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Conserved domains on  [gi|1826610546|gb|QIQ33185|]
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2-oxoacid:ferredoxin oxidoreductase subunit beta [Parageobacillus toebii NBRC 107807]

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
 1-283 0e+00

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


:

Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 517.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   1 MATFKDFRNDVKPNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMA 80
Cdd:PRK11867    5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  81 NRDLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALS 160
Cdd:PRK11867   85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 161 AGATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEIEGYDPSDRTMAMQTVMKYK 240
Cdd:PRK11867  165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1826610546 241 GLVTGLIYQNkEQKSYQELLHGYSETPLTEADLQLSKEKFDEL 283
Cdd:PRK11867  245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-283 0e+00

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 517.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   1 MATFKDFRNDVKPNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMA 80
Cdd:PRK11867    5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  81 NRDLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALS 160
Cdd:PRK11867   85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 161 AGATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEIEGYDPSDRTMAMQTVMKYK 240
Cdd:PRK11867  165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1826610546 241 GLVTGLIYQNkEQKSYQELLHGYSETPLTEADLQLSKEKFDEL 283
Cdd:PRK11867  245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 3-260 1.99e-123

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: 352.91  E-value: 1.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   3 TFKDFRNDVKPNWCPGCGDFSVQAAIQRAAANVgLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANR 82
Cdd:COG1013     3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  83 DLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAG 162
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 163 ATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVN---TYDWFKENLVKVSEIegydpsDRTMAMQTVMKY 239
Cdd:COG1013   162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYEY------DPGEKLRLTYEP 235

                         250       260
                  ....*....|....*....|..
gi 1826610546 240 KG-LVTGLIYQNkeQKSYQELL 260
Cdd:COG1013   236 KDkIPVGEFLKN--QGRFEELI 255
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 15-202 6.66e-122

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: 346.43  E-value: 6.66e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  15 WCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGDGD 94
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  95 GFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSSDL 174
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1826610546 175 KELTSLIEEGIKHKGFSLINVFSPCVTY 202
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 13-286 1.62e-119

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: 344.05  E-value: 1.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  13 PNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGD 92
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  93 GDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSS 172
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 173 DLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEiEGYDPSDRT---------MAMQTVMKYKG-L 242
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDE-EGYDPIVREpeefeekaaAAIKKAMEWGDrI 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1826610546 243 VTGLIYQNKEQKSYQE----LLHGYSETPLTEADLQLSKEKFDELISE 286
Cdd:TIGR02177 240 PIGIFYKNENKPTFEErlekILPRYMSAPPAEQEIKPPIEKPKELLEE 287
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
13-287 6.58e-98

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 289.53  E-value: 6.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  13 PNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGD 92
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  93 GDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSS 172
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 173 DLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEIEGYDPSDRT---------MAMQTVMKY-KGL 242
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDPVVRSpeeadekmaKAIEKALEWgDRI 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1826610546 243 VTGLIYQNKEQKSYQELLH----GYSETPLTEADLQLSKE---KFDELISEF 287
Cdd:NF041171  243 PIGIFYQNELVPTFEERIAerlpNYLDNPPAKQPIEKDGKpvtIIEDIFKEK 294
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
47-195 1.81e-41

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 140.41  E-value: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  47 GIGCSGRIS---------GYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGDGDGFAIGMgHTIHAIRRNIDITYIV 117
Cdd:pfam02775   1 DIGCHQMWAaqyyrfrppRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1826610546 118 MDNQIYGLTKGQTSPRsdvGFKTKSTPQGSVEPALSIMEIALSAGATFVaqsFSSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:pfam02775  80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPALIDV 151
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-283 0e+00

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 517.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   1 MATFKDFRNDVKPNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMA 80
Cdd:PRK11867    5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  81 NRDLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALS 160
Cdd:PRK11867   85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 161 AGATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEIEGYDPSDRTMAMQTVMKYK 240
Cdd:PRK11867  165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1826610546 241 GLVTGLIYQNkEQKSYQELLHGYSETPLTEADLQLSKEKFDEL 283
Cdd:PRK11867  245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 4-288 2.09e-140

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 397.33  E-value: 2.09e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   4 FKDFRNDVKPN-WCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANR 82
Cdd:PRK05778    8 LTYLRYDGLPTtWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  83 DLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAG 162
Cdd:PRK05778   88 DLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 163 ATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYD--------WFKENLVKVSEIEGYDPSDRTMAMQ 234
Cdd:PRK05778  168 ATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTkspaymreYYKKRVYKLKLEEDYDPTDRDKAAE 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1826610546 235 TVMKYKG---LVTGLIYQNkEQKSYQELLHGYSETPLTEADLQLSKEKfdELISEFM 288
Cdd:PRK05778  248 KMLEEELggkIPIGVFYKN-ERPTFEERLEKLIEPLLELPPAALRPGK--EALDTIN 301
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 3-260 1.99e-123

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: 352.91  E-value: 1.99e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   3 TFKDFRNDVKPNWCPGCGDFSVQAAIQRAAANVgLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANR 82
Cdd:COG1013     3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  83 DLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAG 162
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 163 ATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVN---TYDWFKENLVKVSEIegydpsDRTMAMQTVMKY 239
Cdd:COG1013   162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYEY------DPGEKLRLTYEP 235

                         250       260
                  ....*....|....*....|..
gi 1826610546 240 KG-LVTGLIYQNkeQKSYQELL 260
Cdd:COG1013   236 KDkIPVGEFLKN--QGRFEELI 255
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 15-202 6.66e-122

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: 346.43  E-value: 6.66e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  15 WCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGDGD 94
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  95 GFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSSDL 174
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1826610546 175 KELTSLIEEGIKHKGFSLINVFSPCVTY 202
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 13-286 1.62e-119

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: 344.05  E-value: 1.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  13 PNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGD 92
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  93 GDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSS 172
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 173 DLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEiEGYDPSDRT---------MAMQTVMKYKG-L 242
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDE-EGYDPIVREpeefeekaaAAIKKAMEWGDrI 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1826610546 243 VTGLIYQNKEQKSYQE----LLHGYSETPLTEADLQLSKEKFDELISE 286
Cdd:TIGR02177 240 PIGIFYKNENKPTFEErlekILPRYMSAPPAEQEIKPPIEKPKELLEE 287
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 7-287 2.37e-117

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 338.27  E-value: 2.37e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   7 FRNDVKPNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTV 86
Cdd:PRK11866    1 YAVKRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  87 IAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFV 166
Cdd:PRK11866   81 IGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 167 AQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEiEGYDPSDRTMAMQTVMKYKGLV-TG 245
Cdd:PRK11866  161 ARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLEE-TGHDPTNFEQAYKKALEWGDRIpIG 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1826610546 246 LIYQnKEQKSYQELL-HGYSETPLTEADLQlskEKFDELISEF 287
Cdd:PRK11866  240 VFYK-EEKPTYEEELdEILKNPPLADQPLQ---PKPEKDLEEF 278
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
13-287 6.58e-98

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 289.53  E-value: 6.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  13 PNWCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGD 92
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  93 GDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSS 172
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 173 DLKELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENLVKVSEIEGYDPSDRT---------MAMQTVMKY-KGL 242
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDPVVRSpeeadekmaKAIEKALEWgDRI 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1826610546 243 VTGLIYQNKEQKSYQELLH----GYSETPLTEADLQLSKE---KFDELISEF 287
Cdd:NF041171  243 PIGIFYQNELVPTFEERIAerlpNYLDNPPAKQPIEKDGKpvtIIEDIFKEK 294
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 15-284 1.95e-96

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 285.14  E-value: 1.95e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  15 WCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGDGD 94
Cdd:PRK11869   10 WCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  95 GFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSSDL 174
Cdd:PRK11869   90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVARTFSGDI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 175 KELTSLIEEGIKHKGFSLINVFSPCVTYNKVNTYDWFKENlvkVSEIEGYDPSDRTMAMQTVMKYKGLVTGLIYQNkEQK 254
Cdd:PRK11869  170 EETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYREN---TYYLKDHDPTDRELAFKRALETEKLPLGIFYIN-EKP 245

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1826610546 255 SYQELLHGY--SETPLTEADLQLskEKFDELI 284
Cdd:PRK11869  246 TFEELVPAYkgDKTPLWKREPNF--EKLKELI 275
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
8-258 4.95e-68

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 212.67  E-value: 4.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546   8 RNDVKPN-WCPGCGDFSVQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGFHGTHGRALPLAQGVKMANRDLTV 86
Cdd:PRK09628   10 RVDKMPTlWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  87 IAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFV 166
Cdd:PRK09628   90 IVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 167 AQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVT----YNK----VNTYDWFKENLVKVSEIEGYDPSDRtmamqtVMK 238
Cdd:PRK09628  170 ARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHInlgrKNKmgeaVQMLKWIESRTVSKRKFDALSPEER------VGK 243

                         250       260
                  ....*....|....*....|
gi 1826610546 239 YKglvTGLIYQNKEQKSYQE 258
Cdd:PRK09628  244 FP---TGILKHDTDRKEYCE 260
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
47-195 1.81e-41

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 140.41  E-value: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  47 GIGCSGRIS---------GYIHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGDGDGFAIGMgHTIHAIRRNIDITYIV 117
Cdd:pfam02775   1 DIGCHQMWAaqyyrfrppRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1826610546 118 MDNQIYGLTKGQTSPRsdvGFKTKSTPQGSVEPALSIMEIALSAGATFVaqsFSSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:pfam02775  80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPALIDV 151
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 16-207 4.62e-25

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: 99.87  E-value: 4.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  16 CPGCGdfsvQAAIQRAAANVGLEPHQLAVISGIGCSGRISGYIHSYGF-----HGTHGRALPLAQGVKMA-------NRD 83
Cdd:cd02018     8 CAGCG----EVTAVRVVLAALPAPEDTVIANSTGCSSVYASTAPFNSWavpwvNSLFEDANAVASGLKRGlkarfpkDRE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  84 L----TVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALSIMEIAL 159
Cdd:cd02018    84 LdkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1826610546 160 SAGATFVAQSFSSDLKELTSLIEEGI-KHKGFSLINVFSPCVTYNKVNT 207
Cdd:cd02018   164 THGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITEWGIGS 212
PFO_beta_C pfam12367
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ...
 199-260 1.73e-23

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: 90.63  E-value: 1.73e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826610546 199 CVTYNKVNTYDWFKENLVKVSEIegYDPSDRTMAMQTVMKYK-GLVTGLIYQnKEQKSYQELL 260
Cdd:pfam12367   1 CVTFNKVNTYDWYKERVYKLDED--HDPTDREAAMEKALEWGdRIPIGIFYK-EERPTFEERL 60
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 16-201 7.43e-18

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: 80.36  E-value: 7.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  16 CPGCGDFSVQAAIQRAAAnvglepHQLAVISGIGCSGRISG----------YIHSyGFHGTHGRALPLAQGVKM--ANRD 83
Cdd:cd03376     8 CAGCGAALALRHVLKALG------PDTVVVNPTGCLEVITTpypytawrvpWIHV-AFENAAAVASGIEAALKAlgRGKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  84 LTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSV-----EPALSIMEIA 158
Cdd:cd03376    81 ITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVsfgkkQPKKDLPLIM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1826610546 159 LSAGATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVT 201
Cdd:cd03376   161 AAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPT 203
PRK11865 PRK11865
pyruvate synthase subunit beta;
16-201 6.89e-17

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 78.99  E-value: 6.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  16 CPGCG-DFSVQAAIQRAAANVglephqlAVISGIGCSGRISG----------YIHsYGFHGTHGRALPLAQGVKMANRDL 84
Cdd:PRK11865   21 CAGCGaAIAMRLALKALGKNT-------VIVVATGCLEVITTpypetawnvpWIH-VAFENAAAVASGIERAVKALGKKV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  85 TVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSV-----EPALSIMEIAL 159
Cdd:PRK11865   93 NVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgedRPKKNMPLIMA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1826610546 160 SAGATFVAQSFSSDLKELTSLIEEGIKHKGFSLINVFSPCVT 201
Cdd:PRK11865  173 AHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPT 214
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 56-195 1.53e-16

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: 75.37  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  56 GYIHSYGFhGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRsd 135
Cdd:cd00568    38 RFLTSTGF-GAMGYGLPAAIGAALAAPDRPVVCIAGDG-GFMMTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAF-- 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 136 vgfkTKSTPQGSVEPALSIMEIALSAGATFVAqsfSSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:cd00568   114 ----YGGRVSGTDLSNPDFAALAEAYGAKGVR---VEDPEDLEAALAEALAAGGPALIEV 166
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 68-195 2.11e-13

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: 66.85  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  68 GRALPLAQGVKMANRDLTVIAAGGDGDG-FAIgmgHTI-HAIRRNIDITYIVMDNQIYGLTK------GQTSPRSDVGFk 139
Cdd:cd02002    52 GWGLPAAVGAALANPDRKVVAIIGDGSFmYTI---QALwTAARYGLPVTVVILNNRGYGALRsflkrvGPEGPGENAPD- 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1826610546 140 tkstPQGSVEPALSIMEIALSAG--ATFVaqsfsSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:cd02002   128 ----GLDLLDPGIDFAAIAKAFGveAERV-----ETPEELDEALREALAEGGPALIEV 176
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 13-199 6.27e-12

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: 62.68  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  13 PNWCPGCGDFSVQAAIQRAAANvglephQLAVISGIGCSGRisGYIHsyGFHGTH-----GRALPLAQGVKMANRDLTVI 87
Cdd:cd02008     4 PGLCPGCPHRPSFYALRKAFKK------DSIVSGDIGCYTL--GALP--PLNAIDtctcmGASIGVAIGMAKASEDKKVV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  88 AAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKStpqgsvePALSIMEIALSAGATFVA 167
Cdd:cd02008    74 AVIGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPT-------TVIDIEALVRAIGVKRVV 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1826610546 168 QSFSSDLKELTSLIEEGIKHKGFSLINVFSPC 199
Cdd:cd02008   147 VVDPYDLKAIREELKEALAVPGVSVIIAKRPC 178
PRK06163 PRK06163
hypothetical protein; Provisional
 40-195 9.94e-09

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 54.07  E-value: 9.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  40 HQLAVISGIG-------CSGRISgyiHSYGFHGTHGRALPLAQGVKMANRDLTVIAAGGDGDGF-AIGMGHTIhAIRRNI 111
Cdd:PRK06163   28 DEEAVIGGIGntnfdlwAAGQRP---QNFYMLGSMGLAFPIALGVALAQPKRRVIALEGDGSLLmQLGALGTI-AALAPK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546 112 DITYIVMDNQIYGLTKGQTSPRSDVgfktkstpqgsvepalsIMEIALSAGATFVAQSFSSDLKELTSLIEEGIKHKGFS 191
Cdd:PRK06163  104 NLTIIVMDNGVYQITGGQPTLTSQT-----------------VDVVAIARGAGLENSHWAADEAHFEALVDQALSGPGPS 166


                  ....
gi 1826610546 192 LINV 195
Cdd:PRK06163  167 FIAV 170
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 57-124 1.16e-08

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: 55.55  E-value: 1.16e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  57 YIHSYGFhGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMG--HTihAIRRNIDITYIVMDNQIYG 124
Cdd:COG0028   405 FLTSGGL-GTMGYGLPAAIGAKLARPDRPVVAITGDG-GFQMNLQelAT--AVRYGLPVKVVVLNNGGLG 470
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
74-201 3.79e-08

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 53.56  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  74 AQGVKmanrDLTVIAAGGDGDGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKGQTSPRSDVGFKTKSTPQGSVEPALS 153
Cdd:PRK11864   87 ARGEK----GVIVVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKP 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1826610546 154 IMEIALSAGATFVA-------QSFSSDLKELTSLieegikhKGFSLINVFSPCVT 201
Cdd:PRK11864  163 VPDIMAAHKVPYVAtasiaypEDFIRKLKKAKEI-------RGFKFIHLLAPCPP 210
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 90-200 4.11e-08

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: 53.76  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  90 GGDGDGFAIGMG---HTIhAIRRNIDItyIVMDNQIYGLTKGQTSprsdvgfktKSTPQGSVEP-ALS--------IMEI 157
Cdd:cd03377   158 GGDGWAYDIGYGgldHVL-ASGENVNI--LVLDTEVYSNTGGQAS---------KATPLGAVAKfAAAgkrtgkkdLGMI 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1826610546 158 ALSAGATFVAQ-SFSSDLKELTSLIEEGIKHKGFSLINVFSPCV 200
Cdd:cd03377   226 AMSYGNVYVAQiALGANDNQTLKAFREAEAYDGPSLIIAYSPCI 269
PRK08266 PRK08266
hypothetical protein; Provisional
 62-124 3.09e-07

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 51.17  E-value: 3.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826610546  62 GFHGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYG 124
Cdd:PRK08266  399 GYQGTLGYGFPTALGAKVANPDRPVVSITGDG-GFMFGVQELATAVQHNIGVVTVVFNNNAYG 460
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
68-195 1.63e-06

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 49.23  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  68 GRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAI--RRNIDITYIVMDNQIYGLTKGQT--------SPRSDvg 137
Cdd:PRK08327  433 GWALGAALGAKLATPDRLVIATVGDG-SFIFGVPEAAHWVaeRYGLPVLVVVFNNGGWLAVKEAVlevypegyAARKG-- 509

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1826610546 138 fktkSTPQGSVEPALSIMEIALSAGATFVAQSFSSDLKE-LTSLIEEGIKHKGFSLINV 195
Cdd:PRK08327  510 ----TFPGTDFDPRPDFAKIAEAFGGYGERVEDPEELKGaLRRALAAVRKGRRSAVLDV 564
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
58-128 2.19e-06

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 48.83  E-value: 2.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1826610546  58 IHSYGfhGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKG 128
Cdd:PRK07064  400 VHALG--GGIGQGLAMAIGAALAGPGRKTVGLVGDG-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
 62-127 3.04e-06

Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.


Pssm-ID: 238972 [Multi-domain]  Cd Length: 178  Bit Score: 46.37  E-value: 3.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1826610546  62 GFHGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:cd02014    48 GLLATMGNGLPGAIAAKLAYPDRQVIALSGDG-GFAMLMGDLITAVKYNLPVIVVVFNNSDLGFIK 112
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 58-125 4.91e-06

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: 45.95  E-value: 4.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1826610546  58 IHSYGfHGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFaiGMghTIH----AIRRNIDITYIVMDNQIYGL 125
Cdd:cd02015    44 LTSGG-LGTMGFGLPAAIGAKVARPDKTVICIDGDG-SF--QM--NIQelatAAQYNLPVKIVILNNGSLGM 109
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
 65-163 6.59e-06

Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.


Pssm-ID: 238971 [Multi-domain]  Cd Length: 196  Bit Score: 45.96  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  65 GTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTKgqtspRSDVGFKTKSTP 144
Cdd:cd02013    53 GNCGYALPAIIGAKAAAPDRPVVAIAGDG-AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK-----KNQVDFYNNRFV 126

                          90
                  ....*....|....*....
gi 1826610546 145 QGSVEPaLSIMEIALSAGA 163
Cdd:cd02013   127 GTELES-ESFAKIAEACGA 144
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 26-136 4.92e-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: 43.05  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  26 AAIQRAAANVGLEphqlAVISGIGCSGRISGYI--HSYGFH--GTHGRALPLAQGVKMAnRDLTVIAAGGDGdGFAIGMG 101
Cdd:cd03372     3 DAIKTLIADLKDE----LVVSNIGFPSKELYAAgdRPLNFYmlGSMGLASSIGLGLALA-QPRKVIVIDGDG-SLLMNLG 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1826610546 102 H--TIHAIR-RNIDItyIVMDNQIYGLTKGQTSPRSDV 136
Cdd:cd03372    77 AlaTIAAEKpKNLII--VVLDNGAYGSTGNQPTHAGKK 112
PRK06546 PRK06546
pyruvate dehydrogenase; Provisional
 64-195 4.97e-05

pyruvate dehydrogenase; Provisional


Pssm-ID: 180614 [Multi-domain]  Cd Length: 578  Bit Score: 44.59  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  64 HGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK------GQTSPRSDVg 137
Cdd:PRK06546  407 HGSMANALPHAIGAQLADPGRQVISMSGDG-GLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKlemlvdGLPDFGTDH- 484

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1826610546 138 fktkstpqgsvePALSIMEIALSAGATFVAqsfSSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:PRK06546  485 ------------PPVDYAAIAAALGIHAVR---VEDPKDVRGALREAFAHPGPALVDV 527
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
 65-127 1.02e-04

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 43.45  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826610546  65 GTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:PRK07525  435 GNCGYAFPAIIGAKIACPDRPVVGFAGDG-AWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEK 496
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 68-127 1.22e-04

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 43.21  E-value: 1.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  68 GRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:PRK06112  440 GWGVPMAIGAKVARPGAPVICLVGDG-GFAHVWAELETARRMGVPVTIVVLNNGILGFQK 498
PRK12474 PRK12474
hypothetical protein; Provisional
 65-193 2.24e-04

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 42.55  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  65 GTHGRALPLAQGVKMANRDLTVIAAGGDGDGFAIGMGHTIHAiRRNIDITYIVMDNQIYGLTKGQTsprSDVGFKTKSTP 144
Cdd:PRK12474  389 GSIGQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMA-RENLDVTVVIFANRSYAILNGEL---QRVGAQGAGRN 464

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1826610546 145 QGSV----EPALSIMEIALSAGatfVAQSFSSDLKELTSLIEEGIKHKGFSLI 193
Cdd:PRK12474  465 ALSMldlhNPELNWMKIAEGLG---VEASRATTAEEFSAQYAAAMAQRGPRLI 514
PRK09124 PRK09124
ubiquinone-dependent pyruvate dehydrogenase;
64-124 2.42e-04

ubiquinone-dependent pyruvate dehydrogenase;


Pssm-ID: 181661 [Multi-domain]  Cd Length: 574  Bit Score: 42.28  E-value: 2.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1826610546  64 HGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYG 124
Cdd:PRK09124  407 HGSMANAMPQALGAQAAHPGRQVVALSGDG-GFSMLMGDFLSLVQLKLPVKIVVFNNSVLG 466
PRK08979 PRK08979
acetolactate synthase 3 large subunit;
57-127 1.00e-03

acetolactate synthase 3 large subunit;


Pssm-ID: 181602 [Multi-domain]  Cd Length: 572  Bit Score: 40.57  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826610546  57 YIHSYGFhGTHGRALPLAQGVKMANRDLTVIAAGGDGdgfAIGMG--HTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:PRK08979  414 WINSGGL-GTMGFGLPAAMGVKFAMPDETVVCVTGDG---SIQMNiqELSTALQYDIPVKIINLNNRFLGMVK 482
PRK06154 PRK06154
thiamine pyrophosphate-requiring protein;
68-120 1.20e-03

thiamine pyrophosphate-requiring protein;


Pssm-ID: 235718 [Multi-domain]  Cd Length: 565  Bit Score: 40.18  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1826610546  68 GRALPLAQGVKMANRDLTVIAAGGDGdgfAIGM-GHTIH-AIRRNIDITYIVMDN 120
Cdd:PRK06154  434 GYGLGLAMGAKLARPDALVINLWGDA---AFGMtGMDFEtAVRERIPILTILLNN 485
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
 54-195 1.30e-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: 39.21  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  54 ISGYIHSYGFhGTHGRALPLAQGVKMANRDLTVIAAGGDGDGFaigMGHT--IHAIRRNIDITYIVMDNQIYG----LTK 127
Cdd:cd02003    38 PGGYHLEYGY-SCMGYEIAAGLGAKLAKPDREVYVLVGDGSYL---MLHSeiVTAVQEGLKIIIVLFDNHGFGcinnLQE 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1826610546 128 GQTSPRSDVGFKTKSTPQGSVEPALSIMEIALSAGATFVAQSFSSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:cd02003   114 STGSGSFGTEFRDRDQESGQLDGALLPVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVI 181
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
 64-127 1.31e-03

Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.


Pssm-ID: 238968 [Multi-domain]  Cd Length: 177  Bit Score: 38.81  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1826610546  64 HGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:cd02010    47 LATMGVALPGAIGAKLVYPDRKVVAVSGDG-GFMMNSQELETAVRLKIPLVVLIWNDNGYGLIK 109
PRK08611 PRK08611
pyruvate oxidase; Provisional
 65-127 1.37e-03

pyruvate oxidase; Provisional


Pssm-ID: 181502 [Multi-domain]  Cd Length: 576  Bit Score: 39.98  E-value: 1.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826610546  65 GTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:PRK08611  408 GTMGCGLPGAIAAKIAFPDRQAIAICGDG-GFSMVMQDFVTAVKYKLPIVVVVLNNQQLAFIK 469
PRK08978 PRK08978
acetolactate synthase 2 catalytic subunit; Reviewed
 57-127 2.39e-03

acetolactate synthase 2 catalytic subunit; Reviewed


Pssm-ID: 181601 [Multi-domain]  Cd Length: 548  Bit Score: 39.09  E-value: 2.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1826610546  57 YIHSYGFhGTHGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGH--TIHaiRRNIDITYIVMDNQIYGLTK 127
Cdd:PRK08978  394 FITSSGL-GTMGFGLPAAIGAQVARPDDTVICVSGDG-SFMMNVQElgTIK--RKQLPVKIVLLDNQRLGMVR 462
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
 68-195 3.17e-03

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 38.78  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1826610546  68 GRALPLAQGVKMANRDLTVIAAGGDGDG-FAIGMGHTihAIRRNIDITYIVMDNQIYGLTK--GQTsprsdvgFKTKSTP 144
Cdd:PRK07092  410 GYGLPAAVGVALAQPGRRVIGLIGDGSAmYSIQALWS--AAQLKLPVTFVILNNGRYGALRwfAPV-------FGVRDVP 480

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1826610546 145 qGSVEPALSIMEIALSAGATFVAqsfSSDLKELTSLIEEGIKHKGFSLINV 195
Cdd:PRK07092  481 -GLDLPGLDFVALARGYGCEAVR---VSDAAELADALARALAADGPVLVEV 527
PRK08322 PRK08322
acetolactate synthase large subunit;
66-127 7.77e-03

acetolactate synthase large subunit;


Pssm-ID: 236239 [Multi-domain]  Cd Length: 547  Bit Score: 37.50  E-value: 7.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1826610546  66 THGRALPLAQGVKMANRDLTVIAAGGDGdGFAIGMGHTIHAIRRNIDITYIVMDNQIYGLTK 127
Cdd:PRK08322  407 TMGAGLPSAIAAKLVHPDRKVLAVCGDG-GFMMNSQELETAVRLGLPLVVLILNDNAYGMIR 467
 
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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