|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
12-577 |
0e+00 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 1011.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 12 LTDGCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:PRK09259 9 LTDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDI 171
Cdd:PRK09259 89 TALANATTNCFPMIMISGSSEREIVDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 172 PGDVLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMS 251
Cdd:PRK09259 169 PAKVLAQTMDADEALTSLVKVVDPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFLPMS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 252 MAKGLLPDSHPQSAAAARSLAMARADVVLLVGARLNWLLGNGESPQWSADAKFIQVDIEASEFDSNRPIVAPLTGDIGSV 331
Cdd:PRK09259 249 MAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKGKTWGADKKFIQIDIEPQEIDSNRPIAAPVVGDIGSV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 332 MSALLEAAADRSSVASAAWTGELADRKARNSAKMRRRLADDHHPMRFYNALGAIRSVLQRNPDVYVVNEGANALDLARNI 411
Cdd:PRK09259 329 MQALLAGLKQNTFKAPAEWLDALAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVLKENPDIYLVNEGANTLDLARNI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 412 IDMHLPRHRLDSGTWGVMGIGMGYAIAAAVETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGGVYRGDEATi 491
Cdd:PRK09259 409 IDMYKPRHRLDCGTWGVMGIGMGYAIAAAVETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGGIYRGDDVN- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 492 frsaaPVWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPADGVESGHLAKLNTT 571
Cdd:PRK09259 488 -----LSGAGDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINVVIDPAAGTESGHITNLNPK 562
|
....*.
gi 489495942 572 SAATPA 577
Cdd:PRK09259 563 SVAGKK 568
|
|
| oxalate_oxc |
TIGR03254 |
oxalyl-CoA decarboxylase; In a number of bacteria, including Oxalobacter formigenes from the ... |
12-569 |
0e+00 |
|
oxalyl-CoA decarboxylase; In a number of bacteria, including Oxalobacter formigenes from the human gut, a two-gene operon of oxc (oxalyl-CoA decarboxylase) and frc (formyl-CoA transferase) encodes a system for degrading and therefore detoxifying oxalate. Members of this family are the thiamine pyrophosphate (TPP)-containing enzyme oxalyl-CoA decarboxylase. [Cellular processes, Detoxification]
Pssm-ID: 132298 [Multi-domain] Cd Length: 554 Bit Score: 867.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 12 LTDGCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:TIGR03254 2 LTDGFHLVIDALKLNGINTIYGVVGIPVTDLARLAQAKGMRYIGFRHEQSAGYAAAAAGFLTQKPGVCLTVSAPGFLNGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDI 171
Cdd:TIGR03254 82 TALANATTNCFPMIMISGSSERHIVDLQQGDYEEMDQLAAAKPFAKAAYRVLRAEDIGIGIARAIRTAVSGRPGGVYLDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 172 PGDVLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMS 251
Cdd:TIGR03254 162 PAAVLGQTMEAEKAKKTLVKVVDPAPKQLPSPDSVDRAVELLKDAKRPLILLGKGAAYAQADEEIREFVEKTGIPFLPMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 252 MAKGLLPDSHPQSAAAARSLAMARADVVLLVGARLNWLLGNGESPQWSADAKFIQVDIEASEFDSNRPIVAPLTGDIGSV 331
Cdd:TIGR03254 242 MAKGLLPDTHPQSAAAARSFALAEADVVMLVGARLNWLLSHGKGKLWGEDAKFIQVDIEPTEMDSNRPIAAPVVGDIGSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 332 MSALLEAAADRSSVASAAWTGELADRKARNSAKMRRRLADDHHPMRFYNALGAIRSVLQRNPDVYVVNEGANALDLARNI 411
Cdd:TIGR03254 322 VQALLSAAKNGGVKPPADWRNAIKTKSEKNVAKMAERLSASESPMNYHGALEAIRDVLKDNPDIYLVNEGANTLDLARNV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 412 IDMHLPRHRLDSGTWGVMGIGMGYAIAAAVETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGGVYRGDEATI 491
Cdd:TIGR03254 402 IDMYKPRHRLDVGTWGVMGIGMGYAIAAAVETGKPVVALEGDSAFGFSGMEVETICRYNLPVCVVIFNNGGIYRGDDVNV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495942 492 FRSaapvwrhDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPADGVESGHLAKLN 569
Cdd:TIGR03254 482 VGA-------DPAPTVLVHGARYDKMMKAFGGVGYNVTTPDELKAALNEALASGKPTLINAVIDPSAGTESGHIGNLN 552
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
15-568 |
6.87e-144 |
|
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: 426.88 E-value: 6.87e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARA-AQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:COG0028 5 GADALVEALEAEGVETVFGVPGGAILPLYDAlRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMvdLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:COG0028 85 LADAYMDSVPVLAITGQVPTSL--IGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAVEASAASGAIWRPvdpAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:COG0028 163 DVQAAEAEEEPAPPELRGY---RPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 KGLLPDSHPQSAAAARSLAMARA-------DVVLLVGARLNWLLGNGESPqWSADAKFIQVDIEASEFDSNRPIVAPLTG 326
Cdd:COG0028 240 KGAFPEDHPLYLGMLGMHGTPAAnealaeaDLVLAVGARFDDRVTGNWDE-FAPDAKIIHIDIDPAEIGKNYPVDLPIVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 327 DIGSVMSALLEAAADRSSvASAAWTGELADRKARNsakmRRRLADDHHPMRFYNALGAIRSVLqrNPDVYVVNEGANALD 406
Cdd:COG0028 319 DAKAVLAALLEALEPRAD-DRAAWLARIAAWRAEY----LAAYAADDGPIKPQRVIAALREAL--PDDAIVVTDVGQHQM 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 407 LARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGGvYr 485
Cdd:COG0028 392 WAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLaRPDRPVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGG-L- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 486 gdeATIFRSAAPVWRHDPAPTVLnAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPADGVESGHL 565
Cdd:COG0028 470 ---GMVRQWQELFYGGRYSGTDL-PNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEENPPGATL 545
|
...
gi 489495942 566 AKL 568
Cdd:COG0028 546 DEM 548
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
18-558 |
2.62e-84 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 272.75 E-value: 2.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALANA 97
Cdd:PRK05858 10 LAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAMAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 98 TTNCFPMIQISGSSsrPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGDVLG 177
Cdd:PRK05858 90 QFNQSPLVVLGGRA--PALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 178 QAVEASAASGaiwrPVDPAPR-LLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAKGL 256
Cdd:PRK05858 168 SMADDDGRPG----ALTELPAgPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 257 LPDSHPQSAAAARSLAMARADVVLLVGARLNWLLGNGEspqWSADAKFIQVDIEASEFDSNRPIVAPLTGDIGSVMSALL 336
Cdd:PRK05858 244 VPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFGV---FGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSALA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 337 EAAADRSSVASaaWTGELADRKARNSAKMRRRLADDH---HPMRFYnalGAIRSVLQRnpDVYVVNEGANALDLARNIID 413
Cdd:PRK05858 321 GAGGDRTDHQG--WIEELRTAETAARARDAAELADDRdpiHPMRVY---GELAPLLDR--DAIVIGDGGDFVSYAGRYID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 414 MHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGgvyrgdeatif 492
Cdd:PRK05858 394 PYRPGCWLDPGPFGCLGTGPGYALAARLaRPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNG----------- 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 493 rsaapVWRHDPAP----------TVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPAD 558
Cdd:PRK05858 463 -----IWGLEKHPmealygydvaADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSV 533
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
378-555 |
2.04e-74 |
|
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: 234.35 E-value: 2.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 378 FYNALGAIRSVLQRnpDVYVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVET-GRPVVAIEGDSAF 456
Cdd:cd02004 1 PYRVLHELQEALPD--DAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARpDKRVVLVEGDGAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 457 GFSGMEFETICRYRLPVTVVILNNGGVYRGDeatifRSAAPVWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELES 536
Cdd:cd02004 79 GFSGMELETAVRYNLPIVVVVGNNGGWYQGL-----DGQQLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKP 153
|
170
....*....|....*....
gi 489495942 537 ALTDALASNGPSLIDCELD 555
Cdd:cd02004 154 ALKRALASGKPALINVIID 172
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
15-560 |
1.71e-69 |
|
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: 234.23 E-value: 1.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVG---IPITDLARAAqaSGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:TIGR00118 3 GAEAIIESLKDEGVKTVFGYPGgaiLPIYDALYND--SGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVdlqrGD--YQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYL 169
Cdd:TIGR00118 81 TGIATAYMDSIPMVVFTGQVPTSLI----GSdaFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 170 DIPGDVLGQAVEasaasgaiwRPVDP-------APRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEH 242
Cdd:TIGR00118 157 DLPKDVTTAEIE---------YPYPEkvnlpgyRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 243 TGIPFLPMSMAKGLLPDSHPQSA-------AAARSLAMARADVVLLVGARL-NWLLGNGEspQWSADAKFIQVDIEASEF 314
Cdd:TIGR00118 228 IQIPVTTTLMGLGSFPEDHPLSLgmlgmhgTKTANLAVHECDLIIAVGARFdDRVTGNLA--KFAPNAKIIHIDIDPAEI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 315 DSNRPIVAPLTGDIGSVMSALLEAAADRSSVASAAWTGELADRKARNSAKMrrrladDHH-----PMRFYNALGAIrsvl 389
Cdd:TIGR00118 306 GKNVRVDIPIVGDARNVLEELLKKLFELKERKESAWLEQINKWKKEYPLKM------DYTeegikPQQVIEELSRV---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 390 qRNPDVYVVNE-GANALdLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVetGRP---VVAIEGDSAFGFSGMEFET 465
Cdd:TIGR00118 376 -TKDEAIVTTDvGQHQM-WAAQFYPFRKPRRFITSGGLGTMGFGLPAAIGAKV--AKPestVICITGDGSFQMNLQELST 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 466 ICRYRLPVTVVILNNG--GVYRGDEATIFRSaapvwRHdpAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALA 543
Cdd:TIGR00118 452 AVQYDIPVKILILNNRylGMVRQWQELFYEE-----RY--SHTHMGSLPDFVKLAEAYGIKGIRIEKPEELDEKLKEALS 524
|
570
....*....|....*..
gi 489495942 544 SNGPSLIDCELDPADGV 560
Cdd:TIGR00118 525 SNEPVLLDVVVDKPENV 541
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
10-556 |
4.85e-67 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 227.20 E-value: 4.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 10 TVLTDGcHLVVDALKANDVDTIYGVVGIPITDL--ARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGF 87
Cdd:PRK08266 2 TTMTGG-EAIVAGLVAHGVDTVFGLPGAQLYWLfdALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 88 LNGLPALANATTNCFPMIQISGSSSRPMVDLQRGDYQDL-DQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGG 166
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 167 VYLDIPGDVLGQAVEASAAsgaiwRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADnvIREFVEHTGIP 246
Cdd:PRK08266 161 VALEMPWDVFGQRAPVAAA-----PPLRPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAAGAGEE--IRELAEMLQAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 247 FLPMSMAKGLLPDSHPQSAAAARSLAM-ARADVVLLVGARLnwLLGNGESPQWSADAKFIQVDIEASEFDSNRPIVApLT 325
Cdd:PRK08266 234 VVAFRSGRGIVSDRHPLGLNFAAAYELwPQTDVVIGIGSRL--ELPTFRWPWRPDGLKVIRIDIDPTEMRRLKPDVA-IV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 326 GDIGSVMSALLEAAADRSSVaSAAWTGELADRKARNsakmrRRLADDHHPMRFYnaLGAIRSVLQRnpDVYVVNEGANAL 405
Cdd:PRK08266 311 ADAKAGTAALLDALSKAGSK-RPSRRAELRELKAAA-----RQRIQAVQPQASY--LRAIREALPD--DGIFVDELSQVG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 406 DLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNG--G 482
Cdd:PRK08266 381 FASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVaNPDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNayG 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 483 VYRGDEATIFRSAApvwrhdPAPTVLNAHarHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLI--DCELDP 556
Cdd:PRK08266 461 NVRRDQKRRFGGRV------VASDLVNPD--FVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIevPVPRGS 528
|
|
| acolac_catab |
TIGR02418 |
acetolactate synthase, catabolic; Acetolactate synthase (EC 2.2.1.6) combines two molecules of ... |
15-561 |
6.26e-66 |
|
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: 224.24 E-value: 6.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPAL 94
Cdd:TIGR02418 1 GADLVVDQLENQGVRYVFGIPGAKIDRVFDALEDKGIELIVVRHEQNAAFMAQAVGRITGKPGVALVTSGPGCSNLVTGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 95 ANATTNCFPMIQISGSSSRPmvDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGD 174
Cdd:TIGR02418 81 ATANSEGDPVVAIGGQVKRA--DLLKLTHQSMDNVALFRPITKYSAEVQDPDALSEVVANAFRAAESGKPGAAFVSLPQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 175 VLgqaveASAASGAIWRPVdPAPRLLPAPE-AIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:TIGR02418 159 VV-----DSPVSVKAIPAS-YAPKLGAAPDdAIDEVAEAIQNAKLPVLLLGLRASSPETTEAVRRLLKKTQLPVVETFQG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 KGLLP-DSHPQSAAAARSLAMARADvVLLVGARLNWLLGNG----ESPQWSA--DAKFIQVDIEASEFDSNRPIVAPLTG 326
Cdd:TIGR02418 233 AGAVSrELEDHFFGRVGLFRNQPGD-RLLKQADLVITIGYDpieyEPRNWNSenDATIVHIDVEPAQIDNNYQPDLELVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 327 DIGSVMSALLEAAAD-RSSVASAAwtgELADRKA--RNSAKMRRRLADDH-HPMRFYNALGAIrsvlqRNPDVYV-VNEG 401
Cdd:TIGR02418 312 DIASTLDLLAERIPGyELPPDALA---ILEDLKQqrEALDRVPATLKQAHlHPLEIIKAMQAI-----VTDDVTVtVDMG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 402 ANALDLARNiIDMHLPRHRLDSGTWGVMGIGMGYAIAAA-VETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNN 480
Cdd:TIGR02418 384 SHYIWMARY-FRSYRARHLLISNGMQTLGVALPWAIGAAlVRPNTKVVSVSGDGGFLFSSMELETAVRLKLNIVHIIWND 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 481 GG---VYRGDEATIFRSAAPvwrhDPAPTVLNAHarheliAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPA 557
Cdd:TIGR02418 463 NGynmVEFQEEMKYQRSSGV----DFGPIDFVKY------AESFGAKGLRVESPDQLEPTLRQAMEVEGPVVVDIPVDYS 532
|
....
gi 489495942 558 DGVE 561
Cdd:TIGR02418 533 DNPK 536
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
18-555 |
1.21e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 220.85 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALANA 97
Cdd:PRK08322 6 LFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVAYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 98 TTNCFPMIQISGSssRPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGDVlg 177
Cdd:PRK08322 86 QLGGMPMVAITGQ--KPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 178 qaveASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAKGLL 257
Cdd:PRK08322 162 ----AAEETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKGVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 258 PDSHPQSAAAARSLAM-------ARADVVLLVG--------ARLNwllGNGespqwsaDAKFIQVDIEASEFDSNRPIVA 322
Cdd:PRK08322 238 PETHPLSLGTAGLSQGdyvhcaiEHADLIINVGhdviekppFFMN---PNG-------DKKVIHINFLPAEVDPVYFPQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 323 PLTGDIGSVMSALLEAAADRSSVASAAwtgeLADRKARNSAKMRRRLADDHHPMRFYNALGAIRSVLQRNpDVYVVNEGA 402
Cdd:PRK08322 308 EVVGDIANSLWQLKERLADQPHWDFPR----FLKIREAIEAHLEEGADDDRFPMKPQRIVADLRKVMPDD-DIVILDNGA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 403 NALDLARNIIdMHLPRHRLDSGTWGVMGIGMGYAIAAA-VETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNG 481
Cdd:PRK08322 383 YKIWFARNYR-AYEPNTCLLDNALATMGAGLPSAIAAKlVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVLILNDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 482 --GVYRgdeatifrsaapvWRHDpaptvlNAHARHELI----------AEAFGGKGYHVSTPTELESALTDALASNGPSL 549
Cdd:PRK08322 462 ayGMIR-------------WKQE------NMGFEDFGLdfgnpdfvkyAESYGAKGYRVESADDLLPTLEEALAQPGVHV 522
|
....*.
gi 489495942 550 IDCELD 555
Cdd:PRK08322 523 IDCPVD 528
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
15-551 |
7.22e-64 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 220.69 E-value: 7.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVG---IPITD-LARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNG 90
Cdd:PRK07418 21 GAYALMDSLKRHGVKHIFGYPGgaiLPIYDeLYKAEAEGWLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGATNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 91 LPALANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLD 170
Cdd:PRK07418 101 VTGIATAQMDSVPMVVITGQVPRPAIGTDA--FQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRPGPVLID 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 171 IPGDVLGQAVEasaasgaiWRPVDPA--------PRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEH 242
Cdd:PRK07418 179 IPKDVGQEEFD--------YVPVEPGsvkppgyrPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 243 TGIPFLPMSMAKGLLPDSHPQSA-------AAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEFD 315
Cdd:PRK07418 251 FQIPVTTTLMGKGAFDEHHPLSVgmlgmhgTAYANFAVTECDLLIAVGARFDDRV-TGKLDEFASRAKVIHIDIDPAEVG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 316 SNRPIVAPLTGDIGSVMSALLEAAADRS-SVASAAWTGELadrkarNSAKMRRRLADDHHPMRFY--NALGAIRSVLqrn 392
Cdd:PRK07418 330 KNRRPDVPIVGDVRKVLVKLLERSLEPTtPPRTQAWLERI------NRWKQDYPLVVPPYEGEIYpqEVLLAVRDLA--- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 393 PDVYVVNE-GAN---ALDLARNiidmhLPRHRLDSGTWGVMGIGMGYAIAAAVETG-RPVVAIEGDSAFGFSGMEFETIC 467
Cdd:PRK07418 401 PDAYYTTDvGQHqmwAAQFLRN-----GPRRWISSAGLGTMGFGMPAAMGVKVALPdEEVICIAGDASFLMNIQELGTLA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 468 RYRLPVTVVILNNG--GVYRGDEATIFRSaapvwRHDpAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASN 545
Cdd:PRK07418 476 QYGINVKTVIINNGwqGMVRQWQESFYGE-----RYS-ASNMEPGMPDFVKLAEAFGVKGMVISERDQLKDAIAEALAHD 549
|
....*.
gi 489495942 546 GPSLID 551
Cdd:PRK07418 550 GPVLID 555
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
15-561 |
1.46e-59 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 207.40 E-value: 1.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPAL 94
Cdd:PRK08617 7 GADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 95 ANATTNCFPMIQISGSSSRPmvDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGD 174
Cdd:PRK08617 87 VTATAEGDPVVAIGGQVKRA--DRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 175 VLGQAVEASAASGAiwrpvdPAPRLLPAPEA-IDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:PRK08617 165 VVDAPVTSKAIAPL------SKPKLGPASPEdINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 KG------------------------LLPDShpqsaaaarslamaraDVVLLVG-------ARlNWllgNGESpqwsaDA 302
Cdd:PRK08617 239 AGvisreledhffgrvglfrnqpgdeLLKKA----------------DLVITIGydpieyePR-NW---NSEG-----DA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 303 KFIQVDIEASEFDSN-RPIVApLTGDIGSVMSALLEAAADRSSvaSAAWTGELADRKARNSAKMRRRLADDH---HPMRF 378
Cdd:PRK08617 294 TIIHIDVLPAEIDNYyQPERE-LIGDIAATLDLLAEKLDGLSL--SPQSLEILEELRAQLEELAERPARLEEgavHPLRI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 379 YNALGAIrsvlqRNPDVYV-VNEGANALDLARniidmHL----PRHRLDSGTWGVMGIGMGYAIAAA-VETGRPVVAIEG 452
Cdd:PRK08617 371 IRALQDI-----VTDDTTVtVDVGSHYIWMAR-----YFrsyePRHLLFSNGMQTLGVALPWAIAAAlVRPGKKVVSVSG 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 453 DSAFGFSGMEFETICRYRLPVTVVILNNGG---VYRGDEATIFRSAApVwrhDPAPTVLNAHarheliAEAFGGKGYHVS 529
Cdd:PRK08617 441 DGGFLFSAMELETAVRLKLNIVHIIWNDGHynmVEFQEEMKYGRSSG-V---DFGPVDFVKY------AESFGAKGLRVT 510
|
570 580 590
....*....|....*....|....*....|..
gi 489495942 530 TPTELESALTDALASNGPSLIDCELDPADGVE 561
Cdd:PRK08617 511 SPDELEPVLREALATDGPVVIDIPVDYSDNIK 542
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
15-555 |
7.19e-57 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 200.33 E-value: 7.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDL-ARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK08527 5 GSQMVCEALKEEGVKVVFGYPGGAILNIyDEIYKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTNAVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PRK08527 85 LATAYMDSIPLVLISGQVPNSLIGTDA--FQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDIPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVlgqaveaSAASGAIWRPVDPA-----PRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFL 248
Cdd:PRK08527 163 DV-------TATLGEFEYPKEISlktykPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 249 PMSMAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEFDSNRPIV 321
Cdd:PRK08527 236 ETLMARGVLRSDDPlllgmlgMHGSYAANMAMSECDLLISLGARFDDRV-TGKLSEFAKHAKIIHVDIDPSSISKIVNAD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 322 APLTGDIGSVMSALLEAAADRSSVASAAWTGELADRKARnsakmrrrladdhHPMRFYNALGAIRsvlqrnPDVYVVNEG 401
Cdd:PRK08527 315 YPIVGDLKNVLKEMLEELKEENPTTYKEWREILKRYNEL-------------HPLSYEDSDEVLK------PQWVIERVG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 402 ANALDLARNIIDM--H-----------LPRHRLDSGTWGVMGIGMGYAIAAAVETG-RPVVAIEGDSAFGFSGMEFETIC 467
Cdd:PRK08527 376 ELLGDDAIISTDVgqHqmwvaqfypfnYPRQLATSGGLGTMGYGLPAALGAKLAVPdKVVINFTGDGSILMNIQELMTAV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 468 RYRLPVTVVILNNG--GVYRgDEATIFrsaapvWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASN 545
Cdd:PRK08527 456 EYKIPVINIILNNNflGMVR-QWQTFF------YEERYSETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALESD 528
|
570
....*....|
gi 489495942 546 GPSLIDCELD 555
Cdd:PRK08527 529 KVALIDVKID 538
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-557 |
2.64e-56 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 199.22 E-value: 2.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 1 MTTRSASPCTVLTD-GCHLVVDALKANDVDTIYGVvGIPiTDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVC 79
Cdd:PRK06112 1 LSKPLSAPGFTLNGtVAHAIARALKRHGVEQIFGQ-SLP-SALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 80 LTTSGPGFLNGLPALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTA 159
Cdd:PRK06112 79 TAQNGPAATLLVAPLAEALKASVPIVALVQDVNRDQTD--RNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 160 TSGRPGGVYLDIPGDVLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREF 239
Cdd:PRK06112 157 TSGRPGPVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 240 VEHTGIPFLPMSMAKGLLPDSHP------------QSAAAARSLAMARADVVLLVGARLNwllGNGESP--QWSADAKFI 305
Cdd:PRK06112 237 QSLAGLPVATTNMGKGAVDETHPlslgvvgslmgpRSPGRHLRDLVREADVVLLVGTRTN---QNGTDSwsLYPEQAQYI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 306 QVDIEASEFDSNRPIVApLTGDIGSVMSALLEAAADRSSVASAAWTGELADRKARNSAKMRRRLAD----DHHPMRFYNA 381
Cdd:PRK06112 314 HIDVDGEEVGRNYEALR-LVGDARLTLAALTDALRGRDLAARAGRRAALEPAIAAGREAHREDSAPvalsDASPIRPERI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 382 LGAIRSVLqrNPDVYVVNEGANALDLARNIIDMHLPRHRLDSGTwGVMGIGMGYAIAAAVETGRP---VVAIEGDSAFGF 458
Cdd:PRK06112 393 MAELQAVL--TGDTIVVADASYSSIWVANFLTARRAGMRFLTPR-GLAGLGWGVPMAIGAKVARPgapVICLVGDGGFAH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 459 SGMEFETICRYRLPVTVVILNNG--GVYRGDEATIFRSAAPVwrhdpaptVLNAHARHELIAEAFGGKGYHVSTPTELES 536
Cdd:PRK06112 470 VWAELETARRMGVPVTIVVLNNGilGFQKHAETVKFGTHTDA--------CHFAAVDHAAIARACGCDGVRVEDPAELAQ 541
|
570 580
....*....|....*....|.
gi 489495942 537 ALTDALASNGPSLIDCELDPA 557
Cdd:PRK06112 542 ALAAAMAAPGPTLIEVITDPS 562
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-551 |
1.62e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 197.11 E-value: 1.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 2 TTRSASPCTVLTdGCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLT 81
Cdd:PRK06725 5 TTYEKLQCEEVT-GAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 82 TSGPGFLNGLPALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATS 161
Cdd:PRK06725 84 TSGPGATNLVTGLADAYMDSIPLVVITGQVATPLIG--KDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 162 GRPGGVYLDIPGDVLGQAVEASAASGAIWRPVDPAPRllPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVE 241
Cdd:PRK06725 162 GRPGPVLIDIPKDVQNEKVTSFYNEVVEIPGYKPEPR--PDSMKLREVAKAISKAKRPLLYIGGGVIHSGGSEELIEFAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 242 HTGIPFLPMSMAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEF 314
Cdd:PRK06725 240 ENRIPVVSTLMGLGAYPPGDPlflgmlgMHGTYAANMAVTECDLLLALGVRFDDRV-TGKLELFSPHSKKVHIDIDPSEF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 315 DSNRPIVAPLTGDIGSVMSALLEAAAdrsSVASAAWTGELADRKARNSAKMRRRlADDHHPMRFYNALGAIrsvlqRNPD 394
Cdd:PRK06725 319 HKNVAVEYPVVGDVKKALHMLLHMSI---HTQTDEWLQKVKTWKEEYPLSYKQK-ESELKPQHVINLVSEL-----TNGE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 395 VYVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPV 473
Cdd:PRK06725 390 AIVTTEVGQHQMWAAHFYKAKNPRTFLTSGGLGTMGFGFPAAIGAQLaKEEELVICIAGDASFQMNIQELQTIAENNIPV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 474 TVVILNNG--GVYRGDEATIFRSAAPVWRHDpAPTVLNaharhelIAEAFGGKGYHVSTPTELESALTDALASNGPSLID 551
Cdd:PRK06725 470 KVFIINNKflGMVRQWQEMFYENRLSESKIG-SPDFVK-------VAEAYGVKGLRATNSTEAKQVMLEAFAHEGPVVVD 541
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
15-558 |
1.10e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 194.97 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVG---IPITDlarAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGgalLPFYD---ALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVdlqrGD--YQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYL 169
Cdd:PRK06276 80 TGIATAYADSSPVIALTGQVPTKLI----GNdaFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 170 DIPGDVlgQAVEASAASGAIWRPVDPA---PRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIP 246
Cdd:PRK06276 156 DLPKDV--QEGELDLEKYPIPAKIDLPgykPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 247 FLPMSMAKGLLPDSHPQSA-------AAARSLAMARADVVLLVGARL-NWLLGNGESpqWSADAKFIQVDIEASEFDSNR 318
Cdd:PRK06276 234 VCTTLMGKGAFPEDHPLALgmvgmhgTKAANYSVTESDVLIAIGCRFsDRTTGDISS--FAPNAKIIHIDIDPAEIGKNV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 319 PIVAPLTGDIGSVMSALLEAAADRSSVASAAWTGELADRKArnsAKMRRRLADDH--HPMRFYNALGAIRSVLQRNPDVY 396
Cdd:PRK06276 312 RVDVPIVGDAKNVLRDLLAELMKKEIKNKSEWLERVKKLKK---ESIPRMDFDDKpiKPQRVIKELMEVLREIDPSKNTI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 397 VVNE-GANALDLARnIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVET-GRPVVAIEGDSAFGFSGMEFETICRYRLPVT 474
Cdd:PRK06276 389 ITTDvGQNQMWMAH-FFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKpDANVIAITGDGGFLMNSQELATIAEYDIPVV 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 475 VVILNN---GGVYRGDEATIFRSAAPVwRHDPAPTVLNaharhelIAEAFGGKGYHVSTPTELESALTDALASNGPSLID 551
Cdd:PRK06276 468 ICIFDNrtlGMVYQWQNLYYGKRQSEV-HLGETPDFVK-------LAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLD 539
|
....*..
gi 489495942 552 CELDPAD 558
Cdd:PRK06276 540 IIIDPAE 546
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
17-551 |
1.56e-54 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 193.27 E-value: 1.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 17 HLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:PRK07524 6 EALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATAMGQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISGSSSRPMVDLQRGDYQDL-DQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGDV 175
Cdd:PRK07524 86 AYADSIPMLVISSVNRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIPLDV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 176 LGQAVEASAAsgaiwRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADnvIREFVEHTGIPFLPMSMAKG 255
Cdd:PRK07524 166 LAAPADHLLP-----APPTRPARPGPAPAALAQAAERLAAARRPLILAGGGALAAAAA--LRALAERLDAPVALTINAKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 256 LLPDSHPQSAAAARSLAM-----ARADVVLLVGARLN----WLLGNGESPqwsADAKFIQVDIEASEFDSNRPIVAPLTG 326
Cdd:PRK07524 239 LLPAGHPLLLGASQSLPAvraliAEADVVLAVGTELGetdyDVYFDGGFP---LPGELIRIDIDPDQLARNYPPALALVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 327 DIGSVMSALLEAAADRSSVASAAwtgeladrkARNSAKMRRRLADDHHP-MRFYNALgaIRSVLQRNPDVYVVNEGANAL 405
Cdd:PRK07524 316 DARAALEALLARLPGQAAAADWG---------AARVAALRQALRAEWDPlTAAQVAL--LDTILAALPDAIFVGDSTQPV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 406 DLARNIIDMHLPRHRLDSGT-WGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGGV 483
Cdd:PRK07524 385 YAGNLYFDADAPRRWFNASTgYGTLGYGLPAAIGAALgAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLWNNDGY 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495942 484 YRGDEATIFRSAAPVWRHDPAPTVlnaharhELIAEAFGGKGYHVSTPTELESALTDALASNGPSLID 551
Cdd:PRK07524 465 GEIRRYMVARDIEPVGVDPYTPDF-------IALARAFGCAAERVADLEQLQAALRAAFARPGPTLIE 525
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
10-551 |
4.97e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 192.68 E-value: 4.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 10 TVLTDGCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLN 89
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 90 GLPALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYL 169
Cdd:PRK06048 85 LVTGIATAYMDSVPIVALTGQVPRSMIG--NDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 170 DIPGDVLGQAVEASAASGAIWRPVDpaPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLP 249
Cdd:PRK06048 163 DLPKDVTTAEIDFDYPDKVELRGYK--PTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 250 MSMAKGLLPDSHPQSAAAA-------RSLAMARADVVLLVGARL-NWLLGNGESpqWSADAKFIQVDIEASEFDSNRPIV 321
Cdd:PRK06048 241 TLMGIGAIPTEHPLSLGMLgmhgtkyANYAIQESDLIIAVGARFdDRVTGKLAS--FAPNAKIIHIDIDPAEISKNVKVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 322 APLTGDIGSVMSALLEAAADRssvASAAWTGELADRKARNSAKMRRRlaDDHHPMRFynalgAIRSVLQRNPDVYVVNE- 400
Cdd:PRK06048 319 VPIVGDAKQVLKSLIKYVQYC---DRKEWLDKINQWKKEYPLKYKER--EDVIKPQY-----VIEQIYELCPDAIIVTEv 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 401 GANALdLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVetGRP---VVAIEGDSAFGFSGMEFETICRYRLPVTVVI 477
Cdd:PRK06048 389 GQHQM-WAAQYFKYKYPRTFITSGGLGTMGYGFPAAIGAKV--GKPdktVIDIAGDGSFQMNSQELATAVQNDIPVIVAI 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 478 LNNG--GVYRGDEATIFrsaapvwRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLID 551
Cdd:PRK06048 466 LNNGylGMVRQWQELFY-------DKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVASDRPVVID 534
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-560 |
3.43e-53 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 190.30 E-value: 3.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 1 MTTRSASPCTVLTDGCHLVVDALKANDVDTIYGVVGIPITDLARA-AQASGIRYIGFRHEASAGNAAAAAGFLTARPGVC 79
Cdd:PRK08155 1 MASSGTTSTRKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDAlSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 80 LTTSGPGFLNGLPALANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTA 159
Cdd:PRK08155 81 MACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDA--FQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 160 TSGRPGGVYLDIPGDVLGQAVEASAASGaiwrPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREF 239
Cdd:PRK08155 159 QSGRPGPVWIDIPKDVQTAVIELEALPA----PAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARAREL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 240 VEHTGIPFLPMSMAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNwLLGNGESPQWSADAKFIQVDIEAS 312
Cdd:PRK08155 235 AEKAQLPTTMTLMALGMLPKAHPlslgmlgMHGARSTNYILQEADLLIVLGARFD-DRAIGKTEQFCPNAKIIHVDIDRA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 313 EFDSNRPIVAPLTGDIGSVMSALLEAAADRssvASAAWTGELADRKARNSAKMRRrlADDhhPMRFYnalGAIRSVLQRN 392
Cdd:PRK08155 314 ELGKIKQPHVAIQADVDDVLAQLLPLVEAQ---PRAEWHQLVADLQREFPCPIPK--ADD--PLSHY---GLINAVAACV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 393 PDVYVVNEG--------ANALDLARniidmhlPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEF 463
Cdd:PRK08155 384 DDNAIITTDvgqhqmwtAQAYPLNR-------PRQWLTSGGLGTMGFGLPAAIGAALaNPERKVLCFSGDGSLMMNIQEM 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 464 ETICRYRLPVTVVILNN---GGVYRgdEATIF---RSAAPVWRHDPaptvlnahaRHELIAEAFGGKGYHVSTPTELESA 537
Cdd:PRK08155 457 ATAAENQLDVKIILMNNealGLVHQ--QQSLFygqRVFAATYPGKI---------NFMQIAAGFGLETCDLNNEADPQAA 525
|
570 580
....*....|....*....|...
gi 489495942 538 LTDALASNGPSLIDCELDPADGV 560
Cdd:PRK08155 526 LQEAINRPGPALIHVRIDAEEKV 548
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
15-560 |
2.50e-52 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 187.78 E-value: 2.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVG---IPITDlarAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGgaiMPVYD---ALYDGGVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMV--DLqrgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYL 169
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIgtDA----FQEIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 170 DIPGDVLgqavEASAASGAIWRPVDPAPrlLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPflP 249
Cdd:PRK08978 156 DIPKDIQ----LAEGELEPHLTTVENEP--AFPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMP--A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 250 MSMAKGL--LPDSHPQSA-------AAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEFDSNRPI 320
Cdd:PRK08978 228 VATLKGLgaVEADHPYYLgmlgmhgTKAANLAVQECDLLIAVGARFDDRV-TGKLNTFAPHAKVIHLDIDPAEINKLRQA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 321 VAPLTGDIGSVMSALleaaadRSSVASAAWTGELADRKARNSAKMRrrladdhHPMRFYNALGAIRSVLQRNPDVYVV-- 398
Cdd:PRK08978 307 HVALQGDLNALLPAL------QQPLNIDAWRQHCAQLRAEHAWRYD-------HPGEAIYAPALLKQLSDRKPADTVVtt 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 399 NEGANALDLARNiIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVetGRP---VVAIEGDSAFGFSGMEFETICRYRLPVTV 475
Cdd:PRK08978 374 DVGQHQMWVAQH-MRFTRPENFITSSGLGTMGFGLPAAIGAQV--ARPddtVICVSGDGSFMMNVQELGTIKRKQLPVKI 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 476 VILNNG--GVYRGDEATIFRSaapvwRHdpAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCE 553
Cdd:PRK08978 451 VLLDNQrlGMVRQWQQLFFDE-----RY--SETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSEGPYLLHVS 523
|
....*..
gi 489495942 554 LDPADGV 560
Cdd:PRK08978 524 IDELENV 530
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
15-556 |
2.80e-52 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 187.78 E-value: 2.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVG---IPITDLARaaQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:PRK08199 10 GGQILVDALRANGVERVFCVPGesyLAVLDALH--DETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDI 171
Cdd:PRK08199 88 IGVHTAFQDSTPMILFVGQVARDFRE--REAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 172 PGDVLGQAVEASAAsgaiwRPVDPaPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMS 251
Cdd:PRK08199 166 PEDVLSETAEVPDA-----PPYRR-VAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 252 MAKGLLPDSHPQ-------SAAAARSLAMARADVVLLVGARLNWLLGNG----ESPQwsADAKFIQVDIEASE----FDS 316
Cdd:PRK08199 240 RRQDLFDNRHPNyagdlglGINPALAARIREADLVLAVGTRLGEVTTQGytllDIPV--PRQTLVHVHPDAEElgrvYRP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 317 NRPIVAPltgdigsvMSALLEAAADRSSVASAAWTGELADRKARNSAKMRRRladdhhPMRFYNALGAIRSVLQRN--PD 394
Cdd:PRK08199 318 DLAIVAD--------PAAFAAALAALEPPASPAWAEWTAAAHADYLAWSAPL------PGPGAVQLGEVMAWLRERlpAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 395 VYVVNEGAN-ALDLARniidmHLPRHRLDSG---TWGVMGIGMGYAIAAAVE-TGRPVVAIEGDSAFGFSGMEFETICRY 469
Cdd:PRK08199 384 AIITNGAGNyATWLHR-----FFRFRRYRTQlapTSGSMGYGLPAAIAAKLLfPERTVVAFAGDGCFLMNGQELATAVQY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 470 RLPVTVVILNNG--GVYRGDEAtifrsaapvwRHDPAPTVLNAHARHE--LIAEAFGGKGYHVSTPTELESALTDALASN 545
Cdd:PRK08199 459 GLPIIVIVVNNGmyGTIRMHQE----------REYPGRVSGTDLTNPDfaALARAYGGHGETVERTEDFAPAFERALASG 528
|
570
....*....|.
gi 489495942 546 GPSLIDCELDP 556
Cdd:PRK08199 529 KPALIEIRIDP 539
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
15-552 |
2.92e-52 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 188.38 E-value: 2.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVG---IPITDlaRAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:PRK09107 13 GAEMVVQALKDQGVEHIFGYPGgavLPIYD--EIFQQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGATNAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVdlqrGD--YQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYL 169
Cdd:PRK09107 91 TPLQDALMDSIPLVCITGQVPTHLI----GSdaFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 170 DIPGDVlgqaveaSAASGAIWRPVDP------APRLLPAPEAIDRALDVLAQAQRPLLVLGKGA--AYAQADNVIREFVE 241
Cdd:PRK09107 167 DIPKDV-------QFATGTYTPPQKApvhvsyQPKVKGDAEAITEAVELLANAKRPVIYSGGGVinSGPEASRLLRELVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 242 HTGIPFLPMSMAKGLLPDSHPQ-------SAAAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEF 314
Cdd:PRK09107 240 LTGFPITSTLMGLGAYPASGKNwlgmlgmHGTYEANMAMHDCDVMLCVGARFDDRI-TGRLDAFSPNSKKIHIDIDPSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 315 DSNRPIVAPLTGDIGSVMSALLEA--AADRS--SVASAAWTGELADRKARNSAKMRRrlADD-----HHPMRFYNalgai 385
Cdd:PRK09107 319 NKNVRVDVPIIGDVGHVLEDMLRLwkARGKKpdKEALADWWGQIARWRARNSLAYTP--SDDvimpqYAIQRLYE----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 386 rsvLQRNPDVYVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIaaAVETGRP---VVAIEGDSAFGFSGME 462
Cdd:PRK09107 392 ---LTKGRDTYITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAAL--GVQIAHPdalVIDIAGDASIQMCIQE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 463 FETICRYRLPVTVVILNNGgvYRGdeatIFRSaapvWRHdpaptVLN----AHARHEL------IAEAFGGKGYHVSTPT 532
Cdd:PRK09107 467 MSTAVQYNLPVKIFILNNQ--YMG----MVRQ----WQQ-----LLHgnrlSHSYTEAmpdfvkLAEAYGAVGIRCEKPG 531
|
570 580
....*....|....*....|
gi 489495942 533 ELESALTDALASNGPSLIDC 552
Cdd:PRK09107 532 DLDDAIQEMIDVDKPVIFDC 551
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
17-555 |
1.54e-48 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 177.10 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 17 HLVVDALKANDVDTIYGVVGI---PITDlaRAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK07064 7 ELIAAFLEQCGVKTAFGVISIhnmPILD--AIGRRGKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGNAAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRGDYQDL-DQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIP 172
Cdd:PRK07064 85 LVEALTAGTPLLHITGQIETPYLDQDLGYIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVSVEIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 173 GDVLGQAVEASAASGAIwrpvdPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADnvIREFVEhTGIPFLPMSM 252
Cdd:PRK07064 165 IDIQAAEIELPDDLAPV-----HVAVPEPDAAAVAELAERLAAARRPLLWLGGGARHAGAE--VKRLVD-LGFGVVTSTQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 253 AKGLLPDSHPQS-----AAAARSLAMARADVVLLVGARLNwllGNgESPQWSAD--AKFIQVDIEASEFDSNRPIVAPLT 325
Cdd:PRK07064 237 GRGVVPEDHPASlgafnNSAAVEALYKTCDLLLVVGSRLR---GN-ETLKYSLAlpRPLIRVDADAAADGRGYPNDLFVH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 326 GDIGSVMSALLEAAADRSSVaSAAWTGELADRKARNSAKMRRRLADdhhpmrfYNAL-GAIRSVLQRNP----DVYVVNE 400
Cdd:PRK07064 313 GDAARVLARLADRLEGRLSV-DPAFAADLRAAREAAVADLRKGLGP-------YAKLvDALRAALPRDGnwvrDVTISNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 401 G-ANALdlarniIDMHLPRHRLDSgTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVIL 478
Cdd:PRK07064 385 TwGNRL------LPIFEPRANVHA-LGGGIGQGLAMAIGAALaGPGRKTVGLVGDGGLMLNLGELATAVQENANMVIVLM 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 479 NNG--GVYRG--DEATIFRSAApVWRHDPAPTvlnaharheLIAEAFGGKGYHVSTPTELESALTDALASNGPSLIdcEL 554
Cdd:PRK07064 458 NDGgyGVIRNiqDAQYGGRRYY-VELHTPDFA---------LLAASLGLPHWRVTSADDFEAVLREALAKEGPVLV--EV 525
|
.
gi 489495942 555 D 555
Cdd:PRK07064 526 D 526
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
12-552 |
2.05e-47 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 174.89 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 12 LTDGCHLVVDALKANDVDTIYGVVG---IPITD-LARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGF 87
Cdd:CHL00099 9 EKTGAFALIDSLVRHGVKHIFGYPGgaiLPIYDeLYAWEKKGLIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 88 LNGLPALANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGV 167
Cdd:CHL00099 89 TNLVTGIATAQMDSVPLLVITGQVGRAFIGTDA--FQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRPGPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 168 YLDIPGDV-----LGQAVEASAASGAI--WRPVDPaprllPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFV 240
Cdd:CHL00099 167 LIDIPKDVglekfDYYPPEPGNTIIKIlgCRPIYK-----PTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 241 EHTGIPFLPMSMAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASE 313
Cdd:CHL00099 242 ELYKIPVTTTLMGKGIFDEDHPlclgmlgMHGTAYANFAVSECDLLIALGARFDDRV-TGKLDEFACNAQVIHIDIDPAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 314 FDSNR-PIVApLTGDIGSVMSALLEAAADRS----SVASAAWTGELAdrKARNSAKMR-RRLADDHHPMRFYNALGAIRs 387
Cdd:CHL00099 321 IGKNRiPQVA-IVGDVKKVLQELLELLKNSPnlleSEQTQAWRERIN--RWRKEYPLLiPKPSTSLSPQEVINEISQLA- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 388 vlqrnPDVYVVNE-GANALDLARNIidMHLPRHRLDSGTWGVMGIGMGYAIAAAVE-TGRPVVAIEGDSAFGFSGMEFET 465
Cdd:CHL00099 397 -----PDAYFTTDvGQHQMWAAQFL--KCKPRKWLSSAGLGTMGYGLPAAIGAQIAhPNELVICISGDASFQMNLQELGT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 466 ICRYRLPVTVVILNNG--GVYRGDEATIFRSaapvwRHdpaptvlnAHARHE-------LIAEAFGGKGYHVSTPTELES 536
Cdd:CHL00099 470 IAQYNLPIKIIIINNKwqGMVRQWQQAFYGE-----RY--------SHSNMEegapdfvKLAEAYGIKGLRIKSRKDLKS 536
|
570
....*....|....*.
gi 489495942 537 ALTDALASNGPSLIDC 552
Cdd:CHL00099 537 SLKEALDYDGPVLIDC 552
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
15-543 |
9.03e-47 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 172.70 E-value: 9.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQA-SGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK08979 6 GASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGATNTITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PRK08979 86 IATAYMDSIPMVVLSGQVPSNLIG--NDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVIDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:PRK08979 164 DCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVSTLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 KGLLPDSHPQSA-------AAARSLAMARADVVLLVGARLNWLLGNGESpQWSADAKFIQVDIEASEFDSNRPIVAPLTG 326
Cdd:PRK08979 244 LGAFPGTHKNSLgmlgmhgRYEANMAMHNADLIFGIGVRFDDRTTNNLE-KYCPNATILHIDIDPSSISKTVRVDIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 327 DIGSVMSALL----EAAADRSSVASAAWTGELADRKARNSakmrrrLADDHHPMRFyNALGAIRSVLQ-RNPDVYVVNEG 401
Cdd:PRK08979 323 SADKVLDSMLalldESGETNDEAAIASWWNEIEVWRSRNC------LAYDKSSERI-KPQQVIETLYKlTNGDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 402 ANALDLARNIIDMHLPRHRLDSGTWGVMGIG----MGYAIAAAVETgrpVVAIEGDSAFGFSGMEFETICRYRLPVTVVI 477
Cdd:PRK08979 396 GQHQMFAALYYPFDKPRRWINSGGLGTMGFGlpaaMGVKFAMPDET---VVCVTGDGSIQMNIQELSTALQYDIPVKIIN 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 478 LNN---GGV-------YRGDEATIFRSAAPvwrhDPAPtvlnaharhelIAEAFGGKGYHVSTPTELESALTDALA 543
Cdd:PRK08979 473 LNNrflGMVkqwqdmiYQGRHSHSYMDSVP----DFAK-----------IAEAYGHVGIRISDPDELESGLEKALA 533
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
15-555 |
1.18e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 172.33 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGI---PITD-LARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNG 90
Cdd:PRK06456 4 GARILVDSLKREGVKVIFGIPGLsnmQIYDaFVEDLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 91 LPALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLD 170
Cdd:PRK06456 84 VTGLITAYWDSSPVIAITGQVPRSVMG--KMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 171 IPGDVLGQAVEAsaasgAIW--RPVDPAPRLLPA---PEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGI 245
Cdd:PRK06456 162 IPRDIFYEKMEE-----IKWpeKPLVKGYRDFPTridRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 246 PFLPMSMAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWLLGNGESPQWSADAKFIQVDIEASEFDSNR 318
Cdd:PRK06456 237 PIVSTFPGKTAIPHDHPlyfgpmgYYGRAEASMAALESDAMLVVGARFSDRTFTSYDEMVETRKKFIMVNIDPTDGEKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 319 PIVAPLTGD----IGSVMSALLEAAADRSsvaSAAWTGELADRKARNSakmRRRLADDHHPMRFYNALGAIRSVLQRNPd 394
Cdd:PRK06456 317 KVDVGIYGNakiiLRELIKAITELGQKRD---RSAWLKRVKEYKEYYS---QFYYTEENGKLKPWKIMKTIRQALPRDA- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 395 vyVVNEGANALDL-ARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVetGRP---VVAIEGDSAFGFSGMEFETICRYR 470
Cdd:PRK06456 390 --IVTTGVGQHQMwAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKL--ARPdkvVVDLDGDGSFLMTGTNLATAVDEH 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 471 LPVTVVILNNG--GVYRGDEATIFRSAAPVWRHDPAPTVLNaharhelIAEAFGGKGYHVSTPTELESALTDALASNGPS 548
Cdd:PRK06456 466 IPVISVIFDNRtlGLVRQVQDLFFGKRIVGVDYGPSPDFVK-------LAEAFGALGFNVTTYEDIEKSLKSAIKEDIPA 538
|
....*..
gi 489495942 549 LIDCELD 555
Cdd:PRK06456 539 VIRVPVD 545
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
17-558 |
1.50e-46 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 172.11 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 17 HLVVDALKANDVDTIYGVVGIPI---TDLARAAQASgIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPG---FLNG 90
Cdd:PRK08611 8 EALVKLLQDWGIDHVYGIPGDSIdavVDALRKEQDK-IKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGaihLLNG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 91 lpaLANATTNCFPMIQISGSSSRPMvdLQRGDYQdldQLNAARPFVKAA---YRIGQVQDIGRGVARAIRTATSGRpGGV 167
Cdd:PRK08611 87 ---LYDAKMDHVPVLALAGQVTSDL--LGTDFFQ---EVNLEKMFEDVAvynHQIMSAENLPEIVNQAIRTAYEKK-GVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 168 YLDIPGDVLGQAVEASA-ASGAIWRPVDPAPRllpaPEAIDRALDVLAQAQRPLLVLGKGAAYAQADnvIREFVEHTGIP 246
Cdd:PRK08611 158 VLTIPDDLPAQKIKDTTnKTVDTFRPTVPSPK----PKDIKKAAKLINKAKKPVILAGLGAKHAKEE--LLAFAEKAKIP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 247 F---LPmsmAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWllgngeSPQWSADAKFIQVDIEASEFDS 316
Cdd:PRK08611 232 IihtLP---AKGIIPDDHPyslgnlgKIGTKPAYEAMQEADLLIMVGTNYPY------VDYLPKKAKAIQIDTDPANIGK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 317 NRPIVAPLTGDIGSVMSALLEAAAdrsSVASAAWTGELADRKARNSAKMRRRLADDHHPMRFYNALGAIRSVLQRNPdVY 396
Cdd:PRK08611 303 RYPVNVGLVGDAKKALHQLTENIK---HVEDRRFLEACQENMAKWWKWMEEDENNASTPIKPERVMAAIQKIADDDA-VL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 397 VVNEGANALDLARniidmHL---PRHRLDSGTW-GVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRL 471
Cdd:PRK08611 379 SVDVGTVTVWSAR-----YLnlgTNQKFIISSWlGTMGCGLPGAIAAKIaFPDRQAIAICGDGGFSMVMQDFVTAVKYKL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 472 PVTVVILNNGGV----YRGDEATIFRSAAPVWRHDpaptvlnaHARhelIAEAFGGKGYHVSTPTELESALTDALASNGP 547
Cdd:PRK08611 454 PIVVVVLNNQQLafikYEQQAAGELEYAIDLSDMD--------YAK---FAEACGGKGYRVEKAEELDPAFEEALAQDKP 522
|
570
....*....|.
gi 489495942 548 SLIDCELDPAD 558
Cdd:PRK08611 523 VIIDVYVDPNA 533
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
15-551 |
6.84e-45 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 168.24 E-value: 6.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQAS-GIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK07789 33 GAQAVVRSLEELGVDVVFGIPGGAILPVYDPLFDStKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGATNLVTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PRK07789 113 IADANMDSVPVVAITGQVGRGLIGTDA--FQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVDIPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAVEASaasgaiWRP-VD-PAPRLLPAPEA--IDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLP 249
Cdd:PRK07789 191 DALQAQTTFS------WPPrMDlPGYRPVTKPHGkqIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTGIPVVT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 250 MSMAKGLLPDSHPQSA-------AAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEFDSNRPIVA 322
Cdd:PRK07789 265 TLMARGAFPDSHPQHLgmpgmhgTVAAVAALQRSDLLIALGARFDDRV-TGKLDSFAPDAKVIHADIDPAEIGKNRHADV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 323 PLTGDIGSVMSALLEAAADRSSVAS----AAWTGELADrkarnsakMRRRladdhHPMRF---YNALGAIRSVLQR---- 391
Cdd:PRK07789 344 PIVGDVKEVIAELIAALRAEHAAGGkpdlTAWWAYLDG--------WRET-----YPLGYdepSDGSLAPQYVIERlgei 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 392 -NPD-VYVVNEGANALdLARNIIDMHLPRHRLDSGtwgvmGIG-MGYAIAAAV--ETGRP---VVAIEGDSAFGFSGMEF 463
Cdd:PRK07789 411 aGPDaIYVAGVGQHQM-WAAQFIDYEKPRTWLNSG-----GLGtMGYAVPAAMgaKVGRPdkeVWAIDGDGCFQMTNQEL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 464 ETICRYRLPVTVVILNNG--GVYRgDEATIFrsaapvWRHDPAPTVLNAHARH----ELIAEAFGGKGYHVSTPTELESA 537
Cdd:PRK07789 485 ATCAIEGIPIKVALINNGnlGMVR-QWQTLF------YEERYSNTDLHTHSHRipdfVKLAEAYGCVGLRCEREEDVDAV 557
|
570
....*....|....*
gi 489495942 538 LTDALASNG-PSLID 551
Cdd:PRK07789 558 IEKARAINDrPVVID 572
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
20-544 |
1.57e-44 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 166.71 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 20 VDALKANDVDTIYGVVG---IPITDLARAAqasGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:PRK07525 13 VETLQAHGITHAFGIIGsafMDASDLFPPA---GIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISGSSSRPMVDLqrGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRpGGVYLDIPGDVL 176
Cdd:PRK07525 90 AYWAHTPVVLVTPQAGTKTIGQ--GGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDYF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 177 GQAVEAsaasgAIWRPVDpAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPflpmsMAKGL 256
Cdd:PRK07525 167 YGVIDV-----EIPQPVR-LERGAGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAP-----VACGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 257 L-----PDSHPQSA-------AAARSLAMARADVVLLVGARLNWLlgnGESPQ-----WSADAKFIQVDIEASEFDSNRP 319
Cdd:PRK07525 236 LhndafPGSHPLWVgplgyngSKAAMELIAKADVVLALGTRLNPF---GTLPQygidyWPKDAKIIQVDINPDRIGLTKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 320 IVAPLTGDIGSVMSALLE-------AAADRSSVAS------AAWTGELA-------DRKARNSAKMRRRLADDHHPMRFY 379
Cdd:PRK07525 313 VSVGICGDAKAVARELLArlaerlaGDAGREERKAliaaekSAWEQELSswdheddDPGTDWNEEARARKPDYMHPRQAL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 380 NALGAIRSvlqrnPDVYVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGF 458
Cdd:PRK07525 393 REIQKALP-----EDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFPAIIGAKIaCPDRPVVGFAGDGAWGI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 459 SGMEFETICRYRLPVTVVILNNGGvyRGDE---ATIFRSAAPVwrhdpaPTVLNAHARHELIAEAFGGKGYHVSTPTELE 535
Cdd:PRK07525 468 SMNEVMTAVRHNWPVTAVVFRNYQ--WGAEkknQVDFYNNRFV------GTELDNNVSYAGIAEAMGAEGVVVDTQEELG 539
|
....*....
gi 489495942 536 SALTDALAS 544
Cdd:PRK07525 540 PALKRAIDA 548
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
13-551 |
2.21e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 166.15 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 13 TDGCHLVVDALKANDVDTIYGVVGIPITDLARAA-QASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGL 91
Cdd:PRK07282 10 KSGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIyNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 92 PALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDI 171
Cdd:PRK07282 90 TGIADAMSDSVPLLVFTGQVARAGIG--KDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 172 PGDVlgQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMS 251
Cdd:PRK07282 168 PKDV--SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 252 MAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARL-NWLLGNGESpqWSADAKFIQVDIEASEFDSNRPIVAP 323
Cdd:PRK07282 246 LGQGTIATSHPlflgmggMHGSYAANIAMTEADFMINIGSRFdDRLTGNPKT--FAKNAKVAHIDIDPAEIGKIIKTDIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 324 LTGDIGSVMSALLeaAADRSSVASAAWTGELADRKARnsakmRRRLADDHHPMRFYNALGAIRSVLQRNPdVYVVNEGAN 403
Cdd:PRK07282 324 VVGDAKKALQMLL--AEPTVHNNTEKWIEKVTKDKNR-----VRSYDKKERVVQPQAVIERIGELTNGDA-IVVTDVGQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 404 ALDLARniidmHLP----RHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVIL 478
Cdd:PRK07282 396 QMWAAQ-----YYPyqneRQLVTSGGLGTMGFGIPAAIGAKIaNPDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVML 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 479 NN---GGVYRGDEAtifrsaapVWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALtDALASNGPSLID 551
Cdd:PRK07282 471 NNhslGMVRQWQES--------FYEGRTSESVFDTLPDFQLMAQAYGIKHYKFDNPETLAQDL-EVITEDVPMLIE 537
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
15-551 |
5.98e-44 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 165.30 E-value: 5.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARA-AQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQAlTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDA--FQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAV-----EASAASGAIWRPvdPAPrllPAPEAIDRALDVLAQAQRPLLVLGKGAayAQADNVIREFVEHTGIPFL 248
Cdd:PLN02470 173 DIQQQLAvpnwnQPMKLPGYLSRL--PKP---PEKSQLEQIVRLISESKRPVVYVGGGC--LNSSEELREFVELTGIPVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 249 PMSMAKGLLPDSHPQS-------AAAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIEASEFDSNRPIV 321
Cdd:PLN02470 246 STLMGLGAFPASDELSlqmlgmhGTVYANYAVDSADLLLAFGVRFDDRV-TGKLEAFASRASIVHIDIDPAEIGKNKQPH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 322 APLTGDIG---SVMSALLEAAADRSSVASaAWTGELADRKARNSAKMRRRlaDDHHPMRFynalgAIRSVLQRNPDVYVV 398
Cdd:PLN02470 325 VSVCADVKlalQGLNKLLEERKAKRPDFS-AWRAELDEQKEKFPLSYPTF--GDAIPPQY-----AIQVLDELTDGNAII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 399 NEGANALDL-ARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVET-GRPVVAIEGDSAFGFSGMEFETICRYRLPVTVV 476
Cdd:PLN02470 397 STGVGQHQMwAAQWYKYKEPRRWLTSGGLGAMGFGLPAAIGAAAANpDAIVVDIDGDGSFIMNIQELATIHVENLPVKIM 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 477 ILNN---GGVYRGDEATIFRSAAPVWRHDPA------PTVLnaharheLIAEAFGGKGYHVSTPTELESALTDALASNGP 547
Cdd:PLN02470 477 VLNNqhlGMVVQWEDRFYKANRAHTYLGDPDaeaeifPDFL-------KFAEGCKIPAARVTRKSDLREAIQKMLDTPGP 549
|
....
gi 489495942 548 SLID 551
Cdd:PLN02470 550 YLLD 553
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
17-172 |
8.96e-44 |
|
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: 153.07 E-value: 8.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 17 HLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 97 ATTNCFPMIQISGSSSRPmvDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIP 172
Cdd:cd07035 81 AYLDSIPLLVITGQRPTA--GEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLP 154
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
1-560 |
2.05e-43 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 163.39 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 1 MTTRSASPCTVLTDGCHLVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCL 80
Cdd:PRK07710 4 MRTMSSKTEEKLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 81 TTSGPGFLNGLPALANATTNCFPMIQISGSSSRPMVDlqRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTAT 160
Cdd:PRK07710 84 ATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIG--SDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 161 SGRPGGVYLDIPGDVLGQAVEASAAsgaiwRPVD-PA--PRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIR 237
Cdd:PRK07710 162 TGRPGPVLIDIPKDMVVEEGEFCYD-----VQMDlPGyqPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 238 EFVEHTGIPFLPMSMAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWLLgNGESPQWSADAKFIQVDIE 310
Cdd:PRK07710 237 SYAEQQEIPVVHTLLGLGGFPADHPlflgmagMHGTYTANMALYECDLLINIGARFDDRV-TGNLAYFAKEATVAHIDID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 311 ASEFDSNRPIVAPLTGDIGSVMSALLEAAADRSsvASAAWTGELADRKARnsakmrrrladdhHPMRFYNALGAIRSvlQ 390
Cdd:PRK07710 316 PAEIGKNVPTEIPIVADAKQALQVLLQQEGKKE--NHHEWLSLLKNWKEK-------------YPLSYKRNSESIKP--Q 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 391 RNPDV---YVVNEGANALDL------ARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSG 460
Cdd:PRK07710 379 KAIEMlyeITKGEAIVTTDVgqhqmwAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLaKPDETVVAIVGDGGFQMTL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 461 MEFETICRYRLPVTVVILNN---GGVYRGDEatIFrsaapvWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESA 537
Cdd:PRK07710 459 QELSVIKELSLPVKVVILNNealGMVRQWQE--EF------YNQRYSHSLLSCQPDFVKLAEAYGIKGVRIDDELEAKEQ 530
|
570 580
....*....|....*....|...
gi 489495942 538 LTDALASNGPSLIDCELDPADGV 560
Cdd:PRK07710 531 LQHAIELQEPVVIDCRVLQSEKV 553
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
17-182 |
4.92e-43 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 151.62 E-value: 4.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 17 HLVVDALKANDVDTIYGVVGIPITDLARAAQAS-GIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALA 95
Cdd:pfam02776 3 EALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 96 NATTNCFPMIQISGSSSRPMVDlQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGDV 175
Cdd:pfam02776 83 NAYVDSVPLLVISGQRPRSLVG-RGALQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLDV 161
|
....*..
gi 489495942 176 LGQAVEA 182
Cdd:pfam02776 162 LLEEVDE 168
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
15-543 |
1.22e-42 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 161.24 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQA-SGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGsssRPMVDLQRGD-YQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIP 172
Cdd:PRK06882 86 IATAYTDSVPLVILSG---QVPSNLIGTDaFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 173 GDVLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSM 252
Cdd:PRK06882 163 KDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 253 AKGLLPDSHPQ-------SAAAARSLAMARADVVLLVGARLNWLLGNGESpQWSADAKFIQVDIEASEFDSNRPIVAPLT 325
Cdd:PRK06882 243 GLGAYPSTDKQflgmlgmHGTYEANNAMHESDLILGIGVRFDDRTTNNLA-KYCPNAKVIHIDIDPTSISKNVPAYIPIV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 326 GDIGSVMSALLEAAAD----RSSVASAAWTGELADRKARNSAKMRRRlADDHHPMRFYNALGAIrsvlqRNPDVYVVNEG 401
Cdd:PRK06882 322 GSAKNVLEEFLSLLEEenlaKSQTDLTAWWQQINEWKAKKCLEFDRT-SDVIKPQQVVEAIYRL-----TNGDAYVASDV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 402 ANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIaaAVETGRP---VVAIEGDSAFGFSGMEFETICRYRLPVTVVIL 478
Cdd:PRK06882 396 GQHQMFAALHYPFDKPRRWINSGGAGTMGFGLPAAI--GVKFAHPeatVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 479 NNG--GVYRGDEATIFRSaapvwRHdpAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALA 543
Cdd:PRK06882 474 NNRflGMVKQWQDLIYSG-----RH--SQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFS 533
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
19-541 |
1.81e-42 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 160.92 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 19 VVDALKANDVDTIYGVVGIPITDLARAAQASG-IRYIGFRHEASAGNAAAAagFLTARPG---VCLTTSGPGFLNGLPAL 94
Cdd:PRK11269 10 AVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEG--YTRATAGnigVCIGTSGPAGTDMITGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 95 ANATTNCFPMIQISGSSsrPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGD 174
Cdd:PRK11269 88 YSASADSIPILCITGQA--PRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 175 VLGQAVEASAAsgaIWRPVdPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAK 254
Cdd:PRK11269 166 VQVAEIEFDPD---TYEPL-PVYKPAATRAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMGW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 255 GLLPDSHP--------QSAAAARSLAMARADVVLLVGARlnWllGN---GESPQWSADAKFIQVDIEASE----FDSNRP 319
Cdd:PRK11269 242 GAIPDDHPlmagmvglQTSHRYGNATLLASDFVLGIGNR--W--ANrhtGSVEVYTKGRKFVHVDIEPTQigrvFGPDLG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 320 IVapltGDIGSVMSALLEAAADRSSVAS----AAWTGELADRKARnsakMRRRLADDHHPM---RFY----NALGairsv 388
Cdd:PRK11269 318 IV----SDAKAALELLVEVAREWKAAGRlpdrSAWVADCQERKRT----LLRKTHFDNVPIkpqRVYeemnKAFG----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 389 lqrnPDVYVVnegaNALDL----ARNIIDMHLPRHRLDSGTWGVMGIGMGYAI-AAAVETGRPVVAIEGDSAFGFSGMEF 463
Cdd:PRK11269 385 ----RDTCYV----STIGLsqiaAAQFLHVYKPRHWINCGQAGPLGWTIPAALgVRAADPDRNVVALSGDYDFQFLIEEL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 464 ETICRYRLPVTVVILNNGgvYRGdeatIFRSAAPVWRHD----------PAPTVLNAHARHELIAEAFGGKGYHVSTPTE 533
Cdd:PRK11269 457 AVGAQFNLPYIHVLVNNA--YLG----LIRQAQRAFDMDycvqlafeniNSPELNGYGVDHVKVAEGLGCKAIRVFKPED 530
|
....*...
gi 489495942 534 LESALTDA 541
Cdd:PRK11269 531 IAPALEQA 538
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
19-582 |
4.81e-41 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 156.51 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 19 VVDALKANDVDTIYGvvgIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTA--RPGVCLTTSGPGFLNGLPALAN 96
Cdd:PRK06154 26 VAEILKEEGVELLFG---FPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAFGGVAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISGSSSRPMVDLQrgdyQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPGDVL 176
Cdd:PRK06154 103 AYGDSVPVLFLPTGYPRGSTDVA----PNFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVDVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 177 GQAVEASAASgaiWRPVdPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAKGL 256
Cdd:PRK06154 179 AEELDELPLD---HRPS-RRSRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNGKSA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 257 LPDSHP-------QSAAAARSLAMARADVVLLVGARLNWLLGNGESPqwsADAKFIQVDIEASEFDSNRPIVAPLTGDIG 329
Cdd:PRK06154 255 FPEDHPlalgsggRARPATVAHFLREADVLFGIGCSLTRSYYGLPMP---EGKTIIHSTLDDADLNKDYPIDHGLVGDAA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 330 SVMSALLEA--------AADRSSVAsaawtGELADRKARNSAKMRRRLADDHHPMRFYNalgairsvlqrnpdvyVVNEG 401
Cdd:PRK06154 332 LVLKQMIEElrrrvgpdRGRAQQVA-----AEIEAVRAAWLAKWMPKLTSDSTPINPYR----------------VVWEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 402 ANALDLARNII--DMHLPRHRL-------DSGT---WGV---MGIGMGYAIAAAVetGRP---VVAIEGDSAFGFSGMEF 463
Cdd:PRK06154 391 QHAVDIKTVIIthDAGSPRDQLspfyvasRPGSylgWGKttqLGYGLGLAMGAKL--ARPdalVINLWGDAAFGMTGMDF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 464 ETICRYRLPVTVVILNNGgvyrgdEATIFRSAAPVWRHDPAPTVLNAHarHELIAEAFGGKGYHVSTPTELESALTDALa 543
Cdd:PRK06154 469 ETAVRERIPILTILLNNF------SMGGYDKVMPVSTTKYRATDISGD--YAAIARALGGYGERVEDPEMLVPALLRAL- 539
|
570 580 590
....*....|....*....|....*....|....*....
gi 489495942 544 sngpslidceldpaDGVESGHLAKLNTTSAATPAISGDG 582
Cdd:PRK06154 540 --------------RKVKEGTPALLEVITSEETALSRPW 564
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
17-556 |
2.13e-40 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 154.77 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 17 HLVVDALKANDVDTIYGVVGipiTD-------LARAAQASGI--RYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGF 87
Cdd:PRK08327 11 ELFLELLKELGVDYIFINSG---TDyppiieaKARARAAGRPlpEFVICPHEIVAISMAHGYALVTGKPQAVMVHVDVGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 88 LNGLPALANATTNCFPMIQISGSSsrPMvdLQRGDY----------QD-LDQLNAARPFVKAAYRIGQVQDIGRGVARAI 156
Cdd:PRK08327 88 ANALGGVHNAARSRIPVLVFAGRS--PY--TEEGELgsrntrihwtQEmRDQGGLVREYVKWDYEIRRGDQIGEVVARAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 157 RTATSGRPGGVYLDIPGDVLGQAVEASAASGAIWRPVDPAPrllPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVI 236
Cdd:PRK08327 164 QIAMSEPKGPVYLTLPREVLAEEVPEVKADAGRQMAPAPPA---PDPEDIARAAEMLAAAERPVIITWRAGRTAEGFASL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 237 REFVEHTGIP---FLPMSMAkglLPDSHPQSAAAARSLAMARADVVLLVGARLNWLLGNGESPqwsADAKFIQVDIEASE 313
Cdd:PRK08327 241 RRLAEELAIPvveYAGEVVN---YPSDHPLHLGPDPRADLAEADLVLVVDSDVPWIPKKIRPD---ADARVIQIDVDPLK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 314 FDS---NRPIVAPLTGDIGSVMSALLEAAA------DRSSVASAAWTGEL--ADRKARNSAKMRRRLADDHHPmrfyNAL 382
Cdd:PRK08327 315 SRIplwGFPCDLCIQADTSTALDQLEERLKslasaeRRRARRRRAAVRELriRQEAAKRAEIERLKDRGPITP----AYL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 383 GAIRSVLQRNPDVYVVNEGANAldlarniidMHLPRHR----LDSGTWGVMGIGMGYAIAAAVETG-RPVVAIEGDSAFG 457
Cdd:PRK08327 391 SYCLGEVADEYDAIVTEYPFVP---------RQARLNKpgsyFGDGSAGGLGWALGAALGAKLATPdRLVIATVGDGSFI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 458 FSGME--FETICRYRLPVTVVILNNGGVYRGDEAT--IFRSAAPVWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTE 533
Cdd:PRK08327 462 FGVPEaaHWVAERYGLPVLVVVFNNGGWLAVKEAVleVYPEGYAARKGTFPGTDFDPRPDFAKIAEAFGGYGERVEDPEE 541
|
570 580
....*....|....*....|....*..
gi 489495942 534 LESALTDALA----SNGPSLIDCELDP 556
Cdd:PRK08327 542 LKGALRRALAavrkGRRSAVLDVIVDR 568
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
15-560 |
3.21e-40 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 154.58 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAA-QASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIYDELyKQDKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PRK06965 103 IATAYMDSIPMVVISGQVPTAAIGQDA--FQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAVEASAASGAIWRPVDPAPRllPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:PRK06965 181 DVSKTPCEYEYPKSVEMRSYNPVTK--GHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 KGLLPDSHPQ-------SAAAARSLAMARADVVLLVGARL-NWLLGNgesPQ--WSADAKFIQVDIEASEFDSNRPIVAP 323
Cdd:PRK06965 259 LGAYPASDKKflgmlgmHGTYEANMAMQHCDVLIAIGARFdDRVIGN---PAhfASRPRKIIHIDIDPSSISKRVKVDIP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 324 LTGDIGSVMSALL----EAAADRSSVASAAWTGELADRKARNSAKMRRRlADDHHPMRFYNALGAIrsvlqRNPDVYVVN 399
Cdd:PRK06965 336 IVGDVKEVLKELIeqlqTAEHGPDADALAQWWKQIEGWRSRDCLKYDRE-SEIIKPQYVVEKLWEL-----TDGDAFVCS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 400 EGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIaaAVETGRP---VVAIEGDSAFGFSGMEFETICRYRLPVTVV 476
Cdd:PRK06965 410 DVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAM--GIKMAHPdddVVCITGEGSIQMCIQELSTCLQYDTPVKII 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 477 ILNNG--GVYRGDEATIFRSAAPVWRHDPAPTVLNaharhelIAEAFGGKGYHVSTPTELESALTDALA-SNGPSLIDCE 553
Cdd:PRK06965 488 SLNNRylGMVRQWQEIEYSKRYSHSYMDALPDFVK-------LAEAYGHVGMRIEKTSDVEPALREALRlKDRTVFLDFQ 560
|
....*..
gi 489495942 554 LDPADGV 560
Cdd:PRK06965 561 TDPTENV 567
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
18-556 |
5.73e-39 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 150.37 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITDLARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALANA 97
Cdd:PRK06457 7 VIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNGLYDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 98 TTNCFPMIQISGSSSrpmVDLQRGDYqdLDQLNAARPFVKAAY---RIGQVQDIGRGVARAIRTATSGRpGGVYLDIPGD 174
Cdd:PRK06457 87 KMDHAPVIALTGQVE---SDMIGHDY--FQEVNLTKLFDDVAVfnqILINPENAEYIIRRAIREAISKR-GVAHINLPVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 175 VLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRaldvlaqAQRPLLVLGKGAayAQADNVIREFVEHTGIPFLPMSMAK 254
Cdd:PRK06457 161 ILRKSSEYKGSKNTEVGKVKYSIDFSRAKELIKE-------SEKPVLLIGGGT--RGLGKEINRFAEKIGAPIIYTLNGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 255 GLLPDSHPQSA-------AAARSLAMARADVVLLVGARL---NWLlgngespqwSADAKFIQVDIEASEFDSNRPIVAPL 324
Cdd:PRK06457 232 GILPDLDPKVMggigllgTKPSIEAMDKADLLIMLGTSFpyvNFL---------NKSAKVIQVDIDNSNIGKRLDVDLSY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 325 TGDIGSVMSALLEAAADRssvasaaWTGELADRKARNSAKMRRRLADDHHPMRfYNALGAIRSVLQRNPDVYVVNEGANA 404
Cdd:PRK06457 303 PIPVAEFLNIDIEEKSDK-------FYEELKGKKEDWLDSISKQENSLDKPMK-PQRVAYIVSQKCKKDAVIVTDTGNVT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 405 LDLARNiIDMHLPRHRLDSGTWGVMGIGMGYAIAA--AVETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNG- 481
Cdd:PRK06457 375 MWTARH-FRASGEQTFIFSAWLGSMGIGVPGSVGAsfAVENKRQVISFVGDGGFTMTMMELITAKKYDLPVKIIIYNNSk 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 482 -GVYRGDEATIfrsAAPVWRHDpaptVLNAH-ARhelIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDP 556
Cdd:PRK06457 454 lGMIKFEQEVM---GYPEWGVD----LYNPDfTK---IAESIGFKGFRLEEPKEAEEIIEEFLNTKGPAVLDAIVDP 520
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
15-543 |
1.12e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 150.00 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQA-SGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK07979 6 GAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRgdYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PRK07979 86 IATAYMDSIPLVVLSGQVATSLIGYDA--FQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAVEASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:PRK07979 164 DILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSSLMG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 KGLLPDSHPQSA-------AAARSLAMARADVVLLVGARLNWLLGNGESpQWSADAKFIQVDIEASEFDSNRPIVAPLTG 326
Cdd:PRK07979 244 LGAFPATHRQSLgmlgmhgTYEANMTMHNADVIFAVGVRFDDRTTNNLA-KYCPNATVLHIDIDPTSISKTVTADIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 327 DIGSVMSALLEAAADRSSV----ASAAWTGELADRKARNSAKMRRRlADDHHPMrfynalgAIRSVLQR--NPDVYVVNE 400
Cdd:PRK07979 323 DARQVLEQMLELLSQESAHqpldEIRDWWQQIEQWRARQCLKYDTH-SEKIKPQ-------AVIETLWRltKGDAYVTSD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 401 GANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAaaVETGRP---VVAIEGDSAFGFSGMEFETICRYRLPVTVVI 477
Cdd:PRK07979 395 VGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALG--VKMALPeetVVCVTGDGSIQMNIQELSTALQYELPVLVLN 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489495942 478 LNNG--GVYRGDEATIFRSaapvwRHdpAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALA 543
Cdd:PRK07979 473 LNNRylGMVKQWQDMIYSG-----RH--SQSYMQSLPDFVRLAEAYGHVGIQISHPDELESKLSEALE 533
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
12-560 |
2.82e-38 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 148.74 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 12 LTDGCHLVVDALKANDVDTIYGVVGIPITDLARAA-QASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNG 90
Cdd:PRK06466 3 LLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALfKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGATNA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 91 LPALANATTNCFPMIQISGSSSRPMVdlqrGD--YQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVY 168
Cdd:PRK06466 83 ITGIATAYMDSIPMVVLSGQVPSTLI----GEdaFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 169 LDIPGDVLG--QAVEASAASGAIWRPVDPAPRllPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIP 246
Cdd:PRK06466 159 VDIPKDMTNpaEKFEYEYPKKVKLRSYSPAVR--GHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 247 FLPMSMAKGLLPDSHPQSA-------AAARSLAMARADVVLLVGARLNWLLGNGESpQWSADAKFIQVDIEASEFDSNRP 319
Cdd:PRK06466 237 VTNTLMGLGGFPGTDRQFLgmlgmhgTYEANMAMHHADVILAVGARFDDRVTNGPA-KFCPNAKIIHIDIDPASISKTIK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 320 IVAPLTGDIGSVMSALLEAAADRSSV----ASAAWTGELADRKARNSakMRRRLADDHHPMRFYNALGAIRSVlqRNPDV 395
Cdd:PRK06466 316 ADIPIVGPVESVLTEMLAILKEIGEKpdkeALAAWWKQIDEWRGRHG--LFPYDKGDGGIIKPQQVVETLYEV--TNGDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 396 YVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVT 474
Cdd:PRK06466 392 YVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLaFPDQDVACVTGEGSIQMNIQELSTCLQYGLPVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 475 VVILNNG--GVYRGDEATIFRSaapvwRHdpAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALA-SNGPSLID 551
Cdd:PRK06466 472 IINLNNGalGMVRQWQDMQYEG-----RH--SHSYMESLPDFVKLAEAYGHVGIRITDLKDLKPKLEEAFAmKDRLVFID 544
|
....*....
gi 489495942 552 CELDPADGV 560
Cdd:PRK06466 545 IYVDRSEHV 553
|
|
| pyruv_oxi_spxB |
TIGR02720 |
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an ... |
19-565 |
6.11e-36 |
|
pyruvate oxidase; Members of this family are examples of pyruvate oxidase (EC 1.2.3.3), an enzyme with FAD and TPP as cofactors that catalyzes the reaction pyruvate + phosphate + O2 + H2O = acetyl phosphate + CO2 + H2O2. It should not be confused with pyruvate dehydrogenase [cytochrome] (EC 1.2.2.2) as in E. coli PoxB, although the E. coli enzyme is closely homologous and has pyruvate oxidase as an alternate name. [Energy metabolism, Aerobic]
Pssm-ID: 213733 [Multi-domain] Cd Length: 575 Bit Score: 141.90 E-value: 6.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 19 VVDALKANDVDTIYGVVGIPITDL--ARAAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:TIGR02720 5 VLKVLEAWGVDHIYGIPGGSFNSTmdALSAERDRIHYIQVRHEEVGALAAAADAKLTGKIGVCFGSAGPGATHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISGssSRPMVDLQRGDYQDLDQ---LNAARPFVKAAYRIGQVQDIgrgVARAIRTATSgRPGGVYLDIPG 173
Cdd:TIGR02720 85 AKEDHVPVLALVG--QVPTTGMNMDTFQEMNEnpiYADVAVYNRTAMTAESLPHV---IDEAIRRAYA-HNGVAVVTIPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVLGQAVEASAASGAiwrPVDPAPRLLPAP--EAIDRALDVLAQAQRPLLVLGKGAayAQADNVIREFVEHTGIPFLPMS 251
Cdd:TIGR02720 159 DFGWQEIPDNDYYAS---SVSYQTPLLPAPdvEAVTRAVQTLKAAERPVIYYGIGA--RKAGEELEALSEKLKIPLISTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 252 MAKGLLPDSHP-------QSAAAARSLAMARADVVLLVGARLNWllgnGESPQWSADAK-FIQVDIEASEFDSNRPIVAP 323
Cdd:TIGR02720 234 LAKGIIEDRYPaylgsayRVAQKPANEALFQADLVLFVGNNYPF----AEVSKAFKNTKyFIQIDIDPAKLGKRHHTDIA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 324 LTGDIGSVMSALLEAAADRSSvaSAAWTGELADRKarNSAKMRRRLADDHH-PMRFYNALGAIRSVLQRNPdVYVVNEGA 402
Cdd:TIGR02720 310 VLADAKKALAAILAQVEPRES--TPWWQANVANVK--NWRAYLASLEDKTEgPLQAYQVYRAINKIAEDDA-IYSIDVGD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 403 NALDLARnIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVE-TGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNN- 480
Cdd:TIGR02720 385 ININSNR-HLKMTPKNKWITSNLFATMGVGVPGAIAAKLNyPDRQVFNLAGDGAFSMTMQDLLTQVQYHLPVINIVFSNc 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 481 --GGVYRGDEATifrsaapvwrHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDA--LASNGPSLIDCELDP 556
Cdd:TIGR02720 464 tyGFIKDEQEDT----------NQPLIGVDFNDADFAKIAEGVGAVGFRVNKIEQLPAVFEQAkaIKQGKPVLIDAKITG 533
|
....*....
gi 489495942 557 ADGVESGHL 565
Cdd:TIGR02720 534 DRPLPVEKL 542
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
206-335 |
5.55e-34 |
|
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: 125.75 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 206 IDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAKGLLPDSHPQSAAAARSLAMARA-------DV 278
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLGMLGMHGTPAAnealeeaDL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 279 VLLVGARLNWLLGNGESPQWSADAKFIQVDIEASEFDSNRPIVAPLTGDIGSVMSAL 335
Cdd:pfam00205 81 VLAVGARFDDIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
1-555 |
9.88e-34 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 135.08 E-value: 9.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 1 MTTRSASPCTVLtdgcHLVVDALKANDVDTIYGVVGIpiTDLAR-AAQASGIRYIGFRHEASAGNAAAAAGFLTARPGVC 79
Cdd:PRK07092 4 ATAPAAAMTTVR----DATIDLLRRFGITTVFGNPGS--TELPFlRDFPDDFRYVLGLQEAVVVGMADGYAQATGNAAFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 80 LTTSGPGFLNGLPALANATTNCFPMIQISGSSSRPMVDLQrgdyQDLDQLNAA---RPFVKAAYRIGQVQDIGRGVARAI 156
Cdd:PRK07092 78 NLHSAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFE----PFLAAVQAAelpKPYVKWSIEPARAEDVPAAIARAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 157 RTATSGRPGGVYLDIPGDVLGQAVEASAAsgaiwRPVDPAPRllPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVI 236
Cdd:PRK07092 154 HIAMQPPRGPVFVSIPYDDWDQPAEPLPA-----RTVSSAVR--PDPAALARLGDALDAARRPALVVGPAVDRAGAWDDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 237 REFVEHTGIPFL--PMSmAKGLLPDSHPQ------SAAAARSLAMARADVVLLVGARLNWLLGNGESPQWSADAKFIQVD 308
Cdd:PRK07092 227 VRLAERHRAPVWvaPMS-GRCSFPEDHPLfagflpASREKISALLDGHDLVLVIGAPVFTYHVEGPGPHLPEGAELVQLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 309 IEASEfDSNRPIVAPLTGDIGSVMSALLEAAADrssvasaawtgelADRKARNSAKMRRRLADDHHPMRFYNALGAIRSV 388
Cdd:PRK07092 306 DDPGE-AAWAPMGDAIVGDIRLALRDLLALLPP-------------SARPAPPARPMPPPAPAPGEPLSVAFVLQTLAAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 389 lqRNPDVYVVNEGANAldlaRNIIDMHLPRHRLDSGTWGVMGiGMGYAIAAAV-----ETGRPVVAIEGDSAFGFSGMEF 463
Cdd:PRK07092 372 --RPADAIVVEEAPST----RPAMQEHLPMRRQGSFYTMASG-GLGYGLPAAVgvalaQPGRRVIGLIGDGSAMYSIQAL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 464 ETICRYRLPVTVVILNNGGvYrgdEAtiFRSAAPVWRHDPAPTVlnaharhEL-------IAEAFGGKGYHVSTPTELES 536
Cdd:PRK07092 445 WSAAQLKLPVTFVILNNGR-Y---GA--LRWFAPVFGVRDVPGL-------DLpgldfvaLARGYGCEAVRVSDAAELAD 511
|
570
....*....|....*....
gi 489495942 537 ALTDALASNGPSLIDCELD 555
Cdd:PRK07092 512 ALARALAADGPVLVEVEVA 530
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
77-558 |
3.66e-33 |
|
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: 133.36 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 77 GVCLTTSGPGFLNGLPALANATTNCFPMIQISGSssrPMVDLQR-----------GDYQDldQLNAARPFVKAAYRIgQV 145
Cdd:COG3961 69 GALVTTYGVGELSAINGIAGAYAERVPVVHIVGA---PGTRAQRrgpllhhtlgdGDFDH--FLRMFEEVTVAQAVL-TP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 146 QDIGRGVARAIRTA-TSGRPggVYLDIPGDVLGQAVEasaasgaiwRPVDPAPRLLPAP------EAIDRALDVLAQAQR 218
Cdd:COG3961 143 ENAAAEIDRVLAAAlREKRP--VYIELPRDVADAPIE---------PPEAPLPLPPPASdpaalaAAVAAAAERLAKAKR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 219 PLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAKGLLPDSHPQ--------SAAAARSLAMARADVVLLVGARLN-WL 289
Cdd:COG3961 212 PVILAGVEVHRFGLQEELLALAEKTGIPVATTLLGKSVLDESHPQfigtyagaASSPEVREYVENADCVLCLGVVFTdTN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 290 LGNgespqWSAD---AKFIQVDIEASEFDSNrpIVAPLTgdIGSVMSALLEAAADRSSVASAAwTGELADRKARNSAKMR 366
Cdd:COG3961 292 TGG-----FTAQldpERTIDIQPDSVRVGGH--IYPGVS--LADFLEALAELLKKRSAPLPAP-APPPPPPPAAPDAPLT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 367 RRladdhhpmRFYNalgAIRSVLQRNpDVYVVNEGanalDLARNIIDMHLPRH-RLDSGT-WGvmgiGMGYAIAAA--VE 442
Cdd:COG3961 362 QD--------RLWQ---RLQAFLDPG-DIVVADTG----TSLFGAADLRLPEGaTFIAQPlWG----SIGYTLPAAlgAA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 443 TGRP---VVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGGvYrgdeaTIFRsaapvWRHDPAPTVLNAHA-RHELIA 518
Cdd:COG3961 422 LAAPdrrVILLVGDGAFQLTAQELSTMLRYGLKPIIFVLNNDG-Y-----TIER-----AIHGPDGPYNDIANwDYAKLP 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 489495942 519 EAFGGK---GYHVSTPTELESALTDALA-SNGPSLIDCELDPAD 558
Cdd:COG3961 491 EAFGGGnalGFRVTTEGELEEALAAAEAnTDRLTLIEVVLDKMD 534
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
401-552 |
6.91e-32 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 120.38 E-value: 6.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 401 GANALDLARNIiDMHLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILN 479
Cdd:pfam02775 3 GCHQMWAAQYY-RFRPPRRYLTSGGLGTMGYGLPAAIGAKLaRPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 480 NG--GVYRG--DEATIFRSAAPVWRHDPAPtvlnahaRHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDC 552
Cdd:pfam02775 82 NGgyGMTRGqqTPFGGGRYSGPSGKILPPV-------DFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
377-552 |
3.13e-30 |
|
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: 116.20 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 377 RFYNALGAIRsvlqrNPDVYVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAAAVET-GRPVVAIEGDSA 455
Cdd:cd00568 1 RVLAALRAAL-----PEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAApDRPVVCIAGDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 456 FGFSGMEFETICRYRLPVTVVILNNG--GVYRGDEATIFRSAAPVWRHDPAPtvlnaharHELIAEAFGGKGYHVSTPTE 533
Cdd:cd00568 76 FMMTGQELATAVRYGLPVIVVVFNNGgyGTIRMHQEAFYGGRVSGTDLSNPD--------FAALAEAYGAKGVRVEDPED 147
|
170
....*....|....*....
gi 489495942 534 LESALTDALASNGPSLIDC 552
Cdd:cd00568 148 LEAALAEALAAGGPALIEV 166
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
20-556 |
2.40e-28 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 119.32 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 20 VDALKANDVDTIYGVVGI---PITDLARaaQASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:PRK06546 10 VEQLVAAGVKRIYGIVGDslnPIVDAVR--RTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISgsSSRPMVDLQRGDYQDL--DQLnaarpFVKAAY---RIGQVQDIGRGVARAIRTATsGRPGGVYLDI 171
Cdd:PRK06546 88 AHRSGAPVLAIA--SHIPSAQIGSGFFQEThpDRL-----FVECSGyceMVSSAEQAPRVLHSAIQHAV-AGGGVSVVTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 172 PGDVLGQAVEASAASGAIwrpVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADnvIREFVEHTGIPF---- 247
Cdd:PRK06546 160 PGDIADEPAPEGFAPSVI---SPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHAE--VLALAEKIKAPVghsl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 248 -------------LPMSmakGLLpdshpqsAAAARSLAMARADVVLLVGARLNWllgngesPQWSADAKFIQVDIEASEF 314
Cdd:PRK06546 235 rgkewiqydnpfdVGMS---GLL-------GYGAAHEAMHEADLLILLGTDFPY-------DQFLPDVRTAQVDIDPEHL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 315 DSNRPIVAPLTGDIGSVMSALL---EAAADRSSVASAAwtgELADRKARNSAKMRRRLADDH---HPMrfYNAlgairSV 388
Cdd:PRK06546 298 GRRTRVDLAVHGDVAETIRALLplvKEKTDRRFLDRML---KKHARKLEKVVGAYTRKVEKHtpiHPE--YVA-----SI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 389 LQRNPD---VYVVNEGANALDLARNIidMHLPRHR-LDSGTWGVMGIGMGYAI-AAAVETGRPVVAIEGDSAFGFSGMEF 463
Cdd:PRK06546 368 LDELAAddaVFTVDTGMCNVWAARYI--TPNGRRRvIGSFRHGSMANALPHAIgAQLADPGRQVISMSGDGGLSMLLGEL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 464 ETICRYRLPVTVVILNN---GGVyrgdEATIFRSAAPVWRHDpaptvlNAHARHELIAEAFGGKGYHVSTPTELESALTD 540
Cdd:PRK06546 446 LTVKLYDLPVKVVVFNNstlGMV----KLEMLVDGLPDFGTD------HPPVDYAAIAAALGIHAVRVEDPKDVRGALRE 515
|
570
....*....|....*.
gi 489495942 541 ALASNGPSLIDCELDP 556
Cdd:PRK06546 516 AFAHPGPALVDVVTDP 531
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
18-557 |
1.77e-25 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 110.77 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITD----LARAAQasGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPG---FLNG 90
Cdd:PRK08273 8 FILERLREWGVRRVFGYPGDGINGllgaLGRADD--KPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGaihLLNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 91 lpaLANATTNCFPMIQISGSSSRPMVDlqrGDYQ---DLDQL--NAARPFVKAAYRIGQVQDIgrgVARAIRTATSGRpG 165
Cdd:PRK08273 86 ---LYDAKLDHVPVVAIVGQQARAALG---GHYQqevDLQSLfkDVAGAFVQMVTVPEQLRHL---VDRAVRTALAER-T 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 166 GVYLDIPGDVLGQAVEA------SAASGAIWRPvdpaPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADnvIREF 239
Cdd:PRK08273 156 VTAVILPNDVQELEYEPpphahgTVHSGVGYTR----PRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATDE--VIAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 240 VEHTGIPFLPMSMAKGLLPDSHPQSAAAarslamaradvVLLVGARLNW--------LLGNGESPQWS------ADAKFI 305
Cdd:PRK08273 230 AERLGAGVAKALLGKAALPDDLPWVTGS-----------IGLLGTKPSYelmrecdtLLMVGSSFPYSeflpkeGQARGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 306 QVDIEASEFdSNR-PIVAPLTGDIGSVMSAL---LEAAADRSsvasaaWTGELADRKARNSAKMRRRL---ADDHHPMRF 378
Cdd:PRK08273 299 QIDIDGRML-GLRyPMEVNLVGDAAETLRALlplLERKKDRS------WRERIEKWVARWWETLEARAmvpADPVNPQRV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 379 YNALGAirsvlqRNPDVYVV--NEGANALDLARNII---DM--HLprhrldSGTWGVMGIGMGYAIAAA-VETGRPVVAI 450
Cdd:PRK08273 372 FWELSP------RLPDNAILtaDSGSCANWYARDLRmrrGMmaSL------SGTLATMGPAVPYAIAAKfAHPDRPVIAL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 451 EGDSAFGFSGM-EFETICRYR-----LPVTVVILNNGG---------VYRGDeaTIFRSAAPVwrhdpaPTVlnAHARHe 515
Cdd:PRK08273 440 VGDGAMQMNGMaELITVAKYWrqwsdPRLIVLVLNNRDlnqvtweqrVMEGD--PKFEASQDL------PDV--PYARF- 508
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 489495942 516 liAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPA 557
Cdd:PRK08273 509 --AELLGLKGIRVDDPEQLGAAWDEALAADRPVVLEVKTDPN 548
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
18-551 |
7.42e-25 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 108.92 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITDLARAAQASG-IRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:PRK09124 8 YIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISgsSSRPMVDLQRGDYQDLDQLNAAR------PFVKAAYRIGQVqdigrgVARAIRTATSGRpGGVYLD 170
Cdd:PRK09124 88 CHRNHVPVLAIA--AHIPSSEIGSGYFQETHPQELFRecshycELVSNPEQLPRV------LAIAMRKAILNR-GVAVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 171 IPGDVLGQAVEASAAsgAIWrPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVI-------------- 236
Cdd:PRK09124 159 LPGDVALKPAPERAT--PHW-YHAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHDELVAlaetlkapivhalr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 237 -REFVEHTGiPF-LPMSmakGLLPDShpqsaaaARSLAMARADVVLLVGARLNWllgngeSPQWSADAKFIQVDIEASEF 314
Cdd:PRK09124 236 gKEHVEYDN-PYdVGMT---GLIGFS-------SGYHAMMNCDTLLMLGTDFPY------RQFYPTDAKIIQIDINPGSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 315 DSNRPIVAPLTGDIGSVMSAL---LEAAADRSSVasaawtgelaDRKARNSAKMRRRL------ADDHHPMRfYNALGAI 385
Cdd:PRK09124 299 GRRSPVDLGLVGDVKATLAALlplLEEKTDRKFL----------DKALEHYRKARKGLddlavpSDGGKPIH-PQYLARQ 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 386 RSVLQRNPDVYVVNEGANALDLARnIIDMHLPRHRLDSGTWGVMGIGMGYAIAA-AVETGRPVVAIEGDSAFGFSGMEFE 464
Cdd:PRK09124 368 ISEFAADDAIFTCDVGTPTVWAAR-YLKMNGKRRLLGSFNHGSMANAMPQALGAqAAHPGRQVVALSGDGGFSMLMGDFL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 465 TICRYRLPVTVVILNNGGVyrGDEATIFRSAAPV-WRHDPAPTVLNAharhelIAEAFGGKGYHVSTPTELESALTDALA 543
Cdd:PRK09124 447 SLVQLKLPVKIVVFNNSVL--GFVAMEMKAGGYLtDGTDLHNPDFAA------IAEACGITGIRVEKASELDGALQRAFA 518
|
....*...
gi 489495942 544 SNGPSLID 551
Cdd:PRK09124 519 HDGPALVD 526
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
374-556 |
9.10e-25 |
|
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: 101.45 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 374 HPMRFYNALGairsvlQRNPD--VYVVNEGANALDLARNIiDMHLPRHRLDSGTWGVMGIGMGYAIAA-AVETGRPVVAI 450
Cdd:cd02014 3 HPERVAAELN------KRAPDdaIFTIDVGNVTVWAARHL-RMNGKQRFILSGLLATMGNGLPGAIAAkLAYPDRQVIAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 451 EGDSAFGFSGMEFETICRYRLPVTVVILNN---GGVYRGDEATifrsAAPVW---RHDPaptvlnAHARhelIAEAFGGK 524
Cdd:cd02014 76 SGDGGFAMLMGDLITAVKYNLPVIVVVFNNsdlGFIKWEQEVM----GQPEFgvdLPNP------DFAK---IAEAMGIK 142
|
170 180 190
....*....|....*....|....*....|..
gi 489495942 525 GYHVSTPTELESALTDALASNGPSLIDCELDP 556
Cdd:cd02014 143 GIRVEDPDELEAALDEALAADGPVVIDVVTDP 174
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
417-560 |
8.55e-24 |
|
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: 98.72 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 417 PRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNG--GVYRGDEaTIFr 493
Cdd:cd02015 40 PRSWLTSGGLGTMGFGLPAAIGAKVaRPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNGslGMVRQWQ-ELF- 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 494 saapvWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPADGV 560
Cdd:cd02015 118 -----YEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEALASDGPVLLDVLVDPEENV 179
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
384-558 |
4.61e-20 |
|
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: 87.73 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 384 AIRSVLQRNpDVYVVNEGANALDLARNIiDMHLPRHRLDSGTWGVMGIGMGYAIAAA-VETGRPVVAIEGDSAFGFSGME 462
Cdd:cd02010 7 DLRAVMGDD-DIVLLDVGAHKIWMARYY-RTYAPNTCLISNGLATMGVALPGAIGAKlVYPDRKVVAVSGDGGFMMNSQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 463 FETICRYRLPVTVVILNNGG---VYRGDEATIFRSAAPvwrhDPAPTVLNAHarheliAEAFGGKGYHVSTPTELESALT 539
Cdd:cd02010 85 LETAVRLKIPLVVLIWNDNGyglIKWKQEKEYGRDSGV----DFGNPDFVKY------AESFGAKGYRIESADDLLPVLE 154
|
170
....*....|....*....
gi 489495942 540 DALASNGPSLIDCELDPAD 558
Cdd:cd02010 155 RALAADGVHVIDCPVDYSE 173
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
394-554 |
4.37e-19 |
|
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: 84.95 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 394 DVYVVNEGANALDLARNIIDMHLPrHRLDSGTWGVMGIGMGYAIAAAVET-GRPVVAIEGDSAFGFSGMEFETICRYRLP 472
Cdd:cd02002 17 DAIIVDEAVTNGLPLRDQLPLTRP-GSYFTLRGGGLGWGLPAAVGAALANpDRKVVAIIGDGSFMYTIQALWTAARYGLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 473 VTVVILNNGGvYR--GDEATIFRSAAPVWRHDPAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLI 550
Cdd:cd02002 96 VTVVILNNRG-YGalRSFLKRVGPEGPGENAPDGLDLLDPGIDFAAIAKAFGVEAERVETPEELDEALREALAEGGPALI 174
|
....
gi 489495942 551 DCEL 554
Cdd:cd02002 175 EVVV 178
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
18-175 |
6.25e-18 |
|
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: 81.44 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITDLARAAQ-ASGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPALAN 96
Cdd:cd07039 5 VIVETLENWGVKRVYGIPGDSINGLMDALRrEGKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGLYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 97 ATTNCFPMIQISGssSRPMVDLQRGDYQDLDQLNAARP---FVKAAYRIGQVQDIgrgVARAIRTATSGRpgGV-YLDIP 172
Cdd:cd07039 85 AKRDRAPVLAIAG--QVPTDELGTDYFQEVDLLALFKDvavYNETVTSPEQLPEL---LDRAIRTAIAKR--GVaVLILP 157
|
...
gi 489495942 173 GDV 175
Cdd:cd07039 158 GDV 160
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
15-551 |
2.67e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 81.84 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 15 GCHLVVDALKANDVDTIYGVVGIPITDLARAAQA-SGIRYIGFRHEASAGNAAAAAGFLTARPGVCLTTSGPGFLNGLPA 93
Cdd:PRK12474 7 GADSVVDTLLNCGVEVCFANPGTSEMHFVAALDRvPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLANGLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 94 LANATTNCFPMIQISGSSSRPMVDLQRGDYQDLDQLnaARPFVKAAYRIGQVQDIGRGVARAIRTATSGRPGGVYLDIPG 173
Cdd:PRK12474 87 LHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGF--ARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLIMPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 174 DVlgqAVEASAASGAIWRPVDPAPRllpAPEAIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMA 253
Cdd:PRK12474 165 DV---AWNEAAYAAQPLRGIGPAPV---AAETVERIAALLRNGKKSALLLRGSALRGAPLEAAGRIQAKTGVRLYCDTFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 254 ------KGLLPDSHPQSAAAARSLAMARADVVLLVGAR--LNWLLGNGEsPQWSADAkfiqvdieasefdsnrpivaplt 325
Cdd:PRK12474 239 priergAGRVPIERIPYFHEQITAFLKDVEQLVLVGAKppVSFFAYPGK-PSWGAPP----------------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 326 gdiGSVMSALleAAADRSSVASAAWtgeLADR-KARNSAKMRRRLADDHHPMRFYNALGAIRSVLQRNPDVYVVNEGANA 404
Cdd:PRK12474 295 ---GCEIVYL--AQPDEDLAQALQD---LADAvDAPAEPAARTPLALPALPKGALNSLGVAQLIAHRTPDQAIYADEALT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 405 LDLArniIDMHLPRHRLDSG---TWGVMGIGMGYAIAAAVET-GRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNN 480
Cdd:PRK12474 367 SGLF---FDMSYDRARPHTHlplTGGSIGQGLPLAAGAAVAApDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFAN 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 481 GGVyrgdeATIFRSAAPVWRHDPAPTVLNAHARH--EL----IAEAFGGKGYHVSTPTELESALTDALASNGPSLID 551
Cdd:PRK12474 444 RSY-----AILNGELQRVGAQGAGRNALSMLDLHnpELnwmkIAEGLGVEASRATTAEEFSAQYAAAMAQRGPRLIE 515
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
423-558 |
3.07e-16 |
|
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: 76.80 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 423 SGTWGVMGIGMGYAI--AAAVETGRpVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGG-----VYRGDEAT---If 492
Cdd:cd02005 46 QPLWGSIGYSVPAALgaALAAPDRR-VILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGytierAIHGPEASyndI- 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 493 rsaaPVWRHDPAPTVLNAHARheliaeafgGKGYHVSTPTELESALTDALA-SNGPSLIDCELDPAD 558
Cdd:cd02005 124 ----ANWNYTKLPEVFGGGGG---------GLSFRVKTEGELDEALKDALFnRDKLSLIEVILPKDD 177
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
374-543 |
3.88e-14 |
|
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: 71.39 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 374 HPMRfynALGAIRSVLQRnpDVYVVNEGANALDLARNIIDMHLPRHRLDSGTWGVMGIGMGYAIAA-AVETGRPVVAIEG 452
Cdd:cd02013 5 HPRQ---VLRELEKAMPE--DAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAkAAAPDRPVVAIAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 453 DSAFGFSGMEFETICRYRLPVTVVILNNggvyrgdeatifrsaaPVWRHDPAPTVLNAHARH---EL-------IAEAFG 522
Cdd:cd02013 80 DGAWGMSMMEIMTAVRHKLPVTAVVFRN----------------RQWGAEKKNQVDFYNNRFvgtELesesfakIAEACG 143
|
170 180
....*....|....*....|.
gi 489495942 523 GKGYHVSTPTELESALTDALA 543
Cdd:cd02013 144 AKGITVDKPEDVGPALQKAIA 164
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
72-551 |
5.93e-12 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 68.33 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 72 LTARPGVCLTTSGPGFLNGLPALANATTNCFPMIQISGSSSRPMVDLQRGDYQDLDQLnaARPFVKAAYRIGQVQDIGRG 151
Cdd:PRK07586 61 MAGKPAATLLHLGPGLANGLANLHNARRARTPIVNIVGDHATYHRKYDAPLTSDIEAL--ARPVSGWVRRSESAADVAAD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 152 VARAIRTATSGrPGGVYLDI-PGDVlgqaveASAASGAIWRPVDPAPRLLPAPEAIDRALDVLAQAQRPLLVLGKGAAYA 230
Cdd:PRK07586 139 AAAAVAAARGA-PGQVATLIlPADV------AWSEGGPPAPPPPAPAPAAVDPAAVEAAAAALRSGEPTVLLLGGRALRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 231 QADNVIREFVEHTGI----PFLPMSMAKG--LLPDSHPQSAAAARSLAMARADVVLLVGARlnwllgngeSPQwsadAKF 304
Cdd:PRK07586 212 RGLAAAARIAAATGArllaETFPARMERGagRPAVERLPYFAEQALAQLAGVRHLVLVGAK---------APV----AFF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 305 IQVDIeasefdsnRPIVAPLTGDIgsvmsALLEAAADRSSVASAAWTGELADRKARNSAKMRRRLADDHHPMRFYNALGA 384
Cdd:PRK07586 279 AYPGK--------PSRLVPEGCEV-----HTLAGPGEDAAAALEALADALGAKPAAPPLAAPARPPLPTGALTPEAIAQV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 385 IRSVLQRNpdVYVVNEGANAldlARNIIDM--HLPRHRLDSGTWGVMGIGMGYAIAAAV-ETGRPVVAIEGDSAFGFSGM 461
Cdd:PRK07586 346 IAALLPEN--AIVVDESITS---GRGFFPAtaGAAPHDWLTLTGGAIGQGLPLATGAAVaCPDRKVLALQGDGSAMYTIQ 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 462 EFETICRYRLPVTVVILNNGGvYRGDEATIFRSAAPVwrhdPAPtvlnaHARHEL-----------IAEAFGGKGYHVST 530
Cdd:PRK07586 421 ALWTQARENLDVTTVIFANRA-YAILRGELARVGAGN----PGP-----RALDMLdlddpdldwvaLAEGMGVPARRVTT 490
|
490 500
....*....|....*....|.
gi 489495942 531 PTELESALTDALASNGPSLID 551
Cdd:PRK07586 491 AEEFADALAAALAEPGPHLIE 511
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
433-557 |
9.17e-10 |
|
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: 58.47 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 433 MGYAIAAAVET-----GRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGG---VYRGDEATIFRSAAPVWRH--- 501
Cdd:cd02003 50 MGYEIAAGLGAklakpDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGfgcINNLQESTGSGSFGTEFRDrdq 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489495942 502 -------DPAPTVLNAHARheliaeAFGGKGYHVSTPTELESALTDALASNGPSLIDCELDPA 557
Cdd:cd02003 130 esgqldgALLPVDFAANAR------SLGARVEKVKTIEELKAALAKAKASDRTTVIVIKTDPK 186
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
18-173 |
2.95e-09 |
|
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: 56.20 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 18 LVVDALKANDVDTIYGVVGIPITDLARAAQA-SGIRYIGFRHEASAGNAAAAAGFLTARPgVCLTTSGPGFLNGLPALAN 96
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREgDKRIIDTVIHELGAAGAAAGYARAGGPP-VVIVTSGTGLLNAINGLAD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489495942 97 ATTNCFPMIQISGssSRPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQDIGRGVARAIRTATSGrPGGVYLDIPG 173
Cdd:cd06586 81 AAAEHLPVVFLIG--ARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
423-550 |
1.13e-07 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 51.83 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 423 SGTWGVMGIGMGYAIAaaveTGRPVVAIEGDSAF-----GFSGMEfeticRYRLPVTVVILNNGGvyrgdeATIFR---- 493
Cdd:cd02009 51 SGIDGTLSTALGIALA----TDKPTVLLTGDLSFlhdlnGLLLGK-----QEPLNLTIVVINNNG------GGIFSllpq 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489495942 494 --SAAPVWRHDPAPTVLNaharHELIAEAFGGKGYHVSTPTELESALTDALASNGPSLI 550
Cdd:cd02009 116 asFEDEFERLFGTPQGLD----FEHLAKAYGLEYRRVSSLDELEQALESALAQDGPHVI 170
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
205-482 |
5.34e-06 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 49.31 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 205 AIDRALDVLAQAQRPLLVLGKGAAYAQADNVIREFVEHTGIPFLPMSMAKGLLPDSHPQ--------SAAAARSLAMARA 276
Cdd:PLN02573 213 AVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPHfigtywgaVSTPFCAEIVESA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 277 DVVLLVGARLNWLLGNGESPQWSADaKFIQVdieasefDSNRPIVA--PLTGDIgsVMSALLEAaadrssvasaawtgeL 354
Cdd:PLN02573 293 DAYLFAGPIFNDYSSVGYSLLLKKE-KAIIV-------QPDRVTIGngPAFGCV--LMKDFLEA---------------L 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 355 ADRKARNSAKMR--RRL---------ADDHHPMRFYNALGAIRSVLqrNPDVYVVNEGAnalDLARNIIDMHLPRH---- 419
Cdd:PLN02573 348 AKRVKKNTTAYEnyKRIfvpegeplkSEPGEPLRVNVLFKHIQKML--SGDTAVIAETG---DSWFNCQKLKLPEGcgye 422
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489495942 420 ---RLDSGTWGVmGIGMGYAIAAAvetGRPVVAIEGDSAFGFSGMEFETICRYRLPVTVVILNNGG 482
Cdd:PLN02573 423 fqmQYGSIGWSV-GATLGYAQAAP---DKRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGG 484
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
393-541 |
1.00e-05 |
|
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.
Pssm-ID: 238964 [Multi-domain] Cd Length: 202 Bit Score: 46.89 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 393 PDV-YVVNEGANALDLARnIIDMHLPRHRLDSGTWGVMGIGMGYAIA-AAVETGRPVVAIEGDSAFGFSGMEFETICRYR 470
Cdd:cd02006 23 RDVrYVTTIGLSQIAGAQ-MLHVYKPRHWINCGQAGPLGWTVPAALGvAAADPDRQVVALSGDYDFQFMIEELAVGAQHR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 471 LPVTVVILNNGgvYRGdeatIFRSAAPVWRHD----------PAPTVLNAHARHELIAEAFGGKGYHVSTPTELESALTD 540
Cdd:cd02006 102 IPYIHVLVNNA--YLG----LIRQAQRAFDMDyqvnlafeniNSSELGGYGVDHVKVAEGLGCKAIRVTKPEELAAAFEQ 175
|
.
gi 489495942 541 A 541
Cdd:cd02006 176 A 176
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
384-550 |
1.40e-05 |
|
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: 46.15 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 384 AIRSVLQRNP--DVYVVNEGANALDLaRNIIDMHLPRHRLDSGTWGVMG----IGMGYAIAaavETGRPVVAIEGDSAFG 457
Cdd:cd03371 4 AIEIVLSRAPatAAVVSTTGMTSREL-FELRDRPGGGHAQDFLTVGSMGhasqIALGIALA---RPDRKVVCIDGDGAAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 458 FSGMEFETICRYRLPVTV-VILNNGGvyrgdeatifrsaapvwrHDPA---PTVlNAHARHELIAEAFG-GKGYHVSTPT 532
Cdd:cd03371 80 MHMGGLATIGGLAPANLIhIVLNNGA------------------HDSVggqPTV-SFDVSLPAIAKACGyRAVYEVPSLE 140
|
170
....*....|....*...
gi 489495942 533 ELESALTDALASNGPSLI 550
Cdd:cd03371 141 ELVAALAKALAADGPAFI 158
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
20-172 |
1.38e-04 |
|
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: 42.48 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 20 VDALKANDVDTIYGVVG---IPITDLAraAQASGIRYIGFRHEasagnaaaaagfLTA-----------RPGVCLTTSGP 85
Cdd:cd07038 4 LERLKQLGVKHVFGVPGdynLPLLDAI--EENPGLRWVGNCNE------------LNAgyaadgyarvkGLGALVTTYGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 86 GFLNGLPALANATTNCFPMIQISGSSSRPMVD--------LQRGDYQdlDQLNAARPFVKAAYRIGQVQDIGRGVARAIR 157
Cdd:cd07038 70 GELSALNGIAGAYAEHVPVVHIVGAPSTKAQAsglllhhtLGDGDFD--VFLKMFEEITCAAARLTDPENAAEEIDRVLR 147
|
170
....*....|....*.
gi 489495942 158 TA-TSGRPggVYLDIP 172
Cdd:cd07038 148 TAlRESRP--VYIEIP 161
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
73-172 |
5.94e-04 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 40.56 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489495942 73 TARPGVCLTTSGPGFLNGLPALANATTNCFPMIQIsgSSSRPMVDLQRGDYQDLDQLNAARPFVKAAYRIGQVQD----- 147
Cdd:cd07037 58 SGRPVAVVCTSGTAVANLLPAVVEAYYSGVPLLVL--TADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDdddlw 135
|
90 100
....*....|....*....|....*.
gi 489495942 148 -IGRGVARAIRTATSGRPGGVYLDIP 172
Cdd:cd07037 136 yLLRLANRAVLEALSAPPGPVHLNLP 161
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
417-481 |
7.29e-03 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 37.64 E-value: 7.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489495942 417 PRHRLDSGTwgVMGIGMGYAIAAAVET-GRPVVAIEGDSAFGFSGME------FEticryRLPVTVVILNNG 481
Cdd:cd02008 43 PLNAIDTCT--CMGASIGVAIGMAKASeDKKVVAVIGDSTFFHSGILglinavYN-----KANITVVILDNR 107
|
|
| |
