|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09259 |
PRK09259 |
putative oxalyl-CoA decarboxylase; Validated |
5-552 |
0e+00 |
|
putative oxalyl-CoA decarboxylase; Validated
Pssm-ID: 236433 [Multi-domain] Cd Length: 569 Bit Score: 532.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PRK09259 11 DGFHLVIDALKLNGIDTIYGVVGIPITDLARLAQAEGIRYIGFRHEQSAGNAAAAAGFLTQKPGVCLTVSAPGFLNGLTA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRN----QEttGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDI 160
Cdd:PRK09259 91 LANATTNCFPMIMISGSSEREivdlQQ--GDYEELDQLNAAKPFCKAAFRVNRAEDIGIGVARAIRTAVSGRPGGVYLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 161 AGDMVNAKID-----RATVRFVSccPAPPVSQADcREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFL 235
Cdd:PRK09259 169 PAKVLAQTMDadealTSLVKVVD--PAPAQLPAP-EAVDRALDLLKKAKRPLIILGKGAAYAQADEQIREFVEKTGIPFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 236 PTPMGKGVLPDDHPNCVAAARSRALLQADVIVLLGARLNWILHFGFPPRFSANVKIIQVDLCAEELSNNVRAASALLGDI 315
Cdd:PRK09259 246 PMSMAKGLLPDTHPQSAAAARSLALANADVVLLVGARLNWLLSHGKGKTWGADKKFIQIDIEPQEIDSNRPIAAPVVGDI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 316 KMVTSQLLETVRSESWRFPSDsqWWATLREKITANAQITKALSLQTTLPMNYYTAFHHISELLPK--DCIIVSEGANTMD 393
Cdd:PRK09259 326 GSVMQALLAGLKQNTFKAPAE--WLDALAERKEKNAAKMAEKLSTDTQPMNFYNALGAIRDVLKEnpDIYLVNEGANTLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 394 IGRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVleqaqRFGQKVVCVEGDSAFGFSGMEAETMCRYKLPIIIIVINNN 473
Cdd:PRK09259 404 LARNIIDMYKPRHRLDCGTWGVMGIGMGYAIAAAV-----ETGKPVVAIEGDSAFGFSGMEVETICRYNLPVTVVIFNNG 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47085819 474 GIYSGVDpetwkamEKMGDMTTIApPVTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQDSLKNTQmPSLLNVLIDPT 552
Cdd:PRK09259 479 GIYRGDD-------VNLSGAGDPS-PTVLVHHARYDKMMEAFGGVGYNVTTPDELRHALTEAIASGK-PTLINVVIDPA 548
|
|
| oxalate_oxc |
TIGR03254 |
oxalyl-CoA decarboxylase; In a number of bacteria, including Oxalobacter formigenes from the ... |
5-552 |
9.60e-170 |
|
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: 492.81 E-value: 9.60e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:TIGR03254 4 DGFHLVIDALKLNGINTIYGVVGIPVTDLARLAQAKGMRYIGFRHEQSAGYAAAAAGFLTQKPGVCLTVSAPGFLNGLTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRN--QETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIA- 161
Cdd:TIGR03254 84 LANATTNCFPMIMISGSSERHivDLQQGDYEEMDQLAAAKPFAKAAYRVLRAEDIGIGIARAIRTAVSGRPGGVYLDLPa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 162 ---GDMVNA-KIDRATVRFVSccPAPPVSQADcREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPT 237
Cdd:TIGR03254 164 avlGQTMEAeKAKKTLVKVVD--PAPKQLPSP-DSVDRAVELLKDAKRPLILLGKGAAYAQADEEIREFVEKTGIPFLPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 238 PMGKGVLPDDHPNCVAAARSRALLQADVIVLLGARLNWILHFGFPPRFSANVKIIQVDLCAEELSNNVRAASALLGDIKM 317
Cdd:TIGR03254 241 SMAKGLLPDTHPQSAAAARSFALAEADVVMLVGARLNWLLSHGKGKLWGEDAKFIQVDIEPTEMDSNRPIAAPVVGDIGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 318 VTSQLLETVRSESWRFPSDsqWWATLREKITAN-AQITKALSLQTTlPMNYYTAFHHISELLPK--DCIIVSEGANTMDI 394
Cdd:TIGR03254 321 VVQALLSAAKNGGVKPPAD--WRNAIKTKSEKNvAKMAERLSASES-PMNYHGALEAIRDVLKDnpDIYLVNEGANTLDL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 395 GRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVleqaqRFGQKVVCVEGDSAFGFSGMEAETMCRYKLPIIIIVINNNG 474
Cdd:TIGR03254 398 ARNVIDMYKPRHRLDVGTWGVMGIGMGYAIAAAV-----ETGKPVVALEGDSAFGFSGMEVETICRYNLPVCVVIFNNGG 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47085819 475 IYSGVDPetwkamekmgDMTTIAP-PVTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQDSLKNTQmPSLLNVLIDPT 552
Cdd:TIGR03254 473 IYRGDDV----------NVVGADPaPTVLVHGARYDKMMKAFGGVGYNVTTPDELKAALNEALASGK-PTLINAVIDPS 540
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
3-552 |
2.12e-136 |
|
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: 407.24 E-value: 2.12e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMA-AQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHA 81
Cdd:COG0028 2 KMTGADALVEALEAEGVETVFGVPGGAILPLYDAlRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 82 LGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIA 161
Cdd:COG0028 82 VTGLADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEVLRRAFRIATSGRPGPVVLDIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 162 GDMVNAKIDRATVRfVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGK 241
Cdd:COG0028 162 KDVQAAEAEEEPAP-PELRGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLGAPVVTTLMGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 242 GVLPDDHPNCV-------AAARSRALLQADVIVLLGARLNWILhFGFPPRFSANVKIIQVDLCAEELSNNVRAASALLGD 314
Cdd:COG0028 241 GAFPEDHPLYLgmlgmhgTPAANEALAEADLVLAVGARFDDRV-TGNWDEFAPDAKIIHIDIDPAEIGKNYPVDLPIVGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 315 IKMVTSQLLETVRSESWRFPSDSQWWATLREKITANAQitkalslQTTLPMNYYTAFHHISELLPKDCIIVSE-GANTMD 393
Cdd:COG0028 320 AKAVLAALLEALEPRADDRAAWLARIAAWRAEYLAAYA-------ADDGPIKPQRVIAALREALPDDAIVVTDvGQHQMW 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 394 IGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVleqAQRfGQKVVCVEGDSAFGFSGMEAETMCRYKLPIiiivinnn 473
Cdd:COG0028 393 AARYLRFRR-PRRFLTSGGLGTMGYGLPAAIGAKL---ARP-DRPVVAITGDGGFQMNLQELATAVRYGLPV-------- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 474 giysgvdpeTW------------KAMEKMGDMTTIAppvTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQDSLKNTQm 541
Cdd:COG0028 460 ---------KVvvlnngglgmvrQWQELFYGGRYSG---TDLPNPDFAKLAEAFGAKGERVETPEELEAALEEALASDG- 526
|
570
....*....|.
gi 47085819 542 PSLLNVLIDPT 552
Cdd:COG0028 527 PALIDVRVDPE 537
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
6-552 |
1.22e-84 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 273.52 E-value: 1.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 6 GAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGGM 85
Cdd:PRK05858 7 AGRLAARRLKAHGVDTMFTLSGGHLFPLYDGAREEGIRLIDVRHEQTAAFAAEAWAKLTRVPGVAVLTAGPGVTNGMSAM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 86 ANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGDMV 165
Cdd:PRK05858 87 AAAQFNQSPLVVLGGRAPALRWGMGSLQEIDHVPFVAPVTKFAATAQSAENAGRLVDQALQAAVTPHRGPVFVDFPMDHA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 166 NAKIDrATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGVLP 245
Cdd:PRK05858 167 FSMAD-DDGRPGALTELPAGPTPDPDALARAAGLLAEAQRPVIMAGTDVWWGHAEAALLRLAEELGIPVLMNGMGRGVVP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 246 DDHPNCVAAARSRALLQADVIVLLGARLNWILHFGFpprFSANVKIIQVDLCAEELSNNVRAASALLGDIKMVTSQLlet 325
Cdd:PRK05858 246 ADHPLAFSRARGKALGEADVVLVVGVPMDFRLGFGV---FGGTAQLVHVDDAPPQRAHHRPVAAGLYGDLSAILSAL--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 326 vrSESWRFPSDSQ-WWATLREKITANAQITKALSLQTTLPMNYYTAFHHISELLPKDCIIVSEGANTMDIGRTMLLNHLP 404
Cdd:PRK05858 320 --AGAGGDRTDHQgWIEELRTAETAARARDAAELADDRDPIHPMRVYGELAPLLDRDAIVIGDGGDFVSYAGRYIDPYRP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 405 RHRLDAGTFGTMGVGPGFAIAAAVleqaQRFGQKVVCVEGDSAFGFSGMEAETMCRYKLPIIIIVINnngiySGVdpetW 484
Cdd:PRK05858 398 GCWLDPGPFGCLGTGPGYALAARL----ARPSRQVVLLQGDGAFGFSLMDVDTLVRHNLPVVSVIGN-----NGI----W 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 485 kAMEK--MGDMTTIAPPVTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQDSLkNTQMPSLLNVLIDPT 552
Cdd:PRK05858 465 -GLEKhpMEALYGYDVAADLRPGTRYDEVVRALGGHGELVTVPAELGPALERAF-ASGVPYLVNVLTDPS 532
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
367-550 |
3.14e-74 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 233.58 E-value: 3.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 367 YYTAFHHISELLPKDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLEQaqrfGQKVVCVEGDS 446
Cdd:cd02004 1 PYRVLHELQEALPDDAIIVSDGGNTMDWARYILRPRKPRHRLDAGTFGTLGVGLGYAIAAALARP----DKRVVLVEGDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 447 AFGFSGMEAETMCRYKLPIIIIVINNNGIYSGVDPETWKAmekmgdmTTIAPPVTLLPEARYEQVMSAFGGHGYLVRTVE 526
Cdd:cd02004 77 AFGFSGMELETAVRYNLPIVVVVGNNGGWYQGLDGQQLSY-------GLGLPVTTLLPDTRYDLVAEAFGGKGELVTTPE 149
|
170 180
....*....|....*....|....
gi 47085819 527 ELRTALQDSLKnTQMPSLLNVLID 550
Cdd:cd02004 150 ELKPALKRALA-SGKPALINVIID 172
|
|
| acolac_lg |
TIGR00118 |
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form ... |
5-464 |
1.53e-63 |
|
acetolactate synthase, large subunit, biosynthetic type; Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272915 [Multi-domain] Cd Length: 558 Bit Score: 218.05 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAA-GIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:TIGR00118 2 SGAEAIIESLKDEGVKTVFGYPGGAILPIYDALYNDsGIEHILVRHEQGAAHAADGYARASGKVGVVLVTSGPGATNLVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD 163
Cdd:TIGR00118 82 GIATAYMDSIPMVVFTGQVPTSLIGSDAFQEADILGITMPITKHSFQVKSAEDIPRIIKEAFHIATTGRPGPVLVDLPKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 164 MVNAKIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGV 243
Cdd:TIGR00118 162 VTTAEIEYPYPEKVNLPGYRPTVKGHPLQIKKAAELINLAKKPVILVGGGVIIAGASEELKELAERIQIPVTTTLMGLGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 244 LPDDHPNCVA-------AARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDLCAEELSNNVRAAS 309
Cdd:TIGR00118 242 FPEDHPLSLGmlgmhgtKTANLAVHECDLIIAVGAR--------FDDRvtgnlakFAPNAKIIHIDIDPAEIGKNVRVDI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 310 ALLGDIKMVTSQLLETVRSESWRfpSDSQWWATLREkitanaqiTKALSLqttLPMNYY-------TAFHHISELLPKDC 382
Cdd:TIGR00118 314 PIVGDARNVLEELLKKLFELKER--KESAWLEQINK--------WKKEYP---LKMDYTeegikpqQVIEELSRVTKDEA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 383 IIVSE-GANTMDIGRtMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLEQAqrfgQKVVCVEGDSAFGFSGMEAETMCRY 461
Cdd:TIGR00118 381 IVTTDvGQHQMWAAQ-FYPFRKPRRFITSGGLGTMGFGLPAAIGAKVAKPE----STVICITGDGSFQMNLQELSTAVQY 455
|
...
gi 47085819 462 KLP 464
Cdd:TIGR00118 456 DIP 458
|
|
| PRK08611 |
PRK08611 |
pyruvate oxidase; Provisional |
1-551 |
2.24e-57 |
|
pyruvate oxidase; Provisional
Pssm-ID: 181502 [Multi-domain] Cd Length: 576 Bit Score: 201.77 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEV--AMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGL 78
Cdd:PRK08611 1 MAKIKAGEALVKLLQDWGIDHVYGIPGDSIDAVvdALRKEQDKIKFIQVRHEEVAALAAAAYAKLTGKIGVCLSIGGPGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 79 IHALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSiYGRPGACYI 158
Cdd:PRK08611 81 IHLLNGLYDAKMDHVPVLALAGQVTSDLLGTDFFQEVNLEKMFEDVAVYNHQIMSAENLPEIVNQAIRTA-YEKKGVAVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 159 DIAGDMVNAKIDRATVRFVSCCpAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAekEVRELVEVTGIPFLPTP 238
Cdd:PRK08611 160 TIPDDLPAQKIKDTTNKTVDTF-RPTVPSPKPKDIKKAAKLINKAKKPVILAGLGAKHAKE--ELLAFAEKAKIPIIHTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 239 MGKGVLPDDHPNCVA-------AARSRALLQADVIVLLGArlnwilHFGFPPRFSANVKIIQVDLCAEELSNNVRAASAL 311
Cdd:PRK08611 237 PAKGIIPDDHPYSLGnlgkigtKPAYEAMQEADLLIMVGT------NYPYVDYLPKKAKAIQIDTDPANIGKRYPVNVGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 312 LGDIKMVTSQLLETV-RSESWRFPSDSQ-----WWATLREKITanaqitkalslQTTLPMNYYTAFHHISELLPKDCIIv 385
Cdd:PRK08611 311 VGDAKKALHQLTENIkHVEDRRFLEACQenmakWWKWMEEDEN-----------NASTPIKPERVMAAIQKIADDDAVL- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 386 seganTMDIGR-----TMLLNHLPRHR-LDAGTFGTMGVG-PGfAIAAAVLEQAQRfgqkVVCVEGDSAFGFSGMEAETM 458
Cdd:PRK08611 379 -----SVDVGTvtvwsARYLNLGTNQKfIISSWLGTMGCGlPG-AIAAKIAFPDRQ----AIAICGDGGFSMVMQDFVTA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 459 CRYKLPIIIIVINNNGIysgvdpetwkAMEK-----MGDMTTiappVTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQ 533
Cdd:PRK08611 449 VKYKLPIVVVVLNNQQL----------AFIKyeqqaAGELEY----AIDLSDMDYAKFAEACGGKGYRVEKAEELDPAFE 514
|
570
....*....|....*...
gi 47085819 534 DSLKNTQmPSLLNVLIDP 551
Cdd:PRK08611 515 EALAQDK-PVIIDVYVDP 531
|
|
| PRK06276 |
PRK06276 |
acetolactate synthase large subunit; |
5-553 |
2.96e-56 |
|
acetolactate synthase large subunit;
Pssm-ID: 235766 [Multi-domain] Cd Length: 586 Bit Score: 198.82 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PRK06276 2 KGAEAIIKALEAEGVKIIFGYPGGALLPFYDALYDSDLIHILTRHEQAAAHAADGYARASGKVGVCVATSGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRNQETTGAFQEfpqVEACRLY---SKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIA 161
Cdd:PRK06276 82 IATAYADSSPVIALTGQVPTKLIGNDAFQE---IDALGIFmpiTKHNFQIKKPEEIPEIFRAAFEIAKTGRPGPVHIDLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 162 GDMVNAKIDRATVRFVSCCPAP---PVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTP 238
Cdd:PRK06276 159 KDVQEGELDLEKYPIPAKIDLPgykPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIELSELVKIPVCTTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 239 MGKGVLPDDHPNCVA-------AARSRALLQADVIVLLGARlnwilhF-----GFPPRFSANVKIIQVDLCAEELSNNVR 306
Cdd:PRK06276 239 MGKGAFPEDHPLALGmvgmhgtKAANYSVTESDVLIAIGCR------FsdrttGDISSFAPNAKIIHIDIDPAEIGKNVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 307 AASALLGDIKMVTSQLLETVRSESWRfpSDSQWWATLREkitanaqiTKALSLQTT----LPMNYYTAFHHISELLpKDC 382
Cdd:PRK06276 313 VDVPIVGDAKNVLRDLLAELMKKEIK--NKSEWLERVKK--------LKKESIPRMdfddKPIKPQRVIKELMEVL-REI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 383 IIVSEGANTMDIGRT-MLLNHL-----PRHRLDAGTFGTMGVGPGFAIAAAVleqaQRFGQKVVCVEGDSAFGFSGMEAE 456
Cdd:PRK06276 382 DPSKNTIITTDVGQNqMWMAHFfktsaPRSFISSGGLGTMGFGFPAAIGAKV----AKPDANVIAITGDGGFLMNSQELA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 457 TMCRYKLPIIIIVIN----------NNGIYSGVDPETwkameKMGDmttiAPPVTLLPEaryeqvmsAFGGHGYLVRTVE 526
Cdd:PRK06276 458 TIAEYDIPVVICIFDnrtlgmvyqwQNLYYGKRQSEV-----HLGE----TPDFVKLAE--------SYGVKADRVEKPD 520
|
570 580
....*....|....*....|....*..
gi 47085819 527 ELRTALQDSLKNTQmPSLLNVLIDPTS 553
Cdd:PRK06276 521 EIKEALKEAIKSGE-PYLLDIIIDPAE 546
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
5-464 |
6.12e-55 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 194.28 E-value: 6.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PRK08322 2 KAADLFVKCLENEGVEYIFGIPGEENLDLLEALRDSSIKLILTRHEQGAAFMAATYGRLTGKAGVCLSTLGPGATNLVTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGG--SSDRNQEttGAFQefpQVEACRLY---SKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYI- 158
Cdd:PRK08322 82 VAYAQLGGMPMVAITGqkPIKRSKQ--GSFQ---IVDVVAMMaplTKWTRQIVSPDNIPEVVREAFRLAEEERPGAVHLe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 159 ---DIAGDMVNAK-IDRATVRfvsccpaPPVsqADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPF 234
Cdd:PRK08322 157 lpeDIAAEETDGKpLPRSYSR-------RPY--ASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGIPF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 235 LPTPMGKGVLPDDHPNCVAAAR-------SRALLQADVIVLLGARLnwilhFGFPPRF---SANVKIIQVDLCAEELSNN 304
Cdd:PRK08322 228 FTTQMGKGVIPETHPLSLGTAGlsqgdyvHCAIEHADLIINVGHDV-----IEKPPFFmnpNGDKKVIHINFLPAEVDPV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 305 VRAASALLGDIKMVTSQLLETV-RSESWRFPSDSQWWATLREKITANAQitkalslQTTLPMNYYTAFHHISELLPKDCI 383
Cdd:PRK08322 303 YFPQVEVVGDIANSLWQLKERLaDQPHWDFPRFLKIREAIEAHLEEGAD-------DDRFPMKPQRIVADLRKVMPDDDI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 384 IVSE-GANTMDIGRtmllnHLPRHR-----LDAGtFGTMGVG-PGfAIAAAVLeQAQRfgqKVVCVEGDSAFGFSGMEAE 456
Cdd:PRK08322 376 VILDnGAYKIWFAR-----NYRAYEpntclLDNA-LATMGAGlPS-AIAAKLV-HPDR---KVLAVCGDGGFMMNSQELE 444
|
....*...
gi 47085819 457 TMCRYKLP 464
Cdd:PRK08322 445 TAVRLGLP 452
|
|
| PRK08527 |
PRK08527 |
acetolactate synthase large subunit; |
3-550 |
2.00e-54 |
|
acetolactate synthase large subunit;
Pssm-ID: 181458 [Multi-domain] Cd Length: 563 Bit Score: 193.39 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVGVPIIEV--AMAAQAaGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIH 80
Cdd:PRK08527 2 KLSGSQMVCEALKEEGVKVVFGYPGGAILNIydEIYKQN-YFKHILTRHEQAAVHAADGYARASGKVGVAIVTSGPGFTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 81 ALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDI 160
Cdd:PRK08527 81 AVTGLATAYMDSIPLVLISGQVPNSLIGTDAFQEIDAVGISRPCVKHNYLVKSIEELPRILKEAFYIARSGRPGPVHIDI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 161 AGDMVNAKIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK08527 161 PKDVTATLGEFEYPKEISLKTYKPTYKGNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGIPAVETLMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDLCAEELSNNVR 306
Cdd:PRK08527 241 RGVLRSDDPLLLGMlgmhgsyAANMAMSECDLLISLGAR--------FDDRvtgklseFAKHAKIIHVDIDPSSISKIVN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 307 AASALLGDIKMVTSQLLETVRSESwrfPSDSQWWatlREKITanaqitkalSLQTTLPMNYYT---------AFHHISEL 377
Cdd:PRK08527 313 ADYPIVGDLKNVLKEMLEELKEEN---PTTYKEW---REILK---------RYNELHPLSYEDsdevlkpqwVIERVGEL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 378 LPKDCIIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVleqaqRFGQKVVC-VEGDSAFGFSGMEA 455
Cdd:PRK08527 378 LGDDAIISTDvGQHQMWVAQFYPFNY-PRQLATSGGLGTMGYGLPAALGAKL-----AVPDKVVInFTGDGSILMNIQEL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 456 ETMCRYKLPiiIIVINNNGIYSGVdPETWKAM--EKMGDMTTIappvTLLPEarYEQVMSAFGGHGYLVRTVEELRTALQ 533
Cdd:PRK08527 452 MTAVEYKIP--VINIILNNNFLGM-VRQWQTFfyEERYSETDL----STQPD--FVKLAESFGGIGFRVTTKEEFDKALK 522
|
570
....*....|....*..
gi 47085819 534 DSLKnTQMPSLLNVLID 550
Cdd:PRK08527 523 EALE-SDKVALIDVKID 538
|
|
| PRK08617 |
PRK08617 |
acetolactate synthase AlsS; |
5-464 |
3.30e-53 |
|
acetolactate synthase AlsS;
Pssm-ID: 236312 [Multi-domain] Cd Length: 552 Bit Score: 189.68 E-value: 3.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PRK08617 6 YGADLVVDSLINQGVKYVFGIPGAKIDRVFDALEDSGPELIVTRHEQNAAFMAAAIGRLTGKPGVVLVTSGPGVSNLATG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGDM 164
Cdd:PRK08617 86 LVTATAEGDPVVAIGGQVKRADRLKRTHQSMDNVALFRPITKYSAEVQDPDNLSEVLANAFRAAESGRPGAAFVSLPQDV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 165 VNAKidrATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGVL 244
Cdd:PRK08617 166 VDAP---VTSKAIAPLSKPKLGPASPEDINYLAELIKNAKLPVLLLGMRASSPEVTAAIRRLLERTNLPVVETFQAAGVI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 245 PDDHPNC----VAAARSRA----LLQADVIVLLG-------ARlNWILHfgfpprfsANVKIIQVDLCAEELSNNVRAAS 309
Cdd:PRK08617 243 SRELEDHffgrVGLFRNQPgdelLKKADLVITIGydpieyePR-NWNSE--------GDATIIHIDVLPAEIDNYYQPER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 310 ALLGDIKMVTSQLLEtvRSESWRFPSDSQ-WWATLREKITANAQITKALSLQTTLPMNYytaFHHISELLPKDCIIvseg 388
Cdd:PRK08617 314 ELIGDIAATLDLLAE--KLDGLSLSPQSLeILEELRAQLEELAERPARLEEGAVHPLRI---IRALQDIVTDDTTV---- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 389 anTMDIG-------RtmllnHL----PRHRLDAGTFGTMGVGPGFAIAAAVLeqaqRFGQKVVCVEGDSAFGFSGMEAET 457
Cdd:PRK08617 385 --TVDVGshyiwmaR-----YFrsyePRHLLFSNGMQTLGVALPWAIAAALV----RPGKKVVSVSGDGGFLFSAMELET 453
|
....*..
gi 47085819 458 MCRYKLP 464
Cdd:PRK08617 454 AVRLKLN 460
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
1-547 |
3.53e-53 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 189.45 E-value: 3.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEV--AMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGL 78
Cdd:PRK08266 1 MTTMTGGEAIVAGLVAHGVDTVFGLPGAQLYWLfdALYKAGDRIRVIHTRHEQAAGYMAFGYARSTGRPGVCSVVPGPGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 79 IHALGGMANANVNCWPVIVLGGS--SDRNQETTGAFQEFP-QVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGA 155
Cdd:PRK08266 81 LNAGAALLTAYGCNSPVLCLTGQipSALIGKGRGHLHEMPdQLATLRSFTKWAERIEHPSEAPALVAEAFQQMLSGRPRP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 156 CYIDIAGDMVNAKIDRATVRFVSCCPAPPVsqaDCREITQAVRLLKTSQSPLIIIGKGAAYARAekEVRELVEVTGIPFL 235
Cdd:PRK08266 161 VALEMPWDVFGQRAPVAAAPPLRPAPPPAP---DPDAIAAAAALIAAAKNPMIFVGGGAAGAGE--EIRELAEMLQAPVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 236 PTPMGKGVLPDDHP---NCVAAarsRALL-QADVIVLLGARLnwILHFGFPPRFSANVKIIQVDLCAEElsnNVRAAS-- 309
Cdd:PRK08266 236 AFRSGRGIVSDRHPlglNFAAA---YELWpQTDVVIGIGSRL--ELPTFRWPWRPDGLKVIRIDIDPTE---MRRLKPdv 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 310 ALLGDIKMVTSQLLETVRSESWRFPSDSqwwATLREKITANAQITKALSLQttlpMNYYTAfhhISELLPKDCIIVSEGA 389
Cdd:PRK08266 308 AIVADAKAGTAALLDALSKAGSKRPSRR---AELRELKAAARQRIQAVQPQ----ASYLRA---IREALPDDGIFVDELS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 390 NTMDIGRTMLLNHLPRHRLDAGTFGTMGVgpGFAIAAAVleQAQRFGQKVVCVEGDSAFGFSGMEAETMCRYKLPiIIIV 469
Cdd:PRK08266 378 QVGFASWFAFPVYAPRTFVTCGYQGTLGY--GFPTALGA--KVANPDRPVVSITGDGGFMFGVQELATAVQHNIG-VVTV 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 470 INNNGIYSGV---DPETWKAMEKMGDMTTiaPPVTLLPEaryeqvmsAFGGHGYLVRTVEELRTALQDSLKNTQmPSLLN 546
Cdd:PRK08266 453 VFNNNAYGNVrrdQKRRFGGRVVASDLVN--PDFVKLAE--------SFGVAAFRVDSPEELRAALEAALAHGG-PVLIE 521
|
.
gi 47085819 547 V 547
Cdd:PRK08266 522 V 522
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
8-160 |
1.24e-52 |
|
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: 176.57 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 8 QLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGGMAN 87
Cdd:cd07035 1 DALVEALKAEGVDHVFGVPGGAILPLLDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47085819 88 ANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDI 160
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEALRRAFRIALSGRPGPVALDL 153
|
|
| PRK06048 |
PRK06048 |
acetolactate synthase large subunit; |
1-550 |
2.07e-51 |
|
acetolactate synthase large subunit;
Pssm-ID: 180368 [Multi-domain] Cd Length: 561 Bit Score: 184.98 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIH 80
Cdd:PRK06048 5 TEKMTGARAIIKCLEKEGVEVIFGYPGGAIIPVYDELYDSDLRHILVRHEQAAAHAADGYARATGKVGVCVATSGPGATN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 81 ALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDI 160
Cdd:PRK06048 85 LVTGIATAYMDSVPIVALTGQVPRSMIGNDAFQEADITGITMPITKHNYLVQDAKDLPRIIKEAFHIASTGRPGPVLIDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 161 AGDMVNAKIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK06048 165 PKDVTTAEIDFDYPDKVELRGYKPTYKGNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELAETIPAPVTTTLMG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHPNCVAAA-------RSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDLCAEELSNNVR 306
Cdd:PRK06048 245 IGAIPTEHPLSLGMLgmhgtkyANYAIQESDLIIAVGAR--------FDDRvtgklasFAPNAKIIHIDIDPAEISKNVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 307 AASALLGDIKMVTSQLLETVRSESWRfpsdsQWwatlrekitanaqITKALSLQTTLPMNYYT---------AFHHISEL 377
Cdd:PRK06048 317 VDVPIVGDAKQVLKSLIKYVQYCDRK-----EW-------------LDKINQWKKEYPLKYKEredvikpqyVIEQIYEL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 378 LPkDCIIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVleqaqRFGQKVVC-VEGDSAFGFSGMEA 455
Cdd:PRK06048 379 CP-DAIIVTEvGQHQMWAAQYFKYKY-PRTFITSGGLGTMGYGFPAAIGAKV-----GKPDKTVIdIAGDGSFQMNSQEL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 456 ETMCRYKLPiiIIVINNNGIYSGVdPETWKAM--EKMGDMTTIAPPVTllpearYEQVMSAFGGHGYLVRTVEELRTALQ 533
Cdd:PRK06048 452 ATAVQNDIP--VIVAILNNGYLGM-VRQWQELfyDKRYSHTCIKGSVD------FVKLAEAYGALGLRVEKPSEVRPAIE 522
|
570
....*....|....*..
gi 47085819 534 DSLkNTQMPSLLNVLID 550
Cdd:PRK06048 523 EAV-ASDRPVVIDFIVE 538
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
5-464 |
2.61e-51 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 184.70 E-value: 2.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAAcyAASAIGY--LTGRPAVCLVVSGPGLIHAL 82
Cdd:PRK08978 2 NGAQWVVHALRAQGVDTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGA--AMAAIGYarATGKVGVCIATSGPGATNLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 83 GGMANANVNCWPVIVLGGSSDRNQETTGAFQE---FPQVEACrlySKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK08978 80 TGLADALLDSVPVVAITGQVSSPLIGTDAFQEidvLGLSLAC---TKHSFLVQSLEELPEIMAEAFEIASSGRPGPVLVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNAKIDRATVrFVSCCPAPPVSQAdcrEITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPM 239
Cdd:PRK08978 157 IPKDIQLAEGELEPH-LTTVENEPAFPAA---ELEQARALLAQAKKPVLYVGGGVGMAGAVPALREFLAATGMPAVATLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 240 GKGVLPDDHPNCV-------AAARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDLCAEELSNNV 305
Cdd:PRK08978 233 GLGAVEADHPYYLgmlgmhgTKAANLAVQECDLLIAVGAR--------FDDRvtgklntFAPHAKVIHLDIDPAEINKLR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 306 RAASALLGDIKMVTSQLLETVRSESWRfpsdsQWWATLR-----------EKITANAQItkalslqttlpmnyytafHHI 374
Cdd:PRK08978 305 QAHVALQGDLNALLPALQQPLNIDAWR-----QHCAQLRaehawrydhpgEAIYAPALL------------------KQL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 375 SELLPKDCIIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFSGM 453
Cdd:PRK08978 362 SDRKPADTVVTTDvGQHQMWVAQHMRFTR-PENFITSSGLGTM----GFGLPAAIGAQVARPDDTVICVSGDGSFMMNVQ 436
|
490
....*....|.
gi 47085819 454 EAETMCRYKLP 464
Cdd:PRK08978 437 ELGTIKRKQLP 447
|
|
| ilvB |
CHL00099 |
acetohydroxyacid synthase large subunit |
3-551 |
4.57e-50 |
|
acetohydroxyacid synthase large subunit
Pssm-ID: 214363 [Multi-domain] Cd Length: 585 Bit Score: 181.82 E-value: 4.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVG---VPIIEVAMAAQAAG-IKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGL 78
Cdd:CHL00099 9 EKTGAFALIDSLVRHGVKHIFGYPGgaiLPIYDELYAWEKKGlIKHILVRHEQGAAHAADGYARSTGKVGVCFATSGPGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 79 IHALGGMANANVNCWPVIVLGGSSDRNQETTGAFQE-------FPQVeacrlysKFSARPSSLEMIPAVVEKAVRSSIYG 151
Cdd:CHL00099 89 TNLVTGIATAQMDSVPLLVITGQVGRAFIGTDAFQEvdifgitLPIV-------KHSYVVRDARDISRIVAEAFYIAKHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 152 RPGACYIDIAGDMVNAKIDRATV----RFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELV 227
Cdd:CHL00099 162 RPGPVLIDIPKDVGLEKFDYYPPepgnTIIKILGCRPIYKPTIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEITELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 228 EVTGIPFLPTPMGKGVLPDDHPNCVA-------AARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQ 293
Cdd:CHL00099 242 ELYKIPVTTTLMGKGIFDEDHPLCLGmlgmhgtAYANFAVSECDLLIALGAR--------FDDRvtgkldeFACNAQVIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 294 VDLCAEELSNNVRAASALLGDIKMVTSQLLETV-RSESWRFPSDSQWWatlREKITA--------NAQITKALSLQTTLp 364
Cdd:CHL00099 314 IDIDPAEIGKNRIPQVAIVGDVKKVLQELLELLkNSPNLLESEQTQAW---RERINRwrkeypllIPKPSTSLSPQEVI- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 365 mnyytafHHISELLPkDCIIvseganTMDIGR-----TMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLEQaqrfGQKV 439
Cdd:CHL00099 390 -------NEISQLAP-DAYF------TTDVGQhqmwaAQFLKCKPRKWLSSAGLGTMGYGLPAAIGAQIAHP----NELV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 440 VCVEGDSAFGFSGMEAETMCRYKLPIIIIvinnngiysgVDPETWKAMEKM------------GDMTTIAPPVTLLPEar 507
Cdd:CHL00099 452 ICISGDASFQMNLQELGTIAQYNLPIKII----------IINNKWQGMVRQwqqafygeryshSNMEEGAPDFVKLAE-- 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 47085819 508 yeqvmsAFGGHGYLVRTVEELRTALQDSLkNTQMPSLLNVLIDP 551
Cdd:CHL00099 520 ------AYGIKGLRIKSRKDLKSSLKEAL-DYDGPVLIDCQVIE 556
|
|
| PRK06725 |
PRK06725 |
acetolactate synthase large subunit; |
2-464 |
1.48e-49 |
|
acetolactate synthase large subunit;
Pssm-ID: 180672 [Multi-domain] Cd Length: 570 Bit Score: 180.16 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 2 DEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHA 81
Cdd:PRK06725 13 EEVTGAGHVIQCLKKLGVTTVFGYPGGAILPVYDALYESGLKHILTRHEQAAIHAAEGYARASGKVGVVFATSGPGATNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 82 LGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIA 161
Cdd:PRK06725 93 VTGLADAYMDSIPLVVITGQVATPLIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSRIVQEAFYIAESGRPGPVLIDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 162 GDMVNAKI-----DRATVRFVSCCPAPPVSQadCREITQAVRllkTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLP 236
Cdd:PRK06725 173 KDVQNEKVtsfynEVVEIPGYKPEPRPDSMK--LREVAKAIS---KAKRPLLYIGGGVIHSGGSEELIEFARENRIPVVS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 237 TPMGKGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARLNWILHfGFPPRFSANVKIIQVDLCAEELSNNVRAAS 309
Cdd:PRK06725 248 TLMGLGAYPPGDPLFLGMlgmhgtyAANMAVTECDLLLALGVRFDDRVT-GKLELFSPHSKKVHIDIDPSEFHKNVAVEY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 310 ALLGDIKMVTSQLLETVrseswrFPSDSQWWatlrekitanaqITKALSLQTTLPMNYYtafHHISELLPKDCI-IVSEG 388
Cdd:PRK06725 327 PVVGDVKKALHMLLHMS------IHTQTDEW------------LQKVKTWKEEYPLSYK---QKESELKPQHVInLVSEL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 389 AN-----TMDIGR-TMLLNHL-----PRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFSGMEAET 457
Cdd:PRK06725 386 TNgeaivTTEVGQhQMWAAHFykaknPRTFLTSGGLGTM----GFGFPAAIGAQLAKEEELVICIAGDASFQMNIQELQT 461
|
....*..
gi 47085819 458 MCRYKLP 464
Cdd:PRK06725 462 IAENNIP 468
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
6-170 |
3.03e-49 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 168.18 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 6 GAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAA-GIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:pfam02776 1 GAEALADVLKALGVDTVFGVPGGHILPLLDALAKSpGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRNQETTGAFQ-EFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD 163
Cdd:pfam02776 81 LANAYVDSVPLLVISGQRPRSLVGRGALQqELDQLALFRPVTKWAVRVTSADEIPEVLRRAFRAALSGRPGPVYLEIPLD 160
|
....*..
gi 47085819 164 MVNAKID 170
Cdd:pfam02776 161 VLLEEVD 167
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
6-563 |
8.52e-49 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 178.08 E-value: 8.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 6 GAQLIAAALKDQNVEYMFGIvgvPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTG--RPAVCLVVSGPGLIHALG 83
Cdd:PRK06154 22 VAEAVAEILKEEGVELLFGF---PVNELFDAAAAAGIRPVIARTERVAVHMADGYARATSgeRVGVFAVQYGPGAENAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAfqEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD 163
Cdd:PRK06154 99 GVAQAYGDSVPVLFLPTGYPRGSTDVAP--NFESLRNYRHITKWCEQVTLPDEVPELMRRAFTRLRNGRPGPVVLELPVD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 164 MVNAKIDRATVRFvsccpAPP---VSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK06154 177 VLAEELDELPLDH-----RPSrrsRPGADPVEVVEAAALLLAAERPVIYAGQGVLYAQATPELKELAELLEIPVMTTLNG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHPNCVAAArSRA--------LLQADVIVLLGARLNWIlHFGFPprFSANVKIIQVDLCAEELSNNVRAASALL 312
Cdd:PRK06154 252 KSAFPEDHPLALGSG-GRArpatvahfLREADVLFGIGCSLTRS-YYGLP--MPEGKTIIHSTLDDADLNKDYPIDHGLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 313 GDIKMVTSQLLETVRSESWRFPSDSQ------------WWATLREKITANAQitkalslqttlPMNYYTAFHHISELL-P 379
Cdd:PRK06154 328 GDAALVLKQMIEELRRRVGPDRGRAQqvaaeieavraaWLAKWMPKLTSDST-----------PINPYRVVWELQHAVdI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 380 KDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLeqaqRFGQKVVCVEGDSAFGFSGMEAETMC 459
Cdd:PRK06154 397 KTVIITHDAGSPRDQLSPFYVASRPGSYLGWGKTTQLGYGLGLAMGAKLA----RPDALVINLWGDAAFGMTGMDFETAV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 460 RYKLPIIIIVINNNGIySGVDPETWKAMEKMGdmttiAPPVTllpeARYEQVMSAFGGHGYLVRTVEELRTALQDSLKNT 539
Cdd:PRK06154 473 RERIPILTILLNNFSM-GGYDKVMPVSTTKYR-----ATDIS----GDYAAIARALGGYGERVEDPEMLVPALLRALRKV 542
|
570 580
....*....|....*....|....*.
gi 47085819 540 Q--MPSLLNVLidpTSDRKQQEFPWL 563
Cdd:PRK06154 543 KegTPALLEVI---TSEETALSRPWP 565
|
|
| PRK07789 |
PRK07789 |
acetolactate synthase 1 catalytic subunit; Validated |
3-448 |
2.24e-48 |
|
acetolactate synthase 1 catalytic subunit; Validated
Pssm-ID: 236098 [Multi-domain] Cd Length: 612 Bit Score: 177.87 E-value: 2.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVGVPIIEV---AMAAQAagIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK07789 30 RMTGAQAVVRSLEELGVDVVFGIPGGAILPVydpLFDSTK--VRHVLVRHEQGAGHAAEGYAQATGRVGVCMATSGPGAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK07789 108 NLVTPIADANMDSVPVVAITGQVGRGLIGTDAFQEADIVGITMPITKHNFLVTDADDIPRVIAEAFHIASTGRPGPVLVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNA--------KIDRATVRfvsccpapPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTG 231
Cdd:PRK07789 188 IPKDALQAqttfswppRMDLPGYR--------PVTKPHGKQIREAAKLIAAARRPVLYVGGGVIRAEASAELRELAELTG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 232 IPFLPTPMGKGVLPDDHPN---------CVAAArsRALLQADVIVLLGARlnwilhF-----GFPPRFSANVKIIQVDLC 297
Cdd:PRK07789 260 IPVVTTLMARGAFPDSHPQhlgmpgmhgTVAAV--AALQRSDLLIALGAR------FddrvtGKLDSFAPDAKVIHADID 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 298 AEELSNNVRAASALLGDIKMVTSQLLETVRSE--SWRFPSDSQWWATLRekitanaqitkalSLQTTLPMNY------YT 369
Cdd:PRK07789 332 PAEIGKNRHADVPIVGDVKEVIAELIAALRAEhaAGGKPDLTAWWAYLD-------------GWRETYPLGYdepsdgSL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 370 AFHH----ISELLPKDCIIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEG 444
Cdd:PRK07789 399 APQYvierLGEIAGPDAIYVAGvGQHQMWAAQFIDYEK-PRTWLNSGGLGTM----GYAVPAAMGAKVGRPDKEVWAIDG 473
|
....
gi 47085819 445 DSAF 448
Cdd:PRK07789 474 DGCF 477
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
1-448 |
5.81e-47 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 172.97 E-value: 5.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMA-AQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK08155 10 RKRFTGAELIVRLLERQGIRIVTGIPGGAILPLYDAlSQSTQIRHILARHEQGAGFIAQGMARTTGKPAVCMACSGPGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK08155 90 NLVTAIADARLDSIPLVCITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRDIEELPQVISDAFRIAQSGRPGPVWID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNAKIDRATVRFVSC-CPAPPVSQADcreITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTP 238
Cdd:PRK08155 170 IPKDVQTAVIELEALPAPAEkDAAPAFDEES---IRDAAAMINAAKRPVLYLGGGVINSGAPARARELAEKAQLPTTMTL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 239 MGKGVLPDDHPNCVA-----AARSR--ALLQADVIVLLGARLNwILHFGFPPRFSANVKIIQVDLCAEELSNNVRAASAL 311
Cdd:PRK08155 247 MALGMLPKAHPLSLGmlgmhGARSTnyILQEADLLIVLGARFD-DRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 312 LGDIKMVTSQLLETVRseswrfPSDSQWWATLREkitanaqitkalSLQTTLPMN---------YYTAFHHISELLPKDC 382
Cdd:PRK08155 326 QADVDDVLAQLLPLVE------AQPRAEWHQLVA------------DLQREFPCPipkaddplsHYGLINAVAACVDDNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47085819 383 IIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAvLEQAQRfgqKVVCVEGDSAF 448
Cdd:PRK08155 388 IITTDvGQHQMWTAQAYPLNR-PRQWLTSGGLGTMGFGLPAAIGAA-LANPER---KVLCFSGDGSL 449
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
1-565 |
3.00e-46 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 171.19 E-value: 3.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQA-AGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK07979 1 MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTvGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK07979 81 NAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNA--KIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPT 237
Cdd:PRK07979 161 LPKDILNPanKLPYVWPESVSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKLNLPVVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 238 PMGKGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDLCAEELSN 303
Cdd:PRK07979 241 LMGLGAFPATHRQSLGMlgmhgtyEANMTMHNADVIFAVGVR--------FDDRttnnlakYCPNATVLHIDIDPTSISK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 304 NVRAASALLGDIKMVTSQLLETVRSESWRFPSDS--QWWATLrEKITANAQITKALSLQTTLPMNYYTAFHHISEllpkd 381
Cdd:PRK07979 313 TVTADIPIVGDARQVLEQMLELLSQESAHQPLDEirDWWQQI-EQWRARQCLKYDTHSEKIKPQAVIETLWRLTK----- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 382 ciivSEGANTMDIGRTMLLNHL------PRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFSGMEA 455
Cdd:PRK07979 387 ----GDAYVTSDVGQHQMFAALyypfdkPRRWINSGGLGTM----GFGLPAALGVKMALPEETVVCVTGDGSIQMNIQEL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 456 ETMCRYKLPIIIIVINNN----------GIYSGVDPETWkaMEKMGDMTTIAppvtllpearyeqvmSAFGGHGYLVRTV 525
Cdd:PRK07979 459 STALQYELPVLVLNLNNRylgmvkqwqdMIYSGRHSQSY--MQSLPDFVRLA---------------EAYGHVGIQISHP 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 47085819 526 EELRTALQDSLKNTQMPSLlnVLIDPTSDRKQQEFPWLTR 565
Cdd:PRK07979 522 DELESKLSEALEQVRNNRL--VFVDVTVDGSEHVYPMQIR 559
|
|
| PRK07418 |
PRK07418 |
acetolactate synthase large subunit; |
3-549 |
4.10e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 236014 [Multi-domain] Cd Length: 616 Bit Score: 171.39 E-value: 4.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVG---VPIIEVAMAAQAAG-IKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGL 78
Cdd:PRK07418 18 RATGAYALMDSLKRHGVKHIFGYPGgaiLPIYDELYKAEAEGwLKHILVRHEQGAAHAADGYARATGKVGVCFGTSGPGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 79 IHALGGMANANVNCWPVIVLGGSSDRNQETTGAFQE-------FPQVEacrlYSKFSARPSSlemIPAVVEKAVRSSIYG 151
Cdd:PRK07418 98 TNLVTGIATAQMDSVPMVVITGQVPRPAIGTDAFQEtdifgitLPIVK----HSYVVRDPSD---MARIVAEAFHIASSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 152 RPGACYIDIAGDMVNAKIDRATVRFVSCCPA---PPVsQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVE 228
Cdd:PRK07418 171 RPGPVLIDIPKDVGQEEFDYVPVEPGSVKPPgyrPTV-KGNPRQINAALKLIEEAERPLLYVGGGAISAGAHAELKELAE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 229 VTGIPFLPTPMGKGVLPDDHPNCVA-------AARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQV 294
Cdd:PRK07418 250 RFQIPVTTTLMGKGAFDEHHPLSVGmlgmhgtAYANFAVTECDLLIAVGAR--------FDDRvtgkldeFASRAKVIHI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 295 DLCAEELSNNVRAASALLGDIKMVTSQLLEtvRSESWRFPSDSQWWatlREKITanaqitkalSLQTTLPMnyyTAFHHI 374
Cdd:PRK07418 322 DIDPAEVGKNRRPDVPIVGDVRKVLVKLLE--RSLEPTTPPRTQAW---LERIN---------RWKQDYPL---VVPPYE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 375 SELLPKDCII-----VSEGANTMDIGRTML-----LNHLPRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEG 444
Cdd:PRK07418 385 GEIYPQEVLLavrdlAPDAYYTTDVGQHQMwaaqfLRNGPRRWISSAGLGTM----GFGMPAAMGVKVALPDEEVICIAG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 445 DSAFGFSGMEAETMCRYKLPIIIIvinnngiysgVDPETWKAMEKM------------GDMTTIAPPVTLLPEaryeqvm 512
Cdd:PRK07418 461 DASFLMNIQELGTLAQYGINVKTV----------IINNGWQGMVRQwqesfygerysaSNMEPGMPDFVKLAE------- 523
|
570 580 590
....*....|....*....|....*....|....*..
gi 47085819 513 sAFGGHGYLVRTVEELRTALQDSLKNTQmPSLLNVLI 549
Cdd:PRK07418 524 -AFGVKGMVISERDQLKDAIAEALAHDG-PVLIDVHV 558
|
|
| PRK06456 |
PRK06456 |
acetolactate synthase large subunit; |
5-550 |
4.88e-46 |
|
acetolactate synthase large subunit;
Pssm-ID: 180569 [Multi-domain] Cd Length: 572 Bit Score: 170.40 E-value: 4.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMA----AQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIH 80
Cdd:PRK06456 3 TGARILVDSLKREGVKVIFGIPGLSNMQIYDAfvedLANGELRHVLMRHEQAAAHAADGYARASGVPGVCTATSGPGTTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 81 ALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDI 160
Cdd:PRK06456 83 LVTGLITAYWDSSPVIAITGQVPRSVMGKMAFQEADAMGVFENVTKYVIGIKRIDEIPQWIKNAFYIATTGRPGPVVIDI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 161 AGDMVNAKIDRATvrfvscCPAPPVSQA--------DCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGI 232
Cdd:PRK06456 163 PRDIFYEKMEEIK------WPEKPLVKGyrdfptriDRLALKKAAEILINAERPIILVGTGVVWSNATPEVLELAELLHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 233 PFLPTPMGKGVLPDDHPNCVA-------AARSRALLQADVIVLLGARLNWILHFGFPPRFSANVKIIQVDLCAEELSNNV 305
Cdd:PRK06456 237 PIVSTFPGKTAIPHDHPLYFGpmgyygrAEASMAALESDAMLVVGARFSDRTFTSYDEMVETRKKFIMVNIDPTDGEKAI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 306 RAASALLGDIKMVTSQLLETVRSESWRFpSDSQWWATLREKitanaqitkalslqttlpMNYYTAFHH------------ 373
Cdd:PRK06456 317 KVDVGIYGNAKIILRELIKAITELGQKR-DRSAWLKRVKEY------------------KEYYSQFYYteengklkpwki 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 374 ---ISELLPKDCIIvseganTMDIGRTMLLNHL------PRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEG 444
Cdd:PRK06456 378 mktIRQALPRDAIV------TTGVGQHQMWAEVfwevlePRTFLTSSGMGTM----GFGLPAAMGAKLARPDKVVVDLDG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 445 DSAFGFSGMEAETMCRYKLPIIIIVInnngiysgvDPETWKAMEKMGDM--TTIAPPVTLLPEARYEQVMSAFGGHGYLV 522
Cdd:PRK06456 448 DGSFLMTGTNLATAVDEHIPVISVIF---------DNRTLGLVRQVQDLffGKRIVGVDYGPSPDFVKLAEAFGALGFNV 518
|
570 580
....*....|....*....|....*...
gi 47085819 523 RTVEELRTALQDSLKNtQMPSLLNVLID 550
Cdd:PRK06456 519 TTYEDIEKSLKSAIKE-DIPAVIRVPVD 545
|
|
| TPP_enzyme_M |
pfam00205 |
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ... |
193-322 |
4.54e-45 |
|
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: 155.80 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 193 ITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGVLPDDHPNCV-------AAARSRALLQADV 265
Cdd:pfam00205 1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLGIPVVTTLMGKGAFPEDHPLYLgmlgmhgTPAANEALEEADL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 47085819 266 IVLLGARLNWILHFGFPPRFSANVKIIQVDLCAEELSNNVRAASALLGDIKMVTSQL 322
Cdd:pfam00205 81 VLAVGARFDDIRTTGKLPEFAPDAKIIHIDIDPAEIGKNYPVDVPIVGDAKETLEAL 137
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
1-464 |
5.81e-45 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 167.31 E-value: 5.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQA-AGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK08979 1 MEMLSGASMIVRSLIDEGVKHIFGYPGGSVLDIYDALHEkSGIEHILVRHEQAAVHMADGYARATGKVGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK08979 81 NTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVKDAEDIPEIIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNAKI--DRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPT 237
Cdd:PRK08979 161 LPKDCLNPAIlhPYEYPESIKMRSYNPTTSGHKGQIKRGLQALLAAKKPVLYVGGGAIISGADKQILQLAEKLNLPVVST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 238 PMGKGVLPDDHPNCVAAARSRALLQADVivllgARLNWILHFGFPPRFS-----------ANVKIIQVDLCAEELSNNVR 306
Cdd:PRK08979 241 LMGLGAFPGTHKNSLGMLGMHGRYEANM-----AMHNADLIFGIGVRFDdrttnnlekycPNATILHIDIDPSSISKTVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 307 AASALLGDIKMVTSQLLETVRSESWRFPSDS--QWWATL---REKitanaqitKALSLQTTL----PMNYYTAFHHISEl 377
Cdd:PRK08979 316 VDIPIVGSADKVLDSMLALLDESGETNDEAAiaSWWNEIevwRSR--------NCLAYDKSSerikPQQVIETLYKLTN- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 378 lpKDCIIVSegantmDIGRTMLLNHL------PRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFS 451
Cdd:PRK08979 387 --GDAYVAS------DVGQHQMFAALyypfdkPRRWINSGGLGTM----GFGLPAAMGVKFAMPDETVVCVTGDGSIQMN 454
|
490
....*....|...
gi 47085819 452 GMEAETMCRYKLP 464
Cdd:PRK08979 455 IQELSTALQYDIP 467
|
|
| PRK07524 |
PRK07524 |
5-guanidino-2-oxopentanoate decarboxylase; |
5-451 |
2.79e-44 |
|
5-guanidino-2-oxopentanoate decarboxylase;
Pssm-ID: 236041 [Multi-domain] Cd Length: 535 Bit Score: 164.76 E-value: 2.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PRK07524 3 TCGEALVRLLEAYGVETVFGIPGVHTVELYRGLAGSGIRHVTPRHEQGAGFMADGYARVSGKPGVCFIITGPGMTNIATA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRNQ--ETTGAFQEFP-QVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIA 161
Cdd:PRK07524 83 MGQAYADSIPMLVISSVNRRASlgKGRGKLHELPdQRAMVAGVAAFSHTLMSAEDLPEVLARAFAVFDSARPRPVHIEIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 162 GDMVNAKIDR-ATVRFVSCCPAPPVSQAdcreITQAVRLLKTSQSPLIIIGKGAayARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK07524 163 LDVLAAPADHlLPAPPTRPARPGPAPAA----LAQAAERLAAARRPLILAGGGA--LAAAAALRALAERLDAPVALTINA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHPNCVAAARS----RALL-QADVIVLLGARL---NWILHF--GFPprFSANvkIIQVDLCAEELSNNVRAASA 310
Cdd:PRK07524 237 KGLLPAGHPLLLGASQSlpavRALIaEADVVLAVGTELgetDYDVYFdgGFP--LPGE--LIRIDIDPDQLARNYPPALA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 311 LLGDIKMVTSQLLETVRSESWRFPsdsqwWATLREkitanAQITKALSLQTTLPMNYYTAF-HHISELLPkDCIIVSEGA 389
Cdd:PRK07524 313 LVGDARAALEALLARLPGQAAAAD-----WGAARV-----AALRQALRAEWDPLTAAQVALlDTILAALP-DAIFVGDST 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47085819 390 NTMDIGrTMLLNHL-PRHRLDAGT-FGTMGVGPGFAIAAAVLEQaqrfGQKVVCVEGDSAFGFS 451
Cdd:PRK07524 382 QPVYAG-NLYFDADaPRRWFNASTgYGTLGYGLPAAIGAALGAP----ERPVVCLVGDGGLQFT 440
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
1-464 |
2.30e-43 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 163.16 E-value: 2.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQA-AGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK06882 1 MKKLSGAEMVVQSLRDEGVEYVFGYPGGSVLDIYDAIHTlGGIEHVLVRHEQAAVHMADGYARSTGKVGCVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK06882 81 NAITGIATAYTDSVPLVILSGQVPSNLIGTDAFQECDMLGISRPVVKHSFIVKNAEDIPSTIKKAFYIASTGRPGPVVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNA--KIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPT 237
Cdd:PRK06882 161 IPKDMVNPanKFTYEYPEEVSLRSYNPTVQGHKGQIKKALKALLVAKKPVLFVGGGVITAECSEQLTQFAQKLNLPVTSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 238 PMGKGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARlnwilhfgFPPRFSANV-------KIIQVDLCAEELSN 303
Cdd:PRK06882 241 LMGLGAYPSTDKQFLGMlgmhgtyEANNAMHESDLILGIGVR--------FDDRTTNNLakycpnaKVIHIDIDPTSISK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 304 NVRAASALLGDIKMVTSQLLETVRSES-WRFPSD-SQWWATLREkitanAQITKALSLQTTL----PMNYYTAFHHISEl 377
Cdd:PRK06882 313 NVPAYIPIVGSAKNVLEEFLSLLEEENlAKSQTDlTAWWQQINE-----WKAKKCLEFDRTSdvikPQQVVEAIYRLTN- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 378 lpKDCIIVSegantmDIGRTMLLNHL------PRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFS 451
Cdd:PRK06882 387 --GDAYVAS------DVGQHQMFAALhypfdkPRRWINSGGAGTM----GFGLPAAIGVKFAHPEATVVCVTGDGSIQMN 454
|
490
....*....|...
gi 47085819 452 GMEAETMCRYKLP 464
Cdd:PRK06882 455 IQELSTAKQYDIP 467
|
|
| PRK06466 |
PRK06466 |
acetolactate synthase 3 large subunit; |
1-464 |
7.86e-43 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 180578 [Multi-domain] Cd Length: 574 Bit Score: 161.45 E-value: 7.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAA-QAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK06466 1 MELLSGAEMLVRALRDEGVEYIYGYPGGAVLHIYDALfKQDKVEHILVRHEQAATHMADGYARATGKTGVVLVTSGPGAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK06466 81 NAITGIATAYMDSIPMVVLSGQVPSTLIGEDAFQETDMVGISRPIVKHSFMVKHASEIPEIIKKAFYIAQSGRPGPVVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNA--KIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPT 237
Cdd:PRK06466 161 IPKDMTNPaeKFEYEYPKKVKLRSYSPAVRGHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLTELAHLLNLPVTNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 238 PMGKGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARLNWILHFGfPPRFSANVKIIQVDLCAEELSNNVRAASA 310
Cdd:PRK06466 241 LMGLGGFPGTDRQFLGMlgmhgtyEANMAMHHADVILAVGARFDDRVTNG-PAKFCPNAKIIHIDIDPASISKTIKADIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 311 LLGDIKMVTSQLLETVR--SESWRFPSDSQWWATLRE------KITANAQITKALSLQTTLPMNYytafhhisELLPKDC 382
Cdd:PRK06466 320 IVGPVESVLTEMLAILKeiGEKPDKEALAAWWKQIDEwrgrhgLFPYDKGDGGIIKPQQVVETLY--------EVTNGDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 383 IIVSegantmDIGRTMLLNHL------PRHRLDAGTFGTMGVGPGFAIAAAVLEQAqrfgQKVVCVEGDSAFGFSGMEAE 456
Cdd:PRK06466 392 YVTS------DVGQHQMFAAQyykfnkPNRWINSGGLGTMGFGLPAAMGVKLAFPD----QDVACVTGEGSIQMNIQELS 461
|
....*...
gi 47085819 457 TMCRYKLP 464
Cdd:PRK06466 462 TCLQYGLP 469
|
|
| PRK06965 |
PRK06965 |
acetolactate synthase 3 catalytic subunit; Validated |
3-554 |
2.51e-42 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 180780 [Multi-domain] Cd Length: 587 Bit Score: 160.35 E-value: 2.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVG--VPIIEVAMAAQAAgIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIH 80
Cdd:PRK06965 20 DSIGAEILMKALAAEGVEFIWGYPGgaVLYIYDELYKQDK-IQHVLVRHEQAAVHAADGYARATGKVGVALVTSGPGVTN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 81 ALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDI 160
Cdd:PRK06965 99 AVTGIATAYMDSIPMVVISGQVPTAAIGQDAFQECDTVGITRPIVKHNFLVKDVRDLAETVKKAFYIARTGRPGPVVVDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 161 AGDMVNAKIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK06965 179 PKDVSKTPCEYEYPKSVEMRSYNPVTKGHSGQIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLLGYPVTNTLMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARLNWILhFGFPPRFSANV-KIIQVDLCAEELSNNVRAASALL 312
Cdd:PRK06965 259 LGAYPASDKKFLGMlgmhgtyEANMAMQHCDVLIAIGARFDDRV-IGNPAHFASRPrKIIHIDIDPSSISKRVKVDIPIV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 313 GDIKMVTSQLLETVRSESWRFPSD--SQWWATLRE-------KITANAQITKALSLQTTLpmnyytafhhiSELLPKDCI 383
Cdd:PRK06965 338 GDVKEVLKELIEQLQTAEHGPDADalAQWWKQIEGwrsrdclKYDRESEIIKPQYVVEKL-----------WELTDGDAF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 384 IVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVLEQAqrfgQKVVCVEGDSAFGFSGMEAETMCRYK 462
Cdd:PRK06965 407 VCSDvGQHQMWAAQFYRFNE-PRRWINSGGLGTMGVGLPYAMGIKMAHPD----DDVVCITGEGSIQMCIQELSTCLQYD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 463 LPiiIIVINNNGIYSGVdPETWKAMEKMGDMTTiaPPVTLLPEarYEQVMSAFGGHGYLVRTVEELRTALQDSLKNTQMP 542
Cdd:PRK06965 482 TP--VKIISLNNRYLGM-VRQWQEIEYSKRYSH--SYMDALPD--FVKLAEAYGHVGMRIEKTSDVEPALREALRLKDRT 554
|
570
....*....|..
gi 47085819 543 SLLNVLIDPTSD 554
Cdd:PRK06965 555 VFLDFQTDPTEN 566
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
6-464 |
1.27e-41 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 158.36 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 6 GAQLIAAALKDQNVEYMFGIVGVPIIEVAMA-AQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PLN02470 15 GADILVEALEREGVDTVFAYPGGASMEIHQAlTRSNCIRNVLCRHEQGEVFAAEGYAKASGKVGVCIATSGPGATNLVTG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD- 163
Cdd:PLN02470 95 LADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRVIREAFFLASSGRPGPVLVDIPKDi 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 164 -------------MVNAKIDRatvrfvscCPAPPVSQadcrEITQAVRLLKTSQSPLIIIGKGAAYARaeKEVRELVEVT 230
Cdd:PLN02470 175 qqqlavpnwnqpmKLPGYLSR--------LPKPPEKS----QLEQIVRLISESKRPVVYVGGGCLNSS--EELREFVELT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 231 GIPFLPTPMGKGVLPDDHPNCV-------AAARSRALLQADVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDL 296
Cdd:PLN02470 241 GIPVASTLMGLGAFPASDELSLqmlgmhgTVYANYAVDSADLLLAFGVR--------FDDRvtgkleaFASRASIVHIDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 297 CAEELSNNVRAASALLGDIKMVTSQLLETVRSESWRFPSDSQWWATLREKitanaqitkalslQTTLPMNYYT------- 369
Cdd:PLN02470 313 DPAEIGKNKQPHVSVCADVKLALQGLNKLLEERKAKRPDFSAWRAELDEQ-------------KEKFPLSYPTfgdaipp 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 370 --AFHHISELLPKDCIIvSEGANTMDIGRTMLLNH-LPRHRLDAGTFGTMGVGPGFAIAAAvleqAQRFGQKVVCVEGDS 446
Cdd:PLN02470 380 qyAIQVLDELTDGNAII-STGVGQHQMWAAQWYKYkEPRRWLTSGGLGAMGFGLPAAIGAA----AANPDAIVVDIDGDG 454
|
490
....*....|....*...
gi 47085819 447 AFGFSGMEAETMCRYKLP 464
Cdd:PLN02470 455 SFIMNIQELATIHVENLP 472
|
|
| PRK07282 |
PRK07282 |
acetolactate synthase large subunit; |
5-464 |
1.94e-41 |
|
acetolactate synthase large subunit;
Pssm-ID: 180919 [Multi-domain] Cd Length: 566 Bit Score: 157.29 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAA-QAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:PRK07282 11 SGSDLVLETLRDLGVDTIFGYPGGAVLPLYDAIyNFEGIRHILARHEQGALHEAEGYAKSTGKLGVAVVTSGPGATNAIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD 163
Cdd:PRK07282 91 GIADAMSDSVPLLVFTGQVARAGIGKDAFQEADIVGITMPITKYNYQIRETADIPRIITEAVHIATTGRPGPVVIDLPKD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 164 MVNAKIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGV 243
Cdd:PRK07282 171 VSALETDFIYDPEVNLPSYQPTLEPNDMQIKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQIPVVTTLLGQGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 244 LPDDHPNCVAA-------ARSRALLQADVIVLLGARLNWILhFGFPPRFSANVKIIQVDLCAEELSNNVRAASALLGDIK 316
Cdd:PRK07282 251 IATSHPLFLGMggmhgsyAANIAMTEADFMINIGSRFDDRL-TGNPKTFAKNAKVAHIDIDPAEIGKIIKTDIPVVGDAK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 317 MVTSQLLE--TVRseswrfpSDSQWWAtlrEKITANAQITKALSLQTTLpMNYYTAFHHISELLPKDCIIVSE-GANTMD 393
Cdd:PRK07282 330 KALQMLLAepTVH-------NNTEKWI---EKVTKDKNRVRSYDKKERV-VQPQAVIERIGELTNGDAIVVTDvGQHQMW 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47085819 394 IGRTMLLNHlPRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFSGMEAETMCRYKLP 464
Cdd:PRK07282 399 AAQYYPYQN-ERQLVTSGGLGTM----GFGIPAAIGAKIANPDKEVILFVGDGGFQMTNQELAILNIYKVP 464
|
|
| sulphoacet_xsc |
TIGR03457 |
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde ... |
3-552 |
2.96e-41 |
|
sulfoacetaldehyde acetyltransferase; Members of this protein family are sulfoacetaldehyde acetyltransferase, an enzyme of taurine utilization. Taurine, or 2-aminoethanesulfonate, can be used by bacteria as a source of carbon, nitrogen, and sulfur. [Central intermediary metabolism, Other]
Pssm-ID: 132497 [Multi-domain] Cd Length: 579 Bit Score: 157.33 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHAL 82
Cdd:TIGR03457 1 KMTPSEAFVEVLVANGVTHAFGIMGSAFMDAMDLFPPAGIRFIPVVHEQGAGHMADGFARVTGRMSMVIGQNGPGVTNCV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 83 GGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRpGACYIDIAG 162
Cdd:TIGR03457 81 TAIAAAYWAHTPVVIVTPEAGTKTIGLGGFQEADQLPMFQEFTKYQGHVRHPSRMAEVLNRCFERAWREM-GPAQLNIPR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 163 DMVNAKIDRATVRFVSCCPAPpvsqADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKG 242
Cdd:TIGR03457 160 DYFYGEIDVEIPRPVRLDRGA----GGATSLAQAARLLAEAKFPVIISGGGVVMGDAVEECKALAERLGAPVVNSYLHND 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 243 VLPDDHPNCV-------AAARSRALLQADVIVLLGARLNwilHFGFPPR-----FSANVKIIQVDLCAEELSNNVRAASA 310
Cdd:TIGR03457 236 SFPASHPLWVgplgyqgSKAAMKLISDADVVLALGTRLG---PFGTLPQygidyWPKNAKIIQVDANAKMIGLVKKVTVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 311 LLGDIKMVTSQLLETV------------------RSESWrFPSDSQWwatLREKITANAQITKALSLQTTLPMNYYTAFH 372
Cdd:TIGR03457 313 ICGDAKAAAAEILQRLagkagdanraerkakiqaERSAW-EQELSEM---THERDPFSLDMIVEQRQEEGNWLHPRQVLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 373 HISELLPKDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFSG 452
Cdd:TIGR03457 389 ELEKAMPEDAIVSTDIGNINSVANSYLRFEKPRKFLAPMSFGNC----GYAFPTIIGAKIAAPDRPVVAYAGDGAWGMSM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 453 MEAETMCRYKLPIIIIVINNNGiysgvdpetWKAmEKMGDM---------TTIAPPVTLLPEARyeqvmsAFGGHGYLVR 523
Cdd:TIGR03457 465 NEIMTAVRHDIPVTAVVFRNRQ---------WGA-EKKNQVdfynnrfvgTELESELSFAGIAD------AMGAKGVVVD 528
|
570 580 590
....*....|....*....|....*....|.
gi 47085819 524 TVEELRTALQDSL--KNTQMPSLLNVLIDPT 552
Cdd:TIGR03457 529 KPEDVGPALKKAIaaQAEGKTTVIEIVCTRE 559
|
|
| PRK09107 |
PRK09107 |
acetolactate synthase 3 catalytic subunit; Validated |
3-464 |
2.16e-39 |
|
acetolactate synthase 3 catalytic subunit; Validated
Pssm-ID: 236380 [Multi-domain] Cd Length: 595 Bit Score: 152.17 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGIVG---VPIIEVAMaaQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK09107 10 QMTGAEMVVQALKDQGVEHIFGYPGgavLPIYDEIF--QQDDIQHILVRHEQGAGHAAEGYARSTGKPGVVLVTSGPGAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK09107 88 NAVTPLQDALMDSIPLVCITGQVPTHLIGSDAFQECDTVGITRPCTKHNWLVKDVNDLARVIHEAFHVATSGRPGPVVVD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNAKIDRATVRFVSCCPA-PPVSQADCREITQAVRLLKTSQSPLIIIGKGA--AYARAEKEVRELVEVTGIPFLP 236
Cdd:PRK09107 168 IPKDVQFATGTYTPPQKAPVHVSyQPKVKGDAEAITEAVELLANAKRPVIYSGGGVinSGPEASRLLRELVELTGFPITS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 237 TPMGKGVLPDDHPNCVAAARSRALLQA-------DVIVLLGARlnwilhfgFPPR-------FSANVKIIQVDLCAEELS 302
Cdd:PRK09107 248 TLMGLGAYPASGKNWLGMLGMHGTYEAnmamhdcDVMLCVGAR--------FDDRitgrldaFSPNSKKIHIDIDPSSIN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 303 NNVRAASALLGDIKMVTSQLLETVRSESWRFPSD--SQWWATLrEKITANAQITKALSLQTTLPmNYytAFHHISELLP- 379
Cdd:PRK09107 320 KNVRVDVPIIGDVGHVLEDMLRLWKARGKKPDKEalADWWGQI-ARWRARNSLAYTPSDDVIMP-QY--AIQRLYELTKg 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 380 KDCIIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGpgfaIAAAVLEQAQRFGQKVVCVEGDSAFGFSGMEAETM 458
Cdd:PRK09107 396 RDTYITTEvGQHQMWAAQFFGFEE-PNRWMTSGGLGTMGYG----LPAALGVQIAHPDALVIDIAGDASIQMCIQEMSTA 470
|
....*.
gi 47085819 459 CRYKLP 464
Cdd:PRK09107 471 VQYNLP 476
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
1-552 |
9.91e-38 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 147.07 E-value: 9.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVG---VPIIEVAMAAQAAGIK---YVGMRNEQAAcyAASAIGY--LTGRPAVCLV 72
Cdd:PRK08327 4 LTMYTAAELFLELLKELGVDYIFINSGtdyPPIIEAKARARAAGRPlpeFVICPHEIVA--ISMAHGYalVTGKPQAVMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 73 VSGPGLIHALGGMANANVNCWPVIVLGGSSDRNQEttGAF----------QE-FPQVEACRLYSKFSARPSSLEMIPAVV 141
Cdd:PRK08327 82 HVDVGTANALGGVHNAARSRIPVLVFAGRSPYTEE--GELgsrntrihwtQEmRDQGGLVREYVKWDYEIRRGDQIGEVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 142 EKAVRSSIYGRPGACYIDIAGDMVNAKIDRATV---RFVSccPAPPVSQADcrEITQAVRLLKTSQSPLIIIGKGAAYAR 218
Cdd:PRK08327 160 ARAIQIAMSEPKGPVYLTLPREVLAEEVPEVKAdagRQMA--PAPPAPDPE--DIARAAEMLAAAERPVIITWRAGRTAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 219 AEKEVRELVEVTGIP---FLPTPMgkgVLPDDHPnCVAAARSRALL-QADVIVLLGARLNWILHFGFPPrfsANVKIIQV 294
Cdd:PRK08327 236 GFASLRRLAEELAIPvveYAGEVV---NYPSDHP-LHLGPDPRADLaEADLVLVVDSDVPWIPKKIRPD---ADARVIQI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 295 DlcAEELSN-----NVRAASALLGDIKMVTSQLLETVRS----ESWRFPSDSQWWATLREKiTANAQITKALSLQTTLPM 365
Cdd:PRK08327 309 D--VDPLKSriplwGFPCDLCIQADTSTALDQLEERLKSlasaERRRARRRRAAVRELRIR-QEAAKRAEIERLKDRGPI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 366 NYYTAFHHISELLPKDCIIVSEgantmdigRTMLLNHLPRHRldAGTFGTMGVGP--GFAIAAAVLEQAQRFGQKVVCVE 443
Cdd:PRK08327 386 TPAYLSYCLGEVADEYDAIVTE--------YPFVPRQARLNK--PGSYFGDGSAGglGWALGAALGAKLATPDRLVIATV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 444 GDSAFGFSGMEA--ETMCRYKLPIIIIVInnngiysgvDPETWKAME-------------KMGDMttiaPPVTLLPEARY 508
Cdd:PRK08327 456 GDGSFIFGVPEAahWVAERYGLPVLVVVF---------NNGGWLAVKeavlevypegyaaRKGTF----PGTDFDPRPDF 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 47085819 509 EQVMSAFGGHGYLVRTVEELRTALQDSLKNT---QMPSLLNVLIDPT 552
Cdd:PRK08327 523 AKIAEAFGGYGERVEDPEELKGALRRALAAVrkgRRSAVLDVIVDRV 569
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
3-551 |
1.01e-37 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 146.83 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 3 EVTGAQLIAAALKDQNVEYMFGiVGVPIIeVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHAL 82
Cdd:PRK06112 13 NGTVAHAIARALKRHGVEQIFG-QSLPSA-LFLAAEAIGIRQIAYRTENAGGAMADGYARVSGKVAVVTAQNGPAATLLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 83 GGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAG 162
Cdd:PRK06112 91 APLAEALKASVPIVALVQDVNRDQTDRNAFQELDHIALFQSCTKWVRRVTVAERIDDYVDQAFTAATSGRPGPVVLLLPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 163 DMVNAKIDRATVRFVSCCPAPPV--SQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK06112 171 DLLTAAAAAPAAPRSNSLGHFPLdrTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGASAALAALQSLAGLPVATTNMG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHP-------NCVAA-ARSRALL----QADVIVLLGARLN------WILhfgfpprFSANVKIIQVDLCAEELS 302
Cdd:PRK06112 251 KGAVDETHPlslgvvgSLMGPrSPGRHLRdlvrEADVVLLVGTRTNqngtdsWSL-------YPEQAQYIHIDVDGEEVG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 303 NNVRAASaLLGDIKMVTSQLLETVRSE--SWRFPSDSQWWATLREKITANAQITKALSLQTTLPMNYYTAFHHISELLPK 380
Cdd:PRK06112 324 RNYEALR-LVGDARLTLAALTDALRGRdlAARAGRRAALEPAIAAGREAHREDSAPVALSDASPIRPERIMAELQAVLTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 381 DCIIVSEGANTmdigrTM-LLNHLPRHRldAGT-F----GTMGVGPG--FAIAAAVleqaQRFGQKVVCVEGDSAFGFSG 452
Cdd:PRK06112 403 DTIVVADASYS-----SIwVANFLTARR--AGMrFltprGLAGLGWGvpMAIGAKV----ARPGAPVICLVGDGGFAHVW 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 453 MEAETMCRYKLPIIIIVINNNGIYSGVDPETwkamEKMGDMTTiappVTLLPEARYEQVMSAFGGHGYLVRTVEELRTAL 532
Cdd:PRK06112 472 AELETARRMGVPVTIVVLNNGILGFQKHAET----VKFGTHTD----ACHFAAVDHAAIARACGCDGVRVEDPAELAQAL 543
|
570
....*....|....*....
gi 47085819 533 QDSLKNtQMPSLLNVLIDP 551
Cdd:PRK06112 544 AAAMAA-PGPTLIEVITDP 561
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
5-551 |
1.86e-37 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 145.74 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGG 84
Cdd:PRK06457 3 SVAEVIIRVLEDNGIQRIYGIPGDSIDPLVDAIRKSKVKYVQVRHEEGAALAASVEAKITGKPSACMGTSGPGSIHLLNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 85 MANANVNCWPVIVLGGSSDRNQETTGAFQEfpqVEACRLY---SKFSARPSSLEMIPAVVEKAVRSSIYGRpGACYIDIA 161
Cdd:PRK06457 83 LYDAKMDHAPVIALTGQVESDMIGHDYFQE---VNLTKLFddvAVFNQILINPENAEYIIRRAIREAISKR-GVAHINLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 162 GDMVNAKIDRATVRFVsccpapPVSQADCR-EITQAVRLLKTSQSPLIIIGKGAayARAEKEVRELVEVTGIPFLPTPMG 240
Cdd:PRK06457 159 VDILRKSSEYKGSKNT------EVGKVKYSiDFSRAKELIKESEKPVLLIGGGT--RGLGKEINRFAEKIGAPIIYTLNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 241 KGVLPDDHPNCVAA-------ARSRALLQADVIVLLGARLNWIlhfGFPPRfsaNVKIIQVDLCAEELSNNVRAASALLG 313
Cdd:PRK06457 231 KGILPDLDPKVMGGigllgtkPSIEAMDKADLLIMLGTSFPYV---NFLNK---SAKVIQVDIDNSNIGKRLDVDLSYPI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 314 DIkmvtSQLLETVRSESwrfpSDSQWWATLREKITANAQITKALSlQTTLPMNYYTAFHHISELLPKDCIIVSEGANTmd 393
Cdd:PRK06457 305 PV----AEFLNIDIEEK----SDKFYEELKGKKEDWLDSISKQEN-SLDKPMKPQRVAYIVSQKCKKDAVIVTDTGNV-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 394 igrTMLLNhlpRHRLDAG--TF------GTMGVG-PGfAIAAAVLEQAQRfgqKVVCVEGDSAFGFSGMEAETMCRYKLP 464
Cdd:PRK06457 374 ---TMWTA---RHFRASGeqTFifsawlGSMGIGvPG-SVGASFAVENKR---QVISFVGDGGFTMTMMELITAKKYDLP 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 465 iiiiviNNNGIYSGvdpetwkamEKMGdMTTIAPPVTLLPE-------ARYEQVMSAFGGHGYLVRTVEELRTALQDsLK 537
Cdd:PRK06457 444 ------VKIIIYNN---------SKLG-MIKFEQEVMGYPEwgvdlynPDFTKIAESIGFKGFRLEEPKEAEEIIEE-FL 506
|
570
....*....|....
gi 47085819 538 NTQMPSLLNVLIDP 551
Cdd:PRK06457 507 NTKGPAVLDAIVDP 520
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
4-458 |
2.64e-36 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 142.44 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 4 VTGAQLIAAALKDQNVEYMFGIVGV---PIIEvAMAAQAAgIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIH 80
Cdd:PRK07064 3 VTVGELIAAFLEQCGVKTAFGVISIhnmPILD-AIGRRGK-IRFVPARGEAGAVNMADAHARVSGGLGVALTSTGTGAGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 81 ALGGMANANVNCWPVIVLGGSSDRN--QETTGAFQEFP-QVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACY 157
Cdd:PRK07064 81 AAGALVEALTAGTPLLHITGQIETPylDQDLGYIHEAPdQLTMLRAVSKAAFRVRSAETALATIREAVRVALTAPTGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 158 IDIAGDMVNAKIDRATVRFVSCCPAPPVSQAdcrEITQAVRLLKTSQSPLIIIGKGAAYARaeKEVRELVEVtGIPFLPT 237
Cdd:PRK07064 161 VEIPIDIQAAEIELPDDLAPVHVAVPEPDAA---AVAELAERLAAARRPLLWLGGGARHAG--AEVKRLVDL-GFGVVTS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 238 PMGKGVLPDDHPNCVAA----ARSRALLQ-ADVIVLLGARL--NWILHFGFP-PRfsanvKIIQVDLCAEELSNNVRAAS 309
Cdd:PRK07064 235 TQGRGVVPEDHPASLGAfnnsAAVEALYKtCDLLLVVGSRLrgNETLKYSLAlPR-----PLIRVDADAAADGRGYPNDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 310 ALLGDIKMVTSQLLETVRSeswRFPSDSQWWATLREkitANAQITKALSLQttlpMNYYTAF-HHISELLPKDCIIVSeg 388
Cdd:PRK07064 310 FVHGDAARVLARLADRLEG---RLSVDPAFAADLRA---AREAAVADLRKG----LGPYAKLvDALRAALPRDGNWVR-- 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47085819 389 antmDI-------GRTMLLNHLPRHRLDAgTFGTMGVGPGFAIAAAVLEQaqrfGQKVVCVEGDSAFGFSGMEAETM 458
Cdd:PRK07064 378 ----DVtisnstwGNRLLPIFEPRANVHA-LGGGIGQGLAMAIGAALAGP----GRKTVGLVGDGGLMLNLGELATA 445
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
19-549 |
4.41e-35 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 139.36 E-value: 4.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 19 VEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALGGMANANVNCWPVIVL 98
Cdd:PRK07525 21 ITHAFGIIGSAFMDASDLFPPAGIRFIDVAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 99 GGSSDRNQETTGAFQEFPQVEACRLYSKFSAR---PSSL-EMIPAVVEKAVRSSiygrpGACYIDIAGDMVNAKIDR--- 171
Cdd:PRK07525 101 TPQAGTKTIGQGGFQEAEQMPMFEDMTKYQEEvrdPSRMaEVLNRVFDKAKRES-----GPAQINIPRDYFYGVIDVeip 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 172 ATVRFvsccPAPPVSQADCREitqAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGVLPDDHP-- 249
Cdd:PRK07525 176 QPVRL----ERGAGGEQSLAE---AAELLSEAKFPVILSGAGVVLSDAIEECKALAERLDAPVACGYLHNDAFPGSHPlw 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 250 -----NCVAAARSRALLQADVIVLLGARLNwilHFGFPPR-----FSANVKIIQVDLCAEELSNNVRAASALLGDIKMVT 319
Cdd:PRK07525 249 vgplgYNGSKAAMELIAKADVVLALGTRLN---PFGTLPQygidyWPKDAKIIQVDINPDRIGLTKKVSVGICGDAKAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 320 SQLLETVRSeswRFPSD--------------SQW------WATLREK--ITANAQITKAlslqTTLPMNYYTAFHHISEL 377
Cdd:PRK07525 326 RELLARLAE---RLAGDagreerkaliaaekSAWeqelssWDHEDDDpgTDWNEEARAR----KPDYMHPRQALREIQKA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 378 LPKDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMGVGPGfAIAAAVLEQAQRfgqKVVCVEGDSAFGFSGMEAET 457
Cdd:PRK07525 399 LPEDAIVSTDIGNNCSIANSYLRFEKGRKYLAPGSFGNCGYAFP-AIIGAKIACPDR---PVVGFAGDGAWGISMNEVMT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 458 MCRYKLPIIIIVINNNGiysgvdpetWKAmEKMG-----DMTTIAppVTLLPEARYEQVMSAFGGHGYLVRTVEELRTAL 532
Cdd:PRK07525 475 AVRHNWPVTAVVFRNYQ---------WGA-EKKNqvdfyNNRFVG--TELDNNVSYAGIAEAMGAEGVVVDTQEELGPAL 542
|
570
....*....|....*....
gi 47085819 533 QDSLK--NTQMPSLLNVLI 549
Cdd:PRK07525 543 KRAIDaqNEGKTTVIEIMC 561
|
|
| PDC1 |
COG3961 |
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ... |
7-551 |
7.38e-35 |
|
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: 138.37 E-value: 7.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 7 AQLIAAALKDQNVEYMFGIVG---VPIIEVAMAAqaAGIKYVGMRNEQAACYAASaiGYLTGRPAVCLVVS-GPGLIHAL 82
Cdd:COG3961 8 GDYLLDRLAELGIRHIFGVPGdynLPFLDAIEAH--PGIRWVGCCNELNAGYAAD--GYARVNGLGALVTTyGVGELSAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 83 GGMANANVNCWPVIVL-GGSSDRNQET---------TGAFQEFpqveaCRLYSKFSARPSSL------EMIPAVVEKAVR 146
Cdd:COG3961 84 NGIAGAYAERVPVVHIvGAPGTRAQRRgpllhhtlgDGDFDHF-----LRMFEEVTVAQAVLtpenaaAEIDRVLAAALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 147 ssiYGRPGacYIDIAGDMVNAKIDRATVRFVscCPAPPVSQADCREITQAVR-LLKTSQSPLIIIGKGAAYARAEKEVRE 225
Cdd:COG3961 159 ---EKRPV--YIELPRDVADAPIEPPEAPLP--LPPPASDPAALAAAVAAAAeRLAKAKRPVILAGVEVHRFGLQEELLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 226 LVEVTGIPFLPTPMGKGVLPDDHPNCV-----AAARS--RALL-QADVIVLLGARLNWILHFGFPPRFSANvKIIQVDlc 297
Cdd:COG3961 232 LAEKTGIPVATTLLGKSVLDESHPQFIgtyagAASSPevREYVeNADCVLCLGVVFTDTNTGGFTAQLDPE-RTIDIQ-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 298 aeelSNNVRAASALLGDIKMvtSQLLETVRSESWRFPSDSQwwatlrekitANAQITKALSLQTTLPMNYYTAFHHISEL 377
Cdd:COG3961 309 ----PDSVRVGGHIYPGVSL--ADFLEALAELLKKRSAPLP----------APAPPPPPPPAAPDAPLTQDRLWQRLQAF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 378 LPKDCIIVSegantmDIGrTMLLNhLPRHRLDAGT-------FGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGF 450
Cdd:COG3961 373 LDPGDIVVA------DTG-TSLFG-AADLRLPEGAtfiaqplWGSI----GYTLPAALGAALAAPDRRVILLVGDGAFQL 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 451 SGMEAETMCRYKLpiiiivinnngiysgvdpetwkamekmgdmttiaPPVTLL--------------PEA--------RY 508
Cdd:COG3961 441 TAQELSTMLRYGL----------------------------------KPIIFVlnndgytieraihgPDGpyndianwDY 486
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 47085819 509 EQVMSAFGGH---GYLVRTVEELRTALQDSLKNTQMPSLLNVLIDP 551
Cdd:COG3961 487 AKLPEAFGGGnalGFRVTTEGELEEALAAAEANTDRLTLIEVVLDK 532
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
5-551 |
1.02e-34 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 138.08 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMA-AQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:PRK08199 9 TGGQILVDALRANGVERVFCVPGESYLAVLDAlHDETDIRVIVCRQEGGAAMMAEAYGKLTGRPGICFVTRGPGATNASI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD 163
Cdd:PRK08199 89 GVHTAFQDSTPMILFVGQVARDFREREAFQEIDYRRMFGPMAKWVAEIDDAARIPELVSRAFHVATSGRPGPVVLALPED 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 164 MVnakIDRATVRFvsccpAPPVSQADCR----EITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPM 239
Cdd:PRK08199 169 VL---SETAEVPD-----APPYRRVAAApgaaDLARLAELLARAERPLVILGGSGWTEAAVADLRAFAERWGLPVACAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 240 GKGVLPDDHPNCVA----------AARSRallQADVIVLLGARLNWILHFGF----PPRFSAnvKIIQVDLCAEELSNNV 305
Cdd:PRK08199 241 RQDLFDNRHPNYAGdlglginpalAARIR---EADLVLAVGTRLGEVTTQGYtlldIPVPRQ--TLVHVHPDAEELGRVY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 306 RAASALLGDIKMVTSQL--LETVRSESWRfpsdsQWWATLREKITANAQitkalSLQTTLPMNYYTAFHHISELLPKDCI 383
Cdd:PRK08199 316 RPDLAIVADPAAFAAALaaLEPPASPAWA-----EWTAAAHADYLAWSA-----PLPGPGAVQLGEVMAWLRERLPADAI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 384 IvseganTMDIGR--TMLLNHLPRHRLD---AGTFGTMGVGPGFAIAAAvLEQAQRfgqKVVCVEGDSAFGFSGMEAETM 458
Cdd:PRK08199 386 I------TNGAGNyaTWLHRFFRFRRYRtqlAPTSGSMGYGLPAAIAAK-LLFPER---TVVAFAGDGCFLMNGQELATA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 459 CRYKLPIIIIVinnngiysgVDPETWKAM----EKMGDMTTIAppvTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQD 534
Cdd:PRK08199 456 VQYGLPIIVIV---------VNNGMYGTIrmhqEREYPGRVSG---TDLTNPDFAALARAYGGHGETVERTEDFAPAFER 523
|
570
....*....|....*..
gi 47085819 535 SLKNtQMPSLLNVLIDP 551
Cdd:PRK08199 524 ALAS-GKPALIEIRIDP 539
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
4-464 |
8.16e-34 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 135.66 E-value: 8.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 4 VTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:PRK07710 16 MTGAQMLIEALEKEGVEVIFGYPGGAVLPLYDALYDCGIPHILTRHEQGAIHAAEGYARISGKPGVVIATSGPGATNVVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYIDIAGD 163
Cdd:PRK07710 96 GLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVRKASDLPRIIKEAFHIATTGRPGPVLIDIPKD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 164 MVNAKIDRATVRFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGV 243
Cdd:PRK07710 176 MVVEEGEFCYDVQMDLPGYQPNYEPNLLQIRKLVQAVSVAKKPVILAGAGVLHAKASKELTSYAEQQEIPVVHTLLGLGG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 244 LPDDHPNCVAAA-------RSRALLQADVIVLLGARLNWILHfGFPPRFSANVKIIQVDLCAEELSNNVRAASALLGDIK 316
Cdd:PRK07710 256 FPADHPLFLGMAgmhgtytANMALYECDLLINIGARFDDRVT-GNLAYFAKEATVAHIDIDPAEIGKNVPTEIPIVADAK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 317 MVTSQLLEtvrsESWRFPSDSQWWATLREKitanaqitkalslQTTLPMNY---------YTAFHHISELLPKDCIIVSE 387
Cdd:PRK07710 335 QALQVLLQ----QEGKKENHHEWLSLLKNW-------------KEKYPLSYkrnsesikpQKAIEMLYEITKGEAIVTTD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47085819 388 -GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVLEQAqrfgQKVVCVEGDSAFGFSGMEAETMCRYKLP 464
Cdd:PRK07710 398 vGQHQMWAAQYYPFKT-PDKWVTSGGLGTMGFGLPAAIGAQLAKPD----ETVVAIVGDGGFQMTLQELSVIKELSLP 470
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
7-551 |
2.12e-29 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 122.40 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 7 AQLIAAALKDQNVEYMFGIVG---VPIieVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:PRK06546 6 AEQLVEQLVAAGVKRIYGIVGdslNPI--VDAVRRTGGIEWVHVRHEEAAAFAAAAEAQLTGKLAVCAGSCGPGNLHLIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQE-FPQveacRLY---SKFSARPSSLEMIPAVVEKAVRSSIyGRPGACYID 159
Cdd:PRK06546 84 GLYDAHRSGAPVLAIASHIPSAQIGSGFFQEtHPD----RLFvecSGYCEMVSSAEQAPRVLHSAIQHAV-AGGGVSVVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNAKIDRATVRfVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAekEVRELVEVTGIPFLPTPM 239
Cdd:PRK06546 159 LPGDIADEPAPEGFAP-SVISPRRPTVVPDPAEVRALADAINEAKKVTLFAGAGVRGAHA--EVLALAEKIKAPVGHSLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 240 GKGVLPDDHPNCVA-------AARSRALLQADVIVLLGArlnwilhfGFP-PRFSANVKIIQVDLCAEELSNNVRAASAL 311
Cdd:PRK06546 236 GKEWIQYDNPFDVGmsgllgyGAAHEAMHEADLLILLGT--------DFPyDQFLPDVRTAQVDIDPEHLGRRTRVDLAV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 312 LGDIKMVTSQLLETVRSESWRFPSDSqwwaTLREKITANAQITKALS--LQTTLPMNYYTAFHHISELLPKDCIIvsega 389
Cdd:PRK06546 308 HGDVAETIRALLPLVKEKTDRRFLDR----MLKKHARKLEKVVGAYTrkVEKHTPIHPEYVASILDELAADDAVF----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 390 nTMDIGRTML-----LNHLPRHRLdAGTF--GTMGVGPGFAIAAAVleqAQRfGQKVVCVEGDSAFGFSGMEAETMCRYK 462
Cdd:PRK06546 379 -TVDTGMCNVwaaryITPNGRRRV-IGSFrhGSMANALPHAIGAQL---ADP-GRQVISMSGDGGLSMLLGELLTVKLYD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 463 LPIIIIvinnngiysgVDPETWKAMEKMGDMTTIAPPV-TLLPEARYEQVMSAFGGHGYLVRTVEELRTALQDSLKNtQM 541
Cdd:PRK06546 453 LPVKVV----------VFNNSTLGMVKLEMLVDGLPDFgTDHPPVDYAAIAAALGIHAVRVEDPKDVRGALREAFAH-PG 521
|
570
....*....|
gi 47085819 542 PSLLNVLIDP 551
Cdd:PRK06546 522 PALVDVVTDP 531
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
5-163 |
4.58e-28 |
|
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: 109.95 E-value: 4.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAG-IKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:cd07039 1 TVADVIVETLENWGVKRVYGIPGDSINGLMDALRREGkIEFIQVRHEEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIyGRPGACYIDIAGD 163
Cdd:cd07039 81 GLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALFKDVAVYNETVTSPEQLPELLDRAIRTAI-AKRGVAVLILPGD 159
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
5-323 |
5.58e-27 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 115.09 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAG-IKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHALG 83
Cdd:PRK09124 4 TVADYIAKTLEQAGVKRIWGVTGDSLNGLSDSLRRMGtIEWMHTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGAFQE-FPQvEACRLYSKFSARPSSLEMIPAVVEKAVRSSIyGRPGACYIDIAG 162
Cdd:PRK09124 84 GLFDCHRNHVPVLAIAAHIPSSEIGSGYFQEtHPQ-ELFRECSHYCELVSNPEQLPRVLAIAMRKAI-LNRGVAVVVLPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 163 DMVNAKI-DRATVRFVscCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAekEVRELVEVTGIPFLPTPMGK 241
Cdd:PRK09124 162 DVALKPApERATPHWY--HAPQPVVTPAEEELRKLAALLNGSSNITLLCGSGCAGAHD--ELVALAETLKAPIVHALRGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 242 GVLPDDHPNCVA-------AARSRALLQADVIVLLGARlnwilhfgFPPR--FSANVKIIQVDLCAEELSNNVRAASALL 312
Cdd:PRK09124 238 EHVEYDNPYDVGmtgligfSSGYHAMMNCDTLLMLGTD--------FPYRqfYPTDAKIIQIDINPGSLGRRSPVDLGLV 309
|
330
....*....|.
gi 47085819 313 GDIKMVTSQLL 323
Cdd:PRK09124 310 GDVKATLAALL 320
|
|
| PRK11269 |
PRK11269 |
glyoxylate carboligase; Provisional |
1-464 |
7.96e-24 |
|
glyoxylate carboligase; Provisional
Pssm-ID: 183066 [Multi-domain] Cd Length: 591 Bit Score: 105.45 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIEVAMAAQAAG-IKYVGMRNEQAACYAASaiGYL---TGRPAVCLVVSGP 76
Cdd:PRK11269 1 MAKMRAVDAAVLVLEKEGVTTAFGVPGAAINPFYSAMRKHGgIRHILARHVEGASHMAE--GYTratAGNIGVCIGTSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 77 GLIHALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGAC 156
Cdd:PRK11269 79 AGTDMITGLYSASADSIPILCITGQAPRARLHKEDFQAVDIESIAKPVTKWAVTVREPALVPRVFQQAFHLMRSGRPGPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 157 YIDIAGDMVNAKI--DRATVRfvsccPAPPVSQADCR-EITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIP 233
Cdd:PRK11269 159 LIDLPFDVQVAEIefDPDTYE-----PLPVYKPAATRaQIEKALEMLNAAERPLIVAGGGVINADASDLLVEFAELTGVP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 234 FLPTPMGKGVLPDDHP------NCVAAAR--SRALLQADVIVLLGARlnWI-LHFGFPPRFSANVKIIQVDLCAEELSnn 304
Cdd:PRK11269 234 VIPTLMGWGAIPDDHPlmagmvGLQTSHRygNATLLASDFVLGIGNR--WAnRHTGSVEVYTKGRKFVHVDIEPTQIG-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 305 vRAASALLG---DIKMVTSQLLETVRS--ESWRFPSDSQWWATLREKitanaqitKALSLQTT----LPMNYYTAFHHIS 375
Cdd:PRK11269 310 -RVFGPDLGivsDAKAALELLVEVAREwkAAGRLPDRSAWVADCQER--------KRTLLRKThfdnVPIKPQRVYEEMN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 376 ELLPKDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMgvgpGFAIAAAVLEQAQRFGQKVVCVEGDSAFGFSGMEA 455
Cdd:PRK11269 381 KAFGRDTCYVSTIGLSQIAAAQFLHVYKPRHWINCGQAGPL----GWTIPAALGVRAADPDRNVVALSGDYDFQFLIEEL 456
|
....*....
gi 47085819 456 ETMCRYKLP 464
Cdd:PRK11269 457 AVGAQFNLP 465
|
|
| PRK08273 |
PRK08273 |
thiamine pyrophosphate protein; Provisional |
5-461 |
1.83e-21 |
|
thiamine pyrophosphate protein; Provisional
Pssm-ID: 181344 [Multi-domain] Cd Length: 597 Bit Score: 98.44 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 5 TGAQLIAAALKDQNVEYMFGIVGVPI--IEVAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLIHAL 82
Cdd:PRK08273 4 TVADFILERLREWGVRRVFGYPGDGIngLLGALGRADDKPEFVQARHEEMAAFMAVAHAKFTGEVGVCLATSGPGAIHLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 83 GGMANANVNCWPVIVLGGSSDRNQeTTGAFQEfpQVEACRLY----SKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYI 158
Cdd:PRK08273 84 NGLYDAKLDHVPVVAIVGQQARAA-LGGHYQQ--EVDLQSLFkdvaGAFVQMVTVPEQLRHLVDRAVRTALAERTVTAVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 159 ---DIAgDMVNAKIDRA--TVrFVSCCPAPPVSQADCREITQAVRLLKTSQSPLIIIGKGAAYARAekEVRELVEVTGIP 233
Cdd:PRK08273 161 lpnDVQ-ELEYEPPPHAhgTV-HSGVGYTRPRVVPYDEDLRRAAEVLNAGRKVAILVGAGALGATD--EVIAVAERLGAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 234 FLPTPMGKGVLPDDHPNCVAAarsrallqadvIVLLGARLNW----------ILHFGFP-----PRFSAnVKIIQVDLCA 298
Cdd:PRK08273 237 VAKALLGKAALPDDLPWVTGS-----------IGLLGTKPSYelmrecdtllMVGSSFPyseflPKEGQ-ARGVQIDIDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 299 EELSNNVRAASALLGDIKMVTSQLLETVRSE---SWR---FPSDSQWWATLREKITANAQitkalslqttlPMNYYTAFH 372
Cdd:PRK08273 305 RMLGLRYPMEVNLVGDAAETLRALLPLLERKkdrSWReriEKWVARWWETLEARAMVPAD-----------PVNPQRVFW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 373 HISELLPKDCIIvseganTMDIGRTMllNHLPRH-RLD-------AGTFGTMGVGPGFAIAAavleqaqRFG---QKVVC 441
Cdd:PRK08273 374 ELSPRLPDNAIL------TADSGSCA--NWYARDlRMRrgmmaslSGTLATMGPAVPYAIAA-------KFAhpdRPVIA 438
|
490 500
....*....|....*....|.
gi 47085819 442 VEGDSAFGFSGM-EAETMCRY 461
Cdd:PRK08273 439 LVGDGAMQMNGMaELITVAKY 459
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
64-550 |
9.88e-21 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 95.79 E-value: 9.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 64 TGRPAVCLVVSGPGLIHALGGMANANVNCWPVIVLGGSSDRNQETTGAF------QEFPqveacRLYSKFSARPSSLEMI 137
Cdd:PRK07092 71 TGNAAFVNLHSAAGVGNAMGNLFTAFKNHTPLVITAGQQARSILPFEPFlaavqaAELP-----KPYVKWSIEPARAEDV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 138 PAVVEKAVRSSIYGRPGACYIDIAGDmvnakiDRATvrfvsccPAPPVSQadcREITQAVRL-----------LKTSQSP 206
Cdd:PRK07092 146 PAAIARAYHIAMQPPRGPVFVSIPYD------DWDQ-------PAEPLPA---RTVSSAVRPdpaalarlgdaLDAARRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 207 LIIIGKGAAYARAEKEVRELVEVTGIPFLPTPM-GKGVLPDDHPN---CVAAAR---SRALLQADVIVLLGARLNWILHF 279
Cdd:PRK07092 210 ALVVGPAVDRAGAWDDAVRLAERHRAPVWVAPMsGRCSFPEDHPLfagFLPASRekiSALLDGHDLVLVIGAPVFTYHVE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 280 GFPPRFSANVKIIQvdlcaeeLSNNVRAAS------ALLGDIKMVTSQLLETVRseswrfpsdsqwwATLREKITANAQI 353
Cdd:PRK07092 290 GPGPHLPEGAELVQ-------LTDDPGEAAwapmgdAIVGDIRLALRDLLALLP-------------PSARPAPPARPMP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 354 TKALSLQTTLPMNYytAFHHISELLPKDCIIVSEGANTmdigRTMLLNHLPRHRldAGTFGTMGVGP-GFAIAAAVLEQA 432
Cdd:PRK07092 350 PPAPAPGEPLSVAF--VLQTLAALRPADAIVVEEAPST----RPAMQEHLPMRR--QGSFYTMASGGlGYGLPAAVGVAL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 433 QRFGQKVVCVEGDSAFGFSGMEAETMCRYKLPIIIIVinnngiysgVDPETWKAMEKMGDMTTIAP-PVTLLPEARYEQV 511
Cdd:PRK07092 422 AQPGRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVI---------LNNGRYGALRWFAPVFGVRDvPGLDLPGLDFVAL 492
|
490 500 510
....*....|....*....|....*....|....*....
gi 47085819 512 MSAFGGHGYLVRTVEELRTALQDSLKNTQmPSLLNVLID 550
Cdd:PRK07092 493 ARGYGCEAVRVSDAAELADALARALAADG-PVLVEVEVA 530
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
369-549 |
2.08e-20 |
|
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: 88.47 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 369 TAFHHISELLPKDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLeqaqRFGQKVVCVEGDSAF 448
Cdd:cd00568 1 RVLAALRAALPEDAIVVNDAGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALA----APDRPVVCIAGDGGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 449 GFSGMEAETMCRYKLPIIIIVinnngiysgVDPETWKAMEK-MGDMTTIAPPVTLLPEARYEQVMSAFGGHGYLVRTVEE 527
Cdd:cd00568 77 MMTGQELATAVRYGLPVIVVV---------FNNGGYGTIRMhQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPED 147
|
170 180
....*....|....*....|..
gi 47085819 528 LRTALQDSLkNTQMPSLLNVLI 549
Cdd:cd00568 148 LEAALAEAL-AAGGPALIEVKT 168
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
388-547 |
3.36e-19 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 84.56 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 388 GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVLeqaqRFGQKVVCVEGDSAFGFSGMEAETMCRYKLPIII 467
Cdd:pfam02775 3 GCHQMWAAQYYRFRP-PRRYLTSGGLGTMGYGLPAAIGAKLA----RPDRPVVAIAGDGGFQMNLQELATAVRYNLPITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 468 IVinnngiysgVDPETWkAMEK-----MGDMTTIAPPVTLLPEARYEQVMSAFGGHGYLVRTVEELRTALQDSLKNTQmP 542
Cdd:pfam02775 78 VV---------LNNGGY-GMTRgqqtpFGGGRYSGPSGKILPPVDFAKLAEAYGAKGARVESPEELEEALKEALEHDG-P 146
|
....*
gi 47085819 543 SLLNV 547
Cdd:pfam02775 147 ALIDV 151
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
8-162 |
1.90e-12 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 65.06 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 8 QLIAAALKDQNVEYMFGIVGVPIIEVAMAAQA-AGIKYVGMRNEQAACYAASAIGYLTGRPaVCLVVSGPGLIHALGGMA 86
Cdd:cd06586 1 AAFAEVLTAWGVRHVFGYPGDEISSLLDALREgDKRIIDTVIHELGAAGAAAGYARAGGPP-VVIVTSGTGLLNAINGLA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47085819 87 NANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSiYGRPGACYIDIAG 162
Cdd:cd06586 80 DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTA-YASQGPVVVRLPR 154
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
362-552 |
5.43e-12 |
|
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: 64.84 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 362 TLPMNYYTAFHHISELLPKDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMGvgpgFAIAAAVLEQAQRFGQKVVC 441
Cdd:cd02013 1 GNPMHPRQVLRELEKAMPEDAIVSTDIGNICSVANSYLRFEKPRSFIAPLSFGNCG----YALPAIIGAKAAAPDRPVVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 442 VEGDSAFGFSGMEAETMCRYKLPIIIIVinnngiysgVDPETWKAMEK----MGDMTTIAppvTLLPEARYEQVMSAFGG 517
Cdd:cd02013 77 IAGDGAWGMSMMEIMTAVRHKLPVTAVV---------FRNRQWGAEKKnqvdFYNNRFVG---TELESESFAKIAEACGA 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 47085819 518 HGYLVRTVEELRTALQDSL--KNTQMPSLLNVLIDPT 552
Cdd:cd02013 145 KGITVDKPEDVGPALQKAIamMAEGKTTVIEIVCDQE 181
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
364-551 |
4.70e-10 |
|
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: 58.70 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 364 PMNYYTAFHHISELLPKDCIIVSE-GANTMDIGRTMLLNHLPRHRLdAGTFGTMGVG-PGfAIAAAvLEQAQRfgqKVVC 441
Cdd:cd02014 1 PIHPERVAAELNKRAPDDAIFTIDvGNVTVWAARHLRMNGKQRFIL-SGLLATMGNGlPG-AIAAK-LAYPDR---QVIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 442 VEGDSAFGFSGMEAETMCRYKLPIIIiVINNNGIYSGVdpeTWKaMEKMGDMTTiappVTLLPEARYEQVMSAFGGHGYL 521
Cdd:cd02014 75 LSGDGGFAMLMGDLITAVKYNLPVIV-VVFNNSDLGFI---KWE-QEVMGQPEF----GVDLPNPDFAKIAEAMGIKGIR 145
|
170 180 190
....*....|....*....|....*....|
gi 47085819 522 VRTVEELRTALQDSLKnTQMPSLLNVLIDP 551
Cdd:cd02014 146 VEDPDELEAALDEALA-ADGPVVIDVVTDP 174
|
|
| TPP_ALS |
cd02010 |
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ... |
372-550 |
5.57e-10 |
|
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: 58.45 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 372 HHISELLPKDCIIVSE-GANTMDIGRtMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLeqaqRFGQKVVCVEGDSAFGF 450
Cdd:cd02010 6 HDLRAVMGDDDIVLLDvGAHKIWMAR-YYRTYAPNTCLISNGLATMGVALPGAIGAKLV----YPDRKVVAVSGDGGFMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 451 SGMEAETMCRYKLPIIIIVINNngiySGVDPETWKAMEKMG---DMTTIAPPVTLLPEaryeqvmsAFGGHGYLVRTVEE 527
Cdd:cd02010 81 NSQELETAVRLKIPLVVLIWND----NGYGLIKWKQEKEYGrdsGVDFGNPDFVKYAE--------SFGAKGYRIESADD 148
|
170 180
....*....|....*....|...
gi 47085819 528 LRTALQDSLKNTQmPSLLNVLID 550
Cdd:cd02010 149 LLPVLERALAADG-VHVIDCPVD 170
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
374-549 |
1.44e-09 |
|
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: 57.61 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 374 ISELLPKDCIIVSEgANTMDIGRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVleqAQRfGQKVVCVEGDSAFGFSGM 453
Cdd:cd02002 10 LAAALPEDAIIVDE-AVTNGLPLRDQLPLTRPGSYFTLRGGGLGWGLPAAVGAAL---ANP-DRKVVAIIGDGSFMYTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 454 EAETMCRYKLPIIIIVinnngiysgVDPETWKA----MEKMGDMTT----IAPPVTLLPEARYEQVMSAFGGHGYLVRTV 525
Cdd:cd02002 85 ALWTAARYGLPVTVVI---------LNNRGYGAlrsfLKRVGPEGPgenaPDGLDLLDPGIDFAAIAKAFGVEAERVETP 155
|
170 180
....*....|....*....|....
gi 47085819 526 EELRTALqDSLKNTQMPSLLNVLI 549
Cdd:cd02002 156 EELDEAL-REALAEGGPALIEVVV 178
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
370-551 |
1.29e-08 |
|
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: 54.81 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 370 AFHHISELLPKDCIIVSE-GANTMDIGRTMLLNHlPRHRLDAGTFGTMGVGPGFAIAAAVLeqaqRFGQKVVCVEGDSAF 448
Cdd:cd02015 6 VIKELSELTPGDAIVTTDvGQHQMWAAQYYRFKK-PRSWLTSGGLGTMGFGLPAAIGAKVA----RPDKTVICIDGDGSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 449 GFSGMEAETMCRYKLPIIII--------------VINNNGIYSGVDpetwkaMEKMGDMTTIAppvtllpearyeqvmSA 514
Cdd:cd02015 81 QMNIQELATAAQYNLPVKIVilnngslgmvrqwqELFYEGRYSHTT------LDSNPDFVKLA---------------EA 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 47085819 515 FGGHGYLVRTVEELRTALQDSLKnTQMPSLLNVLIDP 551
Cdd:cd02015 140 YGIKGLRVEKPEELEAALKEALA-SDGPVLLDVLVDP 175
|
|
| TPP_PYR_PDC_IPDC_like |
cd07038 |
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ... |
8-161 |
6.25e-07 |
|
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase (IPDC) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. Also belonging to this group is Mycobacterium tuberculosis alpha-keto acid decarboxylase (MtKDC) which participates in amino acid degradation via the Ehrlich pathway, and Lactococcus lactis branched-chain keto acid decarboxylase (KdcA) an enzyme identified as being involved in cheese ripening, which exhibits a very broad substrate range in the decarboxylation and carboligation reactions.
Pssm-ID: 132921 [Multi-domain] Cd Length: 162 Bit Score: 49.42 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 8 QLIAAALKDQNVEYMFGIVG---VPIIEVAMAAQaaGIKYVGMRNEQAACYAASaiGYLTGRPAVCLVVS-GPGLIHALG 83
Cdd:cd07038 1 EYLLERLKQLGVKHVFGVPGdynLPLLDAIEENP--GLRWVGNCNELNAGYAAD--GYARVKGLGALVTTyGVGELSALN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 84 GMANANVNCWPVIVLGGSSDRNQETTGA----------FQEFpqVEACRLYSKFSARPSSLEMIPAVVEKAVRSSI-YGR 152
Cdd:cd07038 77 GIAGAYAEHVPVVHIVGAPSTKAQASGLllhhtlgdgdFDVF--LKMFEEITCAAARLTDPENAAEEIDRVLRTALrESR 154
|
....*....
gi 47085819 153 PGacYIDIA 161
Cdd:cd07038 155 PV--YIEIP 161
|
|
| PLN02573 |
PLN02573 |
pyruvate decarboxylase |
41-250 |
7.89e-07 |
|
pyruvate decarboxylase
Pssm-ID: 215311 [Multi-domain] Cd Length: 578 Bit Score: 52.01 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 41 GIKYVGMRNEQAACYAASaiGYLTGRPAVCLVVS----GPGLIHALGGMANANVncwPVIVLGGSSDRN--------QET 108
Cdd:PLN02573 54 GLNLIGCCNELNAGYAAD--GYARARGVGACVVTftvgGLSVLNAIAGAYSENL---PVICIVGGPNSNdygtnrilHHT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 109 TGAfQEFPQVEAC-RLYSKFSARPSSL----EMIPAVVEKAVRSSiygRPgaCYIDIA---GDMVNAKIDRATVRFVScc 180
Cdd:PLN02573 129 IGL-PDFSQELRCfQTVTCYQAVINNLedahELIDTAISTALKES---KP--VYISVScnlAAIPHPTFSREPVPFFL-- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47085819 181 pAPPVSQADCRE--ITQAVRLLKTSQSPLIIIGKGAAYARAEKEVRELVEVTGIPFLPTPMGKGVLPDDHPN 250
Cdd:PLN02573 201 -TPRLSNKMSLEaaVEAAAEFLNKAVKPVLVGGPKLRVAKACKAFVELADASGYPVAVMPSAKGLVPEHHPH 271
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
1-549 |
2.24e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 47.17 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 1 MDEVTGAQLIAAALKDQNVEYMFGIVGVPIIE-VAMAAQAAGIKYVGMRNEQAACYAASAIGYLTGRPAVCLVVSGPGLI 79
Cdd:PRK12474 2 GQTMNGADSVVDTLLNCGVEVCFANPGTSEMHfVAALDRVPRMRPVLCLFEGVVTGAADGYGRIAGKPAVTLLHLGPGLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 80 HALGGMANANVNCWPVIVLGGSSDRNQETTGAFQEFPQVEACRLYSKFSARPSSLEMIPAVVEKAVRSSIYGRPGACYID 159
Cdd:PRK12474 82 NGLANLHNARRAASPIVNIVGDHAVEHLQYDAPLTSDIDGFARPVSRWVHRSASAGAVDSDVARAVQAAQSAPGGIATLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 160 IAGDMVNAKIDRATVRFVSCCPAPPVSQAdcreITQAVRLLKTS-QSPLIIIGKG--------AAYARAEKEVRELVEVt 230
Cdd:PRK12474 162 MPADVAWNEAAYAAQPLRGIGPAPVAAET----VERIAALLRNGkKSALLLRGSAlrgapleaAGRIQAKTGVRLYCDT- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 231 gipFLP-TPMGKGVLPDDHPNCVAAARSRALLQADVIVLLGARlNWILHFGFPPRFS----ANVKIIQVDLCAEELsnnv 305
Cdd:PRK12474 237 ---FAPrIERGAGRVPIERIPYFHEQITAFLKDVEQLVLVGAK-PPVSFFAYPGKPSwgapPGCEIVYLAQPDEDL---- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 306 raASALlgdikmvtsqlletvrseswrfpsdsQWWATlrekiTANAQITKALSLQTTLP------MNYYTAFHHISELLP 379
Cdd:PRK12474 309 --AQAL--------------------------QDLAD-----AVDAPAEPAARTPLALPalpkgaLNSLGVAQLIAHRTP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 380 kDCIIVSEGANTMDIGRTMLLNHLPRHRLDAGTFGTMGVGPGFAIAAAVLEQaqrfGQKVVCVEGDSAFGFSGMEAETMC 459
Cdd:PRK12474 356 -DQAIYADEALTSGLFFDMSYDRARPHTHLPLTGGSIGQGLPLAAGAAVAAP----DRKVVCPQGDGGAAYTMQALWTMA 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 460 RYKLpiiiivINNNGIYSGVDPET-WKAMEKMGDMTTIAPPVTLL----PEARYEQVMSAFGGHGYLVRTVEELRTALQD 534
Cdd:PRK12474 431 RENL------DVTVVIFANRSYAIlNGELQRVGAQGAGRNALSMLdlhnPELNWMKIAEGLGVEASRATTAEEFSAQYAA 504
|
570
....*....|....*
gi 47085819 535 SLKNtQMPSLLNVLI 549
Cdd:PRK12474 505 AMAQ-RGPRLIEAMI 518
|
|
| TPP_PDC_IPDC |
cd02005 |
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ... |
371-551 |
4.23e-05 |
|
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: 44.45 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 371 FHHISELLPKDCIIVSEGANTMDIGRTMLLnhlPRhrldagtfGTMGVGP------GFAIAAAV-LEQAQRFGqKVVCVE 443
Cdd:cd02005 8 WQQVQNFLKPNDILVAETGTSWFGALDLKL---PK--------GTRFISQplwgsiGYSVPAALgAALAAPDR-RVILLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085819 444 GDSAFGFSGMEAETMCRYKLPIIIIVinnngiysgVDPETWkAMEK-MGDMTT----IAPpvtllpeARYEQVMSAFG-- 516
Cdd:cd02005 76 GDGSFQMTVQELSTMIRYGLNPIIFL---------INNDGY-TIERaIHGPEAsyndIAN-------WNYTKLPEVFGgg 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 47085819 517 --GHGYLVRTVEELRTALQDSLKNTQMPSLLNVLIDP 551
Cdd:cd02005 139 ggGLSFRVKTEGELDEALKDALFNRDKLSLIEVILPK 175
|
|
| |
