NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|813212725|dbj|GAO47769|]
View 

hypothetical protein G7K_1968-t1 [Saitoella complicata NRRL Y-17804]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PDC1 super family cl34705
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
16-608 1.39e-156

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


The actual alignment was detected with superfamily member COG3961:

Pssm-ID: 443161 [Multi-domain]  Cd Length: 545  Bit Score: 487.74  E-value: 1.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   16 IQYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAH 95
Cdd:COG3961     8 GDYLLDRLAE-LGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAINGI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGhphqTLLYSSF---FKEISGSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:COG3961    87 AGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLG----DGDFDHFlrmFEEVTVAQAVLTPENAAAEIDRVLAAALREKRP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  173 VYIALPQDLVEMPLKKEGLS---RPLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPt 249
Cdd:COG3961   163 VYIELPRDVADAPIEPPEAPlplPPPASDPAALAAA----VAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTG- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  250 WPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGS 329
Cdd:COG3961   238 IPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  330 TFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPlptirPASDKFVRHAYFWPRVEKWLREDDVLCVEAGTSSFGAAD 409
Cdd:COG3961   318 IYPGVSLADFLEALAELLKKRSAPLPAPAPPPPPPP-----AAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAAD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  410 VRLPRGATMLSQWLWASIGFSvgatvgaavaaaegfqentkkrkaeeeeTVASNGDG-ADENggdgeakgrRRVICVVGD 488
Cdd:COG3961   393 LRLPEGATFIAQPLWGSIGYT----------------------------LPAALGAAlAAPD---------RRVILLVGD 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  489 GALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRGITREYNAINTgWDYSSTLSYFGsasssspdssASSVSTHVLN 568
Cdd:COG3961   436 GAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYNDIAN-WDYAKLPEAFG----------GGNALGFRVT 504
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 813212725  569 TESEFDEFLTTeANADPGNLRFVIVRFEDLDAPRMLKMMA 608
Cdd:COG3961   505 TEGELEEALAA-AEANTDRLTLIEVVLDKMDAPPLLKRLG 543
Ribosomal_S30 pfam04758
Ribosomal protein S30;
1507-1559 5.44e-32

Ribosomal protein S30;


:

Pssm-ID: 398432  Cd Length: 58  Bit Score: 118.91  E-value: 5.44e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 813212725  1507 KVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKRR 1559
Cdd:pfam04758    1 KVHGSLARAGKVRNQTPKVEKQEKKKKPTGRAKKRLQYNRRFVNVVPGGGRKK 53
 
Name Accession Description Interval E-value
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
16-608 1.39e-156

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: 487.74  E-value: 1.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   16 IQYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAH 95
Cdd:COG3961     8 GDYLLDRLAE-LGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAINGI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGhphqTLLYSSF---FKEISGSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:COG3961    87 AGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLG----DGDFDHFlrmFEEVTVAQAVLTPENAAAEIDRVLAAALREKRP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  173 VYIALPQDLVEMPLKKEGLS---RPLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPt 249
Cdd:COG3961   163 VYIELPRDVADAPIEPPEAPlplPPPASDPAALAAA----VAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTG- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  250 WPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGS 329
Cdd:COG3961   238 IPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  330 TFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPlptirPASDKFVRHAYFWPRVEKWLREDDVLCVEAGTSSFGAAD 409
Cdd:COG3961   318 IYPGVSLADFLEALAELLKKRSAPLPAPAPPPPPPP-----AAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAAD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  410 VRLPRGATMLSQWLWASIGFSvgatvgaavaaaegfqentkkrkaeeeeTVASNGDG-ADENggdgeakgrRRVICVVGD 488
Cdd:COG3961   393 LRLPEGATFIAQPLWGSIGYT----------------------------LPAALGAAlAAPD---------RRVILLVGD 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  489 GALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRGITREYNAINTgWDYSSTLSYFGsasssspdssASSVSTHVLN 568
Cdd:COG3961   436 GAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYNDIAN-WDYAKLPEAFG----------GGNALGFRVT 504
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 813212725  569 TESEFDEFLTTeANADPGNLRFVIVRFEDLDAPRMLKMMA 608
Cdd:COG3961   505 TEGELEEALAA-AEANTDRLTLIEVVLDKMDAPPLLKRLG 543
TPP_PYR_PDC_IPDC_like cd07038
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ...
17-178 1.81e-70

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: 233.16  E-value: 1.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHA 96
Cdd:cd07038     1 EYLLERLKQ-LGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   97 GAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGHPHqtllYSSF---FKEIS-GSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:cd07038    80 GAYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGD----FDVFlkmFEEITcAAARLTDPENAAEEIDRVLRTALRESRP 155

                  ....*.
gi 813212725  173 VYIALP 178
Cdd:cd07038   156 VYIEIP 161
PLN02573 PLN02573
pyruvate decarboxylase
18-541 6.54e-65

pyruvate decarboxylase


Pssm-ID: 215311 [Multi-domain]  Cd Length: 578  Bit Score: 231.90  E-value: 6.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   18 YLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHAG 97
Cdd:PLN02573   21 HLARRLVE-IGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSVLNAIAG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   98 AYAEQIPLIHLVGLPSTSQLSSSEILHHSLGHPH--QTLlysSFFKEISGSMLVVSETTRA-EEIDRALEIGVRRCLPVY 174
Cdd:PLN02573  100 AYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDfsQEL---RCFQTVTCYQAVINNLEDAhELIDTAISTALKESKPVY 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  175 IALPQDLVEMPlkKEGLSR--------PLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIAD----AGASRDNIS--AEV 240
Cdd:PLN02573  177 ISVSCNLAAIP--HPTFSRepvpffltPRLSNKMSLEAA----VEAAAEFLNKAVKPVLVGGpklrVAKACKAFVelADA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  241 SNlisslptWPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELH 320
Cdd:PLN02573  251 SG-------YPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  321 ATWTSV-DGSTFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPLPtIRPASDKFVRHAYFWPRVEKWLREDDVLCVE 399
Cdd:PLN02573  324 PDRVTIgNGPAFGCVLMKDFLEALAKRVKKNTTAYENYKRIFVPEGEP-LKSEPGEPLRVNVLFKHIQKMLSGDTAVIAE 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  400 AGTSSFGAADVRLPRGATMLSQWLWASIGFSVgatvgaavaaaegfqentkkrkaeeeetvasngdGAdeNGGDGEAKGR 479
Cdd:PLN02573  403 TGDSWFNCQKLKLPEGCGYEFQMQYGSIGWSV----------------------------------GA--TLGYAQAAPD 446
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 813212725  480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRgiTREYNAINTgWDYS 541
Cdd:PLN02573  447 KRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVEIH--DGPYNVIKN-WNYT 505
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
17-189 1.54e-34

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 460690 [Multi-domain]  Cd Length: 169  Bit Score: 130.43  E-value: 1.54e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725    17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:pfam02776    3 EALADVLKA-LGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTGL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725    96 AGAYAEQIPLIHLVGLPSTSQLssseilhhSLGHPHQTLLYSSFFKEISGSMLVVSETTRA-EEIDRALEIGV-RRCLPV 173
Cdd:pfam02776   82 ANAYVDSVPLLVISGQRPRSLV--------GRGALQQELDQLALFRPVTKWAVRVTSADEIpEVLRRAFRAALsGRPGPV 153
                          170
                   ....*....|....*.
gi 813212725   174 YIALPQDLVEMPLKKE 189
Cdd:pfam02776  154 YLEIPLDVLLEEVDED 169
Ribosomal_S30 pfam04758
Ribosomal protein S30;
1507-1559 5.44e-32

Ribosomal protein S30;


Pssm-ID: 398432  Cd Length: 58  Bit Score: 118.91  E-value: 5.44e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 813212725  1507 KVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKRR 1559
Cdd:pfam04758    1 KVHGSLARAGKVRNQTPKVEKQEKKKKPTGRAKKRLQYNRRFVNVVPGGGRKK 53
PTZ00467 PTZ00467
40S ribosomal protein S30; Provisional
1505-1558 1.75e-18

40S ribosomal protein S30; Provisional


Pssm-ID: 185646  Cd Length: 66  Bit Score: 80.97  E-value: 1.75e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 813212725 1505 MGKVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKR 1558
Cdd:PTZ00467    1 MGKIHGSLARAGKVKNQTPKVAKQEKPKQPRGRALKRLKYTRRFLAKTVKPGEK 54
 
Name Accession Description Interval E-value
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
16-608 1.39e-156

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: 487.74  E-value: 1.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   16 IQYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAH 95
Cdd:COG3961     8 GDYLLDRLAE-LGIRHIFGVPGDYNLPFLDAIEAHPGIRWVGCCNELNAGYAADGYARVNGLGALVTTYGVGELSAINGI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGhphqTLLYSSF---FKEISGSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:COG3961    87 AGAYAERVPVVHIVGAPGTRAQRRGPLLHHTLG----DGDFDHFlrmFEEVTVAQAVLTPENAAAEIDRVLAAALREKRP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  173 VYIALPQDLVEMPLKKEGLS---RPLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPt 249
Cdd:COG3961   163 VYIELPRDVADAPIEPPEAPlplPPPASDPAALAAA----VAAAAERLAKAKRPVILAGVEVHRFGLQEELLALAEKTG- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  250 WPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGS 329
Cdd:COG3961   238 IPVATTLLGKSVLDESHPQFIGTYAGAASSPEVREYVENADCVLCLGVVFTDTNTGGFTAQLDPERTIDIQPDSVRVGGH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  330 TFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPlptirPASDKFVRHAYFWPRVEKWLREDDVLCVEAGTSSFGAAD 409
Cdd:COG3961   318 IYPGVSLADFLEALAELLKKRSAPLPAPAPPPPPPP-----AAPDAPLTQDRLWQRLQAFLDPGDIVVADTGTSLFGAAD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  410 VRLPRGATMLSQWLWASIGFSvgatvgaavaaaegfqentkkrkaeeeeTVASNGDG-ADENggdgeakgrRRVICVVGD 488
Cdd:COG3961   393 LRLPEGATFIAQPLWGSIGYT----------------------------LPAALGAAlAAPD---------RRVILLVGD 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  489 GALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRGITREYNAINTgWDYSSTLSYFGsasssspdssASSVSTHVLN 568
Cdd:COG3961   436 GAFQLTAQELSTMLRYGLKPIIFVLNNDGYTIERAIHGPDGPYNDIAN-WDYAKLPEAFG----------GGNALGFRVT 504
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 813212725  569 TESEFDEFLTTeANADPGNLRFVIVRFEDLDAPRMLKMMA 608
Cdd:COG3961   505 TEGELEEALAA-AEANTDRLTLIEVVLDKMDAPPLLKRLG 543
TPP_PYR_PDC_IPDC_like cd07038
Pyrimidine (PYR) binding domain of pyruvate decarboxylase (PDC), indolepyruvate decarboxylase ...
17-178 1.81e-70

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: 233.16  E-value: 1.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHA 96
Cdd:cd07038     1 EYLLERLKQ-LGVKHVFGVPGDYNLPLLDAIEENPGLRWVGNCNELNAGYAADGYARVKGLGALVTTYGVGELSALNGIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   97 GAYAEQIPLIHLVGLPSTSQLSSSEILHHSLGHPHqtllYSSF---FKEIS-GSMLVVSETTRAEEIDRALEIGVRRCLP 172
Cdd:cd07038    80 GAYAEHVPVVHIVGAPSTKAQASGLLLHHTLGDGD----FDVFlkmFEEITcAAARLTDPENAAEEIDRVLRTALRESRP 155

                  ....*.
gi 813212725  173 VYIALP 178
Cdd:cd07038   156 VYIEIP 161
PLN02573 PLN02573
pyruvate decarboxylase
18-541 6.54e-65

pyruvate decarboxylase


Pssm-ID: 215311 [Multi-domain]  Cd Length: 578  Bit Score: 231.90  E-value: 6.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   18 YLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHAG 97
Cdd:PLN02573   21 HLARRLVE-IGVTDVFSVPGDFNLTLLDHLIAEPGLNLIGCCNELNAGYAADGYARARGVGACVVTFTVGGLSVLNAIAG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   98 AYAEQIPLIHLVGLPSTSQLSSSEILHHSLGHPH--QTLlysSFFKEISGSMLVVSETTRA-EEIDRALEIGVRRCLPVY 174
Cdd:PLN02573  100 AYSENLPVICIVGGPNSNDYGTNRILHHTIGLPDfsQEL---RCFQTVTCYQAVINNLEDAhELIDTAISTALKESKPVY 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  175 IALPQDLVEMPlkKEGLSR--------PLVKDIDNLSAAemrvISEVLGLLSSCSKPIIIAD----AGASRDNIS--AEV 240
Cdd:PLN02573  177 ISVSCNLAAIP--HPTFSRepvpffltPRLSNKMSLEAA----VEAAAEFLNKAVKPVLVGGpklrVAKACKAFVelADA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  241 SNlisslptWPLFVSAMGKGSVNEQHPSFAGTYMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELH 320
Cdd:PLN02573  251 SG-------YPVAVMPSAKGLVPEHHPHFIGTYWGAVSTPFCAEIVESADAYLFAGPIFNDYSSVGYSLLLKKEKAIIVQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  321 ATWTSV-DGSTFPGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPLPtIRPASDKFVRHAYFWPRVEKWLREDDVLCVE 399
Cdd:PLN02573  324 PDRVTIgNGPAFGCVLMKDFLEALAKRVKKNTTAYENYKRIFVPEGEP-LKSEPGEPLRVNVLFKHIQKMLSGDTAVIAE 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  400 AGTSSFGAADVRLPRGATMLSQWLWASIGFSVgatvgaavaaaegfqentkkrkaeeeetvasngdGAdeNGGDGEAKGR 479
Cdd:PLN02573  403 TGDSWFNCQKLKLPEGCGYEFQMQYGSIGWSV----------------------------------GA--TLGYAQAAPD 446
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 813212725  480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRgiTREYNAINTgWDYS 541
Cdd:PLN02573  447 KRVIACIGDGSFQVTAQDVSTMIRCGQKSIIFLINNGGYTIEVEIH--DGPYNVIKN-WNYT 505
TPP_PDC_IPDC cd02005
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...
378-605 8.38e-52

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: 180.42  E-value: 8.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  378 RHAYFWPRVEKWLREDDVLCVEAGTSSFGAADVRLPRGATMLSQWLWASIGFSvgatvgaavaaaegfqentkkrkaeee 457
Cdd:cd02005     3 TQARLWQQVQNFLKPNDILVAETGTSWFGALDLKLPKGTRFISQPLWGSIGYS--------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  458 eTVASNGDGAdenggdgeAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKYIRGITREYNAINTg 537
Cdd:cd02005    56 -VPAALGAAL--------AAPDRRVILLVGDGSFQMTVQELSTMIRYGLNPIIFLINNDGYTIERAIHGPEASYNDIAN- 125
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 813212725  538 WDYSSTLSYFGsasssspdsSASSVSTHVLNTESEFDEFLtTEANADPGNLRFVIVRFEDLDAPRMLK 605
Cdd:cd02005   126 WNYTKLPEVFG---------GGGGGLSFRVKTEGELDEAL-KDALFNRDKLSLIEVILPKDDAPEALK 183
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
17-518 2.90e-49

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: 184.98  E-value: 2.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:COG0028     7 DALVEALEA-EGVETVFGVPGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGkPGVCLVTSGPGATNLVTGL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGLPSTSQLSSseilhhslgHPHQTLLYSSFFKEISG-SMLVvsetTRAEEIDRALEIGVR-----R 169
Cdd:COG0028    86 ADAYMDSVPVLAITGQVPTSLIGR---------GAFQEVDQVGLFRPITKwSYLV----TDPEDLPEVLRRAFRiatsgR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  170 CLPVYIALPQDLVEMPLKKEGLSRPLvKDIDNLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPt 249
Cdd:COG0028   153 PGPVVLDIPKDVQAAEAEEEPAPPEL-RGYRPRPAPDPEAIEEAAELLAAAKRPVILAGGGARRAGAAEELRALAERLG- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  250 WPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGS 329
Cdd:COG0028   231 APVVTTLMGKGAFPEDHPLYLGM-LGMHGTPAANEALAEADLVLAVGARFDDRVTGNWDEFAPDAKIIHIDIDPAEIGKN 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  330 TFPGVGM----KSLLPRLASSLSPITSSAPIPPSPSLSLPLPTIR--PASDKFVRHAYFWPRVEKWLREDDVLCVEAGTS 403
Cdd:COG0028   310 YPVDLPIvgdaKAVLAALLEALEPRADDRAAWLARIAAWRAEYLAayAADDGPIKPQRVIAALREALPDDAIVVTDVGQH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  404 SFGAAD-VRLPRGATMLSQWLWASIGFsvgatvgaavaaaegfqentkkrkaeeeetvasnGDGAdengGDGEAKGR--R 480
Cdd:COG0028   390 QMWAARyLRFRRPRRFLTSGGLGTMGY----------------------------------GLPA----AIGAKLARpdR 431
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 813212725  481 RVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:COG0028   432 PVVAITGDGGFQMNLQELATAVRYGLPVKVVVLNNGGL 469
TPP_enzyme_N pfam02776
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
17-189 1.54e-34

Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;


Pssm-ID: 460690 [Multi-domain]  Cd Length: 169  Bit Score: 130.43  E-value: 1.54e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725    17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:pfam02776    3 EALADVLKA-LGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGkPGVVLVTSGPGATNALTGL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725    96 AGAYAEQIPLIHLVGLPSTSQLssseilhhSLGHPHQTLLYSSFFKEISGSMLVVSETTRA-EEIDRALEIGV-RRCLPV 173
Cdd:pfam02776   82 ANAYVDSVPLLVISGQRPRSLV--------GRGALQQELDQLALFRPVTKWAVRVTSADEIpEVLRRAFRAALsGRPGPV 153
                          170
                   ....*....|....*.
gi 813212725   174 YIALPQDLVEMPLKKE 189
Cdd:pfam02776  154 YLEIPLDVLLEEVDED 169
Ribosomal_S30 pfam04758
Ribosomal protein S30;
1507-1559 5.44e-32

Ribosomal protein S30;


Pssm-ID: 398432  Cd Length: 58  Bit Score: 118.91  E-value: 5.44e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 813212725  1507 KVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKRR 1559
Cdd:pfam04758    1 KVHGSLARAGKVRNQTPKVEKQEKKKKPTGRAKKRLQYNRRFVNVVPGGGRKK 53
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
17-179 1.72e-26

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: 107.05  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLrDDLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGAGALVTTFGVGELSAMNAHA 96
Cdd:cd06586     1 AAFAEVL-TAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   97 GAYAEQIPLIHLVGLPSTSQlssseilhHSLGHpHQTLLYSSFFKEISGSMLVV-SETTRAEEIDRALEIGVRRCLPVYI 175
Cdd:cd06586    80 DAAAEHLPVVFLIGARGISA--------QAKQT-FQSMFDLGMYRSIPEANISSpSPAELPAGIDHAIRTAYASQGPVVV 150

                  ....
gi 813212725  176 ALPQ 179
Cdd:cd06586   151 RLPR 154
TPP_PYR_POX_like cd07035
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ...
17-179 6.59e-23

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: 96.83  E-value: 6.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:cd07035     1 DALVEALKA-EGVDHVFGVPGGAILPLLDALAR-SGIRYILVRHEQGAVGMADGYARATGkPGVVLVTSGPGLTNAVTGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGLPSTSQLSSseilhhslgHPHQTLLYSSFFKEIS-GSMLVvsetTRAEEIDRALEIGVRRCL--- 171
Cdd:cd07035    79 ANAYLDSIPLLVITGQRPTAGEGR---------GAFQEIDQVALFRPITkWAYRV----TSPEEIPEALRRAFRIALsgr 145
                         170
                  ....*....|
gi 813212725  172 --PVYIALPQ 179
Cdd:cd07035   146 pgPVALDLPK 155
PTZ00467 PTZ00467
40S ribosomal protein S30; Provisional
1505-1558 1.75e-18

40S ribosomal protein S30; Provisional


Pssm-ID: 185646  Cd Length: 66  Bit Score: 80.97  E-value: 1.75e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 813212725 1505 MGKVHGSLARAGKVKSQCPKVEKQEKKKTPKGRAYKRMVYNRRFVNVTLTGGKR 1558
Cdd:PTZ00467    1 MGKIHGSLARAGKVKNQTPKVAKQEKPKQPRGRALKRLKYTRRFLAKTVKPGEK 54
TPP_enzyme_M pfam00205
Thiamine pyrophosphate enzyme, central domain; The central domain of TPP enzymes contains a ...
210-305 3.92e-17

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: 79.53  E-value: 3.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   210 ISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPtWPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAA 289
Cdd:pfam00205    1 IEKAAELLKKAKRPVILAGGGVRRSGASEELRELAEKLG-IPVVTTLMGKGAFPEDHPLYLG-MLGMHGTPAANEALEEA 78
                           90
                   ....*....|....*.
gi 813212725   290 DFVLSIGALASDFNTG 305
Cdd:pfam00205   79 DLVLAVGARFDDIRTT 94
PRK08322 PRK08322
acetolactate synthase large subunit;
32-296 1.91e-16

acetolactate synthase large subunit;


Pssm-ID: 236239 [Multi-domain]  Cd Length: 547  Bit Score: 84.49  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   32 IFGVPGDFNLPALDYVEDFPgMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIHL-- 108
Cdd:PRK08322   19 IFGIPGEENLDLLEALRDSS-IKLILTRHEQGAAFMAATYGRLTGkAGVCLSTLGPGATNLVTGVAYAQLGGMPMVAItg 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  109 -VGLPSTSQLSsseilhhslghpHQTLLYSSFFKEI--------SGSML--VVSETTR-AEEidraleigvRRCLPVYIA 176
Cdd:PRK08322   98 qKPIKRSKQGS------------FQIVDVVAMMAPLtkwtrqivSPDNIpeVVREAFRlAEE---------ERPGAVHLE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  177 LPQDLVEMplkkEGLSRPLVKDIDNLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPTwPLFVSA 256
Cdd:PRK08322  157 LPEDIAAE----ETDGKPLPRSYSRRPYASPKAIERAAEAIQAAKNPLILIGAGANRKTASKALTEFVDKTGI-PFFTTQ 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 813212725  257 MGKGSVNEQHPSFagtyMGTLSLPP---VRTAVEAADFVLSIG 296
Cdd:PRK08322  232 MGKGVIPETHPLS----LGTAGLSQgdyVHCAIEHADLIINVG 270
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
21-296 4.87e-16

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 83.66  E-value: 4.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   21 HRLRDDLH---INSIFG--VPGDFNLPALDYvedfpGMKWIGAVNELNGGYAADGYARVKGAGALVTtfgvgelsAMNAH 95
Cdd:PRK06112   18 HAIARALKrhgVEQIFGqsLPSALFLAAEAI-----GIRQIAYRTENAGGAMADGYARVSGKVAVVT--------AQNGP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGA-----YAE----QIPLIHLVGLPSTSQLSSSEIlhhslghphQTLLYSSFFKEISGSMLVVSETTRAEE-IDRALEI 165
Cdd:PRK06112   85 AATllvapLAEalkaSVPIVALVQDVNRDQTDRNAF---------QELDHIALFQSCTKWVRRVTVAERIDDyVDQAFTA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  166 GVR-RCLPVYIALPQDLVEMPLKKEGLSRPlvkdiDNL-------SAAEMRVISEVLGLLSSCSKPIIIADAGASRDNIS 237
Cdd:PRK06112  156 ATSgRPGPVVLLLPADLLTAAAAAPAAPRS-----NSLghfpldrTVPAPQRLAEAASLLAQAQRPVVVAGGGVHISGAS 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725  238 AEVSNLiSSLPTWPLFVSAMGKGSVNEQHPSFAG---TYMGTLSLPP-VRTAVEAADFVLSIG 296
Cdd:PRK06112  231 AALAAL-QSLAGLPVATTNMGKGAVDETHPLSLGvvgSLMGPRSPGRhLRDLVREADVVLLVG 292
PRK06276 PRK06276
acetolactate synthase large subunit;
29-305 5.50e-16

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 83.27  E-value: 5.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIH 107
Cdd:PRK06276   16 VKIIFGYPGGALLPFYDALYD-SDLIHILTRHEQAAAHAADGYARASGkVGVCVATSGPGATNLVTGIATAYADSSPVIA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  108 LVGLPSTsqlssseilhhslghphqTLLYSSFFKEISGSMLVVSET------TRAEEI----DRALEIGVR-RCLPVYIA 176
Cdd:PRK06276   95 LTGQVPT------------------KLIGNDAFQEIDALGIFMPITkhnfqiKKPEEIpeifRAAFEIAKTgRPGPVHID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  177 LPQDLVEMPLKKEglSRPLVKDID-----NLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLiSSLPTWP 251
Cdd:PRK06276  157 LPKDVQEGELDLE--KYPIPAKIDlpgykPTTFGHPLQIKKAAELIAEAERPVILAGGGVIISGASEELIEL-SELVKIP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 813212725  252 LFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK06276  234 VCTTLMGKGAFPEDHPLALGM-VGMHGTKAANYSVTESDVLIAIGCRFSDRTTG 286
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
19-518 2.72e-13

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 74.61  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   19 LLHRLRddlhINSIFGVPGDFNLPAL-DYVEDFpgmKWIGAVNELNGGYAADGYARVKGAGALV---TTFGVGelSAMNA 94
Cdd:PRK07092   21 LLRRFG----ITTVFGNPGSTELPFLrDFPDDF---RYVLGLQEAVVVGMADGYAQATGNAAFVnlhSAAGVG--NAMGN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   95 HAGAYAEQIPLIHLVGLPSTSQLssseilhhslghPHQTLLYSSFFKEISGSMLVVS-ETTRAEEIDRALEIGVR----- 168
Cdd:PRK07092   92 LFTAFKNHTPLVITAGQQARSIL------------PFEPFLAAVQAAELPKPYVKWSiEPARAEDVPAAIARAYHiamqp 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  169 RCLPVYIALPQDLVEMPlkKEGLSRPLVKDIDNLSAAEMRVISEVLGllsSCSKPIIIADAGASRDNISAEVSNLISSLP 248
Cdd:PRK07092  160 PRGPVFVSIPYDDWDQP--AEPLPARTVSSAVRPDPAALARLGDALD---AARRPALVVGPAVDRAGAWDDAVRLAERHR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  249 TwPLFVSAM-GKGSVNEQHPSFAGTymgtlsLPPVRTAVEAA----DFVLSIGALASDFNT-GFGSMDFEGKVVVEL--- 319
Cdd:PRK07092  235 A-PVWVAPMsGRCSFPEDHPLFAGF------LPASREKISALldghDLVLVIGAPVFTYHVeGPGPHLPEGAELVQLtdd 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  320 --HATWTSVDGSTF--PGVGMKSLLPRLASSLSPITSSAPIPPSPSLSLPlptirPASDKFVRHAYfwprveKWLREDDV 395
Cdd:PRK07092  308 pgEAAWAPMGDAIVgdIRLALRDLLALLPPSARPAPPARPMPPPAPAPGE-----PLSVAFVLQTL------AALRPADA 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  396 LCVEAGTSSFGAadvrlprgatmlsqwlwasigfsvgatvgaavaaaegFQENTKKRKAEEEETVASNGDGADENGGDGE 475
Cdd:PRK07092  377 IVVEEAPSTRPA-------------------------------------MQEHLPMRRQGSFYTMASGGLGYGLPAAVGV 419
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 813212725  476 AKGR--RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:PRK07092  420 ALAQpgRRVIGLIGDGSAMYSIQALWSAAQLKLPVTFVILNNGRY 464
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
28-296 5.55e-13

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 73.49  E-value: 5.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   28 HINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGelsAMNAhAGAYAEQI--- 103
Cdd:PRK07064   17 GVKTAFGVISIHNMPILDAIGRRGKIRFVPARGEAGAVNMADAHARVSGGlGVALTSTGTG---AGNA-AGALVEALtag 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  104 -PLIHLvglpsTSQLsSSEILHHSLGHPHQTLLYSSFFKEISGSMLVVSETTRAEEIdraLEIGVRRCL-----PVYIAL 177
Cdd:PRK07064   93 tPLLHI-----TGQI-ETPYLDQDLGYIHEAPDQLTMLRAVSKAAFRVRSAETALAT---IREAVRVALtaptgPVSVEI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  178 PQDL----VEMPLkkegLSRPLVKDIDNLSAAEmrvISEVLGLLSSCSKPIIIADAGASrdNISAEVSNLISSlpTWPLF 253
Cdd:PRK07064  164 PIDIqaaeIELPD----DLAPVHVAVPEPDAAA---VAELAERLAAARRPLLWLGGGAR--HAGAEVKRLVDL--GFGVV 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 813212725  254 VSAMGKGSVNEQHPSFAGTYMGTlslPPVRTAVEAADFVLSIG 296
Cdd:PRK07064  233 TSTQGRGVVPEDHPASLGAFNNS---AAVEALYKTCDLLLVVG 272
PRK07524 PRK07524
5-guanidino-2-oxopentanoate decarboxylase;
65-311 5.68e-13

5-guanidino-2-oxopentanoate decarboxylase;


Pssm-ID: 236041 [Multi-domain]  Cd Length: 535  Bit Score: 73.47  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   65 GYAADGYARVKG--AGALVTTfGVGELSAMNAHAGAYAEQIPLIHLVGLPSTSQLSsseilhHSLGHPHQTLLYSSFFKE 142
Cdd:PRK07524   52 GFMADGYARVSGkpGVCFIIT-GPGMTNIATAMGQAYADSIPMLVISSVNRRASLG------KGRGKLHELPDQRAMVAG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  143 ISgsmlVVSET-TRAEE----IDRA---LEIGvrRCLPVYIALPQDLVEMPLkKEGLSRPLVKDIDNLSAAEMrvISEVL 214
Cdd:PRK07524  125 VA----AFSHTlMSAEDlpevLARAfavFDSA--RPRPVHIEIPLDVLAAPA-DHLLPAPPTRPARPGPAPAA--LAQAA 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  215 GLLSSCSKPIIIADAGASRDNisAEVSNLISSLPTwPLFVSAMGKGSVNEQHPSFAGtymGTLSLPPVRTAVEAADFVLS 294
Cdd:PRK07524  196 ERLAAARRPLILAGGGALAAA--AALRALAERLDA-PVALTINAKGLLPAGHPLLLG---ASQSLPAVRALIAEADVVLA 269
                         250
                  ....*....|....*..
gi 813212725  295 IGalasdfnTGFGSMDF 311
Cdd:PRK07524  270 VG-------TELGETDY 279
PRK06048 PRK06048
acetolactate synthase large subunit;
29-305 1.69e-12

acetolactate synthase large subunit;


Pssm-ID: 180368 [Multi-domain]  Cd Length: 561  Bit Score: 72.11  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIH 107
Cdd:PRK06048   23 VEVIFGYPGGAIIPVYDELYD-SDLRHILVRHEQAAAHAADGYARATGkVGVCVATSGPGATNLVTGIATAYMDSVPIVA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  108 LVGLPSTSqlssseilhhslghphqtLLYSSFFKE--ISGSMLVVSE----TTRAEEIDR----ALEIG-VRRCLPVYIA 176
Cdd:PRK06048  102 LTGQVPRS------------------MIGNDAFQEadITGITMPITKhnylVQDAKDLPRiikeAFHIAsTGRPGPVLID 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  177 LPQDL------------VEMPLKKeglsrPLVKdidnlsaAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLI 244
Cdd:PRK06048  164 LPKDVttaeidfdypdkVELRGYK-----PTYK-------GNPQQIKRAAELIMKAERPIIYAGGGVISSNASEELVELA 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 813212725  245 SSLPTwPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK06048  232 ETIPA-PVTTTLMGIGAIPTEHPLSLG-MLGMHGTKYANYAIQESDLIIAVGARFDDRVTG 290
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
476-518 3.25e-12

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 65.68  E-value: 3.25e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 813212725   476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:pfam02775   43 ARPDRPVVAIAGDGGFQMNLQELATAVRYNLPITVVVLNNGGY 85
PRK06456 PRK06456
acetolactate synthase large subunit;
29-336 4.08e-12

acetolactate synthase large subunit;


Pssm-ID: 180569 [Multi-domain]  Cd Length: 572  Bit Score: 71.02  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALD-YVEDFPG--MKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK06456   17 VKVIFGIPGLSNMQIYDaFVEDLANgeLRHVLMRHEQAAAHAADGYARASGVpGVCTATSGPGTTNLVTGLITAYWDSSP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  105 LIHLVGlpstsQLSSSEILHHSLGHPHQTLLYSSFFKeisgsmlVVSETTRAEEIDRALE-----IGVRRCLPVYIALPQ 179
Cdd:PRK06456   97 VIAITG-----QVPRSVMGKMAFQEADAMGVFENVTK-------YVIGIKRIDEIPQWIKnafyiATTGRPGPVVIDIPR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  180 DLVEMPLKK-EGLSRPLVKDIDNLSAAEMRV-ISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLiSSLPTWPLFVSAM 257
Cdd:PRK06456  165 DIFYEKMEEiKWPEKPLVKGYRDFPTRIDRLaLKKAAEILINAERPIILVGTGVVWSNATPEVLEL-AELLHIPIVSTFP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  258 GKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFN-TGFGSMDFEGKVVVELHATWTSVDGSTFPGVGM 336
Cdd:PRK06456  244 GKTAIPHDHPLYFGP-MGYYGRAEASMAALESDAMLVVGARFSDRTfTSYDEMVETRKKFIMVNIDPTDGEKAIKVDVGI 322
PRK07282 PRK07282
acetolactate synthase large subunit;
17-305 7.84e-12

acetolactate synthase large subunit;


Pssm-ID: 180919 [Multi-domain]  Cd Length: 566  Bit Score: 69.85  E-value: 7.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLRDdLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGELSAMNAH 95
Cdd:PRK07282   14 DLVLETLRD-LGVDTIFGYPGGAVLPLYDAIYNFEGIRHILARHEQGALHEAEGYAKSTGKlGVAVVTSGPGATNAITGI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGLPSTSQLSSSEILH-HSLGHPHQTLLYSSFFKEISGSMLVVSEttraeeidrALEIGVR-RCLPV 173
Cdd:PRK07282   93 ADAMSDSVPLLVFTGQVARAGIGKDAFQEaDIVGITMPITKYNYQIRETADIPRIITE---------AVHIATTgRPGPV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  174 YIALPQDLVEmpLKKEGLSRPLVK---DIDNLSAAEMRvISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPTw 250
Cdd:PRK07282  164 VIDLPKDVSA--LETDFIYDPEVNlpsYQPTLEPNDMQ-IKKILKQLSKAKKPVILAGGGINYAEAATELNAFAERYQI- 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 813212725  251 PLFVSAMGKGSVNEQHPSFAGtyMGTLSLP-PVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK07282  240 PVVTTLLGQGTIATSHPLFLG--MGGMHGSyAANIAMTEADFMINIGSRFDDRLTG 293
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
390-518 4.96e-11

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: 63.04  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  390 LREDDVLCVEAGTSSFGAAD-VRLPRGATMLSQWLWASIGFSVGAtvgaavaaaegfqentkkrkaeeeetvasnGDGAd 468
Cdd:cd00568    10 LPEDAIVVNDAGNSAYWAYRyLPLRRGRRFLTSTGFGAMGYGLPA------------------------------AIGA- 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 813212725  469 enggdGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:cd00568    59 -----ALAAPDRPVVCIAGDGGFMMTGQELATAVRYGLPVIVVVFNNGGY 103
PRK06882 PRK06882
acetolactate synthase 3 large subunit;
17-516 9.02e-11

acetolactate synthase 3 large subunit;


Pssm-ID: 168717 [Multi-domain]  Cd Length: 574  Bit Score: 66.48  E-value: 9.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   17 QYLLHRLRDDlHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAH 95
Cdd:PRK06882    8 EMVVQSLRDE-GVEYVFGYPGGSVLDIYDAIHTLGGIEHVLVRHEQAAVHMADGYARSTGkVGCVLVTSGPGATNAITGI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   96 AGAYAEQIPLIHLVGlpstsQLSSSeilhhslghphqtLLYSSFFKE----------ISGSMLVVSETTRAEEIDRALEI 165
Cdd:PRK06882   87 ATAYTDSVPLVILSG-----QVPSN-------------LIGTDAFQEcdmlgisrpvVKHSFIVKNAEDIPSTIKKAFYI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  166 G-VRRCLPVYIALPQDLVEmPLKKEGLSRPlvkdidnlSAAEMRV-----------ISEVLGLLSSCSKPIIIADAGASR 233
Cdd:PRK06882  149 AsTGRPGPVVIDIPKDMVN-PANKFTYEYP--------EEVSLRSynptvqghkgqIKKALKALLVAKKPVLFVGGGVIT 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  234 DNISAEVSNLISSLpTWPLFVSAMGKGSvneqHPSFAGTYMGTLSLP---PVRTAVEAADFVLSIGALASDFNTGFGSMD 310
Cdd:PRK06882  220 AECSEQLTQFAQKL-NLPVTSSLMGLGA----YPSTDKQFLGMLGMHgtyEANNAMHESDLILGIGVRFDDRTTNNLAKY 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  311 FEGKVVVELHATWTSVD---GSTFPGVG-MKSLLPRLASSLSpitssapippspslslPLPTIRPASDKfvrhAYFWPRV 386
Cdd:PRK06882  295 CPNAKVIHIDIDPTSISknvPAYIPIVGsAKNVLEEFLSLLE----------------EENLAKSQTDL----TAWWQQI 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  387 EKWlreDDVLCVEAGTSSfgaaDVRLPRGATMLSQWLWASIGFSVGATVGAAVAAAEGFQENtKKRKAEEEETVASNGDG 466
Cdd:PRK06882  355 NEW---KAKKCLEFDRTS----DVIKPQQVVEAIYRLTNGDAYVASDVGQHQMFAALHYPFD-KPRRWINSGGAGTMGFG 426
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 813212725  467 ADENGGDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK06882  427 LPAAIGVKFAHPEATVVCVTGDGSIQMNIQELSTAKQYDIPVVIVSLNNR 476
PRK07979 PRK07979
acetolactate synthase 3 large subunit;
26-516 2.29e-09

acetolactate synthase 3 large subunit;


Pssm-ID: 181185 [Multi-domain]  Cd Length: 574  Bit Score: 62.18  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   26 DLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK07979   16 DQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGeVGVVLVTSGPGATNAITGIATAYMDSIP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  105 LIHLVGlpstsQLSSSEILHHSLGHPHQTLLYSSFFKEisgSMLVvsetTRAEEIDRALE-----IGVRRCLPVYIALPQ 179
Cdd:PRK07979   96 LVVLSG-----QVATSLIGYDAFQECDMVGISRPVVKH---SFLV----KQTEDIPQVLKkafwlAASGRPGPVVVDLPK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  180 DLVEmPLKKEGLSRP---LVKDIDNLSAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLpTWPLFVSA 256
Cdd:PRK07979  164 DILN-PANKLPYVWPesvSMRSYNPTTQGHKGQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKELVEKL-NLPVVSSL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  257 MGKGsvneqhpSFAGTYMGTLSLPPVRTAVEA------ADFVLSIGALASDFNTGFGSMDFEGKVVVELHATWTSVDGST 330
Cdd:PRK07979  242 MGLG-------AFPATHRQSLGMLGMHGTYEAnmtmhnADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  331 ---FPGVG--------MKSLLPRLASSLSPitssapippspslslplPTIRPasdkfvrhayFWPRVEKWlREDDVLCVE 399
Cdd:PRK07979  315 tadIPIVGdarqvleqMLELLSQESAHQPL-----------------DEIRD----------WWQQIEQW-RARQCLKYD 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  400 AGTSSFGAADV-----RLPRGATMLSQWLWASIGFSvgatvgaavaaaEGFQENTKKRKAEEEETVASNGDGADENGGDG 474
Cdd:PRK07979  367 THSEKIKPQAVietlwRLTKGDAYVTSDVGQHQMFA------------ALYYPFDKPRRWINSGGLGTMGFGLPAALGVK 434
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 813212725  475 EAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK07979  435 MALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVLNLNNR 476
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
29-311 6.48e-09

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 60.40  E-value: 6.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALDYvedFP--GMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPL 105
Cdd:PRK07525   21 ITHAFGIIGSAFMDASDL---FPpaGIRFIDVAHEQNAGHMADGYTRVTGrMGMVIGQNGPGITNFVTAVATAYWAHTPV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  106 IhLVglpsTSQLSSSEIlhhSLGHpHQTLLYSSFFKEISGSMLVVSETTRAEEI-DRALEIGVRRCLPVYIALPQDL--- 181
Cdd:PRK07525   98 V-LV----TPQAGTKTI---GQGG-FQEAEQMPMFEDMTKYQEEVRDPSRMAEVlNRVFDKAKRESGPAQINIPRDYfyg 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  182 ---VEMPlKKEGLSRPlvkdidnlsAAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLpTWPLFVSAMG 258
Cdd:PRK07525  169 vidVEIP-QPVRLERG---------AGGEQSLAEAAELLSEAKFPVILSGAGVVLSDAIEECKALAERL-DAPVACGYLH 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  259 KGSVNEQHPSFAGT--YMGTlslppvRTAVE---AADFVLSIGALASDFNT--GFGsMDF 311
Cdd:PRK07525  238 NDAFPGSHPLWVGPlgYNGS------KAAMEliaKADVVLALGTRLNPFGTlpQYG-IDY 290
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
476-516 2.39e-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: 55.58  E-value: 2.39e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 813212725  476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:cd02015    65 ARPDKTVICIDGDGSFQMNIQELATAAQYNLPVKIVILNNG 105
PRK08979 PRK08979
acetolactate synthase 3 large subunit;
26-516 4.88e-08

acetolactate synthase 3 large subunit;


Pssm-ID: 181602 [Multi-domain]  Cd Length: 572  Bit Score: 57.52  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   26 DLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK08979   16 DEGVKHIFGYPGGSVLDIYDALHEKSGIEHILVRHEQAAVHMADGYARATGkVGVVLVTSGPGATNTITGIATAYMDSIP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  105 LIHLVGlpstsQLSSSeilhhslghphqtLLYSSFFKE----------ISGSMLVVSETTRAEEIDRALEIGVR-RCLPV 173
Cdd:PRK08979   96 MVVLSG-----QVPSN-------------LIGNDAFQEcdmigisrpvVKHSFLVKDAEDIPEIIKKAFYIASTgRPGPV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  174 YIALPQDLVEmPLKKEGLSRPlvkdidnlSAAEMRV-----------ISEVLGLLSSCSKPIIIADAGASRDNISAEVSN 242
Cdd:PRK08979  158 VIDLPKDCLN-PAILHPYEYP--------ESIKMRSynpttsghkgqIKRGLQALLAAKKPVLYVGGGAIISGADKQILQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  243 LISSLpTWPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTgfGSMDFEGKVVVELHat 322
Cdd:PRK08979  229 LAEKL-NLPVVSTLMGLGAFPGTHKNSLGM-LGMHGRYEANMAMHNADLIFGIGVRFDDRTT--NNLEKYCPNATILH-- 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  323 wTSVDGSTFPGVgMKSLLPRLASSLSPITSSAPIPPSPSLSLPLPTIrpasdkfvrhAYFWPRVEKWlREDDVLCVEAGT 402
Cdd:PRK08979  303 -IDIDPSSISKT-VRVDIPIVGSADKVLDSMLALLDESGETNDEAAI----------ASWWNEIEVW-RSRNCLAYDKSS 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  403 SSFGAADV-----RLPRGATMLSQWLWASIGFSvgatvgaavaaaEGFQENTKKRKAEEEETVASNGDGADENGGDGEAK 477
Cdd:PRK08979  370 ERIKPQQVietlyKLTNGDAYVASDVGQHQMFA------------ALYYPFDKPRRWINSGGLGTMGFGLPAAMGVKFAM 437
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 813212725  478 GRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK08979  438 PDETVVCVTGDGSIQMNIQELSTALQYDIPVKIINLNNR 476
TPP_PYR_POX cd07039
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ...
32-185 5.14e-08

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: 54.09  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   32 IFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGELSAMNAHAGAYAEQIPLIHLVG 110
Cdd:cd07039    18 VYGIPGDSINGLMDALRREGKIEFIQVRHEEAAAFAASAEAKLTGKlGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAG 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 813212725  111 lpstsQLSSSEILHHSlghpHQTLLYSSFFKEISG-SMLVVSETTRAEEIDRALEIGV-RRCLPVyIALPQDLVEMP 185
Cdd:cd07039    98 -----QVPTDELGTDY----FQEVDLLALFKDVAVyNETVTSPEQLPELLDRAIRTAIaKRGVAV-LILPGDVQDAP 164
PRK06965 PRK06965
acetolactate synthase 3 catalytic subunit; Validated
66-543 7.98e-08

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 180780 [Multi-domain]  Cd Length: 587  Bit Score: 57.12  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   66 YAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLI--------HLVGLPSTSQLSSSEILHHSLGHphqtlly 136
Cdd:PRK06965   73 HAADGYARATGkVGVALVTSGPGVTNAVTGIATAYMDSIPMVvisgqvptAAIGQDAFQECDTVGITRPIVKH------- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  137 ssffkeisgSMLVVSETTRAEEIDRALEIG-VRRCLPVYIALPQDLvemPLKKEGLSRPlvkdidnlSAAEMRV------ 209
Cdd:PRK06965  146 ---------NFLVKDVRDLAETVKKAFYIArTGRPGPVVVDIPKDV---SKTPCEYEYP--------KSVEMRSynpvtk 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  210 -----ISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLpTWPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRT 284
Cdd:PRK06965  206 ghsgqIRKAVSLLLSAKRPYIYTGGGVILANASRELRQLADLL-GYPVTNTLMGLGAYPASDKKFLGM-LGMHGTYEANM 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  285 AVEAADFVLSIGALASDFNTG----FGSMdfEGKVV-VELHATWTS----VDgstFPGVG-MKSLLPRLASSLSpitssa 354
Cdd:PRK06965  284 AMQHCDVLIAIGARFDDRVIGnpahFASR--PRKIIhIDIDPSSISkrvkVD---IPIVGdVKEVLKELIEQLQ------ 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  355 pippspslslpLPTIRPASDKFvrhAYFWPRVEKWLREDdvlCVEAGTSSfgaaDVRLPRgatMLSQWLWASIGFSVGAT 434
Cdd:PRK06965  353 -----------TAEHGPDADAL---AQWWKQIEGWRSRD---CLKYDRES----EIIKPQ---YVVEKLWELTDGDAFVC 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  435 VGAAVAAAEGFQentKKRKAEEEETVASNGDGADENG-----GDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGAT 509
Cdd:PRK06965  409 SDVGQHQMWAAQ---FYRFNEPRRWINSGGLGTMGVGlpyamGIKMAHPDDDVVCITGEGSIQMCIQELSTCLQYDTPVK 485
                         490       500       510
                  ....*....|....*....|....*....|....
gi 813212725  510 IFVVDNRgytvekYIrGITREYNAINTGWDYSST 543
Cdd:PRK06965  486 IISLNNR------YL-GMVRQWQEIEYSKRYSHS 512
ilvB CHL00099
acetohydroxyacid synthase large subunit
29-516 9.56e-08

acetohydroxyacid synthase large subunit


Pssm-ID: 214363 [Multi-domain]  Cd Length: 585  Bit Score: 56.63  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALDYV---EDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:CHL00099   25 VKHIFGYPGGAILPIYDELyawEKKGLIKHILVRHEQGAAHAADGYARSTGkVGVCFATSGPGATNLVTGIATAQMDSVP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  105 LIHLVGlpstsQLSSSEIlhhslGhphqtllySSFFKE--ISGSML-------VVSETTRAEEI-DRALEIGVR-RCLPV 173
Cdd:CHL00099  105 LLVITG-----QVGRAFI-----G--------TDAFQEvdIFGITLpivkhsyVVRDARDISRIvAEAFYIAKHgRPGPV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  174 YIALPQDL------------VEMPLKKEGLsRPLVKDidnlsaaEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVS 241
Cdd:CHL00099  167 LIDIPKDVglekfdyyppepGNTIIKILGC-RPIYKP-------TIKRIEQAAKLILQSSQPLLYVGGGAIISDAHQEIT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  242 NLISSLPTwPLFVSAMGKGSVNEQHPsfagTYMGTLSL---PPVRTAVEAADFVLSIGALASDFNTG----FGSmdfeGK 314
Cdd:CHL00099  239 ELAELYKI-PVTTTLMGKGIFDEDHP----LCLGMLGMhgtAYANFAVSECDLLIALGARFDDRVTGkldeFAC----NA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  315 VVVELHATWTSVDGSTFPGVGM----KSLLPRLASSLSpitssapippspslslpLPTIRPASDKFvrhaYFW-PRVEKW 389
Cdd:CHL00099  310 QVIHIDIDPAEIGKNRIPQVAIvgdvKKVLQELLELLK-----------------NSPNLLESEQT----QAWrERINRW 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  390 lREDDVLCVEAGTSSFGAADV-----RLPRGA---TMLSQ-WLWASigfsvgatvgaavaaaeGFQEnTKKRKAEEEETV 460
Cdd:CHL00099  369 -RKEYPLLIPKPSTSLSPQEVineisQLAPDAyftTDVGQhQMWAA-----------------QFLK-CKPRKWLSSAGL 429
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 813212725  461 ASNGDGADENGGDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:CHL00099  430 GTMGYGLPAAIGAQIAHPNELVICISGDASFQMNLQELGTIAQYNLPIKIIIINNK 485
PRK08266 PRK08266
hypothetical protein; Provisional
29-296 1.30e-07

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 56.17  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALDYVEDFPG-MKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLI 106
Cdd:PRK08266   19 VDTVFGLPGAQLYWLFDALYKAGDrIRVIHTRHEQAAGYMAFGYARSTGrPGVCSVVPGPGVLNAGAALLTAYGCNSPVL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  107 HLvglpsTSQLSSSEI------LHHSlghPHQTLLYSSFFKeISGSMLVVSE--TTRAEEIDRALEiGVRRclPVYIALP 178
Cdd:PRK08266   99 CL-----TGQIPSALIgkgrghLHEM---PDQLATLRSFTK-WAERIEHPSEapALVAEAFQQMLS-GRPR--PVALEMP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  179 QDL------VEMPLKKEGLSRPLVkDIDNLSAAEmrvisevlGLLSSCSKPIIIADAGASrdNISAEVSNLISSLPTwPL 252
Cdd:PRK08266  167 WDVfgqrapVAAAPPLRPAPPPAP-DPDAIAAAA--------ALIAAAKNPMIFVGGGAA--GAGEEIRELAEMLQA-PV 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 813212725  253 FVSAMGKGSVNEQHPSFagtymgtLSLPPVRTAVEAADFVLSIG 296
Cdd:PRK08266  235 VAFRSGRGIVSDRHPLG-------LNFAAAYELWPQTDVVIGIG 271
PRK07789 PRK07789
acetolactate synthase 1 catalytic subunit; Validated
25-305 6.56e-07

acetolactate synthase 1 catalytic subunit; Validated


Pssm-ID: 236098 [Multi-domain]  Cd Length: 612  Bit Score: 54.22  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   25 DDLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQI 103
Cdd:PRK07789   42 EELGVDVVFGIPGGAILPVYDPLFDSTKVRHVLVRHEQGAGHAAEGYAQATGrVGVCMATSGPGATNLVTPIADANMDSV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  104 PLIHLVGlpstsQLSSSeilhhslghphqtLLYSSFFKE--ISG--------SMLVvsetTRAEEIDRALEIGVR----- 168
Cdd:PRK07789  122 PVVAITG-----QVGRG-------------LIGTDAFQEadIVGitmpitkhNFLV----TDADDIPRVIAEAFHiastg 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  169 RCLPVYIALPQDL------------VEMPlkkeGLsRPLVKdidnlsaAEMRVISEVLGLLSSCSKPIIIADAGASRDNI 236
Cdd:PRK07789  180 RPGPVLVDIPKDAlqaqttfswpprMDLP----GY-RPVTK-------PHGKQIREAAKLIAAARRPVLYVGGGVIRAEA 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725  237 SAEVSNLiSSLPTWPLFVSAMGKGSVNEQHPSFAGtyM----GTLslpPVRTAVEAADFVLSIGALASDFNTG 305
Cdd:PRK07789  248 SAELREL-AELTGIPVVTTLMARGAFPDSHPQHLG--MpgmhGTV---AAVAALQRSDLLIALGARFDDRVTG 314
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
476-518 9.41e-07

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: 50.67  E-value: 9.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 813212725  476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:cd02002    64 ANPDRKVVAIIGDGSFMYTIQALWTAARYGLPVTVVILNNRGY 106
PRK09336 PRK09336
30S ribosomal protein S30e; Provisional
1509-1552 1.84e-06

30S ribosomal protein S30e; Provisional


Pssm-ID: 181786  Cd Length: 50  Bit Score: 46.32  E-value: 1.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 813212725 1509 HGSLARAGKVKSQCPKVEKQEKKKTPKgRAYKRMVYNRRFVNVT 1552
Cdd:PRK09336    4 HGSLTKAGKVRSQTPKIPPKPKKNEVP-RVRNRREYERRVLKAR 46
PRK06725 PRK06725
acetolactate synthase large subunit;
27-516 2.03e-06

acetolactate synthase large subunit;


Pssm-ID: 180672 [Multi-domain]  Cd Length: 570  Bit Score: 52.28  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   27 LHINSIFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPL 105
Cdd:PRK06725   28 LGVTTVFGYPGGAILPVYDALYE-SGLKHILTRHEQAAIHAAEGYARASGkVGVVFATSGPGATNLVTGLADAYMDSIPL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  106 IHLVGLPSTSqlssseilhhslghphqtLLYSSFFKEISGSMLVVSETTRAEEIDRALEIG--VRRCL---------PVY 174
Cdd:PRK06725  107 VVITGQVATP------------------LIGKDGFQEADVVGITVPVTKHNYQVRDVNQLSriVQEAFyiaesgrpgPVL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  175 IALPQDLVEMPLKKEGLSRPLVKDIDNLSAAEMRVISEVLGLLSSCSKPII-----IADAGASRDNISAEVSNLIsslpt 249
Cdd:PRK06725  169 IDIPKDVQNEKVTSFYNEVVEIPGYKPEPRPDSMKLREVAKAISKAKRPLLyigggVIHSGGSEELIEFARENRI----- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  250 wPLFVSAMGKGSVNEQHPSFAGTyMGTLSLPPVRTAVEAADFVLSIGALASDFNTG---------------FGSMDFEGK 314
Cdd:PRK06725  244 -PVVSTLMGLGAYPPGDPLFLGM-LGMHGTYAANMAVTECDLLLALGVRFDDRVTGklelfsphskkvhidIDPSEFHKN 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  315 VVVELhatwtsvdgstfPGVG-MKSLLPRLASSLSPITSSAPIPPSPSLSLPLPTIRPASDKFVRHAYFWPRVEKWLRED 393
Cdd:PRK06725  322 VAVEY------------PVVGdVKKALHMLLHMSIHTQTDEWLQKVKTWKEEYPLSYKQKESELKPQHVINLVSELTNGE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  394 DVLCVEAGTSSFGAA---DVRLPRgaTMLSQWLWASIGFSvgatvgaavaaaegFQENTKKRKAEEEETvasngdgaden 470
Cdd:PRK06725  390 AIVTTEVGQHQMWAAhfyKAKNPR--TFLTSGGLGTMGFG--------------FPAAIGAQLAKEEEL----------- 442
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 813212725  471 ggdgeakgrrrVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK06725  443 -----------VICIAGDASFQMNIQELQTIAENNIPVKVFIINNK 477
PRK06466 PRK06466
acetolactate synthase 3 large subunit;
19-297 2.66e-06

acetolactate synthase 3 large subunit;


Pssm-ID: 180578 [Multi-domain]  Cd Length: 574  Bit Score: 52.05  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   19 LLHRLRDDlHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAG 97
Cdd:PRK06466   10 LVRALRDE-GVEYIYGYPGGAVLHIYDALFKQDKVEHILVRHEQAATHMADGYARATGkTGVVLVTSGPGATNAITGIAT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   98 AYAEQIPLIHLVG-LPSTS------QLS-----SSEILHHSLGHPHQtllyssffKEIsgsmlvvsettrAEEIDRALEI 165
Cdd:PRK06466   89 AYMDSIPMVVLSGqVPSTLigedafQETdmvgiSRPIVKHSFMVKHA--------SEI------------PEIIKKAFYI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  166 -GVRRCLPVYIALPQDLVEmPLKKEGLSRPLVKDIDNLSAA---EMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVS 241
Cdd:PRK06466  149 aQSGRPGPVVVDIPKDMTN-PAEKFEYEYPKKVKLRSYSPAvrgHSGQIRKAVEMLLAAKRPVIYSGGGVVLGNASALLT 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 813212725  242 NLISSLpTWPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAADFVLSIGA 297
Cdd:PRK06466  228 ELAHLL-NLPVTNTLMGLGGFPGTDRQFLG-MLGMHGTYEANMAMHHADVILAVGA 281
PRK07710 PRK07710
acetolactate synthase large subunit;
32-305 4.32e-05

acetolactate synthase large subunit;


Pssm-ID: 236076 [Multi-domain]  Cd Length: 571  Bit Score: 48.22  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   32 IFGVPGDFNLPALDYVEDfPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIHLVG 110
Cdd:PRK07710   34 IFGYPGGAVLPLYDALYD-CGIPHILTRHEQGAIHAAEGYARISGkPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  111 LPSTSqlssseilhhslghphqtLLYSSFFKE--ISGSMLVVS----ETTRAEEIDR----ALEIGVR-RCLPVYIALPQ 179
Cdd:PRK07710  113 QVATS------------------VIGSDAFQEadIMGITMPVTkhnyQVRKASDLPRiikeAFHIATTgRPGPVLIDIPK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  180 DLV----------EMPLKK-EGLSRPLVKDIDNLSAAemrvisevlglLSSCSKPIIIADAGASRDNISAEVSNLISSLP 248
Cdd:PRK07710  175 DMVveegefcydvQMDLPGyQPNYEPNLLQIRKLVQA-----------VSVAKKPVILAGAGVLHAKASKELTSYAEQQE 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725  249 TwPLFVSAMGKGSVNEQHPSFA------GTYMGTLslppvrtAVEAADFVLSIGALASDFNTG 305
Cdd:PRK07710  244 I-PVVHTLLGLGGFPADHPLFLgmagmhGTYTANM-------ALYECDLLINIGARFDDRVTG 298
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
32-518 5.65e-05

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 47.56  E-value: 5.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   32 IFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA-GALVTTFGVGelsAMNAHAG---AYAEQIPLIH 107
Cdd:PRK08199   26 VFCVPGESYLAVLDALHDETDIRVIVCRQEGGAAMMAEAYGKLTGRpGICFVTRGPG---ATNASIGvhtAFQDSTPMIL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  108 LVGlpstsQLSSseilHHSLGHPHQTLLYSSFFkeisGSMlvvseTTRAEEIDRALEIG--VRRCL---------PVYIA 176
Cdd:PRK08199  103 FVG-----QVAR----DFREREAFQEIDYRRMF----GPM-----AKWVAEIDDAARIPelVSRAFhvatsgrpgPVVLA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  177 LPQD-LVE------MPLKKEGLSRPLVKDIDNLSAaemrvisevlgLLSSCSKPIIIA-----DAGASRDNIS-AEVSNL 243
Cdd:PRK08199  165 LPEDvLSEtaevpdAPPYRRVAAAPGAADLARLAE-----------LLARAERPLVILggsgwTEAAVADLRAfAERWGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  244 isslptwPLFVSAMGKGSVNEQHPSFAGtYMGTLSLPPVRTAVEAADFVLSIGALASDFNT-GFGSMDFEG--KVVVELH 320
Cdd:PRK08199  234 -------PVACAFRRQDLFDNRHPNYAG-DLGLGINPALAARIREADLVLAVGTRLGEVTTqGYTLLDIPVprQTLVHVH 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  321 ATwTSVDGSTF-PGVGMKSLLPRLASSLSPITSSApippspslslplpTIRPASDKFVRHAYF--W------------PR 385
Cdd:PRK08199  306 PD-AEELGRVYrPDLAIVADPAAFAAALAALEPPA-------------SPAWAEWTAAAHADYlaWsaplpgpgavqlGE 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  386 VEKWLRE----DDVLCVEAGT-SSFGAADVRLPRGATMLSqwlwasigfsvgatvgaavaaaegfqentkkrkaeeeETV 460
Cdd:PRK08199  372 VMAWLRErlpaDAIITNGAGNyATWLHRFFRFRRYRTQLA-------------------------------------PTS 414
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 813212725  461 ASNGDGADENGGDGEAKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:PRK08199  415 GSMGYGLPAAIAAKLLFPERTVVAFAGDGCFLMNGQELATAVQYGLPIIVIVVNNGMY 472
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
480-516 6.19e-05

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: 45.21  E-value: 6.19e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 813212725  480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:cd02014    70 RQVIALSGDGGFAMLMGDLITAVKYNLPVIVVVFNNS 106
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
476-517 7.70e-05

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: 44.83  E-value: 7.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 813212725  476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRG 517
Cdd:cd02004    63 ARPDKRVVLVEGDGAFGFSGMELETAVRYNLPIVVVVGNNGG 104
PRK08273 PRK08273
thiamine pyrophosphate protein; Provisional
18-231 2.17e-04

thiamine pyrophosphate protein; Provisional


Pssm-ID: 181344 [Multi-domain]  Cd Length: 597  Bit Score: 46.06  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   18 YLLHRLRDdLHINSIFGVPGDFN---LPALDYVEDfpGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMN 93
Cdd:PRK08273    8 FILERLRE-WGVRRVFGYPGDGInglLGALGRADD--KPEFVQARHEEMAAFMAVAHAKFTGeVGVCLATSGPGAIHLLN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   94 AHAGAYAEQIPLIHLVGLPSTSQLSsseilhhslGHPHQTLLYSSFFKEISGS---MLVVSETTRaEEIDRALEIGVRRC 170
Cdd:PRK08273   85 GLYDAKLDHVPVVAIVGQQARAALG---------GHYQQEVDLQSLFKDVAGAfvqMVTVPEQLR-HLVDRAVRTALAER 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725  171 LPVYIALPQDLVEMPLKKE-----------GLSRP-LVKDIDNLSAAemrviSEVlglLSSCSKPIIIADAGA 231
Cdd:PRK08273  155 TVTAVILPNDVQELEYEPPphahgtvhsgvGYTRPrVVPYDEDLRRA-----AEV---LNAGRKVAILVGAGA 219
PRK08527 PRK08527
acetolactate synthase large subunit;
32-305 4.83e-04

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 44.70  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   32 IFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIPLIHLVG 110
Cdd:PRK08527   21 VFGYPGGAILNIYDEIYKQNYFKHILTRHEQAAVHAADGYARASGkVGVAIVTSGPGFTNAVTGLATAYMDSIPLVLISG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  111 LPSTSQLSS---SEILHHSLGHP---HQTLLyssffKEISGSMLVVSEttrAEEIDRALEIGvrrclPVYIALPQDL--- 181
Cdd:PRK08527  101 QVPNSLIGTdafQEIDAVGISRPcvkHNYLV-----KSIEELPRILKE---AFYIARSGRPG-----PVHIDIPKDVtat 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  182 ---------VEMPLKKeglsrPLVKdidnlsaAEMRVISEVLGLLSSCSKPIIIADAGASRDNISAEVSNLISSLPTwPL 252
Cdd:PRK08527  168 lgefeypkeISLKTYK-----PTYK-------GNSRQIKKAAEAIKEAKKPLFYLGGGAILSNASEEIRELVKKTGI-PA 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 813212725  253 FVSAMGKGSVNEQHPSFA------GTYMGTLslppvrtAVEAADFVLSIGALASDFNTG 305
Cdd:PRK08527  235 VETLMARGVLRSDDPLLLgmlgmhGSYAANM-------AMSECDLLISLGARFDDRVTG 286
PRK09107 PRK09107
acetolactate synthase 3 catalytic subunit; Validated
26-115 4.85e-04

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 236380 [Multi-domain]  Cd Length: 595  Bit Score: 44.70  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   26 DLHINSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKG-AGALVTTFGVGELSAMNAHAGAYAEQIP 104
Cdd:PRK09107   23 DQGVEHIFGYPGGAVLPIYDEIFQQDDIQHILVRHEQGAGHAAEGYARSTGkPGVVLVTSGPGATNAVTPLQDALMDSIP 102
                          90
                  ....*....|.
gi 813212725  105 LIHLVGLPSTS 115
Cdd:PRK09107  103 LVCITGQVPTH 113
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
480-522 4.96e-04

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: 42.88  E-value: 4.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 813212725  480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEK 522
Cdd:cd02013    72 RPVVAIAGDGAWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
PRK07418 PRK07418
acetolactate synthase large subunit;
480-516 5.70e-04

acetolactate synthase large subunit;


Pssm-ID: 236014 [Multi-domain]  Cd Length: 616  Bit Score: 44.66  E-value: 5.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 813212725  480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNR 516
Cdd:PRK07418  453 EEVICIAGDASFLMNIQELGTLAQYGINVKTVIINNG 489
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
476-518 7.18e-04

Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.


Pssm-ID: 238961 [Multi-domain]  Cd Length: 205  Bit Score: 42.68  E-value: 7.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 813212725  476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGY 518
Cdd:cd02003    63 AKPDREVYVLVGDGSYLMLHSEIVTAVQEGLKIIIVLFDNHGF 105
PRK11269 PRK11269
glyoxylate carboligase; Provisional
29-305 9.82e-04

glyoxylate carboligase; Provisional


Pssm-ID: 183066 [Multi-domain]  Cd Length: 591  Bit Score: 43.82  E-value: 9.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725   29 INSIFGVPGDFNLPALDYVEDFPGMKWIGAVNELNGGYAADGYARVKGA--GALVTTFGVGELSAMNAHAGAYAEQIPLI 106
Cdd:PRK11269   19 VTTAFGVPGAAINPFYSAMRKHGGIRHILARHVEGASHMAEGYTRATAGniGVCIGTSGPAGTDMITGLYSASADSIPIL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  107 HLVGLPSTSQLSSSEIlhhslghphQTLLYSSFFKEISGSMLVVSETTRAEEI-DRALEIgVR--RCLPVYIALPQDlVE 183
Cdd:PRK11269   99 CITGQAPRARLHKEDF---------QAVDIESIAKPVTKWAVTVREPALVPRVfQQAFHL-MRsgRPGPVLIDLPFD-VQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 813212725  184 M-----------PLKkegLSRPlvkdidnlsAAEMRVISEVLGLLSSCSKPIIIADAGAsrdnISAEVSNLI---SSLPT 249
Cdd:PRK11269  168 VaeiefdpdtyePLP---VYKP---------AATRAQIEKALEMLNAAERPLIVAGGGV----INADASDLLvefAELTG 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 813212725  250 WPLFVSAMGKGSVNEQHPSFAGTyMGtlslppVRTA-------VEAADFVLSIGALASDFNTG 305
Cdd:PRK11269  232 VPVIPTLMGWGAIPDDHPLMAGM-VG------LQTShrygnatLLASDFVLGIGNRWANRHTG 287
PRK08611 PRK08611
pyruvate oxidase; Provisional
480-523 1.48e-03

pyruvate oxidase; Provisional


Pssm-ID: 181502 [Multi-domain]  Cd Length: 576  Bit Score: 43.07  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 813212725  480 RRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDNRGYTVEKY 523
Cdd:PRK08611  427 RQAIAICGDGGFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIKY 470
PRK09107 PRK09107
acetolactate synthase 3 catalytic subunit; Validated
482-515 1.91e-03

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 236380 [Multi-domain]  Cd Length: 595  Bit Score: 42.77  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 813212725  482 VICVVGDGALQMGIQEISNLVRYNLGATIFVVDN 515
Cdd:PRK09107  451 VIDIAGDASIQMCIQEMSTAVQYNLPVKIFILNN 484
PRK08155 PRK08155
acetolactate synthase large subunit;
476-515 5.43e-03

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 41.23  E-value: 5.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 813212725  476 AKGRRRVICVVGDGALQMGIQEISNLVRYNLGATIFVVDN 515
Cdd:PRK08155  434 ANPERKVLCFSGDGSLMMNIQEMATAAENQLDVKIILMNN 473
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH