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Conserved domains on  [gi|1900713664|gb|QNR22652|]
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2-oxoacid:ferredoxin oxidoreductase subunit beta [Croceimicrobium hydrocarbonivorans]

Protein Classification

2-oxoacid:ferredoxin oxidoreductase subunit beta( domain architecture ID 11485631)

2-oxoacid:ferredoxin oxidoreductase subunit beta is a component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 3-333 5.99e-171

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


:

Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 476.26  E-value: 5.99e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664   3 TTNTLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK11867    2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK11867   82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVF-NDGTFLNFTDKKLKDENVllleegqplvydqgkk 241
Cdd:PRK11867  162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVKVHDA---------------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 242 girlnglkpeivnleegaslndlwihDSRDATKAYVLSRFFDDSLPRPFGIFYQEDRPCYEDDLLDQIdhakgvQGEGDL 321
Cdd:PRK11867  226 --------------------------EGYDPTNALAAMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI------EGPLAL 273

                         330
                  ....*....|..
gi 1900713664 322 DDLLRGKRSWTV 333
Cdd:PRK11867  274 QDLLMGGDTWTV 285
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 3-333 5.99e-171

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 476.26  E-value: 5.99e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664   3 TTNTLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK11867    2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK11867   82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVF-NDGTFLNFTDKKLKDENVllleegqplvydqgkk 241
Cdd:PRK11867  162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVKVHDA---------------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 242 girlnglkpeivnleegaslndlwihDSRDATKAYVLSRFFDDSLPRPFGIFYQEDRPCYEDDLLDQIdhakgvQGEGDL 321
Cdd:PRK11867  226 --------------------------EGYDPTNALAAMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI------EGPLAL 273

                         330
                  ....*....|..
gi 1900713664 322 DDLLRGKRSWTV 333
Cdd:PRK11867  274 QDLLMGGDTWTV 285
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 20-212 7.78e-125

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: 355.68  E-value: 7.78e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNVFNDGTF 212
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTFPLGVF 193
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 6-209 2.47e-108

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: 316.32  E-value: 2.47e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664   6 TLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIaREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKIT 85
Cdd:COG1013     1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLD-GDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  86 NPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALG 165
Cdd:COG1013    80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1900713664 166 ADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVFND 209
Cdd:COG1013   160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 18-306 3.95e-92

2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of beta subunits, representing mostly pyruvate and 2-ketoisovalerate specific enzymes.


Pssm-ID: 274015 [Multi-domain]  Cd Length: 287  Bit Score: 276.26  E-value: 3.95e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDgtfLNfTDKKLKDENVLLLEEG-QPLVYDQGKkgirlnglkpeivnle 256
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK---IN-TYEWYRERVYKLDEEGyDPIVREPEE---------------- 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1900713664 257 egaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:TIGR02177 221 -----------FEEKAAAAIKKAMEWGDRI--PIGIFYKnENKPTFEERLE 258
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
18-306 2.09e-85

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 259.48  E-value: 2.09e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDGTFLNFTDK---KLKDEnvllleegqplvydqgkkgirlNGLKPEIVN 254
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKrvyKLDDE----------------------PGWDPVVRS 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1900713664 255 LEEgaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:NF041171  221 PEE----------ADEKMAKAIEKALEWGDRI--PIGIFYQnELVPTFEERIA 261
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
52-200 3.21e-35

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 125.39  E-value: 3.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  52 GIGCSSRF---------PYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGDGLSIgGNHLIHLLRRNVDLNVLL 122
Cdd:pfam02775   1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 123 FNNQIYGLTKGQYSPTselGKKTKSSPLGSLDHPFNP--LALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:pfam02775  80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFakLAEAYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 3-333 5.99e-171

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 476.26  E-value: 5.99e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664   3 TTNTLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK11867    2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK11867   82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVF-NDGTFLNFTDKKLKDENVllleegqplvydqgkk 241
Cdd:PRK11867  162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVKVHDA---------------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 242 girlnglkpeivnleegaslndlwihDSRDATKAYVLSRFFDDSLPRPFGIFYQEDRPCYEDDLLDQIdhakgvQGEGDL 321
Cdd:PRK11867  226 --------------------------EGYDPTNALAAMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI------EGPLAL 273

                         330
                  ....*....|..
gi 1900713664 322 DDLLRGKRSWTV 333
Cdd:PRK11867  274 QDLLMGGDTWTV 285
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 20-212 7.78e-125

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: 355.68  E-value: 7.78e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNVFNDGTF 212
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTFPLGVF 193
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 4-305 6.82e-111

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 324.52  E-value: 6.82e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664   4 TNTLSARDFSSD-QEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK05778    3 KNALGLTYLRYDgLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK05778   83 KLANPDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVFNDgtflNFTDKKLKDENVLLLEEGqplVYDqgkkg 242
Cdd:PRK05778  163 ALAAGATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNG----RNTSTKSPAYMREYYKKR---VYK----- 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900713664 243 irlnglkpeiVNLEEGaslndlwiHDSRDATKAyvlsrfFDDSLPR------PFGIFYQEDRPCYEDDL 305
Cdd:PRK05778  231 ----------LKLEED--------YDPTDRDKA------AEKMLEEelggkiPIGVFYKNERPTFEERL 275
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 6-209 2.47e-108

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: 316.32  E-value: 2.47e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664   6 TLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIaREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKIT 85
Cdd:COG1013     1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLD-GDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  86 NPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALG 165
Cdd:COG1013    80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1900713664 166 ADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVFND 209
Cdd:COG1013   160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 20-306 1.13e-93

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 279.72  E-value: 1.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:PRK11866    9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:PRK11866   89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNVFNdgtflnftdkklkdenvllleegqplvydqgkkgiRLNG---LKPEIVNLE 256
Cdd:PRK11866  169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFN-----------------------------------KLNTydwFRPRVYKLE 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1900713664 257 EGAslndlwiHDSRDATKAYVLSRFFDDSLprPFGIFYQEDRPCYEDDLL 306
Cdd:PRK11866  214 ETG-------HDPTNFEQAYKKALEWGDRI--PIGVFYKEEKPTYEEELD 254
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 18-306 3.95e-92

2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of beta subunits, representing mostly pyruvate and 2-ketoisovalerate specific enzymes.


Pssm-ID: 274015 [Multi-domain]  Cd Length: 287  Bit Score: 276.26  E-value: 3.95e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDgtfLNfTDKKLKDENVLLLEEG-QPLVYDQGKkgirlnglkpeivnle 256
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK---IN-TYEWYRERVYKLDEEGyDPIVREPEE---------------- 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1900713664 257 egaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:TIGR02177 221 -----------FEEKAAAAIKKAMEWGDRI--PIGIFYKnENKPTFEERLE 258
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
18-306 2.09e-85

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 259.48  E-value: 2.09e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDGTFLNFTDK---KLKDEnvllleegqplvydqgkkgirlNGLKPEIVN 254
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKrvyKLDDE----------------------PGWDPVVRS 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1900713664 255 LEEgaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:NF041171  221 PEE----------ADEKMAKAIEKALEWGDRI--PIGIFYQnELVPTFEERIA 261
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 15-305 4.00e-73

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 227.36  E-value: 4.00e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  15 DQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVI 94
Cdd:PRK11869    5 KYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  95 TGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARS 174
Cdd:PRK11869   85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 175 IDRDPKHLREILSASHQHKGTSFIEVYQNCNVFND-GTFLNFTdkklkdENVLLLEEgqplvydqgkkgirlnglkpeiv 253
Cdd:PRK11869  165 FSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKvNTYQWYR------ENTYYLKD----------------------- 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 254 nleegaslndlwiHDSRDATKAyvlsrfFDDSL---PRPFGIFYQEDRPCYEDDL 305
Cdd:PRK11869  216 -------------HDPTDRELA------FKRALeteKLPLGIFYINEKPTFEELV 251
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
20-206 2.90e-67

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 212.28  E-value: 2.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:PRK09628   18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:PRK09628   98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177

                         170       180
                  ....*....|....*....|....*..
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNV 206
Cdd:PRK09628  178 QKLEKLLVKGFSHKGFSFFDVFSNCHI 204
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
52-200 3.21e-35

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 125.39  E-value: 3.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  52 GIGCSSRF---------PYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGDGLSIgGNHLIHLLRRNVDLNVLL 122
Cdd:pfam02775   1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 123 FNNQIYGLTKGQYSPTselGKKTKSSPLGSLDHPFNP--LALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:pfam02775  80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFakLAEAYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 21-223 1.56e-22

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: 94.09  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  21 CPGCGDYSILKQMQSVVPelgiAREDIVFISGIGCSS----RFPYymNTYGMHSIH---GRAPAIATGLK-----ITNPD 88
Cdd:cd02018     8 CAGCGEVTAVRVVLAALP----APEDTVIANSTGCSSvyasTAPF--NSWAVPWVNslfEDANAVASGLKrglkaRFPKD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  89 L------SIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:cd02018    82 ReldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLI 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 163 ALGADASFVARSIDRDPKH-LREILSASHQHKGTSFIEVYQNCNV---FNDGTFLNFTDKKLKDE 223
Cdd:cd02018   162 AATHGCVYVARLSPALKKHfLKVVKEAISRTDGPTFIHAYTPCITewgIGSGKSLELARKAVKSR 226
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 29-200 2.69e-18

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: 80.76  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  29 ILKQMQSVVPElgiareDIVFISGIGCSSRFPYYM---------NTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGd 99
Cdd:cd00568     2 VLAALRAALPE------DAIVVNDAGNSAYWAYRYlplrrgrrfLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYsptselGKKTKSSPLGSLDHP--FNPLALALGADASFVarsidR 177
Cdd:cd00568    75 GFMMTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQ------EAFYGGRVSGTDLSNpdFAALAEAYGAKGVRV-----E 143

                         170       180
                  ....*....|....*....|...
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEV 200
Cdd:cd00568   144 DPEDLEAALAEALAAGGPALIEV 166
PRK11865 PRK11865
pyruvate synthase subunit beta;
21-204 2.87e-12

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 66.28  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  21 CPGCGDYSILKQMqsvvpeLGIAREDIVFISGIGCSS--RFPYYMNTYGMHSIH---GRAPAIATG----LKITNPDLSI 91
Cdd:PRK11865   21 CAGCGAAIAMRLA------LKALGKNTVIVVATGCLEviTTPYPETAWNVPWIHvafENAAAVASGieraVKALGKKVNV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  92 WVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSL----DHPFNPLALALGA- 166
Cdd:PRK11865   95 VAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgeDRPKKNMPLIMAAh 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1900713664 167 DASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNC 204
Cdd:PRK11865  175 GIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPC 212
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 21-204 1.80e-08

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: 54.17  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  21 CPGCGDYSILKQMqsvvpeLGIAREDIVFISGIGCSSRF--PYYMNTYGMHSIH---GRAPAIATG----LKIT--NPDL 89
Cdd:cd03376     8 CAGCGAALALRHV------LKALGPDTVVVNPTGCLEVIttPYPYTAWRVPWIHvafENAAAVASGieaaLKALgrGKDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  90 SIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLD-----HPFNPLALAL 164
Cdd:cd03376    82 TVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSfgkkqPKKDLPLIMA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1900713664 165 GADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNC 204
Cdd:cd03376   162 AHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPC 201
PRK08266 PRK08266
hypothetical protein; Provisional
 28-200 1.54e-07

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 52.71  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  28 SILKQMQSVVPELGIAREDIvfiSGIGCSSR--FPYYM-NTY---GMHSIHGRAPAIATGLKITNPDLSIWVITGDGdGL 101
Cdd:PRK08266  357 SYLRAIREALPDDGIFVDEL---SQVGFASWfaFPVYApRTFvtcGYQGTLGYGFPTALGAKVANPDRPVVSITGDG-GF 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 102 SIGGNHLIHLLRRNVDLNVLLFNNQIYG----LTKGQYsptselGKKTKSSPLGSLDhpFNPLALALGADASFVarsidR 177
Cdd:PRK08266  433 MFGVQELATAVQHNIGVVTVVFNNNAYGnvrrDQKRRF------GGRVVASDLVNPD--FVKLAESFGVAAFRV-----D 499

                         170       180
                  ....*....|....*....|...
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEV 200
Cdd:PRK08266  500 SPEELRAALEAALAHGGPVLIEV 522
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 43-200 2.08e-06

Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.


Pssm-ID: 239468 [Multi-domain]  Cd Length: 188  Bit Score: 47.69  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  43 AREDIVFISGIGCSSRFPY-YMNTYGMHSIH--------GRAPAIATGLKITNPDLSIWVITGDG------DGLSIGGNH 107
Cdd:cd03371    12 APATAAVVSTTGMTSRELFeLRDRPGGGHAQdfltvgsmGHASQIALGIALARPDRKVVCIDGDGaalmhmGGLATIGGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 108 ----LIHllrrnvdlnvLLFNNQIYGLTKGQysPTSelgkktkssplgSLDHPFNPLALALGADASFVARSIDRDPKHLR 183
Cdd:cd03371    92 apanLIH----------IVLNNGAHDSVGGQ--PTV------------SFDVSLPAIAKACGYRAVYEVPSLEELVAALA 147

                         170
                  ....*....|....*..
gi 1900713664 184 EILSAShqhkGTSFIEV 200
Cdd:cd03371   148 KALAAD----GPAFIEV 160
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
23-133 2.25e-06

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 49.22  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  23 GCGDYSIL-KQMQSVVPELGIAREDIVfISGIGCSSR-FPYYMNTYGMHSIH---GRAPAIATGLKITNPDLSIWVITGD 97
Cdd:PRK07064  354 GLGPYAKLvDALRAALPRDGNWVRDVT-ISNSTWGNRlLPIFEPRANVHALGggiGQGLAMAIGAALAGPGRKTVGLVGD 432

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1900713664  98 GdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKG 133
Cdd:PRK07064  433 G-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
PFO_beta_C pfam12367
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ...
 249-303 6.25e-06

Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in bacteria and archaea, and is approximately 70 amino acids in length. The family is found in association with pfam02775. There are two completely conserved residues (A and G) that may be functionally important. PFO is involved in carbon dioxide fixation via a reductive TCA cycle. It forms a heterodimer (alpha/beta). The beta subunit has binding motifs for Fe-S clusters and thiamine pyrophosphate.


Pssm-ID: 463551 [Multi-domain]  Cd Length: 62  Bit Score: 43.25  E-value: 6.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 249 KPEIVNLEEgaslndlwIHDSRDATKAYVLSRFFDDSLPrpFGIFYQEDRPCYED 303
Cdd:pfam12367  14 KERVYKLDE--------DHDPTDREAAMEKALEWGDRIP--IGIFYKEERPTFEE 58
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 90-152 3.68e-05

Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze 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 PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.


Pssm-ID: 239472  Cd Length: 365  Bit Score: 44.90  E-value: 3.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900713664  90 SIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSptselgkktKSSPLGS 152
Cdd:cd03377   153 SVWIIGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQAS---------KATPLGA 206
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 78-200 4.37e-05

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 45.14  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  78 IATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKgqYSPTSELGKKTKSSPLGSLDHPf 157
Cdd:PRK06112  445 MAIGAKVARPGAPVICLVGDG-GFAHVWAELETARRMGVPVTIVVLNNGILGFQK--HAETVKFGTHTDACHFAAVDHA- 520

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1900713664 158 nPLALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:PRK06112  521 -AIARACGCDGVRV-----EDPAELAQALAAAMAAPGPTLIEV 557
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 76-200 5.79e-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: 44.77  E-value: 5.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  76 PAiATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYspTSELGKKTKSSPLGSLDh 155
Cdd:COG0028   419 PA-AIGAKLARPDRPVVAITGDG-GFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQ--ELFYGGRYSGTDLPNPD- 493

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1900713664 156 pFNPLALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:COG0028   494 -FAKLAEAFGAKGERV-----ETPEELEAALEEALASDGPALIDV 532
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 76-200 1.46e-04

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: 42.10  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  76 PAiATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLT--------KGQYSPTselgkktks 147
Cdd:cd02015    57 PA-AIGAKVARPDKTVICIDGDG-SFQMNIQELATAAQYNLPVKIVILNNGSLGMVrqwqelfyEGRYSHT--------- 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1900713664 148 splgslDHPFNP----LALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:cd02015   126 ------TLDSNPdfvkLAEAYGIKGLRV-----EKPEELEAALKEALASDGPVLLDV 171
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
 77-200 1.08e-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: 39.60  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  77 AIATGLKITNPDLSIWVITGDGDGLsIGGNHLIHLLRRNVDLNVLLFNNQIYG------LTKGQYSPTSELgkKTKSSPL 150
Cdd:cd02003    55 AAGLGAKLAKPDREVYVLVGDGSYL-MLHSEIVTAVQEGLKIIIVLFDNHGFGcinnlqESTGSGSFGTEF--RDRDQES 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 151 GSLDHPFNPLALA-----LGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:cd02003   132 GQLDGALLPVDFAanarsLGARVEKV-----KTIEELKAALAKAKASDRTTVIVI 181
PRK06546 PRK06546
pyruvate dehydrogenase; Provisional
 42-200 1.12e-03

pyruvate dehydrogenase; Provisional


Pssm-ID: 180614 [Multi-domain]  Cd Length: 578  Bit Score: 40.74  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  42 IAREDIVFISGIG-CSSRFPYYMNTYGMHSI-----HGR-APAI--ATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLL 112
Cdd:PRK06546  371 LAADDAVFTVDTGmCNVWAARYITPNGRRRVigsfrHGSmANALphAIGAQLADPGRQVISMSGDG-GLSMLLGELLTVK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 113 RRNVDLNVLLFNNQIYGLTKgqysptseLGKKTKSSPLGSLDHP---FNPLALALGADASFVarsidRDPKHLREILSAS 189
Cdd:PRK06546  450 LYDLPVKVVVFNNSTLGMVK--------LEMLVDGLPDFGTDHPpvdYAAIAAALGIHAVRV-----EDPKDVRGALREA 516

                         170
                  ....*....|.
gi 1900713664 190 HQHKGTSFIEV 200
Cdd:PRK06546  517 FAHPGPALVDV 527
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 45-139 1.54e-03

Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.


Pssm-ID: 238959 [Multi-domain]  Cd Length: 157  Bit Score: 38.62  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664  45 EDIVFISGIGCSSRFPYYM----NTYGMHSIHGRAPAIATGLKITNPDLsiwVITGDGDG--------LSIGGNH----L 108
Cdd:cd02001    13 GDTPIVSTTGYASRELYDVqdrdGHFYMLGSMGLAGSIGLGLALGLSRK---VIVVDGDGsllmnpgvLLTAGEFtplnL 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1900713664 109 IHLLrrnvdlnvllFNNQIYGLTKGQYSPTS 139
Cdd:cd02001    90 ILVV----------LDNRAYGSTGGQPTPSS 110
 
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.
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