|
Name |
Accession |
Description |
Interval |
E-value |
| oxalate_oxc |
TIGR03254 |
oxalyl-CoA decarboxylase; In a number of bacteria, including Oxalobacter formigenes from the ... |
6-559 |
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: 1025.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNG 85
Cdd:TIGR03254 1 ALTDGFHLVIDALKLNGINTIYGVVGIPVTDLARLAQAKGMRYIGFRHEQSAGYAAAAAGFLTQKPGVCLTVSAPGFLNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 86 LTALANATVNGFPMIMISGSSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLD 165
Cdd:TIGR03254 81 LTALANATTNCFPMIMISGSSERHIVDLQQGDYEEMDQLAAAKPFAKAAYRVLRAEDIGIGIARAIRTAVSGRPGGVYLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 166 LPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPM 245
Cdd:TIGR03254 161 LPAAVLGQTMEAEKAKKTLVKVVDPAPKQLPSPDSVDRAVELLKDAKRPLILLGKGAAYAQADEEIREFVEKTGIPFLPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 246 SMAKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGK-KGWAADTQFIQLDIEPQEIDSNRPIAVPVVGDIAS 324
Cdd:TIGR03254 241 SMAKGLLPDTHPQSAAAARSFALAEADVVMLVGARLNWLLSHGKgKLWGEDAKFIQVDIEPTEMDSNRPIAAPVVGDIGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 325 SMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARN 404
Cdd:TIGR03254 321 VVQALLSAAKNGGVKPPADWRNAIKTKSEKNVAKMAERLSASESPMNYHGALEAIRDVLKDNPDIYLVNEGANTLDLARN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 405 IIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGIYRGDGVD 484
Cdd:TIGR03254 401 VIDMYKPRHRLDVGTWGVMGIGMGYAIAAAVETGKPVVALEGDSAFGFSGMEVETICRYNLPVCVVIFNNGGIYRGDDVN 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130305 485 LSGAgAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESGHITKLNPK 559
Cdd:TIGR03254 481 VVGA-DPAPTVLVHGARYDKMMKAFGGVGYNVTTPDELKAALNEALASGKPTLINAVIDPSAGTESGHIGNLNPK 554
|
|
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
1-564 |
0e+00 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 1018.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 1 MSDQLQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAP 80
Cdd:PRK09259 3 MSDQLQLTDGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 81 GFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPG 160
Cdd:PRK09259 83 GFLNGLTALANATTNCFPMIMISGSSEREIVDLQQGDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 161 GVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQI 240
Cdd:PRK09259 163 GVYLDLPAKVLAQTMDADEALTSLVKVVDPAPAQLPAPEAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 241 PFLPMSMAKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGK-KGWAADTQFIQLDIEPQEIDSNRPIAVPVV 319
Cdd:PRK09259 243 PFLPMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKgKTWGADKKFIQIDIEPQEIDSNRPIAAPVV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 320 GDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTL 399
Cdd:PRK09259 323 GDIGSVMQALLAGLKQNTFKAPAEWLDALAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVLKENPDIYLVNEGANTL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 400 DNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGIYR 479
Cdd:PRK09259 403 DLARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAVETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNGGIYR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 480 GDGVDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESGHITKLNPK 559
Cdd:PRK09259 483 GDDVNLSGAGDPSPTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGKPTLINVVIDPAAGTESGHITNLNPK 562
|
....*
gi 16130305 560 QVAGN 564
Cdd:PRK09259 563 SVAGK 567
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
6-556 |
1.06e-138 |
|
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: 413.02 E-value: 1.06e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARH-AQAEGIRYIGFRHEQSAgyaaaasGF-------LTQKPGICLTV 77
Cdd:COG0028 1 MKMTGADALVEALEAEGVETVFGVPGGAILPLYDAlRRQSGIRHILVRHEQGA-------AFmadgyarATGKPGVCLVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 78 SAPGFLNGLTALANATVNGFPMIMISGSSDRAivDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSG 157
Cdd:COG0028 74 SGPGATNLVTGLADAYMDSVPVLAITGQVPTS--LIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 158 RPGGVYLDLPANVLAATMEKDEALttiVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIES 237
Cdd:COG0028 152 RPGPVVLDIPKDVQAAEAEEEPAP---PELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 238 AQIPFLPMSMAKGILEDTHP-------LSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDS 310
Cdd:COG0028 229 LGAPVVTTLMGKGAFPEDHPlylgmlgMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 311 NRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQnaqkmHEKLSTDTQPLNYFNALSAVRDVLREnqDIY 390
Cdd:COG0028 309 NYPVDLPIVGDAKAVLAALLEALEPRADDRAAWLARIAAWRAEY-----LAAYAADDGPIKPQRVIAALREALPD--DAI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 391 LVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLPVTI 469
Cdd:COG0028 382 VVTDVGQHQMWAARYLRFRRPRRFLTSGGLGTMGYGLPAAIGAKLArPDRPVVAITGDGGFQMNLQELATAVRYGLPVKV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 470 VIFNNG--GIYRgDGVDLSGAGAPSPTDlLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAG 547
Cdd:COG0028 462 VVLNNGglGMVR-QWQELFYGGRYSGTD-LPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDGPALIDVRVDPEEN 539
|
....*....
gi 16130305 548 TESGHITKL 556
Cdd:COG0028 540 PPGATLDEM 548
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
13-546 |
2.86e-76 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 251.18 E-value: 2.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 13 IIVEALKQNNIDTIYGVVG---IPVTDMARHaqaEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTAL 89
Cdd:PRK05858 10 LAARRLKAHGVDTMFTLSGghlFPLYDGARE---EGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 90 ANATVNGFPMIMISGssdRAiVDLQ--QGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLP 167
Cdd:PRK05858 87 AAAQFNQSPLVVLGG---RA-PALRwgMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 168 ANVLAATMEKDEalTTIVKVENPSpALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSM 247
Cdd:PRK05858 163 MDHAFSMADDDG--RPGALTELPA-GPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 248 AKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGwaADTQFIQLDIEPQEIDSNRPIAVPVVGDIASSMQ 327
Cdd:PRK05858 240 GRGVVPADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFGVFG--GTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 328 GMLAELKQNTFTTPlvWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRDVLreNQDIYLVNEGANTLDNARNIID 407
Cdd:PRK05858 318 ALAGAGGDRTDHQG--WIEELRTAETAARARDAAELADDRDPIHPMRVYGELAPLL--DRDAIVIGDGGDFVSYAGRYID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 408 MYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNG--GIYRGDGVD 484
Cdd:PRK05858 394 PYRPGCWLDPGPFGCLGTGPGYALAARLArPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGNNGiwGLEKHPMEA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130305 485 LSGAGAPSptDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAA 546
Cdd:PRK05858 474 LYGYDVAA--DLRPGTRYDEVVRALGGHGELVTVPAELGPALERAFASGVPYLVNVLTDPSV 533
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
372-543 |
1.70e-72 |
|
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: 228.96 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 372 YFNALSAVRDVLREnqDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASV-TSGSPVVAIEGDSAF 450
Cdd:cd02004 1 PYRVLHELQEALPD--DAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALaRPDKRVVLVEGDGAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 451 GFSGMEIETICRYNLPVTIVIFNNGGIYRGDGVD-LSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTG 529
Cdd:cd02004 79 GFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQqLSYGLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPEELKPALKRA 158
|
170
....*....|....
gi 16130305 530 IQSRKPTIINVVID 543
Cdd:cd02004 159 LASGKPALINVIID 172
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
6-540 |
1.78e-65 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 222.58 E-value: 1.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTDGmHIIVEALKQNNIDTIYGVVGIPVTDM--ARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFL 83
Cdd:PRK08266 3 TMTGG-EAIVAGLVAHGVDTVFGLPGAQLYWLfdALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 84 NGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEEL-DQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGV 162
Cdd:PRK08266 82 NAGAALLTAYGCNSPVLCLTGQIPSALIGKGRGHLHEMpDQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 163 YLDLPANVLAATMEKDEALTTivkveNPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAysQADEQLREFIESAQIPF 242
Cdd:PRK08266 162 ALEMPWDVFGQRAPVAAAPPL-----RPAPPPAPDPDAIAAAAALIAAAKNPMIFVGGGAA--GAGEEIRELAEMLQAPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 243 LPMSMAKGILEDTHPLSAAAARSFAL-ANADVVMLVGARLnwLLAHGKKGWAADTQ-FIQLDIEPQEIDSnRPIAVPVVG 320
Cdd:PRK08266 235 VAFRSGRGIVSDRHPLGLNFAAAYELwPQTDVVIGIGSRL--ELPTFRWPWRPDGLkVIRIDIDPTEMRR-LKPDVAIVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 321 DIASSMQGMLAEL-KQNTFTTPLvwRDILNIHKQQNAQkmhekLSTDTQP-LNYFNALsavRDVLREnqDIYLVNEGANT 398
Cdd:PRK08266 312 DAKAGTAALLDALsKAGSKRPSR--RAELRELKAAARQ-----RIQAVQPqASYLRAI---REALPD--DGIFVDELSQV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 399 LDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNG-- 475
Cdd:PRK08266 380 GFASWFAFPVYAPRTFVTCGYQGTLGYGFPTALGAKVANpDRPVVSITGDGGFMFGVQELATAVQHNIGVVTVVFNNNay 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130305 476 GIYRGDGVDLSGaGAPSPTDlLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINV 540
Cdd:PRK08266 460 GNVRRDQKRRFG-GRVVASD-LVNPDFVKLAESFGVAAFRVDSPEELRAALEAALAHGGPVLIEV 522
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
10-545 |
8.97e-61 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 211.15 E-value: 8.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVG---IPVTDMARHAQaegIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGL 86
Cdd:PRK06276 3 GAEAIIKALEAEGVKIIFGYPGgalLPFYDALYDSD---LIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 87 TALANATVNGFPMIMISGssdRAIVDLQQGD-YEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLD 165
Cdd:PRK06276 80 TGIATAYADSSPVIALTG---QVPTKLIGNDaFQEIDALGIFMPITKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 166 LPANVlaATMEKDEALTTI---VKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPF 242
Cdd:PRK06276 157 LPKDV--QEGELDLEKYPIpakIDLPGYKPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 243 LPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIA 315
Cdd:PRK06276 235 CTTLMGKGAFPEDHPLALgmvgmhgTKAANYSVTESDVLIAIGCRFSDRTTGDISSFAPNAKIIHIDIDPAEIGKNVRVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 316 VPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMheklSTDTQPLN---YFNALSAVRDVLRENQDIYLV 392
Cdd:PRK06276 315 VPIVGDAKNVLRDLLAELMKKEIKNKSEWLERVKKLKKESIPRM----DFDDKPIKpqrVIKELMEVLREIDPSKNTIIT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 393 NE-GANTLDNARnIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIV 470
Cdd:PRK06276 391 TDvGQNQMWMAH-FFKTSAPRSFISSGGLGTMGFGFPAAIGAKVAKpDANVIAITGDGGFLMNSQELATIAEYDIPVVIC 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130305 471 IFNN---GGIYRGDgvDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPA 545
Cdd:PRK06276 470 IFDNrtlGMVYQWQ--NLYYGKRQSEVHLGETPDFVKLAESYGVKADRVEKPDEIKEALKEAIKSGEPYLLDIIIDPA 545
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
6-543 |
1.94e-60 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 209.57 E-value: 1.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTdGMHIIVEALKQNNIDTIYGVVGIPVTDMARHA-QAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLN 84
Cdd:PRK08527 2 KLS-GSQMVCEALKEEGVKVVFGYPGGAILNIYDEIyKQNYFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 85 GLTALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYL 164
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDA--FQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 165 DLPANVLAATME---KDEalttiVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIP 241
Cdd:PRK08527 159 DIPKDVTATLGEfeyPKE-----ISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 242 FLPMSMAKGILEDTHPLSAAAA-------RSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPI 314
Cdd:PRK08527 234 AVETLMARGVLRSDDPLLLGMLgmhgsyaANMAMSECDLLISLGARFDDRVTGKLSEFAKHAKIIHVDIDPSSISKIVNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 315 AVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNaqkmheklstdtqPLNYFNAlsavRDVLRENQDIYLVNE 394
Cdd:PRK08527 314 DYPIVGDLKNVLKEMLEELKEENPTTYKEWREILKRYNELH-------------PLSYEDS----DEVLKPQWVIERVGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 395 GANtlDNARNIID-----MY--------KPRRRLDCGTWGVMGIGMGYAIGASVTSGS-PVVAIEGDSAFGFSGMEIETI 460
Cdd:PRK08527 377 LLG--DDAIISTDvgqhqMWvaqfypfnYPRQLATSGGLGTMGYGLPAALGAKLAVPDkVVINFTGDGSILMNIQELMTA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 461 CRYNLPVTIVIFNNG--GIYR-------GDGVdlsgagapSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQ 531
Cdd:PRK08527 455 VEYKIPVINIILNNNflGMVRqwqtffyEERY--------SETDLSTQPDFVKLAESFGGIGFRVTTKEEFDKALKEALE 526
|
570
....*....|..
gi 16130305 532 SRKPTIINVVID 543
Cdd:PRK08527 527 SDKVALIDVKID 538
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
14-543 |
5.16e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 194.66 E-value: 5.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 14 IVEALKQNNIDTIYGVVG---IPVTDMARHAqaeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALA 90
Cdd:PRK08322 7 FVKCLENEGVEYIFGIPGeenLDLLEALRDS---SIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTGVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 91 NATVNGFPMIMISGSsdRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPANV 170
Cdd:PRK08322 84 YAQLGGMPMVAITGQ--KPIKRSKQGSFQIVDVVAMMAPLTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLELPEDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 171 laATMEKDEALTTIVKVENPSPAllpcPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKG 250
Cdd:PRK08322 162 --AAEETDGKPLPRSYSRRPYAS----PKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPFFTTQMGKG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 251 ILEDTHPLSAAAARSFAL-------ANADVVMLVGARL------NWLLAHGKKgwaadtqFIQLDIEPQEIDSNRPIAVP 317
Cdd:PRK08322 236 VIPETHPLSLGTAGLSQGdyvhcaiEHADLIINVGHDViekppfFMNPNGDKK-------VIHINFLPAEVDPVYFPQVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 318 VVGDIASSMQGMLAEL-KQNTFTTPlvwrDILNIHKQQNAQkmHEKLSTDTQ-PLNYFNALSAVRDVLRENqDIYLVNEG 395
Cdd:PRK08322 309 VVGDIANSLWQLKERLaDQPHWDFP----RFLKIREAIEAH--LEEGADDDRfPMKPQRIVADLRKVMPDD-DIVILDNG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 396 ANTLDNARNiidmYKPRRR----LDCGtWGVMGIGMGYAIGAS-VTSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIV 470
Cdd:PRK08322 382 AYKIWFARN----YRAYEPntclLDNA-LATMGAGLPSAIAAKlVHPDRKVLAVCGDGGFMMNSQELETAVRLGLPLVVL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 471 IFNNGG-----------IYRGDGVDLsgaGAPsptDLLHHArydklmDAFRGVGYNVTTTDELRHALTTGIQSRKPTIIN 539
Cdd:PRK08322 457 ILNDNAygmirwkqenmGFEDFGLDF---GNP---DFVKYA------ESYGAKGYRVESADDLLPTLEEALAQPGVHVID 524
|
....
gi 16130305 540 VVID 543
Cdd:PRK08322 525 CPVD 528
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
4-542 |
2.49e-53 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 191.42 E-value: 2.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 4 QLQMTdGMHIIVEALKQNNIDTIYGVVG---IPVTDMARHAQAEG-IRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSA 79
Cdd:PRK07418 16 PQRAT-GAYALMDSLKRHGVKHIFGYPGgaiLPIYDELYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 80 PGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRP 159
Cdd:PRK07418 95 PGATNLVTGIATAQMDSVPMVVITGQVPRPAIGTDA--FQETDIFGITLPIVKHSYVVRDPSDMARIVAEAFHIASSGRP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 160 GGVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQ 239
Cdd:PRK07418 173 GPVLIDIPKDVGQEEFDYVPVEPGSVKPPGYRPTVKGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAERFQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 240 IPFLPMSMAKGILEDTHPLSAAAARSFALANA-------DVVMLVGARLNWLLAhGKKG-WAADTQFIQLDIEPQEIDSN 311
Cdd:PRK07418 253 IPVTTTLMGKGAFDEHHPLSVGMLGMHGTAYAnfavtecDLLIAVGARFDDRVT-GKLDeFASRAKVIHIDIDPAEVGKN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 312 RPIAVPVVGDIASSMQGMLAELKQNTFTTPL-VWRDILNIHKQQNA-QKMHEKLSTDTQPLnyfnaLSAVRDVLRENqdI 389
Cdd:PRK07418 332 RRPDVPIVGDVRKVLVKLLERSLEPTTPPRTqAWLERINRWKQDYPlVVPPYEGEIYPQEV-----LLAVRDLAPDA--Y 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 390 YLVNEG------ANTLDNArniidmykPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICR 462
Cdd:PRK07418 405 YTTDVGqhqmwaAQFLRNG--------PRRWISSAGLGTMGFGMPAAMGVKVAlPDEEVICIAGDASFLMNIQELGTLAQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 463 YNLPVTIVIFNNG--GIYR-------GDGVDLSG--AGAPSptdllhharYDKLMDAFRGVGYNVTTTDELRHALTTGIQ 531
Cdd:PRK07418 477 YGINVKTVIINNGwqGMVRqwqesfyGERYSASNmePGMPD---------FVKLAEAFGVKGMVISERDQLKDAIAEALA 547
|
570
....*....|.
gi 16130305 532 SRKPTIINVVI 542
Cdd:PRK07418 548 HDGPVLIDVHV 558
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-543 |
2.60e-53 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 190.37 E-value: 2.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 1 MSDQLQMTDGMHIIVEALKQNNIDTIYGVVG---IPVTDMARHAqaeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTV 77
Cdd:PRK06048 1 MTGSTEKMTGARAIIKCLEKEGVEVIFGYPGgaiIPVYDELYDS---DLRHILVRHEQAAAHAADGYARATGKVGVCVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 78 SAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSG 157
Cdd:PRK06048 78 SGPGATNLVTGIATAYMDSVPIVALTGQVPRSMIG--NDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 158 RPGGVYLDLPANVLAATMEKDEAlttiVKVENP--SPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFI 235
Cdd:PRK06048 156 RPGPVLIDLPKDVTTAEIDFDYP----DKVELRgyKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 236 ESAQIPFLPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEI 308
Cdd:PRK06048 232 ETIPAPVTTTLMGIGAIPTEHPLSLgmlgmhgTKYANYAIQESDLIIAVGARFDDRVTGKLASFAPNAKIIHIDIDPAEI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 309 DSNRPIAVPVVGDIASSMQGMLAELKQNTFTTplvWRDILNIHKQQnaqkmheklstdtQPLNYFNAlsavRDVLRENQD 388
Cdd:PRK06048 312 SKNVKVDVPIVGDAKQVLKSLIKYVQYCDRKE---WLDKINQWKKE-------------YPLKYKER----EDVIKPQYV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 389 IYLVNE-----------GANTLDNARnIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVtsGSP---VVAIEGDSAFGFSG 454
Cdd:PRK06048 372 IEQIYElcpdaiivtevGQHQMWAAQ-YFKYKYPRTFITSGGLGTMGYGFPAAIGAKV--GKPdktVIDIAGDGSFQMNS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 455 MEIETICRYNLPVTIVIFNNG--GIYRgDGVDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQS 532
Cdd:PRK06048 449 QELATAVQNDIPVIVAILNNGylGMVR-QWQELFYDKRYSHTCIKGSVDFVKLAEAYGALGLRVEKPSEVRPAIEEAVAS 527
|
570
....*....|.
gi 16130305 533 RKPTIINVVID 543
Cdd:PRK06048 528 DRPVVIDFIVE 538
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
7-540 |
1.85e-52 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 187.49 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 7 MTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGL 86
Cdd:PRK07524 1 MTTCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 87 TALANATVNGFPMIMISGSSDRAIVDLQQGDYEEL-DQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLD 165
Cdd:PRK07524 81 TAMGQAYADSIPMLVISSVNRRASLGKGRGKLHELpDQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 166 LPANVLAAtmEKDEALTTIvkVENPSPAlLPCPKSVTSAISLLAKAERPLIILGKGAAysQADEQLREFIESAQIPFLPM 245
Cdd:PRK07524 161 IPLDVLAA--PADHLLPAP--PTRPARP-GPAPAALAQAAERLAAARRPLILAGGGAL--AAAAALRALAERLDAPVALT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 246 SMAKGILEDTHPLSAAAARSFAL-----ANADVVMLVGARLN----WLLAHGkkGWAADTQFIQLDIEPQEIDSNRPIAV 316
Cdd:PRK07524 234 INAKGLLPAGHPLLLGASQSLPAvraliAEADVVLAVGTELGetdyDVYFDG--GFPLPGELIRIDIDPDQLARNYPPAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 317 PVVGDIASSMQGMLAELKQNTFTTPlvwrdilniHKQQNAQKMHEKLSTDTQPL--NYFNALSAVRDVLrenQDIYLVNE 394
Cdd:PRK07524 312 ALVGDARAALEALLARLPGQAAAAD---------WGAARVAALRQALRAEWDPLtaAQVALLDTILAAL---PDAIFVGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 395 GANTLDNARNIIDMYKPRRRLDCGT-WGVMGIGMGYAIGASV-TSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIF 472
Cdd:PRK07524 380 STQPVYAGNLYFDADAPRRWFNASTgYGTLGYGLPAAIGAALgAPERPVVCLVGDGGLQFTLPELASAVEADLPLIVLLW 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130305 473 NNGGiYRG-----DGVDLSGAGA-PSPTDLLHHARydklmdAFRGVGYNVTTTDELRHALTTGIQSRKPTIINV 540
Cdd:PRK07524 460 NNDG-YGEirrymVARDIEPVGVdPYTPDFIALAR------AFGCAAERVADLEQLQAALRAAFARPGPTLIEV 526
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
1-546 |
9.22e-51 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 183.81 E-value: 9.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 1 MSDQLQMTdGMHIIVEALKQNNIDTIYGVvGIPvTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAP 80
Cdd:PRK06112 8 PGFTLNGT-VAHAIARALKRHGVEQIFGQ-SLP-SALFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 81 GFLNGLTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPG 160
Cdd:PRK06112 85 AATLLVAPLAEALKASVPIVALVQDVNRDQTD--RNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 161 GVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQI 240
Cdd:PRK06112 163 PVVLLLPADLLTAAAAAPAAPRSNSLGHFPLDRTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 241 PFLPMSMAKGILEDTHPLSAAAARSFALAN------------ADVVMLVGARLNwllAHGKKGWA---ADTQFIQLDIEP 305
Cdd:PRK06112 243 PVATTNMGKGAVDETHPLSLGVVGSLMGPRspgrhlrdlvreADVVLLVGTRTN---QNGTDSWSlypEQAQYIHIDVDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 306 QEIDSNRPiAVPVVGDIASSMQGMLAELKQNTFTTPLVWR----DILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRD 381
Cdd:PRK06112 320 EEVGRNYE-ALRLVGDARLTLAALTDALRGRDLAARAGRRaalePAIAAGREAHREDSAPVALSDASPIRPERIMAELQA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 382 VLREnqDIYLVNEG-------ANTLDNARNIIDMYKPRrrldcgtwGVMGIGMG--YAIGASVTS-GSPVVAIEGDSAFG 451
Cdd:PRK06112 399 VLTG--DTIVVADAsyssiwvANFLTARRAGMRFLTPR--------GLAGLGWGvpMAIGAKVARpGAPVICLVGDGGFA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 452 FSGMEIETICRYNLPVTIVIFNNGGIYRGDGVDLSGAGapSPTDLLHHARYD--KLMDAFRGVGYNVTTTDELRHALTTG 529
Cdd:PRK06112 469 HVWAELETARRMGVPVTIVVLNNGILGFQKHAETVKFG--THTDACHFAAVDhaAIARACGCDGVRVEDPAELAQALAAA 546
|
570
....*....|....*..
gi 16130305 530 IQSRKPTIINVVIDPAA 546
Cdd:PRK06112 547 MAAPGPTLIEVITDPSA 563
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
14-542 |
1.98e-50 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 182.89 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 14 IVEALKQNNIDTIYGVVG---IPVTDMARHAqaeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALA 90
Cdd:PRK07525 12 FVETLQAHGITHAFGIIGsafMDASDLFPPA---GIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 91 NATVNGFPMIMISGSSdrAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRpGGVYLDLPANV 170
Cdd:PRK07525 89 TAYWAHTPVVLVTPQA--GTKTIGQGGFQEAEQMPMFEDMTKYQEEVRDPSRMAEVLNRVFDKAKRES-GPAQINIPRDY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 171 LaaTMEKDEALTTIVKVENPSPAllpcPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPflpmsMAKG 250
Cdd:PRK07525 166 F--YGVIDVEIPQPVRLERGAGG----EQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAP-----VACG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 251 ILED-----THPLSA-------AAARSFALANADVVMLVGARLNW---LLAHGKKGWAADTQFIQLDIEPQEIDSNRPIA 315
Cdd:PRK07525 235 YLHNdafpgSHPLWVgplgyngSKAAMELIAKADVVLALGTRLNPfgtLPQYGIDYWPKDAKIIQVDINPDRIGLTKKVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 316 VPVVGDIASSMQGMLAELKQNT-------------FTTPLVWrdilnihKQQNAQKMHEK--LSTD---------TQPLN 371
Cdd:PRK07525 315 VGICGDAKAVARELLARLAERLagdagreerkaliAAEKSAW-------EQELSSWDHEDddPGTDwneeararkPDYMH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 372 YFNALSAVRDVLREN----QDIYLVNEGANTLdnarniIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEG 446
Cdd:PRK07525 388 PRQALREIQKALPEDaivsTDIGNNCSIANSY------LRFEKGRKYLAPGSFGNCGYAFPAIIGAKIACpDRPVVGFAG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 447 DSAFGFSGMEIETICRYNLPVTIVIFNNG--GIYRGDGVD-----LSGAGAPSPTDllhharYDKLMDAFRGVGYNVTTT 519
Cdd:PRK07525 462 DGAWGISMNEVMTAVRHNWPVTAVVFRNYqwGAEKKNQVDfynnrFVGTELDNNVS------YAGIAEAMGAEGVVVDTQ 535
|
570 580
....*....|....*....|....*.
gi 16130305 520 DELRHALTTGIQSR---KPTIINVVI 542
Cdd:PRK07525 536 EELGPALKRAIDAQnegKTTVIEIMC 561
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
12-554 |
1.15e-48 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 177.89 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 12 HIIVEALKQNNIDTIYGVVG--I-PVTDMARHAQaEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTA 88
Cdd:PRK08611 8 EALVKLLQDWGIDHVYGIPGdsIdAVVDALRKEQ-DKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGAIHLLNG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 89 LANATVNGFPMIMISGSSDRAIvdLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRpGGVYLDLPA 168
Cdd:PRK08611 87 LYDAKMDHVPVLALAGQVTSDL--LGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTAYEKK-GVAVLTIPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 169 NVLAATmEKDEALTTIVKVENPSPAllPCPKSVTSAISLLAKAERPLIILGKGAaySQADEQLREFIESAQIPF---LPm 245
Cdd:PRK08611 164 DLPAQK-IKDTTNKTVDTFRPTVPS--PKPKDIKKAAKLINKAKKPVILAGLGA--KHAKEELLAFAEKAKIPIihtLP- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 246 smAKGILEDTHPLSA-------AAARSFALANADVVMLVGAR---LNWLlahgkkgwAADTQFIQLDIEPQEIDSNRPIA 315
Cdd:PRK08611 238 --AKGIIPDDHPYSLgnlgkigTKPAYEAMQEADLLIMVGTNypyVDYL--------PKKAKAIQIDTDPANIGKRYPVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 316 VPVVGDIASSmqgmLAELkqNTFTTPLVWRDILNiHKQQNAQK----MHEKLSTDTQPLNYFNALSAVRDVlRENQDIYL 391
Cdd:PRK08611 308 VGLVGDAKKA----LHQL--TENIKHVEDRRFLE-ACQENMAKwwkwMEEDENNASTPIKPERVMAAIQKI-ADDDAVLS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 392 VNEGANTLDNARNiIDMyKPRRRLDCGTW-GVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLPVTI 469
Cdd:PRK08611 380 VDVGTVTVWSARY-LNL-GTNQKFIISSWlGTMGCGLPGAIAAKIAfPDRQAIAICGDGGFSMVMQDFVTAVKYKLPIVV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 470 VIFNNGGI----Y----RGD---GVDLSGagapsptdlLHHARYdklMDAFRGVGYNVTTTDELRHALTTGIQSRKPTII 538
Cdd:PRK08611 458 VVLNNQQLafikYeqqaAGEleyAIDLSD---------MDYAKF---AEACGGKGYRVEKAEELDPAFEEALAQDKPVII 525
|
570
....*....|....*.
gi 16130305 539 NVVIDPAAGTESGHIT 554
Cdd:PRK08611 526 DVYVDPNAAPLPGKIV 541
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
10-178 |
6.98e-46 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 158.94 E-value: 6.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAE-GIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTA 88
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 89 LANATVNGFPMIMISGSSDRAIVDlQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPA 168
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVG-RGALQQELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPL 159
|
170
....*....|
gi 16130305 169 NVLAATMEKD 178
Cdd:pfam02776 160 DVLLEEVDED 169
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
7-543 |
1.15e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 166.55 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 7 MTDGMHIIVEALKQNNIDTIYGVVGI---PVTD-MARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGF 82
Cdd:PRK06456 1 MPTGARILVDSLKREGVKVIFGIPGLsnmQIYDaFVEDLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 83 LNGLTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGV 162
Cdd:PRK06456 81 TNLVTGLITAYWDSSPVIAITGQVPRSVMG--KMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 163 YLDLPANVLAATMEKDEALTT-IVKVENPSPALLPcPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIP 241
Cdd:PRK06456 159 VIDIPRDIFYEKMEEIKWPEKpLVKGYRDFPTRID-RLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHIP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 242 FLPMSMAKGILEDTHPLSAAAARSFALANA-------DVVMLVGARL--------NWLLAHGKKgwaadtqFIQLDIEPQ 306
Cdd:PRK06456 238 IVSTFPGKTAIPHDHPLYFGPMGYYGRAEAsmaalesDAMLVVGARFsdrtftsyDEMVETRKK-------FIMVNIDPT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 307 EIDSNRPIAVPVVGDiassMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMHEKL--STDTQPLNYFNALSAVRDVLR 384
Cdd:PRK06456 311 DGEKAIKVDVGIYGN----AKIILRELIKAITELGQKRDRSAWLKRVKEYKEYYSQFyyTEENGKLKPWKIMKTIRQALP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 385 ENQdIYLVNEGANTLdNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVtsGSP---VVAIEGDSAFGFSGMEIETIC 461
Cdd:PRK06456 387 RDA-IVTTGVGQHQM-WAEVFWEVLEPRTFLTSSGMGTMGFGLPAAMGAKL--ARPdkvVVDLDGDGSFLMTGTNLATAV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 462 RYNLPVTIVIFNNG--GIYRG----------DGVDLsgagAPSPTdllhharYDKLMDAFRGVGYNVTTTDELRHALTTG 529
Cdd:PRK06456 463 DEHIPVISVIFDNRtlGLVRQvqdlffgkriVGVDY----GPSPD-------FVKLAEAFGALGFNVTTYEDIEKSLKSA 531
|
570
....*....|....
gi 16130305 530 IQSRKPTIINVVID 543
Cdd:PRK06456 532 IKEDIPAVIRVPVD 545
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
6-543 |
1.46e-44 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 166.30 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTDGMHIIvEALKQNNIDTIYGVVG---IPVTDMARHAqaeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGF 82
Cdd:PRK06725 14 EVTGAGHVI-QCLKKLGVTTVFGYPGgaiLPVYDALYES---GLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 83 LNGLTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGV 162
Cdd:PRK06725 90 TNLVTGLADAYMDSIPLVVITGQVATPLIG--KDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 163 YLDLPANVL--AATMEKDEalttivKVENPSPALLPCPKS-----VTSAISllaKAERPLIILGKGAAYSQADEQLREFI 235
Cdd:PRK06725 168 LIDIPKDVQneKVTSFYNE------VVEIPGYKPEPRPDSmklreVAKAIS---KAKRPLLYIGGGVIHSGGSEELIEFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 236 ESAQIPFLPMSMAKGILEDTHP-------LSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEI 308
Cdd:PRK06725 239 RENRIPVVSTLMGLGAYPPGDPlflgmlgMHGTYAANMAVTECDLLLALGVRFDDRVTGKLELFSPHSKKVHIDIDPSEF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 309 DSNRPIAVPVVGDIASSMQGMLAElkqntfttplvwrdilNIHKQQNAQKMHEKLSTDTQPLNYfnalSAVRDVLRENQD 388
Cdd:PRK06725 319 HKNVAVEYPVVGDVKKALHMLLHM----------------SIHTQTDEWLQKVKTWKEEYPLSY----KQKESELKPQHV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 389 IYLVNEgantLDNARNIID------------MYK---PRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGF 452
Cdd:PRK06725 379 INLVSE----LTNGEAIVTtevgqhqmwaahFYKaknPRTFLTSGGLGTMGFGFPAAIGAQLAKeEELVICIAGDASFQM 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 453 SGMEIETICRYNLPVTIVIFNNG--GIYRG-------DGVDLSGAGAPSptdllhharYDKLMDAFRGVGYNVTTTDELR 523
Cdd:PRK06725 455 NIQELQTIAENNIPVKVFIINNKflGMVRQwqemfyeNRLSESKIGSPD---------FVKVAEAYGVKGLRATNSTEAK 525
|
570 580
....*....|....*....|
gi 16130305 524 HALTTGIQSRKPTIINVVID 543
Cdd:PRK06725 526 QVMLEAFAHEGPVVVDFCVE 545
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
5-526 |
2.62e-44 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 165.76 E-value: 2.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 5 LQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDM--ARHAQAeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGF 82
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIydALHEKS-GIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 83 LNGLTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGV 162
Cdd:PRK08979 80 TNTITGIATAYMDSIPMVVLSGQVPSNLIG--NDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 163 YLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPF 242
Cdd:PRK08979 158 VIDLPKDCLNPAILHPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 243 LPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIA 315
Cdd:PRK08979 238 VSTLMGLGAFPGTHKNSLgmlgmhgRYEANMAMHNADLIFGIGVRFDDRTTNNLEKYCPNATILHIDIDPSSISKTVRVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 316 VPVVGDIASSMQGMLAELKQ----NTFTTPLVWRDILNIHKQQNAQKmHEKLSTDTQPLNYFNALSAVrdvlrENQDIYL 391
Cdd:PRK08979 318 IPIVGSADKVLDSMLALLDEsgetNDEAAIASWWNEIEVWRSRNCLA-YDKSSERIKPQQVIETLYKL-----TNGDAYV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 392 VNE-GANTLDNArniidMY----KPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNL 465
Cdd:PRK08979 392 ASDvGQHQMFAA-----LYypfdKPRRWINSGGLGTMGFGLPAAMGVKFAmPDETVVCVTGDGSIQMNIQELSTALQYDI 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130305 466 PVTIVIFNN---GGIYRGDGVDLSGAGAPSPTDLLhhARYDKLMDAFRGVGYNVTTTDELRHAL 526
Cdd:PRK08979 467 PVKIINLNNrflGMVKQWQDMIYQGRHSHSYMDSV--PDFAKIAEAYGHVGIRISDPDELESGL 528
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
9-541 |
2.95e-44 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 165.37 E-value: 2.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 9 DGMHIIVEALKQNNIDTIYGvvgIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLT--QKPGICLTVSAPGFLNGL 86
Cdd:PRK06154 21 KVAEAVAEILKEEGVELLFG---FPVNELFDAAAAAGIRPVIARTERVAVHMADGYARATsgERVGVFAVQYGPGAENAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 87 TALANATVNGFPMIMISGSSDRAIVDLQQgDYEELDQMnaaKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDL 166
Cdd:PRK06154 98 GGVAQAYGDSVPVLFLPTGYPRGSTDVAP-NFESLRNY---RHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 167 PANVLAATMEKDEALTTivkvenPSPAL--LPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLP 244
Cdd:PRK06154 174 PVDVLAEELDELPLDHR------PSRRSrpGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 245 MSMAKGILEDTHP-------LSAAAARSFALANADVVMLVGA---RLNWLLAhgkkgWAADTQFIQLDIEPQEIDSNRPI 314
Cdd:PRK06154 248 TLNGKSAFPEDHPlalgsggRARPATVAHFLREADVLFGIGCsltRSYYGLP-----MPEGKTIIHSTLDDADLNKDYPI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 315 AVPVVGDIASSMQGMLAELKqNTFT-----TPLVWRDILNIHKQQNAQKMhEKLSTDTQPLNYFNalsavrdVLRENQDI 389
Cdd:PRK06154 323 DHGLVGDAALVLKQMIEELR-RRVGpdrgrAQQVAAEIEAVRAAWLAKWM-PKLTSDSTPINPYR-------VVWELQHA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 390 YLVNEGANTLD--NARNIID-MYKPRRRLDCGTWGV---MGIGMGYAIGASVTSGSPVVA-IEGDSAFGFSGMEIETICR 462
Cdd:PRK06154 394 VDIKTVIITHDagSPRDQLSpFYVASRPGSYLGWGKttqLGYGLGLAMGAKLARPDALVInLWGDAAFGMTGMDFETAVR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 463 YNLPVTIVIFNNG--GIYrgDGVDLSGAGAPSPTDLLHHarYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRK---PTI 537
Cdd:PRK06154 474 ERIPILTILLNNFsmGGY--DKVMPVSTTKYRATDISGD--YAAIARALGGYGERVEDPEMLVPALLRALRKVKegtPAL 549
|
....
gi 16130305 538 INVV 541
Cdd:PRK06154 550 LEVI 553
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
12-168 |
3.20e-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: 153.84 E-value: 3.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 12 HIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALAN 91
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130305 92 ATVNGFPMIMISGSSDRAivDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPA 168
Cdd:cd07035 81 AYLDSIPLLVITGQRPTA--GEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDLPK 155
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
10-543 |
6.15e-44 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 164.26 E-value: 6.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTAL 89
Cdd:PRK08617 7 GADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 90 ANATVNGFPMIMISGSSDRAivDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPAN 169
Cdd:PRK08617 87 VTATAEGDPVVAIGGQVKRA--DRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 170 VLAATMEkDEALTTIVKVE-NPSPallpcPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMA 248
Cdd:PRK08617 165 VVDAPVT-SKAIAPLSKPKlGPAS-----PEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 249 KGI----LEDT----------HPLSAAAARsfalanADVVMLVG-------ARLnwllahgkkgWAA--DTQFIQLDIEP 305
Cdd:PRK08617 239 AGVisreLEDHffgrvglfrnQPGDELLKK------ADLVITIGydpieyePRN----------WNSegDATIIHIDVLP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 306 QEIDSN-RPiAVPVVGDIASSMQGMLAELKQntFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRDVLr 384
Cdd:PRK08617 303 AEIDNYyQP-ERELIGDIAATLDLLAEKLDG--LSLSPQSLEILEELRAQLEELAERPARLEEGAVHPLRIIRALQDIV- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 385 eNQDIYLvneganTLDNARNIIDM------YKPRRRLDCGTWGVMGIGMGYAIGAS-VTSGSPVVAIEGDSAFGFSGMEI 457
Cdd:PRK08617 379 -TDDTTV------TVDVGSHYIWMaryfrsYEPRHLLFSNGMQTLGVALPWAIAAAlVRPGKKVVSVSGDGGFLFSAMEL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 458 ETICRYNLPVTIVIFNNGGiY------------RGDGVDLsgagapSPTDLLHHArydklmDAFRGVGYNVTTTDELRHA 525
Cdd:PRK08617 452 ETAVRLKLNIVHIIWNDGH-YnmvefqeemkygRSSGVDF------GPVDFVKYA------ESFGAKGLRVTSPDELEPV 518
|
570
....*....|....*...
gi 16130305 526 LTTGIQSRKPTIINVVID 543
Cdd:PRK08617 519 LREALATDGPVVIDIPVD 536
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
4-544 |
1.07e-43 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 164.10 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 4 QLQMTDGMHIIVEALKQNNIDTIYGVVG---IPVTDMARHAQAEG-IRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSA 79
Cdd:CHL00099 6 TLREKTGAFALIDSLVRHGVKHIFGYPGgaiLPIYDELYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 80 PGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRP 159
Cdd:CHL00099 86 PGATNLVTGIATAQMDSVPLLVITGQVGRAFIGTDA--FQEVDIFGITLPIVKHSYVVRDARDISRIVAEAFYIAKHGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 160 GGVYLDLPANVlaaTMEK-----DEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREF 234
Cdd:CHL00099 164 GPVLIDIPKDV---GLEKfdyypPEPGNTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 235 IESAQIPFLPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQE 307
Cdd:CHL00099 241 AELYKIPVTTTLMGKGIFDEDHPLCLgmlgmhgTAYANFAVSECDLLIALGARFDDRVTGKLDEFACNAQVIHIDIDPAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 308 IDSNRPIAVPVVGDIASSMQGMLAELKQNT-FTTP---LVWRDilNIHKQQNAQKM----HEKLSTDTQPLNYFNALSav 379
Cdd:CHL00099 321 IGKNRIPQVAIVGDVKKVLQELLELLKNSPnLLESeqtQAWRE--RINRWRKEYPLlipkPSTSLSPQEVINEISQLA-- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 380 rdvlrenQDIYLVNE-GANTLDNARNIidMYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEI 457
Cdd:CHL00099 397 -------PDAYFTTDvGQHQMWAAQFL--KCKPRKWLSSAGLGTMGYGLPAAIGAQIAhPNELVICISGDASFQMNLQEL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 458 ETICRYNLPVTIVIFNNG--GIYR-------GDGVDLSG--AGAPSptdllhharYDKLMDAFRGVGYNVTTTDELRHAL 526
Cdd:CHL00099 468 GTIAQYNLPIKIIIINNKwqGMVRqwqqafyGERYSHSNmeEGAPD---------FVKLAEAYGIKGLRIKSRKDLKSSL 538
|
570
....*....|....*...
gi 16130305 527 TTGIQSRKPTIINVVIDP 544
Cdd:CHL00099 539 KEALDYDGPVLIDCQVIE 556
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
1-556 |
1.86e-43 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 162.74 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 1 MSDQLQMTDGMHIIVEALKQNNIDTIYGVVG---IPVTDmARHaQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTV 77
Cdd:PRK08199 1 MTSTPRARTGGQILVDALRANGVERVFCVPGesyLAVLD-ALH-DETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 78 SAPGFLN---GL-TALANATvngfPMIMISGSSDRAIVD---LQQGDYEeldQMNAakPYAKAAFRVNQPQDLGIALARA 150
Cdd:PRK08199 79 RGPGATNasiGVhTAFQDST----PMILFVGQVARDFREreaFQEIDYR---RMFG--PMAKWVAEIDDAARIPELVSRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 151 IRVSVSGRPGGVYLDLPANVLAATMEKDEALTTivkvenPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQ 230
Cdd:PRK08199 150 FHVATSGRPGPVVLALPEDVLSETAEVPDAPPY------RRVAAAPGAADLARLAELLARAERPLVILGGSGWTEAAVAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 231 LREFIESAQIP----F----------------LPMSMAKGILEDTHplsaaaarsfalaNADVVMLVGARLNWLLAHGKK 290
Cdd:PRK08199 224 LRAFAERWGLPvacaFrrqdlfdnrhpnyagdLGLGINPALAARIR-------------EADLVLAVGTRLGEVTTQGYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 291 ---GWAADTQFIQLDIEPQEIDSNRPIAVPvvgdIASSMQGMLAELKQNTFTTPLVWRDilnihkqqNAQKMHEKLSTDT 367
Cdd:PRK08199 291 lldIPVPRQTLVHVHPDAEELGRVYRPDLA----IVADPAAFAAALAALEPPASPAWAE--------WTAAAHADYLAWS 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 368 QPLNYFNA--LSAVRDVLREN--QDIYLVNeGANtldNARNIIDMYKPRRRLDCG---TWGVMGIGMGYAIGASVTS-GS 439
Cdd:PRK08199 359 APLPGPGAvqLGEVMAWLRERlpADAIITN-GAG---NYATWLHRFFRFRRYRTQlapTSGSMGYGLPAAIAAKLLFpER 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 440 PVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNgGIYrgdGV-----DLSGAGAPSPTDlLHHARYDKLMDAFRGVGY 514
Cdd:PRK08199 435 TVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNN-GMY---GTirmhqEREYPGRVSGTD-LTNPDFAALARAYGGHGE 509
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 16130305 515 NVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESGHITKL 556
Cdd:PRK08199 510 TVERTEDFAPAFERALASGKPALIEIRIDPEAITPTATLSQI 551
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
8-474 |
3.86e-43 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 162.30 E-value: 3.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 8 TDGMHIIVEALKQNNIDTIYGVVG---IPVTDmARHAQaEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLN 84
Cdd:PRK07282 10 KSGSDLVLETLRDLGVDTIFGYPGgavLPLYD-AIYNF-EGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 85 GLTALANATVNGFPMIMISGSSDRAivDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYL 164
Cdd:PRK07282 88 AITGIADAMSDSVPLLVFTGQVARA--GIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 165 DLPANVlaATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLP 244
Cdd:PRK07282 166 DLPKDV--SALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 245 MSMAKGILEDTHPLSAAA-------ARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIAVP 317
Cdd:PRK07282 244 TLLGQGTIATSHPLFLGMggmhgsyAANIAMTEADFMINIGSRFDDRLTGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 318 VVGDIASSMQGMLAELKQNTFTTPlvWrdILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAvrdvLRENQDIYLVNEGAN 397
Cdd:PRK07282 324 VVGDAKKALQMLLAEPTVHNNTEK--W--IEKVTKDKNRVRSYDKKERVVQPQAVIERIGE----LTNGDAIVVTDVGQH 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130305 398 TLDNARNIidMYKPRRRL-DCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNN 474
Cdd:PRK07282 396 QMWAAQYY--PYQNERQLvTSGGLGTMGFGIPAAIGAKIANpDKEVILFVGDGGFQMTNQELAILNIYKVPIKVVMLNN 472
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-544 |
5.63e-43 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 161.80 E-value: 5.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 1 MSDQLQMTdGMHIIVEALKQNNIDTIYGVVG---IPVTDMArhAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTV 77
Cdd:PRK08155 7 TSTRKRFT-GAELIVRLLERQGIRIVTGIPGgaiLPLYDAL--SQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 78 SAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSG 157
Cdd:PRK08155 84 SGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDA--FQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 158 RPGGVYLDLPANVLAATMEKDEalttIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIES 237
Cdd:PRK08155 162 RPGPVWIDIPKDVQTAVIELEA----LPAPAEKDAAPAFDEESIRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 238 AQIPFLPMSMAKGILEDTHPLS-------AAAARSFALANADVVMLVGARLNwLLAHGK-KGWAADTQFIQLDIEPQEID 309
Cdd:PRK08155 238 AQLPTTMTLMALGMLPKAHPLSlgmlgmhGARSTNYILQEADLLIVLGARFD-DRAIGKtEQFCPNAKIIHVDIDRAELG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 310 SNRPIAVPVVGDIASSMQGMLAELKQNTFTtplVWRDILNIHKQQNAQKMheklSTDTQPLNYFNALSAVRDVLrENQDI 389
Cdd:PRK08155 317 KIKQPHVAIQADVDDVLAQLLPLVEAQPRA---EWHQLVADLQREFPCPI----PKADDPLSHYGLINAVAACV-DDNAI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 390 YLVNEGANTLDNARnIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVT 468
Cdd:PRK08155 389 ITTDVGQHQMWTAQ-AYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANpERKVLCFSGDGSLMMNIQEMATAAENQLDVK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 469 IVIFNN---GGIYRGD----GVDLSGAGAPSPTDLLHHARydklmdafrgvGYNVTTTD-----ELRHALTTGIQSRKPT 536
Cdd:PRK08155 468 IILMNNealGLVHQQQslfyGQRVFAATYPGKINFMQIAA-----------GFGLETCDlnneaDPQAALQEAINRPGPA 536
|
....*...
gi 16130305 537 IINVVIDP 544
Cdd:PRK08155 537 LIHVRIDA 544
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
6-554 |
1.07e-42 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 161.69 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTdGMHIIVEALKQNNIDTIYGVVG---IPVTD--MArhaqAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAP 80
Cdd:PRK07789 30 RMT-GAQAVVRSLEELGVDVVFGIPGgaiLPVYDplFD----STKVRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 81 GFLNGLTALANATVNGFPMIMISGSSDRAIV--DLQQgdyeELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGR 158
Cdd:PRK07789 105 GATNLVTPIADANMDSVPVVAITGQVGRGLIgtDAFQ----EADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 159 PGGVYLDLPANVLAATMEkdeaLTTIVKVENPS--PALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIE 236
Cdd:PRK07789 181 PGPVLVDIPKDALQAQTT----FSWPPRMDLPGyrPVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 237 SAQIPFLPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEID 309
Cdd:PRK07789 257 LTGIPVVTTLMARGAFPDSHPQHLgmpgmhgTVAAVAALQRSDLLIALGARFDDRVTGKLDSFAPDAKVIHADIDPAEIG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 310 SNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLV----WRDILNihkqqnaqKMHEklstdTQPLNY------------- 372
Cdd:PRK07789 337 KNRHADVPIVGDVKEVIAELIAALRAEHAAGGKPdltaWWAYLD--------GWRE-----TYPLGYdepsdgslapqyv 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 373 FNALSAVRDvlreNQDIYLVNEGANTLdNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVtsGSP---VVAIEGDSA 449
Cdd:PRK07789 404 IERLGEIAG----PDAIYVAGVGQHQM-WAAQFIDYEKPRTWLNSGGLGTMGYAVPAAMGAKV--GRPdkeVWAIDGDGC 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 450 FGFSGMEIETICRYNLPVTIVIFNNG--GIYRgDGVDLSGAGAPSPTDLLHHARY--D--KLMDAFRGVGYNVTTTDELR 523
Cdd:PRK07789 477 FQMTNQELATCAIEGIPIKVALINNGnlGMVR-QWQTLFYEERYSNTDLHTHSHRipDfvKLAEAYGCVGLRCEREEDVD 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 16130305 524 HALttgiqsRKPTIIN---VVID----------P--AAGTESGHIT 554
Cdd:PRK07789 556 AVI------EKARAINdrpVVIDfvvgkdamvwPmvAAGTSNDEIQ 595
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
10-546 |
1.67e-41 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 157.35 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVG---IPVTDMARHAqaeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGL 86
Cdd:PRK08978 3 GAQWVVHALRAQGVDTVFGYPGgaiMPVYDALYDG---GVEHLLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 87 TALANATVNGFPMIMISGSSDRAIV--DLQQgdyeELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYL 164
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIgtDAFQ----EIDVLGLSLACTKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 165 DLPANVLAATMEkdeaLTTIVKVENPSPAllPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPflP 244
Cdd:PRK08978 156 DIPKDIQLAEGE----LEPHLTTVENEPA--FPAAELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMP--A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 245 MSMAKGI--LEDTHPLSA-------AAARSFALANADVVMLVGARLNwLLAHGK-KGWAADTQFIQLDIEPQEIDSNRPI 314
Cdd:PRK08978 228 VATLKGLgaVEADHPYYLgmlgmhgTKAANLAVQECDLLIAVGARFD-DRVTGKlNTFAPHAKVIHLDIDPAEINKLRQA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 315 AVPVVGDIASsmqgMLAELKQNTFTTPlvWRdilnihkQQNAQKMHE-KLSTDtqplnyfnalsavrdvlRENQDIY--- 390
Cdd:PRK08978 307 HVALQGDLNA----LLPALQQPLNIDA--WR-------QHCAQLRAEhAWRYD-----------------HPGEAIYapa 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 391 LVNEGANTL-DNARNIID-----MY--------KPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGM 455
Cdd:PRK08978 357 LLKQLSDRKpADTVVTTDvgqhqMWvaqhmrftRPENFITSSGLGTMGFGLPAAIGAQVARpDDTVICVSGDGSFMMNVQ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 456 EIETICRYNLPVTIVIFNNG--GIYRgDGVDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSR 533
Cdd:PRK08978 437 ELGTIKRKQLPVKIVLLDNQrlGMVR-QWQQLFFDERYSETDLSDNPDFVMLASAFGIPGQTITRKDQVEAALDTLLNSE 515
|
570
....*....|...
gi 16130305 534 KPTIINVVIDPAA 546
Cdd:PRK08978 516 GPYLLHVSIDELE 528
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
6-537 |
3.47e-41 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 157.18 E-value: 3.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTdGMHIIVEALKQNNIDTIYGVVG---IPVTDMARhaQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGF 82
Cdd:PRK09107 10 QMT-GAEMVVQALKDQGVEHIFGYPGgavLPIYDEIF--QQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 83 LNGLTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGV 162
Cdd:PRK09107 87 TNAVTPLQDALMDSIPLVCITGQVPTHLIG--SDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 163 YLDLPANVLAATMEKdEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYS--QADEQLREFIESAQI 240
Cdd:PRK09107 165 VVDIPKDVQFATGTY-TPPQKAPVHVSYQPKVKGDAEAITEAVELLANAKRPVIYSGGGVINSgpEASRLLRELVELTGF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 241 PFLPMSMAKGILEDTHPLSAAAARSFALANA-------DVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRP 313
Cdd:PRK09107 244 PITSTLMGLGAYPASGKNWLGMLGMHGTYEAnmamhdcDVMLCVGARFDDRITGRLDAFSPNSKKIHIDIDPSSINKNVR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 314 IAVPVVGDIASSMQGMLAELKQ-----NTFTTPLVWRDILNIHKQQN-AQKMHEKLSTDTQPLNYFNALSAVRDVlrenq 387
Cdd:PRK09107 324 VDVPIIGDVGHVLEDMLRLWKArgkkpDKEALADWWGQIARWRARNSlAYTPSDDVIMPQYAIQRLYELTKGRDT----- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 388 diYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLP 466
Cdd:PRK09107 399 --YITTEVGQHQMWAAQFFGFEEPNRWMTSGGLGTMGYGLPAALGVQIAhPDALVIDIAGDASIQMCIQEMSTAVQYNLP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 467 VTIVIFNNG--GIYRgdgvdlsgagapSPTDLLHHARYD-----------KLMDAFRGVGYNVTTTDELRHALTTGIQSR 533
Cdd:PRK09107 477 VKIFILNNQymGMVR------------QWQQLLHGNRLShsyteampdfvKLAEAYGAVGIRCEKPGDLDDAIQEMIDVD 544
|
....
gi 16130305 534 KPTI 537
Cdd:PRK09107 545 KPVI 548
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
5-563 |
1.02e-40 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 155.39 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 5 LQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDM--ARHAQAeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGF 82
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIydALHTVG-GIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 83 LNGLTALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGV 162
Cdd:PRK07979 80 TNAITGIATAYMDSIPLVVLSGQVATSLIGYDA--FQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 163 YLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPF 242
Cdd:PRK07979 158 VVDLPKDILNPANKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 243 LPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIA 315
Cdd:PRK07979 238 VSSLMGLGAFPATHRQSLgmlgmhgTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 316 VPVVGDIASSMQGMLAELKQNTFTTPL-VWRDILNIHKQQNAQKM--HEKLSTDTQPlnyfnalSAVRDVLRE--NQDIY 390
Cdd:PRK07979 318 IPIVGDARQVLEQMLELLSQESAHQPLdEIRDWWQQIEQWRARQClkYDTHSEKIKP-------QAVIETLWRltKGDAY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 391 LVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLPVTI 469
Cdd:PRK07979 391 VTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMAlPEETVVCVTGDGSIQMNIQELSTALQYELPVLV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 470 VIFNN---GGIYRGDGVDLSGAGAPSPTDLLhhARYDKLMDAFRGVGYNVTTTDELRHALTTG---IQSRKPTIINVVID 543
Cdd:PRK07979 471 LNLNNrylGMVKQWQDMIYSGRHSQSYMQSL--PDFVRLAEAYGHVGIQISHPDELESKLSEAleqVRNNRLVFVDVTVD 548
|
570 580
....*....|....*....|
gi 16130305 544 paagtESGHITklnPKQVAG 563
Cdd:PRK07979 549 -----GSEHVY---PMQIRG 560
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
5-563 |
2.41e-40 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 154.52 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 5 LQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDM--ARHAQAEgIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGF 82
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIydALFKQDK-VEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 83 LNGLTALANATVNGFPMIMISGSSDRAIVdlqqGD--YEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPG 160
Cdd:PRK06466 80 TNAITGIATAYMDSIPMVVLSGQVPSTLI----GEdaFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 161 GVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQI 240
Cdd:PRK06466 156 PVVVDIPKDMTNPAEKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 241 PFLPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRP 313
Cdd:PRK06466 236 PVTNTLMGLGGFPGTDRQFLgmlgmhgTYEANMAMHHADVILAVGARFDDRVTNGPAKFCPNAKIIHIDIDPASISKTIK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 314 IAVPVVGDIASSMQGMLAELKQ-----NTFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVrdvlrENQD 388
Cdd:PRK06466 316 ADIPIVGPVESVLTEMLAILKEigekpDKEALAAWWKQIDEWRGRHGLFPYDKGDGGIIKPQQVVETLYEV-----TNGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 389 IYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLPV 467
Cdd:PRK06466 391 AYVTSDVGQHQMFAAQYYKFNKPNRWINSGGLGTMGFGLPAAMGVKLAfPDQDVACVTGEGSIQMNIQELSTCLQYGLPV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 468 TIVIFNNG--GIYRgdgvdlsgagapSPTDLLHHARYD-----------KLMDAFRGVGYNVTTTDELRHALTTGIQSR- 533
Cdd:PRK06466 471 KIINLNNGalGMVR------------QWQDMQYEGRHShsymeslpdfvKLAEAYGHVGIRITDLKDLKPKLEEAFAMKd 538
|
570 580 590
....*....|....*....|....*....|
gi 16130305 534 KPTIINVVIDPaagteSGHITklnPKQVAG 563
Cdd:PRK06466 539 RLVFIDIYVDR-----SEHVY---PMQIAD 560
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
10-563 |
5.24e-40 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 153.53 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVGIPVTDM--ARHAQAeGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLT 87
Cdd:PRK06882 6 GAEMVVQSLRDEGVEYVFGYPGGSVLDIydAIHTLG-GIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGATNAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 88 ALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLP 167
Cdd:PRK06882 85 GIATAYTDSVPLVILSGQVPSNLIGTDA--FQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVIDIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 168 ANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSM 247
Cdd:PRK06882 163 KDMVNPANKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSSLM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 248 AKGILEDTHP-------LSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIAVPVVG 320
Cdd:PRK06882 243 GLGAYPSTDKqflgmlgMHGTYEANNAMHESDLILGIGVRFDDRTTNNLAKYCPNAKVIHIDIDPTSISKNVPAYIPIVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 321 DIASSMQGMLAELKQNTFTTPLVwrDILNIHKQQNAQKMHEKLSTDtQPLNYFNALSAVRDVLR-ENQDIYLVNEGANTL 399
Cdd:PRK06882 323 SAKNVLEEFLSLLEEENLAKSQT--DLTAWWQQINEWKAKKCLEFD-RTSDVIKPQQVVEAIYRlTNGDAYVASDVGQHQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 400 DNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVT-SGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNggiy 478
Cdd:PRK06882 400 MFAALHYPFDKPRRWINSGGAGTMGFGLPAAIGVKFAhPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNN---- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 479 RGDGV-----DLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSR-KPTIINVVIDpaagtESGH 552
Cdd:PRK06882 476 RFLGMvkqwqDLIYSGRHSQVYMNSLPDFAKLAEAYGHVGIQIDTPDELEEKLTQAFSIKdKLVFVDVNVD-----ETEH 550
|
570
....*....|.
gi 16130305 553 ITklnPKQVAG 563
Cdd:PRK06882 551 VY---PMQIRG 558
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
6-540 |
1.19e-38 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 149.53 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNG 85
Cdd:PRK07710 14 KLMTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 86 LTALANATVNGFPMIMISGSSDRAIVDlqQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLD 165
Cdd:PRK07710 94 VTGLADAMIDSLPLVVFTGQVATSVIG--SDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 166 LPANVLAATMEKDEAlttiVKVENP--SPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFL 243
Cdd:PRK07710 172 IPKDMVVEEGEFCYD----VQMDLPgyQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 244 PMSMAKGILEDTHPLSAAAARSFALANA-------DVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIAV 316
Cdd:PRK07710 248 HTLLGLGGFPADHPLFLGMAGMHGTYTAnmalyecDLLINIGARFDDRVTGNLAYFAKEATVAHIDIDPAEIGKNVPTEI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 317 PVVGDIASSMQGMLAELKQNTFTTPlvWRDILNIHKQQnaqkmheklstdtQPLNYFNAlsavRDVLRENQDIYLVNEGA 396
Cdd:PRK07710 328 PIVADAKQALQVLLQQEGKKENHHE--WLSLLKNWKEK-------------YPLSYKRN----SESIKPQKAIEMLYEIT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 397 N-----TLDN------ARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSP-VVAIEGDSAFGFSGMEIETICRYN 464
Cdd:PRK07710 389 KgeaivTTDVgqhqmwAAQYYPFKTPDKWVTSGGLGTMGFGLPAAIGAQLAKPDEtVVAIVGDGGFQMTLQELSVIKELS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 465 LPVTIVIFNNG--GIYRgdgvdlsgagapSPTDLLHHARYD-----------KLMDAFRGVGYNVTTTDELRHALTTGIQ 531
Cdd:PRK07710 469 LPVKVVILNNEalGMVR------------QWQEEFYNQRYShsllscqpdfvKLAEAYGIKGVRIDDELEAKEQLQHAIE 536
|
....*....
gi 16130305 532 SRKPTIINV 540
Cdd:PRK07710 537 LQEPVVIDC 545
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
2-544 |
1.19e-37 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 146.68 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 2 SDQLQMTDGMHIIVEALKQNNIDTIYGVVGipvTD-------MARhAQAEGI---RYIGFRHEQSAGYAAAASGFLTQKP 71
Cdd:PRK08327 1 SMALTMYTAAELFLELLKELGVDYIFINSG---TDyppiieaKAR-ARAAGRplpEFVICPHEIVAISMAHGYALVTGKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 72 GICLTVSAPGFLNGLTALANATVNGFPMIMISGSS-----------DRAIVDLQqgdyEELDQMNAAKPYAKAAFRVNQP 140
Cdd:PRK08327 77 QAVMVHVDVGTANALGGVHNAARSRIPVLVFAGRSpyteegelgsrNTRIHWTQ----EMRDQGGLVREYVKWDYEIRRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 141 QDLGIALARAIRVSVSGRPGGVYLDLPANVLAATMEKDEALTTIvkveNPSPALL-PCPKSVTSAISLLAKAERPLIILG 219
Cdd:PRK08327 153 DQIGEVVARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKADAGR----QMAPAPPaPDPEDIARAAEMLAAAERPVIITW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 220 KGAAYSQADEQLREFIESAQIP---FLPMSMAkgiLEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGKKgwAADT 296
Cdd:PRK08327 229 RAGRTAEGFASLRRLAEELAIPvveYAGEVVN---YPSDHPLHLGPDPRADLAEADLVLVVDSDVPWIPKKIRP--DADA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 297 QFIQLDIEPQEIDS---NRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRD----ILNIHKQQNAQKMHEKLS-TDTQ 368
Cdd:PRK08327 304 RVIQIDVDPLKSRIplwGFPCDLCIQADTSTALDQLEERLKSLASAERRRARRrraaVRELRIRQEAAKRAEIERlKDRG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 369 PLNYFNALSAVRDVLRENQDIylVNEGANTLDNARniidMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGS-PVVAIEGD 447
Cdd:PRK08327 384 PITPAYLSYCLGEVADEYDAI--VTEYPFVPRQAR----LNKPGSYFGDGSAGGLGWALGAALGAKLATPDrLVIATVGD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 448 SAFGFSgmeIETIC-----RYNLPVTIVIFNNGG----------IYRgDGVDLSGAGAPSpTDLLHHARYDKLMDAFRGV 512
Cdd:PRK08327 458 GSFIFG---VPEAAhwvaeRYGLPVLVVVFNNGGwlavkeavleVYP-EGYAARKGTFPG-TDFDPRPDFAKIAEAFGGY 532
|
570 580 590
....*....|....*....|....*....|....*.
gi 16130305 513 GYNVTTTDELRHALTTGI----QSRKPTIINVVIDP 544
Cdd:PRK08327 533 GERVEDPEELKGALRRALaavrKGRRSAVLDVIVDR 568
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
10-544 |
4.99e-37 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 144.95 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVGIPVTDM--ARHAQaEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLT 87
Cdd:PRK06965 23 GAEILMKALAAEGVEFIWGYPGGAVLYIydELYKQ-DKIQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTNAVT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 88 ALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLP 167
Cdd:PRK06965 102 GIATAYMDSIPMVVISGQVPTAAIGQDA--FQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDIP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 168 ANVlaaTMEKDE-ALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMS 246
Cdd:PRK06965 180 KDV---SKTPCEyEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 247 MAKGILEDTHP-------LSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAA-DTQFIQLDIEPQEIDSNRPIAVPV 318
Cdd:PRK06965 257 MGLGAYPASDKkflgmlgMHGTYEANMAMQHCDVLIAIGARFDDRVIGNPAHFASrPRKIIHIDIDPSSISKRVKVDIPI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 319 VGDIASSMQGMLAELKQNTF---TTPLV--WRDILNIHKQQNaqkMHEKLSTDTQPLNYfnalsaVRDVLRE--NQDIYL 391
Cdd:PRK06965 337 VGDVKEVLKELIEQLQTAEHgpdADALAqwWKQIEGWRSRDC---LKYDRESEIIKPQY------VVEKLWEltDGDAFV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 392 VNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIV 470
Cdd:PRK06965 408 CSDVGQHQMWAAQFYRFNEPRRWINSGGLGTMGVGLPYAMGIKMAHpDDDVVCITGEGSIQMCIQELSTCLQYDTPVKII 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130305 471 IFNN---GGIYRGDGVDLSGAGAPSPTDLLhhARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTI-INVVIDP 544
Cdd:PRK06965 488 SLNNrylGMVRQWQEIEYSKRYSHSYMDAL--PDFVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRTVfLDFQTDP 563
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
10-542 |
7.41e-36 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 141.80 E-value: 7.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 10 GMHIIVEALKQNNIDTIYGVVGipVTDMARH---AQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGL 86
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPG--GASMEIHqalTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 87 TALANATVNGFPMIMISGSSDRAIVDLQQgdYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDL 166
Cdd:PLN02470 93 TGLADALLDSVPLVAITGQVPRRMIGTDA--FQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 167 PanvlaatmeKDEALTTIVKVENPsPALLP-----CPKSVTSA-----ISLLAKAERPLIILGKGAaySQADEQLREFIE 236
Cdd:PLN02470 171 P---------KDIQQQLAVPNWNQ-PMKLPgylsrLPKPPEKSqleqiVRLISESKRPVVYVGGGC--LNSSEELREFVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 237 SAQIPFLPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEID 309
Cdd:PLN02470 239 LTGIPVASTLMGLGAFPASDELSLqmlgmhgTVYANYAVDSADLLLAFGVRFDDRVTGKLEAFASRASIVHIDIDPAEIG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 310 SNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLV--WRDILNIHKQQNaqkmheklstdtqPLNYfnalSAVRDVLRENQ 387
Cdd:PLN02470 319 KNKQPHVSVCADVKLALQGLNKLLEERKAKRPDFsaWRAELDEQKEKF-------------PLSY----PTFGDAIPPQY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 388 DIYLVNEgantLDNARNII-------DMY--------KPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFG 451
Cdd:PLN02470 382 AIQVLDE----LTDGNAIIstgvgqhQMWaaqwykykEPRRWLTSGGLGAMGFGLPAAIGAAAANpDAIVVDIDGDGSFI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 452 FSGMEIETICRYNLPVTIVIFNNGGI----------YRGDGVDlSGAGAPSPTDLLhHARYDKLMDAFRGVGYNVTTTDE 521
Cdd:PLN02470 458 MNIQELATIHVENLPVKIMVLNNQHLgmvvqwedrfYKANRAH-TYLGDPDAEAEI-FPDFLKFAEGCKIPAARVTRKSD 535
|
570 580
....*....|....*....|.
gi 16130305 522 LRHALTTGIQSRKPTIINVVI 542
Cdd:PLN02470 536 LREAIQKMLDTPGPYLLDVIV 556
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
7-544 |
9.32e-36 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 140.74 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 7 MTDGMHIIVEALKQNNIDTIYGVVGI---PVTDMARHAQaegIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFL 83
Cdd:PRK06457 1 MPSVAEVIIRVLEDNGIQRIYGIPGDsidPLVDAIRKSK---VKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 84 NGLTALANATVNGFPMIMISGSSDraiVDLQQGDYeeLDQMNAAKPYAKAAF---RVNQPQDLGIALARAIRVSVSGRpG 160
Cdd:PRK06457 78 HLLNGLYDAKMDHAPVIALTGQVE---SDMIGHDY--FQEVNLTKLFDDVAVfnqILINPENAEYIIRRAIREAISKR-G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 161 GVYLDLPANVLAATMEKDEALTTIVkvenPSPALLPCPKsvtSAISLLAKAERPLIILGKGAaySQADEQLREFIESAQI 240
Cdd:PRK06457 152 VAHINLPVDILRKSSEYKGSKNTEV----GKVKYSIDFS---RAKELIKESEKPVLLIGGGT--RGLGKEINRFAEKIGA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 241 PFLPMSMAKGILEDTHPLSA-------AAARSFALANADVVMLVGARLNWLLAHGKkgwaaDTQFIQLDIEPQEIDSNRP 313
Cdd:PRK06457 223 PIIYTLNGKGILPDLDPKVMggigllgTKPSIEAMDKADLLIMLGTSFPYVNFLNK-----SAKVIQVDIDNSNIGKRLD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 314 IAVPVVGDIASSMQGMLAElKQNTFTTPLV-----WRDilNIHKQQNaqkmheKLSTDTQPlnyfNALSAVRDVLRENQD 388
Cdd:PRK06457 298 VDLSYPIPVAEFLNIDIEE-KSDKFYEELKgkkedWLD--SISKQEN------SLDKPMKP----QRVAYIVSQKCKKDA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 389 IYLVNEGANTLDNARNIidMYKPRRRLDCGTW-GVMGIGMGYAIGASVTSGSP--VVAIEGDSAFGFSGMEIETICRYNL 465
Cdd:PRK06457 365 VIVTDTGNVTMWTARHF--RASGEQTFIFSAWlGSMGIGVPGSVGASFAVENKrqVISFVGDGGFTMTMMELITAKKYDL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 466 PVTIVIFNN---GGI--------YRGDGVDlsgagapsptdlLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRK 534
Cdd:PRK06457 443 PVKIIIYNNsklGMIkfeqevmgYPEWGVD------------LYNPDFTKIAESIGFKGFRLEEPKEAEEIIEEFLNTKG 510
|
570
....*....|
gi 16130305 535 PTIINVVIDP 544
Cdd:PRK06457 511 PAVLDAIVDP 520
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
15-474 |
8.40e-35 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 138.57 E-value: 8.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 15 VEALKQNNIDTIYGVVGIPVTDMARHAQAEG-IRYIGFRHEQSAGYAAAAsgFLTQKPG---ICLTVSAPGFLNGLTALA 90
Cdd:PRK11269 11 VLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAEG--YTRATAGnigVCIGTSGPAGTDMITGLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 91 NATVNGFPMIMISGSSDRAIvdLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPANV 170
Cdd:PRK11269 89 SASADSIPILCITGQAPRAR--LHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPVLIDLPFDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 171 LAATMEKDEALTTIVKVENPSPAllpcPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKG 250
Cdd:PRK11269 167 QVAEIEFDPDTYEPLPVYKPAAT----RAQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVPVIPTLMGWG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 251 ILEDTHPLSAAAARSFAL---ANA-----DVVMLVGARlnWLLAH--GKKGWAADTQFIQLDIEPQEIDSNRPIAVPVVG 320
Cdd:PRK11269 243 AIPDDHPLMAGMVGLQTShryGNAtllasDFVLGIGNR--WANRHtgSVEVYTKGRKFVHVDIEPTQIGRVFGPDLGIVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 321 DIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLN---YFNALSAV--RDVlrenqdIYLVNEG 395
Cdd:PRK11269 321 DAKAALELLVEVAREWKAAGRLPDRSAWVADCQERKRTLLRKTHFDNVPIKpqrVYEEMNKAfgRDT------CYVSTIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 396 ANTLDNARnIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNN 474
Cdd:PRK11269 395 LSQIAAAQ-FLHVYKPRHWINCGQAGPLGWTIPAALGVRAADpDRNVVALSGDYDFQFLIEELAVGAQFNLPYIHVLVNN 473
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
201-327 |
4.87e-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: 4.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 201 VTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKGILEDTHP-------LSAAAARSFALANADV 273
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPlylgmlgMHGTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 16130305 274 VMLVGARLNWLLAHGKKG-WAADTQFIQLDIEPQEIDSNRPIAVPVVGDIASSMQ 327
Cdd:pfam00205 81 VLAVGARFDDIRTTGKLPeFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLE 135
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
6-540 |
1.65e-33 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 134.35 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 6 QMTDGMHIIVEALKQNNIDTIYGVVGI---PVTD-MARHaqaEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPG 81
Cdd:PRK07064 1 EKVTVGELIAAFLEQCGVKTAFGVISIhnmPILDaIGRR---GKIRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 82 FLNGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEEL-DQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPG 160
Cdd:PRK07064 78 AGNAAGALVEALTAGTPLLHITGQIETPYLDQDLGYIHEApDQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 161 GVYLDLPANVLAATMEKDEALTTIvkvenPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAysQADEQLREFIEsAQI 240
Cdd:PRK07064 158 PVSVEIPIDIQAAEIELPDDLAPV-----HVAVPEPDAAAVAELAERLAAARRPLLWLGGGAR--HAGAEVKRLVD-LGF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 241 PFLPMSMAKGILEDTHPLS-----AAAARSFALANADVVMLVGARL------NWLLahgkkgwAADTQFIQLDIEPQEID 309
Cdd:PRK07064 230 GVVTSTQGRGVVPEDHPASlgafnNSAAVEALYKTCDLLLVVGSRLrgnetlKYSL-------ALPRPLIRVDADAAADG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 310 SNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHkQQNAQKMHEKLStdtqplNYFNALSAVRDVLREN--- 386
Cdd:PRK07064 303 RGYPNDLFVHGDAARVLARLADRLEGRLSVDPAFAADLRAAR-EAAVADLRKGLG------PYAKLVDALRAALPRDgnw 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 387 -QDIYLVNegaNTLDNarNIIDMYKPRRRLDcGTWGVMGIGMGYAIGASV-TSGSPVVAIEGDSAFGFSGMEIETICRYN 464
Cdd:PRK07064 376 vRDVTISN---STWGN--RLLPIFEPRANVH-ALGGGIGQGLAMAIGAALaGPGRKTVGLVGDGGLMLNLGELATAVQEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 465 LPVTIVIFNNGGiYrgdGV-----DLSGAGAPSPTDlLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIIN 539
Cdd:PRK07064 450 ANMVIVLMNDGG-Y---GVirniqDAQYGGRRYYVE-LHTPDFALLAASLGLPHWRVTSADDFEAVLREALAKEGPVLVE 524
|
.
gi 16130305 540 V 540
Cdd:PRK07064 525 V 525
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
395-540 |
1.42e-27 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 108.06 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 395 GANTLDNARNIiDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFN 473
Cdd:pfam02775 3 GCHQMWAAQYY-RFRPPRRYLTSGGLGTMGYGLPAAIGAKLARpDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLN 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130305 474 NG--GIYRGdGVDLSGAGAPSPTD--LLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINV 540
Cdd:pfam02775 82 NGgyGMTRG-QQTPFGGGRYSGPSgkILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
376-542 |
4.19e-27 |
|
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: 107.34 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 376 LSAVRDVLREnqDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSG 454
Cdd:cd00568 3 LAALRAALPE--DAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAApDRPVVCIAGDGGFMMTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 455 MEIETICRYNLPVTIVIFNNGG---IYRGDGVdlSGAGAPSPTDlLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQ 531
Cdd:cd00568 81 QELATAVRYGLPVIVVVFNNGGygtIRMHQEA--FYGGRVSGTD-LSNPDFAALAEAYGAKGVRVEDPEDLEAALAEALA 157
|
170
....*....|.
gi 16130305 532 SRKPTIINVVI 542
Cdd:cd00568 158 AGGPALIEVKT 168
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
98-544 |
1.15e-25 |
|
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: 111.02 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 98 PMIMISGSSDRAIVD--------LQQGDYEelDQMNAAKPYAKAAFRVNqPQDlgiALA---RAIRVSVS-GRPggVYLD 165
Cdd:COG3961 95 PVVHIVGAPGTRAQRrgpllhhtLGDGDFD--HFLRMFEEVTVAQAVLT-PEN---AAAeidRVLAAALReKRP--VYIE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 166 LPANVLAATMEKDEALTTIVKVENPSPALlpcpKSVTSAI-SLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLP 244
Cdd:COG3961 167 LPRDVADAPIEPPEAPLPLPPPASDPAAL----AAAVAAAaERLAKAKRPVILAGVEVHRFGLQEELLALAEKTGIPVAT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 245 MSMAKGILEDTHP--------LSAAAARSFALANADVVMLVGARLN-WLLAhgkkGWAAD---TQFIqlDIEPQEIDSNR 312
Cdd:COG3961 243 TLLGKSVLDESHPqfigtyagAASSPEVREYVENADCVLCLGVVFTdTNTG----GFTAQldpERTI--DIQPDSVRVGG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 313 PIAVPVvgDIASSMQGMLAELKQNTFTTPLVwrdilnihkqqnAQKMHEKLSTDTQPLNYFNALSAVRDVLRENqDIYLV 392
Cdd:COG3961 317 HIYPGV--SLADFLEALAELLKKRSAPLPAP------------APPPPPPPAAPDAPLTQDRLWQRLQAFLDPG-DIVVA 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 393 NEGantlDNARNIIDMYKPRR-RLDCGT-WGVMGIGMGYAIGASVtsGSP---VVAIEGDSAFGFSGMEIETICRYNLPV 467
Cdd:COG3961 382 DTG----TSLFGAADLRLPEGaTFIAQPlWGSIGYTLPAALGAAL--AAPdrrVILLVGDGAFQLTAQELSTMLRYGLKP 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 468 TIVIFNNGG------IYRGDGvdlsgagapsPTDLLHHARYDKLMDAFRG---VGYNVTTTDELRHALTTGIQSRK-PTI 537
Cdd:COG3961 456 IIFVLNNDGytieraIHGPDG----------PYNDIANWDYAKLPEAFGGgnaLGFRVTTEGELEEALAAAEANTDrLTL 525
|
....*..
gi 16130305 538 INVVIDP 544
Cdd:COG3961 526 IEVVLDK 532
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
14-546 |
3.97e-22 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 100.06 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 14 IVEALKQNNIDTIYGVVGI---PVTDMARhaQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALA 90
Cdd:PRK06546 9 LVEQLVAAGVKRIYGIVGDslnPIVDAVR--RTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLINGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 91 NATVNGFPMIMIS--------GSS-------DRAIVDLQqgDYEELdqmnaakpyakaafrVNQPQDLGIALARAIRVSV 155
Cdd:PRK06546 87 DAHRSGAPVLAIAshipsaqiGSGffqethpDRLFVECS--GYCEM---------------VSSAEQAPRVLHSAIQHAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 156 sGRPGGVYLDLPANVlaaTMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYsqADEQLREFI 235
Cdd:PRK06546 150 -AGGGVSVVTLPGDI---ADEPAPEGFAPSVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRG--AHAEVLALA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 236 ESAQIPF-----------------LPMSmakGIL------EDTHplsaaaarsfalaNADVVMLVGARL---NWLlahgk 289
Cdd:PRK06546 224 EKIKAPVghslrgkewiqydnpfdVGMS---GLLgygaahEAMH-------------EADLLILLGTDFpydQFL----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 290 kgwaADTQFIQLDIEPQEIDSNRPIAVPVVGDIASSMQGMLAELKQNTFttplvwRDILNIHKQQNAQKMHEKLSTDT-- 367
Cdd:PRK06546 283 ----PDVRTAQVDIDPEHLGRRTRVDLAVHGDVAETIRALLPLVKEKTD------RRFLDRMLKKHARKLEKVVGAYTrk 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 368 ----QPLNYFNALSAVRDVLRENQdIYLVNEGANTLDNARNIidMYKPRRRLdCGTW--GVMGIGMGYAIGASVTS-GSP 440
Cdd:PRK06546 353 vekhTPIHPEYVASILDELAADDA-VFTVDTGMCNVWAARYI--TPNGRRRV-IGSFrhGSMANALPHAIGAQLADpGRQ 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 441 VVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNG--GIYRgdgVDLSGAGAPS-PTDlLHHARYDKLMDAFRGVGYNVT 517
Cdd:PRK06546 429 VISMSGDGGLSMLLGELLTVKLYDLPVKVVVFNNStlGMVK---LEMLVDGLPDfGTD-HPPVDYAAIAAALGIHAVRVE 504
|
570 580
....*....|....*....|....*....
gi 16130305 518 TTDELRHALTTGIQSRKPTIINVVIDPAA 546
Cdd:PRK06546 505 DPKDVRGALREAFAHPGPALVDVVTDPNA 533
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
389-546 |
6.93e-22 |
|
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: 92.98 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 389 IYLVNEGANTLDNARNIiDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPV 467
Cdd:cd02014 20 IFTIDVGNVTVWAARHL-RMNGKQRFILSGLLATMGNGLPGAIAAKLAYpDRQVIALSGDGGFAMLMGDLITAVKYNLPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 468 TIVIFNNGGI------YRGDGVDLSGagapspTDlLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVV 541
Cdd:cd02014 99 IVVVFNNSDLgfikweQEVMGQPEFG------VD-LPNPDFAKIAEAMGIKGIRVEDPDELEAALDEALAADGPVVIDVV 171
|
....*
gi 16130305 542 IDPAA 546
Cdd:cd02014 172 TDPNE 176
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
377-542 |
4.38e-21 |
|
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: 90.73 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 377 SAVRDVLREnqDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTwGVMGIGMGYAIGASV-TSGSPVVAIEGDSAFGFSGM 455
Cdd:cd02002 8 AALAAALPE--DAIIVDEAVTNGLPLRDQLPLTRPGSYFTLRG-GGLGWGLPAAVGAALaNPDRKVVAIIGDGSFMYTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 456 EIETICRYNLPVTIVIFNNGG--IYRGD----GVDLSGAGAPSPTDLLH-HARYDKLMDAFRGVGYNVTTTDELRHALTT 528
Cdd:cd02002 85 ALWTAARYGLPVTVVILNNRGygALRSFlkrvGPEGPGENAPDGLDLLDpGIDFAAIAKAFGVEAERVETPEELDEALRE 164
|
170
....*....|....
gi 16130305 529 GIQSRKPTIINVVI 542
Cdd:cd02002 165 ALAEGGPALIEVVV 178
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
406-546 |
2.02e-20 |
|
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: 89.09 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 406 IDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNggiyRGDGV- 483
Cdd:cd02015 35 YRFKKPRSWLTSGGLGTMGFGLPAAIGAKVARpDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNN----GSLGMv 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130305 484 ----DLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAA 546
Cdd:cd02015 111 rqwqELFYEGRYSHTTLDSNPDFVKLAEAYGIKGLRVEKPEELEAALKEALASDGPVLLDVLVDPEE 177
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
367-547 |
4.41e-20 |
|
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: 88.34 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 367 TQPLNYFNALSAVRDVLREnqDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIE 445
Cdd:cd02013 1 GNPMHPRQVLRELEKAMPE--DAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCGYALPAIIGAKAAApDRPVVAIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 446 GDSAFGFSGMEIETICRYNLPVTIVIFNNG--GIYRGDGVD-----LSGAGAPSPtdllhhaRYDKLMDAFRGVGYNVTT 518
Cdd:cd02013 79 GDGAWGMSMMEIMTAVRHKLPVTAVVFRNRqwGAEKKNQVDfynnrFVGTELESE-------SFAKIAEACGAKGITVDK 151
|
170 180 190
....*....|....*....|....*....|..
gi 16130305 519 TDELRHALTTGIQSR---KPTIINVVIDPAAG 547
Cdd:cd02013 152 PEDVGPALQKAIAMMaegKTTVIEIVCDQELG 183
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
14-545 |
3.55e-17 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 84.96 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 14 IVEALKQNNIDTIYGVVG--IPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALAN 91
Cdd:PRK08273 9 ILERLREWGVRRVFGYPGdgINGLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLLNGLYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 92 ATVNGFPMIMISGSSDRAIVDlqqGDY-EELDQMNAAKPYAKA-AFRVNQPQDLGIALARAIRVSVSGRpGGVYLDLPAN 169
Cdd:PRK08273 89 AKLDHVPVVAIVGQQARAALG---GHYqQEVDLQSLFKDVAGAfVQMVTVPEQLRHLVDRAVRTALAER-TVTAVILPND 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 170 V--LAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAysQADEQLREFIE----------- 236
Cdd:PRK08273 165 VqeLEYEPPPHAHGTVHSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGAL--GATDEVIAVAErlgagvakall 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 237 -----SAQIPFLPMSMakGILeDTHPlsaaaaRSFALANADVVMLVGARLNWllahgkkgwaadTQF---------IQLD 302
Cdd:PRK08273 243 gkaalPDDLPWVTGSI--GLL-GTKP------SYELMRECDTLLMVGSSFPY------------SEFlpkegqargVQID 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 303 IEPQEIdSNR-PIAVPVVGDIASSMQGMLAELKQNTFTTplvWRDIL--NIHKQQnaQKMHEKLSTDTQPLN---YFNAL 376
Cdd:PRK08273 302 IDGRML-GLRyPMEVNLVGDAAETLRALLPLLERKKDRS---WRERIekWVARWW--ETLEARAMVPADPVNpqrVFWEL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 377 SAvrdVLRENQdIYLVNEGANTLDNARNIidmyKPRRRLDC---GTWGVMGIGMGYAIGAS-VTSGSPVVAIEGDSAFGF 452
Cdd:PRK08273 376 SP---RLPDNA-ILTADSGSCANWYARDL----RMRRGMMAslsGTLATMGPAVPYAIAAKfAHPDRPVIALVGDGAMQM 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 453 SGM-EIETICRY-----NLPVTIVIFNNGgiyrgdgvDLSG--------AGAP--SPTDLL---HHARYDKLMdAFRGVg 513
Cdd:PRK08273 448 NGMaELITVAKYwrqwsDPRLIVLVLNNR--------DLNQvtweqrvmEGDPkfEASQDLpdvPYARFAELL-GLKGI- 517
|
570 580 590
....*....|....*....|....*....|..
gi 16130305 514 yNVTTTDELRHALTTGIQSRKPTIINVVIDPA 545
Cdd:PRK08273 518 -RVDDPEQLGAAWDEALAADRPVVLEVKTDPN 548
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
78-543 |
2.06e-16 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 82.31 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 78 SAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQ----QGDYEELdqmnaAKPYAKAAFRVNQPQDLGIALARAIRV 153
Cdd:PRK07092 81 SAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEpflaAVQAAEL-----PKPYVKWSIEPARAEDVPAAIARAYHI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 154 SVSGRPGGVYLDLPANVLAATMEkDEALTTIVKVENPSPALLpcpksvTSAISLLAKAERPLIILGKGAAYSQADEQLRE 233
Cdd:PRK07092 156 AMQPPRGPVFVSIPYDDWDQPAE-PLPARTVSSAVRPDPAAL------ARLGDALDAARRPALVVGPAVDRAGAWDDAVR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 234 FIESAQIP---------------------FLPMSMAKgILE--DTHplsaaaarsfalanaDVVMLVGARLNWLLAHGKK 290
Cdd:PRK07092 229 LAERHRAPvwvapmsgrcsfpedhplfagFLPASREK-ISAllDGH---------------DLVLVIGAPVFTYHVEGPG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 291 GWAAD-TQFIQLDIEPQEIdSNRPIAVPVVGDIASSMQGMLAELKQNTFTTPlvwrdilnihkqqNAQKMHEKLSTDTQP 369
Cdd:PRK07092 293 PHLPEgAELVQLTDDPGEA-AWAPMGDAIVGDIRLALRDLLALLPPSARPAP-------------PARPMPPPAPAPGEP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 370 LNYFNALSAVRDVLRENqDIYlVNEGANTldnaRNIIDMYKPRRRLDCGTWGVMGiGMGYAIGASV-----TSGSPVVAI 444
Cdd:PRK07092 359 LSVAFVLQTLAALRPAD-AIV-VEEAPST----RPAMQEHLPMRRQGSFYTMASG-GLGYGLPAAVgvalaQPGRRVIGL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 445 EGDSAFGFSGMEIETICRYNLPVTIVIFNNG------------GIYRGDGVDLSGagapspTDLLHHARydklmdAFRGV 512
Cdd:PRK07092 432 IGDGSAMYSIQALWSAAQLKLPVTFVILNNGrygalrwfapvfGVRDVPGLDLPG------LDFVALAR------GYGCE 499
|
490 500 510
....*....|....*....|....*....|.
gi 16130305 513 GYNVTTTDELRHALTTGIQSRKPTIINVVID 543
Cdd:PRK07092 500 AVRVSDAAELADALARALAADGPVLVEVEVA 530
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
13-543 |
4.18e-16 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 81.19 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 13 IIVEALKQNNIDTIYGVVGIP---VTDMARhaQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTAL 89
Cdd:PRK09124 8 YIAKTLEQAGVKRIWGVTGDSlngLSDSLR--RMGTIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 90 ANATVNGFPMIMISG---SSDRAIVDLQQGDYEELdqmnaakpyakaaFR--------VNQPQDLGIALARAIRVSVSGR 158
Cdd:PRK09124 86 FDCHRNHVPVLAIAAhipSSEIGSGYFQETHPQEL-------------FRecshycelVSNPEQLPRVLAIAMRKAILNR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 159 pgGV-YLDLPANVLAATMEKDEALTTIVKvenPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAysQADEQLREFIES 237
Cdd:PRK09124 153 --GVaVVVLPGDVALKPAPERATPHWYHA---PQPVVTPAEEELRKLAALLNGSSNITLLCGSGCA--GAHDELVALAET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 238 AQIPFLPMSMAKGILEDTHPLSAA-------AARSFALANADVVMLVGARLNWllahgKKGWAADTQFIQLDIEPQEIDS 310
Cdd:PRK09124 226 LKAPIVHALRGKEHVEYDNPYDVGmtgligfSSGYHAMMNCDTLLMLGTDFPY-----RQFYPTDAKIIQIDINPGSLGR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 311 NRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVwrdilniHKQQNAQKMHEKL------STDTQPLN--YfnaLSAVRDV 382
Cdd:PRK09124 301 RSPVDLGLVGDVKATLAALLPLLEEKTDRKFLD-------KALEHYRKARKGLddlavpSDGGKPIHpqY---LARQISE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 383 LRENQDIYLVNEGANTLDNARnIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTS-GSPVVAIEGDSafGFSGM--EIET 459
Cdd:PRK09124 371 FAADDAIFTCDVGTPTVWAAR-YLKMNGKRRLLGSFNHGSMANAMPQALGAQAAHpGRQVVALSGDG--GFSMLmgDFLS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 460 ICRYNLPVTIVIFNNG-----------GIYRGDGVDLsgagapSPTDLlhhARYDKLMDAFrgvGYNVTTTDELRHALTT 528
Cdd:PRK09124 448 LVQLKLPVKIVVFNNSvlgfvamemkaGGYLTDGTDL------HNPDF---AAIAEACGIT---GIRVEKASELDGALQR 515
|
570
....*....|....*
gi 16130305 529 GIQSRKPTIINVVID 543
Cdd:PRK09124 516 AFAHDGPALVDVVTA 530
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
376-543 |
3.22e-15 |
|
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: 73.86 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 376 LSAVRDVLREnQDIYLVNEGANTLDNARNIiDMYKPRRRLDCGTWGVMGIGMGYAIGAS-VTSGSPVVAIEGDSAFGFSG 454
Cdd:cd02010 5 VHDLRAVMGD-DDIVLLDVGAHKIWMARYY-RTYAPNTCLISNGLATMGVALPGAIGAKlVYPDRKVVAVSGDGGFMMNS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 455 MEIETICRYNLPVTIVIFNNGG-----------IYRGDGVDLsgagapSPTDLLHHArydklmDAFRGVGYNVTTTDELR 523
Cdd:cd02010 83 QELETAVRLKIPLVVLIWNDNGyglikwkqekeYGRDSGVDF------GNPDFVKYA------ESFGAKGYRIESADDLL 150
|
170 180
....*....|....*....|
gi 16130305 524 HALTTGIQSRKPTIINVVID 543
Cdd:cd02010 151 PVLERALAADGVHVIDCPVD 170
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
13-170 |
1.06e-14 |
|
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: 71.81 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 13 IIVEALKQNNIDTIYGVVG---IPVTDMARHAqaEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTAL 89
Cdd:cd07039 5 VIVETLENWGVKRVYGIPGdsiNGLMDALRRE--GKIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 90 ANATVNGFPMIMISGSSDRAIV--DLQQgdyeELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRpgGV-YLDL 166
Cdd:cd07039 83 YDAKRDRAPVLAIAGQVPTDELgtDYFQ----EVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAIAKR--GVaVLIL 156
|
....
gi 16130305 167 PANV 170
Cdd:cd07039 157 PGDV 160
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
383-544 |
7.88e-14 |
|
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: 69.87 E-value: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 383 LRENqDIyLVNEGANTLDNARNIidMYKPRRRLDC-GTWGVMGIGMGYAIGASVTSGSP-VVAIEGDSAFGFSGMEIETI 460
Cdd:cd02005 15 LKPN-DI-LVAETGTSWFGALDL--KLPKGTRFISqPLWGSIGYSVPAALGAALAAPDRrVILLVGDGSFQMTVQELSTM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 461 CRYNLPVTIVIFNNGG--IYRgdgvdlsgagapsptdLLHHA----------RYDKLMDAF----RGVGYNVTTTDELRH 524
Cdd:cd02005 91 IRYGLNPIIFLINNDGytIER----------------AIHGPeasyndianwNYTKLPEVFggggGGLSFRVKTEGELDE 154
|
170 180
....*....|....*....|.
gi 16130305 525 ALTT-GIQSRKPTIINVVIDP 544
Cdd:cd02005 155 ALKDaLFNRDKLSLIEVILPK 175
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
67-542 |
5.85e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 64.89 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 67 LTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISGssDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIA 146
Cdd:PRK12474 65 IAGKPAVTLLHLGPGLANGLANLHNARRAASPIVNIVG--DHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 147 LARAIRVSVSGRPGGVYLDLPANvlaatMEKDEALTTIVKVENPSPALLPcPKSVTSAISLLAKAERPLIILgKGAAYSQ 226
Cdd:PRK12474 143 VARAVQAAQSAPGGIATLIMPAD-----VAWNEAAYAAQPLRGIGPAPVA-AETVERIAALLRNGKKSALLL-RGSALRG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 227 ADEQLREFIES---------------------AQIPFLPMSMAKGI--LEDthplsaaaarsfalanADVVMLVGAR--L 281
Cdd:PRK12474 216 APLEAAGRIQAktgvrlycdtfapriergagrVPIERIPYFHEQITafLKD----------------VEQLVLVGAKppV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 282 NWLLAHGKKGWAA--DTQFIQLdIEPQEidsnrpiavpvvgDIASSMQGMLAELK---QNTFTTPLVWRDIlnihkqqna 356
Cdd:PRK12474 280 SFFAYPGKPSWGAppGCEIVYL-AQPDE-------------DLAQALQDLADAVDapaEPAARTPLALPAL--------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 357 qkmheklstdtqPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARNII-DMYKPRRRLDCgTWGVMGIGMGYAIGASV 435
Cdd:PRK12474 337 ------------PKGALNSLGVAQLIAHRTPDQAIYADEALTSGLFFDMSyDRARPHTHLPL-TGGSIGQGLPLAAGAAV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 436 TS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGiYRGDGVDLS--GAGAPSPTDL----LHHARYDkLMDA 508
Cdd:PRK12474 404 AApDRKVVCPQGDGGAAYTMQALWTMARENLDVTVVIFANRS-YAILNGELQrvGAQGAGRNALsmldLHNPELN-WMKI 481
|
490 500 510
....*....|....*....|....*....|....*..
gi 16130305 509 FRGVGYN---VTTTDELRHALTTGIQSRKPTIINVVI 542
Cdd:PRK12474 482 AEGLGVEasrATTAEEFSAQYAAAMAQRGPRLIEAMI 518
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
427-551 |
2.78e-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: 60.01 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 427 MGYAIGASVTS-----GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGI--------------------YRGD 481
Cdd:cd02003 50 MGYEIAAGLGAklakpDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGFgcinnlqestgsgsfgtefrDRDQ 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130305 482 GVdLSGAGAPSPTDLLHHArydklmdafRGVG---YNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESG 551
Cdd:cd02003 130 ES-GQLDGALLPVDFAANA---------RSLGarvEKVKTIEELKAALAKAKASDRTTVIVIKTDPKSMTPGY 192
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
419-542 |
1.16e-09 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 60.63 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 419 TWGVMGIGMGYAIGASVTS-GSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGiYRGDGVDLSGAGAPSPTDL- 496
Cdd:PRK07586 383 TGGAIGQGLPLATGAAVACpDRKVLALQGDGSAMYTIQALWTQARENLDVTTVIFANRA-YAILRGELARVGAGNPGPRa 461
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16130305 497 -----LHHARYD--KLMDAFrGV-GYNVTTTDELRHALTTGIQSRKPTIINVVI 542
Cdd:PRK07586 462 ldmldLDDPDLDwvALAEGM-GVpARRVTTAEEFADALAAALAEPGPHLIEAVV 514
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
421-543 |
1.03e-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: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 421 GVMGI--GMGYAIGASVTSGSPVVAIEGDSAF-----GFSGMEIETicrynLPVTIVIFNN--GGIYRGdgvdLSGAGAP 491
Cdd:cd02009 49 GASGIdgTLSTALGIALATDKPTVLLTGDLSFlhdlnGLLLGKQEP-----LNLTIVVINNngGGIFSL----LPQASFE 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130305 492 SPTDLLHHARYD---KLMDAFRGVGY-NVTTTDELRHALTTGIQSRKPTIINVVID 543
Cdd:cd02009 120 DEFERLFGTPQGldfEHLAKAYGLEYrRVSSLDELEQALESALAQDGPHVIEVKTD 175
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
13-168 |
1.63e-06 |
|
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: 48.11 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130305 13 IIVEALKQNNIDTIYGVVG---IPVTDMARHAQaeGIRYIGFRHEQSAGYAAAASGFLTqKPGICLTVSAPGFLNGLTAL 89
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGdeiSSLLDALREGD--KRIIDTVIHELGAAGAAAGYARAG-GPPVVIVTSGTGLLNAINGL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130305 90 ANATVNGFPMIMISGssDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGrPGGVYLDLPA 168
Cdd:cd06586 79 ADAAAEHLPVVFLIG--ARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAS-QGPVVVRLPR 154
|
|
| TPP_Gcl |
cd02006 |
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ... |
402-474 |
1.71e-04 |
|
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: 43.04 E-value: 1.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130305 402 ARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGasVTSGSP---VVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNN 474
Cdd:cd02006 38 GAQMLHVYKPRHWINCGQAGPLGWTVPAALG--VAAADPdrqVVALSGDYDFQFMIEELAVGAQHRIPYIHVLVNN 111
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
408-475 |
6.70e-04 |
|
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: 40.72 E-value: 6.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130305 408 MYKPRRRLDCGTwgVMGIGMGYAIGAS-VTSGSPVVAIEGDSAFGFSGME--IETIcrYN-LPVTIVIFNNG 475
Cdd:cd02008 40 ALPPLNAIDTCT--CMGASIGVAIGMAkASEDKKVVAVIGDSTFFHSGILglINAV--YNkANITVVILDNR 107
|
|
| |
