NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|260213474|emb|CBE05165|]
View 

putative subunit of oxidoreductase [Clostridioides difficile R20291]

Protein Classification

thiamine pyrophosphate-dependent enzyme( domain architecture ID 22)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation

CATH:  3.40.50.1220
Gene Ontology:  GO:0030976|GO:0003824
PubMed:  12735696|15514159
SCOP:  3001790

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 12-245 2.26e-87

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


:

Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 259.69  E-value: 2.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  12 SIPNKFCPGCGHGIVNRIIAEVIEEHGYEKNHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQ 91
Cdd:COG1013   10 TPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVFG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  92 GDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKVPEMVANfFDVAY 171
Cdd:COG1013   90 GDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIAAA-HGATY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474 172 VARGSVHSPKeiiNLKKYIKNAIEaqlnGEGYSLVEILAPCPTNWGVSLEKSIKWMEEEIVPYY---------------- 235
Cdd:COG1013  165 VARASVGDPK---DLKKKIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLYeydpgeklrltyepkd 237

                        250
                 ....*....|..
gi 260213474 236 --ALGEFKQRDG 245
Cdd:COG1013  238 kiPVGEFLKNQG 249
 
Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 12-245 2.26e-87

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 259.69  E-value: 2.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  12 SIPNKFCPGCGHGIVNRIIAEVIEEHGYEKNHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQ 91
Cdd:COG1013   10 TPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVFG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  92 GDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKVPEMVANfFDVAY 171
Cdd:COG1013   90 GDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIAAA-HGATY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474 172 VARGSVHSPKeiiNLKKYIKNAIEaqlnGEGYSLVEILAPCPTNWGVSLEKSIKWMEEEIVPYY---------------- 235
Cdd:COG1013  165 VARASVGDPK---DLKKKIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLYeydpgeklrltyepkd 237

                        250
                 ....*....|..
gi 260213474 236 --ALGEFKQRDG 245
Cdd:COG1013  238 kiPVGEFLKNQG 249
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 17-215 1.54e-58

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 183.88  E-value: 1.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  17 FCPGCGHGIVNRIIAEVIEEHGYEK-NHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQGDGD 95
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPeKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  96 AYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGRdIKTTGSPLKVPEMVanffDVAYVARG 175
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGN-IEEPFNPLALALAA----GATFVARG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 260213474 176 SVHSPKEiinLKKYIKNAIEaqlnGEGYSLVEILAPCPTN 215
Cdd:cd03375  156 FSGDIKQ---LKEIIKKAIQ----HKGFSFVEVLSPCPTF 188
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 16-233 1.65e-42

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 145.75  E-value: 1.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  16 KFCPGCGHGIVNRIIAEVIEEHGYEK-NHVLTLGVGCVCN----MNFswNGdkMQTAHGRASSTAIGVKVALPDTLVMTY 90
Cdd:PRK11867  18 RWCPGCGDGSILAALQRALAELGLDPeNVAVVSGIGCSGRlpgyINT--YG--FHTIHGRALAIATGLKLANPDLTVIVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  91 QGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKVPEMV----ANF 166
Cdd:PRK11867  94 TGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYG----SIEPPFNPVELAlgagATF 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260213474 167 fdvayVARGSVHSPKEiinLKKYIKNAIEAQlngeGYSLVEILAPCPTNWGVSlekSIKWMEEEIVP 233
Cdd:PRK11867 170 -----VARGFDSDVKQ---LTELIKAAINHK----GFSFVEILQPCPTFNNVN---TFDWFKERLVK 221
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
42-208 5.18e-19

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 80.71  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474   42 NHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQGDGDAYVIgLSETLNTAYRNHNVTVFVINN 121
Cdd:pfam02775   4 CHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVVLNN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  122 NNFAMTGGqmsWTTMPGQVTTTSVNGRDIKTTgSPLKVPEmvanffdvAYVARG-SVHSPKEiinlkkyIKNAIEAQLNG 200
Cdd:pfam02775  83 GGYGMTRG---QQTPFGGGRYSGPSGKILPPV-DFAKLAE--------AYGAKGaRVESPEE-------LEEALKEALEH 143


                  ....*...
gi 260213474  201 EGYSLVEI 208
Cdd:pfam02775 144 DGPALIDV 151
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 92-212 1.59e-04

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 42.45  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474    92 GDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGRdiKTTGSPLKVPEMVANFFDVAY 171
Cdd:TIGR02176  959 GDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGK--RTSKKDLGMMAMTYGYVYVAQ 1036

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 260213474   172 VARGSvhspkeiiNLKKYIKNAIEAQlNGEGYSLVEILAPC 212
Cdd:TIGR02176 1037 VSMGA--------NMQQTLKAFREAE-AYDGPSIVIAYSPC 1068
 
Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 12-245 2.26e-87

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 259.69  E-value: 2.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  12 SIPNKFCPGCGHGIVNRIIAEVIEEHGYEKNHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQ 91
Cdd:COG1013   10 TPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVFG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  92 GDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKVPEMVANfFDVAY 171
Cdd:COG1013   90 GDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIAAA-HGATY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474 172 VARGSVHSPKeiiNLKKYIKNAIEaqlnGEGYSLVEILAPCPTNWGVSLEKSIKWMEEEIVPYY---------------- 235
Cdd:COG1013  165 VARASVGDPK---DLKKKIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLYeydpgeklrltyepkd 237

                        250
                 ....*....|..
gi 260213474 236 --ALGEFKQRDG 245
Cdd:COG1013  238 kiPVGEFLKNQG 249
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 17-215 1.54e-58

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 183.88  E-value: 1.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  17 FCPGCGHGIVNRIIAEVIEEHGYEK-NHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQGDGD 95
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPeKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  96 AYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGRdIKTTGSPLKVPEMVanffDVAYVARG 175
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGN-IEEPFNPLALALAA----GATFVARG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 260213474 176 SVHSPKEiinLKKYIKNAIEaqlnGEGYSLVEILAPCPTN 215
Cdd:cd03375  156 FSGDIKQ---LKEIIKKAIQ----HKGFSFVEVLSPCPTF 188
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 16-233 1.65e-42

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 145.75  E-value: 1.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  16 KFCPGCGHGIVNRIIAEVIEEHGYEK-NHVLTLGVGCVCN----MNFswNGdkMQTAHGRASSTAIGVKVALPDTLVMTY 90
Cdd:PRK11867  18 RWCPGCGDGSILAALQRALAELGLDPeNVAVVSGIGCSGRlpgyINT--YG--FHTIHGRALAIATGLKLANPDLTVIVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  91 QGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKVPEMV----ANF 166
Cdd:PRK11867  94 TGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYG----SIEPPFNPVELAlgagATF 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260213474 167 fdvayVARGSVHSPKEiinLKKYIKNAIEAQlngeGYSLVEILAPCPTNWGVSlekSIKWMEEEIVP 233
Cdd:PRK11867 170 -----VARGFDSDVKQ---LTELIKAAINHK----GFSFVEILQPCPTFNNVN---TFDWFKERLVK 221
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 14-233 3.57e-39

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 137.32  E-value: 3.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  14 PNKFCPGCGHGIVNRIIAEVIEEHGYEKNHVLTL-GVGCVcnmnfSW-----NGDKMQTAHGRASSTAIGVKVALPDTLV 87
Cdd:PRK05778  17 PTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVsGIGCS-----SKipgyfLSHGLHTLHGRAIAFATGAKLANPDLEV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  88 MTYQGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKvPEMVANFF 167
Cdd:PRK05778  92 IVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYG----NIEPPID-PCALALAA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260213474 168 DVAYVARGSVHSPKEiinLKKYIKNAIEAqlngEGYSLVEILAPCPTNWGV-----SLEKSIKWMEEEIVP 233
Cdd:PRK05778 167 GATFVARSFAGDVKQ---LVELIKKAISH----KGFAFIDVLSPCVTFNGRntstkSPAYMREYYKKRVYK 230
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 11-214 1.42e-30

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 114.47  E-value: 1.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  11 VSIPNKFCPGCG-HGIVNRIIAEVIEEHGYEKNHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMT 89
Cdd:PRK11866   3 VKRPPIWCPGCGnYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  90 YQGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrDIKTTGSPLKVpeMVANffDV 169
Cdd:PRK11866  83 YGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDG-NIEEPFNPIAL--ALAA--GA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 260213474 170 AYVARGsvhSPKEIINLKKYIKNAIEAQlngeGYSLVEILAPCPT 214
Cdd:PRK11866 158 TFVARG---FSGDVKHLKEIIKEAIKHK----GFSFIDVLSPCVT 195
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
13-233 2.11e-27

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 105.97  E-value: 2.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  13 IPNKFCPGCGHGIVNRIIAEVIEEHGYEKNHV-LTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQ 91
Cdd:PRK09628  14 MPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVcVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  92 GDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrDIKTTGSPLKVPEMVANFFdvay 171
Cdd:PRK09628  94 GDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYG-NIDPTFDACKLATAAGASF---- 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260213474 172 VARGSVHSPKEiinLKKYIKNAIEAqlngEGYSLVEILAPCPTNWG-----VSLEKSIKWMEEEIVP 233
Cdd:PRK09628 169 VARESVIDPQK---LEKLLVKGFSH----KGFSFFDVFSNCHINLGrknkmGEAVQMLKWIESRTVS 228
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 18-225 1.05e-26

Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.


Pssm-ID: 239471 [Multi-domain]  Cd Length: 235  Bit Score: 103.09  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  18 CPGCGHGIVNRIIAEVIEEhgyekNHVLTLGVGC--VCNMNF---SWNGDKMQTAHGRASSTAIGVKVALP------DTL 86
Cdd:cd03376    8 CAGCGAALALRHVLKALGP-----DTVVVNPTGCleVITTPYpytAWRVPWIHVAFENAAAVASGIEAALKalgrgkDIT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  87 VMTYQGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGRDIKTTGSPLK-VPEMVAN 165
Cdd:cd03376   83 VVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSFGKKQPKKdLPLIMAA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474 166 fFDVAYVARGSVHSPKEIInlKKyIKNAIEAqlngEGYSLVEILAPCPTNWGVSLEKSIK 225
Cdd:cd03376  163 -HNIPYVATASVAYPEDLY--KK-VKKALSI----EGPAYIHILSPCPTGWRFDPSKTIE 214
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 17-214 1.06e-25

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 101.78  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  17 FCPGCGHGIVNRIIAEVIEEHGYE-KNHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQGDGD 95
Cdd:PRK11869  10 WCPGCGNFGIRNALMKALSELNLKpRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  96 AYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGrdikTTGSPLKvPEMVANFFDVAYVAR- 174
Cdd:PRK11869  90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWG----VFEEPFN-PIALAIALDASFVARt 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 260213474 175 --GSVHSPKEIinlkkyIKNAIeaqlNGEGYSLVEILAPCPT 214
Cdd:PRK11869 165 fsGDIEETKEI------LKEAI----KHKGLAIVDIFQPCVS 196
PRK11865 PRK11865
pyruvate synthase subunit beta;
18-225 2.06e-22

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 93.24  E-value: 2.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  18 CPGCGHGIVNRIIAEvieehGYEKNHVLTLGVGC--VCNMNF---SWNGDKMQTAHGRASSTAIGVKVALP----DTLVM 88
Cdd:PRK11865  21 CAGCGAAIAMRLALK-----ALGKNTVIVVATGCleVITTPYpetAWNVPWIHVAFENAAAVASGIERAVKalgkKVNVV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  89 TYQGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGRDIKTTGSPLKVPEMVANFFD 168
Cdd:PRK11865  96 AIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRGEDRPKKNMPLIMAAHG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260213474 169 VAYVARGSVHSPKEIInlkKYIKNAIEAqlngEGYSLVEILAPCPTNWGVSLEKSIK 225
Cdd:PRK11865 176 IPYVATASIGYPEDFM---EKVKKAKEV----EGPAYIQVLQPCPTGWGFPPEKTIE 225
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 18-227 3.56e-21

Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238976 [Multi-domain]  Cd Length: 237  Bit Score: 88.70  E-value: 3.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  18 CPGCGHGIVNRIIAEVIEEHGyekNHVLTLGVGC--VCNMNFSWNGDKMQTAH---GRASSTAIGVKVAL---------- 82
Cdd:cd02018    8 CAGCGEVTAVRVVLAALPAPE---DTVIANSTGCssVYASTAPFNSWAVPWVNslfEDANAVASGLKRGLkarfpkdrel 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  83 ---PDtlVMTYQGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSvngrdikTTGSPLKV 159
Cdd:cd02018   85 dkkKD--VVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMA-------PAGKKEDK 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474 160 PEMV--ANFFDVAYVARGSVHSPkeiinlKKYIKNAIEAQLNGEGYSLVEILAPCPTNWGVSLEKSIKWM 227
Cdd:cd02018  156 KDLVliAATHGCVYVARLSPALK------KHFLKVVKEAISRTDGPTFIHAYTPCITEWGIGSGKSLELA 219
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
42-208 5.18e-19

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 80.71  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474   42 NHVLTLGVGCVCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQGDGDAYVIgLSETLNTAYRNHNVTVFVINN 121
Cdd:pfam02775   4 CHQMWAAQYYRFRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVVLNN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  122 NNFAMTGGqmsWTTMPGQVTTTSVNGRDIKTTgSPLKVPEmvanffdvAYVARG-SVHSPKEiinlkkyIKNAIEAQLNG 200
Cdd:pfam02775  83 GGYGMTRG---QQTPFGGGRYSGPSGKILPPV-DFAKLAE--------AYGAKGaRVESPEE-------LEEALKEALEH 143


                  ....*...
gi 260213474  201 EGYSLVEI 208
Cdd:pfam02775 144 DGPALIDV 151
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
15-225 6.32e-17

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 78.21  E-value: 6.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  15 NKFCPGCGHGIVNRIIAEVieehgYEKNHVLTLGVGCVCNMNFSWNGDK-----MQTAHGRASSTAIGVKVALP-----D 84
Cdd:PRK11864  18 NAACPGCGAPLGLRYLLKA-----LGEKTVLVIPASCSTVIQGDTPKSPltvpvLHTAFAATAAVASGIEEALKargekG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  85 TLVMTYQGDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNG-RDIKTtgsplKVPEMV 163
Cdd:PRK11864  93 VIVVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGkREHKK-----PVPDIM 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260213474 164 ANfFDVAYVARGSVHSPKEIInlkKYIKNAIEAqlngEGYSLVEILAPCPTNWGVSLEKSIK 225
Cdd:PRK11864 168 AA-HKVPYVATASIAYPEDFI---RKLKKAKEI----RGFKFIHLLAPCPPGWRFDPDKTIE 221
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 17-130 3.83e-11

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.


Pssm-ID: 238966 [Multi-domain]  Cd Length: 178  Bit Score: 59.98  E-value: 3.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  17 FCPGCGHGIVNRIIAEVIEehgyeKNHVLTLGVGC-VCNMNFSWNGDKMQTAHGRASSTAIGVKVALPDTLVMTYQGDGD 95
Cdd:cd02008    6 LCPGCPHRPSFYALRKAFK-----KDSIVSGDIGCyTLGALPPLNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDST 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 260213474  96 AYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQ 130
Cdd:cd02008   81 FFHSGILGLINAVYNKANITVVILDNRTTAMTGGQ 115
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 67-131 4.14e-07

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: 48.41  E-value: 4.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260213474  67 AHGRASSTAIGVKVALPDTLVMTYQGDGDAYViGLSEtLNTAYRNH-NVTVFVINNNNFAMTGGQM 131
Cdd:cd00568   47 AMGYGLPAAIGAALAAPDRPVVCIAGDGGFMM-TGQE-LATAVRYGlPVIVVVFNNGGYGTIRMHQ 110
PRK08266 PRK08266
hypothetical protein; Provisional
 74-219 2.58e-05

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 44.62  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  74 TAIGVKVALPDTLVMTYQGDGdAYVIGLSEtLNTAYR-NHNVTVFVINNNNFamtggqmswttmpGQVTTTSVNGRDIKT 152
Cdd:PRK08266 410 TALGAKVANPDRPVVSITGDG-GFMFGVQE-LATAVQhNIGVVTVVFNNNAY-------------GNVRRDQKRRFGGRV 474

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260213474 153 TGSPLKVPEMVAnfFDVAYVARGS-VHSPKEiinlkkyIKNAIEAQLNGEGYSLVEIlaPCPTNWGVS 219
Cdd:PRK08266 475 VASDLVNPDFVK--LAESFGVAAFrVDSPEE-------LRAALEAALAHGGPVLIEV--PVPRGSEAS 531
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 75-126 5.71e-05

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: 43.61  E-value: 5.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260213474  75 AIGVKVALPDTLVMTYQGDGdAYVIGLSEtLNTAYRNH-NVTVFVINNNNFAM 126
Cdd:COG0028  421 AIGAKLARPDRPVVAITGDG-GFQMNLQE-LATAVRYGlPVKVVVLNNGGLGM 471
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 92-212 1.59e-04

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 42.45  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474    92 GDGDAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGGQMSWTTMPGQVTTTSVNGRdiKTTGSPLKVPEMVANFFDVAY 171
Cdd:TIGR02176  959 GDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGK--RTSKKDLGMMAMTYGYVYVAQ 1036

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 260213474   172 VARGSvhspkeiiNLKKYIKNAIEAQlNGEGYSLVEILAPC 212
Cdd:TIGR02176 1037 VSMGA--------NMQQTLKAFREAE-AYDGPSIVIAYSPC 1068
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 75-125 3.74e-04

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: 40.27  E-value: 3.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260213474  75 AIGVKVALPDTLVMTYQGDGDA-YVIGlseTLNTAYR-NHNVTVFVINNNNFA 125
Cdd:cd02002   58 AVGAALANPDRKVVAIIGDGSFmYTIQ---ALWTAARyGLPVTVVILNNRGYG 107
PRK12474 PRK12474
hypothetical protein; Provisional
 26-132 7.51e-04

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 40.24  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  26 VNRIIAEVIEEHGYEKNHVLTLGVGCVCNMNFSWNGDKMQT---AHGRASSTAIGVKVALPDTLVMTYQGDGDA-YVIgl 101
Cdd:PRK12474 346 VAQLIAHRTPDQAIYADEALTSGLFFDMSYDRARPHTHLPLtggSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAaYTM-- 423

                         90       100       110
                 ....*....|....*....|....*....|..
gi 260213474 102 sETLNTAYR-NHNVTVFVINNNNFAMTGGQMS 132
Cdd:PRK12474 424 -QALWTMAReNLDVTVVIFANRSYAILNGELQ 454
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 46-148 8.97e-04

Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.


Pssm-ID: 238962 [Multi-domain]  Cd Length: 172  Bit Score: 39.05  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  46 TLGVGcvcnMNFswngdkmqtahgrasstAIGVKVALPDTLVMTYQGDGdAYVIGLSEtLNTAYRnHN--VTVFVINNNN 123
Cdd:cd02004   49 TLGVG----LGY-----------------AIAAALARPDKRVVLVEGDG-AFGFSGME-LETAVR-YNlpIVVVVGNNGG 104

                         90       100
                 ....*....|....*....|....*.
gi 260213474 124 FAMTGGQMSWTTMPGQ-VTTTSVNGR 148
Cdd:cd02004  105 WYQGLDGQQLSYGLGLpVTTLLPDTR 130
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
 69-121 1.66e-03

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 39.21  E-value: 1.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260213474  69 GRASSTAIGVKVALPDTLVMTYQGDGdAYVIGLSETLNTAYRNHNVTVFVINN 121
Cdd:PRK07525 438 GYAFPAIIGAKIACPDRPVVGFAGDG-AWGISMNEVMTAVRHNWPVTAVVFRN 489
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 74-126 1.88e-03

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: 38.25  E-value: 1.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260213474  74 TAIGVKVALPDTLVMTYQGDGdayviGLSETLN---TAYRNH-NVTVFVINNNNFAM 126
Cdd:cd02015   58 AAIGAKVARPDKTVICIDGDG-----SFQMNIQelaTAAQYNlPVKIVILNNGSLGM 109
PRK06276 PRK06276
acetolactate synthase large subunit;
28-126 3.88e-03

acetolactate synthase large subunit;


Pssm-ID: 235766 [Multi-domain]  Cd Length: 586  Bit Score: 38.20  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260213474  28 RIIAEVIEEHGYEKNHVLTLGVGcvcnMNFSWNGDKMQTAHGRA--SS-----------TAIGVKVALPDTLVMTYQGDG 94
Cdd:PRK06276 372 KELMEVLREIDPSKNTIITTDVG----QNQMWMAHFFKTSAPRSfiSSgglgtmgfgfpAAIGAKVAKPDANVIAITGDG 447

                         90       100       110
                 ....*....|....*....|....*....|....
gi 260213474  95 DAYVIglSETLNTAyRNHN--VTVFVINNNNFAM 126
Cdd:PRK06276 448 GFLMN--SQELATI-AEYDipVVICIFDNRTLGM 478
PRK08527 PRK08527
acetolactate synthase large subunit;
75-136 4.68e-03

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 37.77  E-value: 4.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260213474  75 AIGVKVALPDTLVMTYQGDGdAYVIGLSEtLNTAYRNHNVTVFVINNNNFamTGGQMSWTTM 136
Cdd:PRK08527 423 ALGAKLAVPDKVVINFTGDG-SILMNIQE-LMTAVEYKIPVINIILNNNF--LGMVRQWQTF 480
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
 75-132 6.67e-03

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: 36.51  E-value: 6.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 260213474  75 AIGVKVALPDTLVMTYQGDGdAYVIGLSETLNTAYRNHNVTVFVINNNNFAMTGG-QMS 132
Cdd:cd02003   57 GLGAKLAKPDREVYVLVGDG-SYLMLHSEIVTAVQEGLKIIIVLFDNHGFGCINNlQES 114
 
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