGLLgamqadhklgniEWLEWCRKINQKYPA 368
Cdd:PRK07092 285 ---TYHVEGPGPhlpeGAELVQLTDDPGEAAWAP--MGDAIVGDIRLALRDLL------------ALLPPSARPAPPARP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 369 VQPHHYTPHSPVNPYVFMDRLSQYLDEGDVTVTGNGSAcVCSFQA-MVIKKNQRLFT-NSGcaSMGYGLPAALGAAVALG 446
Cdd:PRK07092 348 MPPPAPAPGEPLSVAFVLQTLAALRPADAIVVEEAPST-RPAMQEhLPMRRQGSFYTmASG--GLGYGLPAAVGVALAQP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 447 GKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQtqtniFnARFCGVNETSGISFPSAD--KIARAYGF 524
Cdd:PRK07092 425 GRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRYGALRW-----F-APVFGVRDVPGLDLPGLDfvALARGYGC 498
|
490 500 510
....*....|....*....|....*....|.
gi 501445419 525 EFIKIDAVEDMDEKIKKVLLSDTSIVCEVIL 555
Cdd:PRK07092 499 EAVRVSDAAELADALARALAADGPVLVEVEV 529
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
1-471 |
7.76e-16 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 80.72 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGAMHLNDSLG---NHPELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPG 77
Cdd:PRK08273 1 MSQTVADFILERLREWGVRRVFGYPGDGINGLLGALGradDKPEFVQA--RHEEMAAFMAVAHAKFTGEVGVCLATSGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 78 GTNAITGVMGGWVDSIPMFVISGQVKFSTtiastnvplrqLG---DQEfniVDSVRCM----TKYAVMLTEPESIAYHLE 150
Cdd:PRK08273 79 AIHLLNGLYDAKLDHVPVVAIVGQQARAA-----------LGghyQQE---VDLQSLFkdvaGAFVQMVTVPEQLRHLVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 151 RALFLAgHGRPGPVWLDIPLNVQGALIETDALQH--------YD-----PSEDAVQVVAppsndvysqlieKICNA-RKP 216
Cdd:PRK08273 145 RAVRTA-LAERTVTAVILPNDVQELEYEPPPHAHgtvhsgvgYTrprvvPYDEDLRRAA------------EVLNAgRKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 217 VILAGSGIRlsGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGCrmnirqiS 296
Cdd:PRK08273 212 AILVGAGAL--GATDEVIAVAERLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYELMRECDTLLMVGS-------S 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 297 YNWENF---AKDAYLVAVDIDAGEL--KKPTltvDMPIHADLGDFLPGLLGAMQADHKLG---NIE-WLEWCRKINQKYP 367
Cdd:PRK08273 283 FPYSEFlpkEGQARGVQIDIDGRMLglRYPM---EVNLVGDAAETLRALLPLLERKKDRSwreRIEkWVARWWETLEARA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 368 AVqphhytPHSPVNP-YVFMDrLSQYLDEgDVTVTGN-GSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVAL 445
Cdd:PRK08273 360 MV------PADPVNPqRVFWE-LSPRLPD-NAILTADsGSCANWYARDLRMRRGMMASLSGTLATMGPAVPYAIAAKFAH 431
|
490 500
....*....|....*....|....*..
gi 501445419 446 GGKRVICLDGDGSIQMN-LQELQTIIH 471
Cdd:PRK08273 432 PDRPVIALVGDGAMQMNgMAELITVAK 458
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
1-566 |
1.72e-13 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 73.10 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 1 MEMKVSDYIASFMVENGITDLFTVTGGGamhLN---DSLGNHPELVSTYNHHEQACAIAAEAYARLTGRIAlVCVTS-GP 76
Cdd:PRK06546 1 MAKTVAEQLVEQLVAAGVKRIYGIVGDS---LNpivDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLA-VCAGScGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 77 GGTNAITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLG---------DQEFNivdsvRCmTKYAVMLTEPEsiay 147
Cdd:PRK06546 77 GNLHLINGLYDAHRSGAPVLAIASH-----------IPSAQIGsgffqethpDRLFV-----EC-SGYCEMVSSAE---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 148 HLERALFLAGH---GRPGPVWLDIPlnvqGALIETDALQHYDPSEDAVQ--VVAPPSNDVySQLIEKICNARKPVILAGS 222
Cdd:PRK06546 136 QAPRVLHSAIQhavAGGGVSVVTLP----GDIADEPAPEGFAPSVISPRrpTVVPDPAEV-RALADAINEAKKVTLFAGA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 223 GIRlsGSHDVFIQLLEKLNIPVVTAWNAHDNLWDDHPLYCGRPGTIGTRGGNFVVQNCDLLLSLGcrmnirqISYNWENF 302
Cdd:PRK06546 211 GVR--GAHAEVLALAEKIKAPVGHSLRGKEWIQYDNPFDVGMSGLLGYGAAHEAMHEADLLILLG-------TDFPYDQF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 303 AKDAYLVAVDIDAGELKKPTlTVDMPIHADLGD----FLPGL--------LGAMQADHKlgniewlewcRKINQKYPAvq 370
Cdd:PRK06546 282 LPDVRTAQVDIDPEHLGRRT-RVDLAVHGDVAEtiraLLPLVkektdrrfLDRMLKKHA----------RKLEKVVGA-- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 371 phhYT----PHSPVNPYVFMDRLSQYLDEGDV-TV-TGngsacVCS-FQAMVIKKN--QRLFTNSGCASMGYGLPAALGA 441
Cdd:PRK06546 349 ---YTrkveKHTPIHPEYVASILDELAADDAVfTVdTG-----MCNvWAARYITPNgrRRVIGSFRHGSMANALPHAIGA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 442 AVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNN------------DGYHSIrqtqtnifnarfcgvnetsG 509
Cdd:PRK06546 421 QLADPGRQVISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNstlgmvklemlvDGLPDF-------------------G 481
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 510 ISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVILNP-AQGFEPKLS 566
Cdd:PRK06546 482 TDHPPVDyaAIAAALGIHAVRVEDPKDVRGALREAFAHPGPALVDVVTDPnALSIPPTIT 541
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
4-175 |
7.79e-13 |
|
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: 66.81 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 4 KVSDYIASFMVENGITDLFTVTGGGAMHLNDSLGNH--PELVSTynHHEQACAIAAEAYARLTGRIALVCVTSGPGGTNA 81
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREgkIEFIQV--RHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 82 ITGVMGGWVDSIPMFVISGQvkfsttiastnVPLRQLGD---QEFNIVDSVRCMTKYAVMLTEPESIAYHLERALFLAgH 158
Cdd:cd07039 79 LNGLYDAKRDRAPVLAIAGQ-----------VPTDELGTdyfQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTA-I 146
|
170
....*....|....*..
gi 501445419 159 GRPGPVWLDIPLNVQGA 175
Cdd:cd07039 147 AKRGVAVLILPGDVQDA 163
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
7-169 |
6.17e-12 |
|
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: 63.90 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 7 DYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGRiALVCVTSGPGGTNAITGVM 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGP-PVVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 87 GGWVDSIPMFVISGQVKFSTTIASTNvplrqlgdQEFNIVDSVRCMTKYAVMLTEPESIAYHLERAlFLAGHGRPGPVWL 166
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTF--------QSMFDLGMYRSIPEANISSPSPAELPAGIDHA-IRTAYASQGPVVV 150
|
...
gi 501445419 167 DIP 169
Cdd:cd06586 151 RLP 153
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
7-169 |
3.72e-10 |
|
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: 58.66 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 7 DYIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGrIALVCVTSGPGGTNAITGVM 86
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKG-LGALVTTYGVGELSALNGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 87 GGWVDSIPMFVISGQvkFSTTIASTNVPL-RQLGDQEF----NIVDSVRCmtkYAVMLTEPESIAYHLERALFLA-GHGR 160
Cdd:cd07038 80 GAYAEHVPVVHIVGA--PSTKAQASGLLLhHTLGDGDFdvflKMFEEITC---AAARLTDPENAAEEIDRVLRTAlRESR 154
|
....*....
gi 501445419 161 pgPVWLDIP 169
Cdd:cd07038 155 --PVYIEIP 161
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
378-560 |
6.56e-09 |
|
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: 55.98 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 378 SPVNPYVFMDRLSQYLDEGDVTVTGNGSACVCSFQAMVIKKNQRLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDG 457
Cdd:cd02013 2 NPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAAPDRPVVAIAGDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 458 SIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGvNETSGISFpsaDKIARAYGFEFIKIDAVEDMDE 537
Cdd:cd02013 82 AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEKKNQVDFYNNRFVG-TELESESF---AKIAEACGAKGITVDKPEDVGP 157
|
170 180
....*....|....*....|....*.
gi 501445419 538 KIKKVL---LSDTSIVCEVILNPAQG 560
Cdd:cd02013 158 ALQKAIammAEGKTTVIEIVCDQELG 183
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
419-553 |
7.26e-09 |
|
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: 55.37 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 419 NQRLFTNsGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFn 498
Cdd:cd02010 39 NTCLISN-GLATMGVALPGAIGAKLVYPDRKVVAVSGDGGFMMNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQEKEY- 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 501445419 499 arfcgvNETSGISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSD--TSIVCEV 553
Cdd:cd02010 117 ------GRDSGVDFGNPDfvKYAESFGAKGYRIESADDLLPVLERALAADgvHVIDCPV 169
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
422-555 |
2.56e-08 |
|
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: 53.75 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 422 LFTNSGcASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQtqtniFNARF 501
Cdd:cd02002 43 YFTLRG-GGLGWGLPAAVGAALANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGYGALRS-----FLKRV 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501445419 502 CGVNETS------GISFPSAD--KIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVIL 555
Cdd:cd02002 117 GPEGPGEnapdglDLLDPGIDfaAIAKAFGVEAERVETPEELDEALREALAEGGPALIEVVV 178
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
8-486 |
2.49e-06 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 50.47 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 8 YIASFMVENGITDLFTVTGGGAMHLNDSLGNHPELVSTYNHHEQACAIAAEAYARLTGrIALVCVTSGPGGTNAITGVMG 87
Cdd:PLN02573 21 HLARRLVEIGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARG-VGACVVTFTVGGLSVLNAIAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 88 GWVDSIPMFVISGQVKfSTTIASTNVPLRQLGDQEFNivDSVRC---MTKYAVMLTEPESIAYHLERALFLAGHGRPgPV 164
Cdd:PLN02573 100 AYSENLPVICIVGGPN-SNDYGTNRILHHTIGLPDFS--QELRCfqtVTCYQAVINNLEDAHELIDTAISTALKESK-PV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 165 WLDIPLNVQGalietdaLQHYDPSEDAVQVVAPPSNDVYSQL-------IEKICNARKPVILAGSGIRLSGSHDVFIQLL 237
Cdd:PLN02573 176 YISVSCNLAA-------IPHPTFSREPVPFFLTPRLSNKMSLeaaveaaAEFLNKAVKPVLVGGPKLRVAKACKAFVELA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 238 EKLNIPVVTAWNAHDNLWDDHPLYCGRP-GTIGTRGGNFVVQNCDLLLSLGCRMNIRQiSYNWENFAKDAYLVAVDIDAG 316
Cdd:PLN02573 249 DASGYPVAVMPSAKGLVPEHHPHFIGTYwGAVSTPFCAEIVESADAYLFAGPIFNDYS-SVGYSLLLKKEKAIIVQPDRV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 317 EL-KKPTL-TVDMPihadlgDFLPGLlgAMQADHklgNIEWLEWCRKINqkYPAVQPHHYTPHSPVNPYVFMDRLSQYLD 394
Cdd:PLN02573 328 TIgNGPAFgCVLMK------DFLEAL--AKRVKK---NTTAYENYKRIF--VPEGEPLKSEPGEPLRVNVLFKHIQKMLS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 395 eGDVTV---TGNgSACVCsfqamvikknQRLFTNSGC--------ASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNL 463
Cdd:PLN02573 395 -GDTAViaeTGD-SWFNC----------QKLKLPEGCgyefqmqyGSIGWSVGATLGYAQAAPDKRVIACIGDGSFQVTA 462
|
490 500
....*....|....*....|...
gi 501445419 464 QELQTIIHNKLNLKIFWLNNDGY 486
Cdd:PLN02573 463 QDVSTMIRCGQKSIIFLINNGGY 485
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
448-554 |
2.69e-05 |
|
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: 44.97 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 448 KRVICLDGDGSIQMNLQELQTI-IHNKLNLKIFWLNNDGYHSIrqtqtnifnarfcGVNETSGISFPSADKIARAYGFE- 525
Cdd:cd03372 60 RKVIVIDGDGSLLMNLGALATIaAEKPKNLIIVVLDNGAYGST-------------GNQPTHAGKKTDLEAVAKACGLDn 126
|
90 100
....*....|....*....|....*....
gi 501445419 526 FIKIDAVEDMDEKIKKVLLSDTSIVCEVI 554
Cdd:cd03372 127 VATVASEEAFEKAVEQALDGPSFIHVKIK 155
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
388-558 |
3.39e-05 |
|
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: 44.99 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 388 RLSQYLDEGDVTVTGNGSA---CVCSFQAMVIKKnqrLFTNSGCASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQ 464
Cdd:cd02003 7 ALNEAIGDDDVVINAAGSLpgdLHKLWRARTPGG---YHLEYGYSCMGYEIAAGLGAKLAKPDREVYVLVGDGSYLMLHS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 465 ELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFC--------GVNETSGiSFPSAD--KIARAYGFEFIKIDAVED 534
Cdd:cd02003 84 EIVTAVQEGLKIIIVLFDNHGFGCINNLQESTGSGSFGtefrdrdqESGQLDG-ALLPVDfaANARSLGARVEKVKTIEE 162
|
170 180
....*....|....*....|....
gi 501445419 535 MDEKIKKVLLSDTSIVCEVILNPA 558
Cdd:cd02003 163 LKAALAKAKASDRTTVIVIKTDPK 186
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
429-555 |
2.32e-04 |
|
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: 42.13 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 429 ASMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQELQTIIHNKLNLKIFWLNNDGYHSIRQTQTNIFNArfcGVNETS 508
Cdd:cd02004 48 GTLGVGLGYAIAAALARPDKRVVLVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSYGL---GLPVTT 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 501445419 509 GISFPSADKIARAYGFEFIKIDAVEDMDEKIKKVLLSDTSIVCEVIL 555
Cdd:cd02004 125 LLPDTRYDLVAEAFGGKGELVTTPEELKPALKRALASGKPALINVII 171
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
388-509 |
2.39e-03 |
|
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: 39.60 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501445419 388 RLSQYLDEGDVTV--TGNGSACVCSFQAMVIKKNQRLFTNSGcaSMGYGLPAALGAAVALGGKRVICLDGDGSIQMNLQE 465
Cdd:cd03371 7 IVLSRAPATAAVVstTGMTSRELFELRDRPGGGHAQDFLTVG--SMGHASQIALGIALARPDRKVVCIDGDGAALMHMGG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 501445419 466 LQTI-IHNKLNLKIFWLNNDGYHSIRQTQTNIFNARFCGVNETSG 509
Cdd:cd03371 85 LATIgGLAPANLIHIVLNNGAHDSVGGQPTVSFDVSLPAIAKACG 129
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| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
448-488 |
6.09e-03 |
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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: 37.85 E-value: 6.09e-03
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....*....|....*....|....*....|....*....|..
gi 501445419 448 KRVICLDGDGSIQMNLQELQTI-IHNKLNLKIFWLNNDGYHS 488
Cdd:cd02001 60 RKVIVVDGDGSLLMNPGVLLTAgEFTPLNLILVVLDNRAYGS 101
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