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Conserved domains on  [gi|1539990514|emb|VEG56748|]
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2-oxoglutarate ferredoxin oxidoreductase subunit beta [Mycolicibacterium aurum]

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
 23-358 0e+00

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


:

Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 502.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  23 TTDQPQKAKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATG 102
Cdd:PRK11867    1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 103 LALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVS 182
Cdd:PRK11867   81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 183 LALGAEATFVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCPIF-NDGSFDALRKEgaeerlinvrhgepitfgadge 261
Cdd:PRK11867  161 LALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKER---------------------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 262 ycvvksgfgleaaktadvsadEIVVHDATVEDPAYAFAlSRLSEQNLDHMVMGIFRQVSKPTYDDAARAQItaareakaH 341
Cdd:PRK11867  219 ---------------------LVKVHDAEGYDPTNALA-AMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI--------E 268

                         330
                  ....*....|....*..
gi 1539990514 342 DTAALQSLLRGKDTWNV 358
Cdd:PRK11867  269 GPLALQDLLMGGDTWTV 285
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 23-358 0e+00

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 502.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  23 TTDQPQKAKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATG 102
Cdd:PRK11867    1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 103 LALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVS 182
Cdd:PRK11867   81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 183 LALGAEATFVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCPIF-NDGSFDALRKEgaeerlinvrhgepitfgadge 261
Cdd:PRK11867  161 LALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKER---------------------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 262 ycvvksgfgleaaktadvsadEIVVHDATVEDPAYAFAlSRLSEQNLDHMVMGIFRQVSKPTYDDAARAQItaareakaH 341
Cdd:PRK11867  219 ---------------------LVKVHDAEGYDPTNALA-AMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI--------E 268

                         330
                  ....*....|....*..
gi 1539990514 342 DTAALQSLLRGKDTWNV 358
Cdd:PRK11867  269 GPLALQDLLMGGDTWTV 285
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 41-228 5.28e-117

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: 336.80  E-value: 5.28e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  41 WCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGD 120
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 121 ALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDSDR 200
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1539990514 201 KGLSEVLRGAAQHRGAALVEIMQDCPIF 228
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 29-230 3.00e-102

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: 302.06  E-value: 3.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  29 KAKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRrENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALARE 108
Cdd:COG1013     3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDG-DKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 109 DLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAE 188
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539990514 189 ATFVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCPIFND 230
Cdd:COG1013   162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 39-230 2.04e-87

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: 265.47  E-value: 2.04e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  39 VRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGD 118
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 119 GDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDS 198
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539990514 199 DRKGLSEVLRGAAQHRGAALVEIMQDCPIFND 230
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
39-230 2.96e-75

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 234.45  E-value: 2.96e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  39 VRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGD 118
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 119 GDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDS 198
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539990514 199 DRKGLSEVLRGAAQHRGAALVEIMQDCPIFND 230
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYND 194
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
73-221 2.22e-35

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 126.55  E-value: 2.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  73 GIGCSSRF---------PYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGDALSIGgNHLIHALRRNINITILL 143
Cdd:pfam02775   1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 144 FNNRIYGLTKGQYSPtseTGKVTKSTPMGSLDYPFNPVSLA--LGAEATFVgraldSDRKGLSEVLRGAAQHRGAALVEI 221
Cdd:pfam02775  80 LNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAeaYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 23-358 0e+00

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 502.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  23 TTDQPQKAKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATG 102
Cdd:PRK11867    1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 103 LALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVS 182
Cdd:PRK11867   81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 183 LALGAEATFVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCPIF-NDGSFDALRKEgaeerlinvrhgepitfgadge 261
Cdd:PRK11867  161 LALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKER---------------------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 262 ycvvksgfgleaaktadvsadEIVVHDATVEDPAYAFAlSRLSEQNLDHMVMGIFRQVSKPTYDDAARAQItaareakaH 341
Cdd:PRK11867  219 ---------------------LVKVHDAEGYDPTNALA-AMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI--------E 268

                         330
                  ....*....|....*..
gi 1539990514 342 DTAALQSLLRGKDTWNV 358
Cdd:PRK11867  269 GPLALQDLLMGGDTWTV 285
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 41-228 5.28e-117

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: 336.80  E-value: 5.28e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  41 WCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGD 120
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 121 ALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDSDR 200
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1539990514 201 KGLSEVLRGAAQHRGAALVEIMQDCPIF 228
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 29-230 3.00e-102

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: 302.06  E-value: 3.00e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  29 KAKDFTSDQEVRWCPGCGDYVILNTIRNFLPELGLRrENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALARE 108
Cdd:COG1013     3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDG-DKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 109 DLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAE 188
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539990514 189 ATFVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCPIFND 230
Cdd:COG1013   162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 41-326 3.12e-99

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 296.02  E-value: 3.12e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  41 WCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGD 120
Cdd:PRK05778   20 WCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 121 ALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDSDR 200
Cdd:PRK05778  100 LASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFVARSFAGDV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 201 KGLSEVLRGAAQHRGAALVEIMQDCPIFNDgsfdalrkegaeerlinvRHGEPITFGADGEYcvvksgfgleaaktadvS 280
Cdd:PRK05778  180 KQLVELIKKAISHKGFAFIDVLSPCVTFNG------------------RNTSTKSPAYMREY-----------------Y 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1539990514 281 ADEIV-VHDATVEDPA-YAFALSRLSEQNL-DHMVMGIFRQVSKPTYDD 326
Cdd:PRK05778  225 KKRVYkLKLEEDYDPTdRDKAAEKMLEEELgGKIPIGVFYKNERPTFEE 273
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 39-230 2.04e-87

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: 265.47  E-value: 2.04e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  39 VRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGD 118
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 119 GDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDS 198
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539990514 199 DRKGLSEVLRGAAQHRGAALVEIMQDCPIFND 230
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 41-327 4.49e-83

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 253.91  E-value: 4.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  41 WCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGD 120
Cdd:PRK11866    9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 121 ALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDSDR 200
Cdd:PRK11866   89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 201 KGLSEVLRGAAQHRGAALVEIMQDCPIFND-GSFDALRkegaeERLinvrhgepitfgadgeYCVVKSGfgleaaktadv 279
Cdd:PRK11866  169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFNKlNTYDWFR-----PRV----------------YKLEETG----------- 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1539990514 280 sadeivvHDATVEDPAYAFALsrlseQNLDHMVMGIFRQVSKPTYDDA 327
Cdd:PRK11866  217 -------HDPTNFEQAYKKAL-----EWGDRIPIGVFYKEEKPTYEEE 252
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
39-230 2.96e-75

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 234.45  E-value: 2.96e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  39 VRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGD 118
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 119 GDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDS 198
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1539990514 199 DRKGLSEVLRGAAQHRGAALVEIMQDCPIFND 230
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYND 194
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 34-229 1.33e-69

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 219.65  E-value: 1.33e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  34 TSDQEVRWCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVW 113
Cdd:PRK11869    3 PEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 114 VVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVG 193
Cdd:PRK11869   83 AEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVA 162

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1539990514 194 RALDSDRKGLSEVLRGAAQHRGAALVEIMQDCPIFN 229
Cdd:PRK11869  163 RTFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFN 198
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
41-227 1.79e-58

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 190.71  E-value: 1.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  41 WCPGCGDYVILNTIRNFLPELGLRRENIAFVSGIGCSSRFPYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGD 120
Cdd:PRK09628   18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 121 ALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVSLALGAEATFVGRALDSDR 200
Cdd:PRK09628   98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177

                         170       180
                  ....*....|....*....|....*..
gi 1539990514 201 KGLSEVLRGAAQHRGAALVEIMQDCPI 227
Cdd:PRK09628  178 QKLEKLLVKGFSHKGFSFFDVFSNCHI 204
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
73-221 2.22e-35

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 126.55  E-value: 2.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  73 GIGCSSRF---------PYYLETYGFHSIHGRAPTIATGLALAREDLSVWVVTGDGDALSIGgNHLIHALRRNINITILL 143
Cdd:pfam02775   1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 144 FNNRIYGLTKGQYSPtseTGKVTKSTPMGSLDYPFNPVSLA--LGAEATFVgraldSDRKGLSEVLRGAAQHRGAALVEI 221
Cdd:pfam02775  80 LNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAeaYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 50-223 1.24e-17

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: 79.22  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  50 ILNTIRNFLPElglrreNIAFVSGIGCSSRFPYYL------ETYGFHSIHGR---APTIATGLALAREDLSVWVVTGDGD 120
Cdd:cd00568     2 VLAALRAALPE------DAIVVNDAGNSAYWAYRYlplrrgRRFLTSTGFGAmgyGLPAAIGAALAAPDRPVVCIAGDGG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 121 ALSiGGNHLIHALRRNINITILLFNNRIYGLTKGQYsptsetGKVTKSTPMGSLDYPFNPVSLA--LGAEATFVGRALDs 198
Cdd:cd00568    76 FMM-TGQELATAVRYGLPVIVVVFNNGGYGTIRMHQ------EAFYGGRVSGTDLSNPDFAALAeaYGAKGVRVEDPED- 147

                         170       180
                  ....*....|....*....|....*
gi 1539990514 199 drkgLSEVLRGAAQHRGAALVEIMQ 223
Cdd:cd00568   148 ----LEAALAEALAAGGPALIEVKT 168
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 42-225 5.79e-15

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: 73.67  E-value: 5.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  42 CPGCGDYVILNTIRNFLPElglrRENIAFVSGIGCSSrfpYYLETYGF--------HSIHGRAPTIATGL-----ALARE 108
Cdd:cd02018     8 CAGCGEVTAVRVVLAALPA----PEDTVIANSTGCSS---VYASTAPFnswavpwvNSLFEDANAVASGLkrglkARFPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 109 DL------SVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPFNPVS 182
Cdd:cd02018    81 DReldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1539990514 183 LALGAEATFVGRALDSDRKGLSEVLRGA-AQHRGAALVEIMQDC 225
Cdd:cd02018   161 IAATHGCVYVARLSPALKKHFLKVVKEAiSRTDGPTFIHAYTPC 204
PRK11865 PRK11865
pyruvate synthase subunit beta;
40-226 1.25e-12

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 67.43  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  40 RWCPGCGDYVILntiRNFLPELGlrrENIAFVSGIGCSS----RFPYylETYGFHSIH---GRAPTIATGLALA----RE 108
Cdd:PRK11865   19 RACAGCGAAIAM---RLALKALG---KNTVIVVATGCLEvittPYPE--TAWNVPWIHvafENAAAVASGIERAvkalGK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 109 DLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSL----DYPFNPVSLA 184
Cdd:PRK11865   91 KVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgeDRPKKNMPLI 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1539990514 185 LGAE-ATFVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCP 226
Cdd:PRK11865  171 MAAHgIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCP 213
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 40-226 5.66e-09

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: 56.09  E-value: 5.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  40 RWCPGCGDYVILntiRNFLPELGlrrENIAFVSGIGCSS-----------RFPYyletygFHSIHGRAPTIATGLALA-- 106
Cdd:cd03376     6 RACAGCGAALAL---RHVLKALG---PDTVVVNPTGCLEvittpypytawRVPW------IHVAFENAAAVASGIEAAlk 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 107 ----REDLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMG--SLDYPFNP 180
Cdd:cd03376    74 algrGKDITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGkvSFGKKQPK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1539990514 181 VSLALGAEAT---FVGRALDSDRKGLSEVLRGAAQHRGAALVEIMQDCP 226
Cdd:cd03376   154 KDLPLIMAAHnipYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCP 202
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 66-221 3.17e-08

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: 53.09  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  66 ENIAFVSGIGCSSRFPYYL-ETYGFHSIH--------GRAPTIATGLALAREDLSVWVVTGDGDAL-------SIGG--- 126
Cdd:cd03371    14 ATAAVVSTTGMTSRELFELrDRPGGGHAQdfltvgsmGHASQIALGIALARPDRKVVCIDGDGAALmhmgglaTIGGlap 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 127 NHLIHalrrninitiLLFNNRIYGLTKGQysPTSetgkvtkstpmgSLDYPFNPVSLALGAEATFVGraldSDRKGLSEV 206
Cdd:cd03371    94 ANLIH----------IVLNNGAHDSVGGQ--PTV------------SFDVSLPAIAKACGYRAVYEV----PSLEELVAA 145

                         170
                  ....*....|....*
gi 1539990514 207 LRGAAQHRGAALVEI 221
Cdd:cd03371   146 LAKALAADGPAFIEV 160
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 100-222 3.27e-07

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 49.90  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 100 ATGLALAREDLSVWVVTGDGDAL-SIGGnhLIHALRRNINITILLFNNRIYGLTK------GQYSPTSETGKVtkstpMG 172
Cdd:cd02002    58 AVGAALANPDRKVVAIIGDGSFMyTIQA--LWTAARYGLPVTVVILNNRGYGALRsflkrvGPEGPGENAPDG-----LD 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539990514 173 SLDYPFNPVSLA--LGAEATFVGRALDsdrkgLSEVLRGAAQHRGAALVEIM 222
Cdd:cd02002   131 LLDPGIDFAAIAkaFGVEAERVETPEE-----LDEALREALAEGGPALIEVV 177
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 42-225 4.39e-07

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: 49.58  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  42 CPGCGDYVILNTIRnflpelGLRRENIAFVSGIGCSSR--FPYYLETYGFHSIhGRAPTIATGLALAREDLSVWVVTGDG 119
Cdd:cd02008     7 CPGCPHRPSFYALR------KAFKKDSIVSGDIGCYTLgaLPPLNAIDTCTCM-GASIGVAIGMAKASEDKKVVAVIGDS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 120 DALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMgsldyPFNPVSLALGAEatFVgRALDS- 198
Cdd:cd02008    80 TFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTVI-----DIEALVRAIGVK--RV-VVVDPy 151

                         170       180
                  ....*....|....*....|....*..
gi 1539990514 199 DRKGLSEVLRGAAQHRGAALVEIMQDC 225
Cdd:cd02008   152 DLKAIREELKEALAVPGVSVIIAKRPC 178
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 100-222 2.94e-06

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: 46.76  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 100 ATGLALAREDLSVWVVTGDGdALSIGGNHLIHALRRNINITILLFNN-RIYGLTKGQysptseTGKVTKSTPMGSLDYP- 177
Cdd:cd02004    57 AIAAALARPDKRVVLVEGDG-AFGFSGMELETAVRYNLPIVVVVGNNgGWYQGLDGQ------QLSYGLGLPVTTLLPDt 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1539990514 178 -FNPVSLALGAEATFVGRALDsdrkgLSEVLRGAAQHRGAALVEIM 222
Cdd:cd02004   130 rYDLVAEAFGGKGELVTTPEE-----LKPALKRALASGKPALINVI 170
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 66-162 4.01e-06

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: 46.33  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  66 ENIAFVSGIGCSSRFPYYLET-----YGFHSIhGRAPTIATGLALAREDlSVWVVTGDGDALSIGGNHLIHALRRNINIT 140
Cdd:cd02001    13 GDTPIVSTTGYASRELYDVQDrdghfYMLGSM-GLAGSIGLGLALGLSR-KVIVVDGDGSLLMNPGVLLTAGEFTPLNLI 90

                          90       100
                  ....*....|....*....|..
gi 1539990514 141 ILLFNNRIYGLTKGQYSPTSET 162
Cdd:cd02001    91 LVVLDNRAYGSTGGQPTPSSNV 112
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 100-222 4.29e-06

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: 48.62  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 100 ATGLALAREDLSVWVVTGDGdALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYspTSETGKVTKSTPMGSLDYpfn 179
Cdd:COG0028   421 AIGAKLARPDRPVVAITGDG-GFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQ--ELFYGGRYSGTDLPNPDF--- 494

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1539990514 180 pVSLA--LGAEATFVgraldSDRKGLSEVLRGAAQHRGAALVEIM 222
Cdd:COG0028   495 -AKLAeaFGAKGERV-----ETPEELEAALEEALASDGPALIDVR 533
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 111-173 4.51e-06

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: 47.98  E-value: 4.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539990514 111 SVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSptsetgkvtKSTPMGS 173
Cdd:cd03377   153 SVWIIGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQAS---------KATPLGA 206
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
42-227 5.79e-06

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 47.39  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  42 CPGCGdyvILNTIRNFLPELGlrrENIAFVSGIGCSS----RFPYY-LETYGFHSIHGRAPTIATGL-----ALAREDLS 111
Cdd:PRK11864   21 CPGCG---APLGLRYLLKALG---EKTVLVIPASCSTviqgDTPKSpLTVPVLHTAFAATAAVASGIeealkARGEKGVI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 112 VWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSLDYPfNPVSLALGA-EAT 190
Cdd:PRK11864   95 VVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHK-KPVPDIMAAhKVP 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539990514 191 FVGRA-----LDSDRKglsevLRGAAQHRGAALVEIMQDCPI 227
Cdd:PRK11864  174 YVATAsiaypEDFIRK-----LKKAKEIRGFKFIHLLAPCPP 210
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 71-160 2.45e-05

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. 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. ComDE requires TPP and divalent metal cation cofactors.


Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 44.20  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  71 VSGIGCSSRFPYY-----LETYGFHSIhGRAPTIATGLALAREDlSVWVVTGDGDALSIGGNHLIHALRRNINITILLFN 145
Cdd:cd03372    18 VSNIGFPSKELYAagdrpLNFYMLGSM-GLASSIGLGLALAQPR-KVIVIDGDGSLLMNLGALATIAAEKPKNLIIVVLD 95

                          90
                  ....*....|....*
gi 1539990514 146 NRIYGLTKGQYSPTS 160
Cdd:cd03372    96 NGAYGSTGNQPTHAG 110
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 111-167 3.95e-05

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: 45.53  E-value: 3.95e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539990514  111 SVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKVTK 167
Cdd:TIGR02176  953 SVWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAK 1009
PRK06163 PRK06163
hypothetical protein; Provisional
 94-165 5.70e-05

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 43.67  E-value: 5.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539990514  94 GRAPTIATGLALAREDLSVWVVTGDGDALSIGGNHLIHALRRNINITILLFNNRIYGLTKGQYSPTSETGKV 165
Cdd:PRK06163   60 GLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTVDV 131
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
 100-224 6.98e-05

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 44.56  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 100 ATGLALAREDLSVWVVTGDGDAlsiggNHLIHAL----RRNINITILLFNNRIYGLTKGqYSPTSETGKVtKSTPMGSLD 175
Cdd:PRK07092  416 AVGVALAQPGRRVIGLIGDGSA-----MYSIQALwsaaQLKLPVTFVILNNGRYGALRW-FAPVFGVRDV-PGLDLPGLD 488

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1539990514 176 YpfnpVSLA--LGAEATFVGRALDsdrkgLSEVLRGAAQHRGAALVEIMQD 224
Cdd:PRK07092  489 F----VALArgYGCEAVRVSDAAE-----LADALARALAADGPVLVEVEVA 530
PRK07586 PRK07586
acetolactate synthase large subunit;
100-222 1.00e-04

acetolactate synthase large subunit;


Pssm-ID: 236063 [Multi-domain]  Cd Length: 514  Bit Score: 44.06  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 100 ATGLALAREDLSVWVVTGDGDALsiggnHLIHAL----RRNINITILLFNNRIYGLTKGQYSPT--SETGKVTKStpMGS 173
Cdd:PRK07586  394 ATGAAVACPDRKVLALQGDGSAM-----YTIQALwtqaRENLDVTTVIFANRAYAILRGELARVgaGNPGPRALD--MLD 466

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539990514 174 LDYP-FNPVSLA--LGAEATFVGRALDsdrkgLSEVLRGAAQHRGAALVEIM 222
Cdd:PRK07586  467 LDDPdLDWVALAegMGVPARRVTTAEE-----FADALAAALAEPGPHLIEAV 513
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
 82-232 2.17e-04

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


Pssm-ID: 238961 [Multi-domain]  Cd Length: 205  Bit Score: 41.91  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  82 YYLEtYGF----HSIHGraptiATGLALAREDLSVWVVTGDGDALsIGGNHLIHALRRNINITILLFNNRIYG----LTK 153
Cdd:cd02003    41 YHLE-YGYscmgYEIAA-----GLGAKLAKPDREVYVLVGDGSYL-MLHSEIVTAVQEGLKIIIVLFDNHGFGcinnLQE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 154 GQYSPTSETGKVTKSTPMGSLDYPFNPVSLA-----LGAEATFVGraldsDRKGLSEVLRGAAQHRGAALVEIMQDCPIF 228
Cdd:cd02003   114 STGSGSFGTEFRDRDQESGQLDGALLPVDFAanarsLGARVEKVK-----TIEELKAALAKAKASDRTTVIVIKTDPKSM 188


                  ....
gi 1539990514 229 NDGS 232
Cdd:cd02003   189 TPGY 192
PRK12474 PRK12474
hypothetical protein; Provisional
 99-222 2.37e-04

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 42.94  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  99 IATGLALAREDLSVWVVTGDGdalsiGGNHLIHAL----RRNINITILLFNNRIYGLTKGQYSPTSETGKVTKSTPMGSL 174
Cdd:PRK12474  397 LAAGAAVAAPDRKVVCPQGDG-----GAAYTMQALwtmaRENLDVTVVIFANRSYAILNGELQRVGAQGAGRNALSMLDL 471

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1539990514 175 DYP-FNPVSLA--LGAEAtfvGRALDSDRkgLSEVLRGAAQHRGAALVEIM 222
Cdd:PRK12474  472 HNPeLNWMKIAegLGVEA---SRATTAEE--FSAQYAAAMAQRGPRLIEAM 517
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
44-221 6.67e-04

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 41.51  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  44 GCGDYVILN-TIRNFLPELGLRRENIAfVSGIGCSSR-FPYYLETYGFHSIH---GRAPTIATGLALAREDLSVWVVTGD 118
Cdd:PRK07064  354 GLGPYAKLVdALRAALPRDGNWVRDVT-ISNSTWGNRlLPIFEPRANVHALGggiGQGLAMAIGAALAGPGRKTVGLVGD 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514 119 GdALSIGGNHLIHALRRNINITILLFNNRIYGLTKG----QYSptSETGKVTKSTPmgslDYPFnpVSLALGAEATFVGR 194
Cdd:PRK07064  433 G-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRNiqdaQYG--GRRYYVELHTP----DFAL--LAASLGLPHWRVTS 503

                         170       180
                  ....*....|....*....|....*..
gi 1539990514 195 ALDSDRkglseVLRGAAQHRGAALVEI 221
Cdd:PRK07064  504 ADDFEA-----VLREALAKEGPVLVEV 525
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 99-224 1.94e-03

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 40.13  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539990514  99 IATGLALAREDLSVWVVTGDGdalsiGGNH----LIHALRRNINITILLFNNRIYGLTKgqYSPTSETGKVTKSTPMGSL 174
Cdd:PRK06112  445 MAIGAKVARPGAPVICLVGDG-----GFAHvwaeLETARRMGVPVTIVVLNNGILGFQK--HAETVKFGTHTDACHFAAV 517

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1539990514 175 DYPfnPVSLALGAEATFVGRALDsdrkgLSEVLRGAAQHRGAALVEIMQD 224
Cdd:PRK06112  518 DHA--AIARACGCDGVRVEDPAE-----LAQALAAAMAAPGPTLIEVITD 560
 
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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