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Conserved domains on  [gi|308825554|emb|CBH21592|]
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2-oxoglutarate synthase subunit korB (2-ketoglutarate oxidoreductase beta chain) (KOR) (2-oxoglutarate-ferredoxin oxidoreductase subunit beta) [Acetoanaerobium sticklandii]

Protein Classification

2-oxoacid:ferredoxin oxidoreductase subunit beta( domain architecture ID 11481655)

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
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 1-266 2.86e-140

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


:

Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 396.17  E-value: 2.86e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   1 MRTDRLPHIWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLH 80
Cdd:PRK05778  11 LRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK05778  91 VIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 161 VARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKNKKGGAVDLLNHLKDTFVDIKV------------KDKLS 228
Cdd:PRK05778 171 VARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTKSPAYMREYYKKRVYKLKLeedydptdrdkaAEKML 250

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 308825554 229 PEKLENKMFMGEFHNSVEPEYTAEYDKIIELFSTGGEE 266
Cdd:PRK05778 251 EEELGGKIPIGVFYKNERPTFEERLEKLIEPLLELPPA 288
 
Name Accession Description Interval E-value
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 1-266 2.86e-140

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 396.17  E-value: 2.86e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   1 MRTDRLPHIWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLH 80
Cdd:PRK05778  11 LRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK05778  91 VIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 161 VARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKNKKGGAVDLLNHLKDTFVDIKV------------KDKLS 228
Cdd:PRK05778 171 VARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTKSPAYMREYYKKRVYKLKLeedydptdrdkaAEKML 250

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 308825554 229 PEKLENKMFMGEFHNSVEPEYTAEYDKIIELFSTGGEE 266
Cdd:PRK05778 251 EEELGGKIPIGVFYKNERPTFEERLEKLIEPLLELPPA 288
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 6-258 2.25e-119

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: 341.74  E-value: 2.25e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   6 LPHIWCPGCGHGILMRAIAVAIEDLkLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVT 85
Cdd:COG1013   11 PGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVFG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  86 GDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARST 165
Cdd:COG1013   90 GDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVARAS 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 166 AYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKnkkggAVDLLNHLKDTFVDIKVKDKLSPEKL----ENKMFMGEF 241
Cdd:COG1013  170 VGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRD-----PSKTIEWAKEGMWPLYEYDPGEKLRLtyepKDKIPVGEF 244

                        250
                 ....*....|....*..
gi 308825554 242 HNsVEPEYTAEYDKIIE 258
Cdd:COG1013  245 LK-NQGRFEELIEEIQK 260
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 10-197 2.49e-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: 333.72  E-value: 2.49e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  10 WCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVTGDGD 89
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  90 ASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARSTAYHA 169
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                        170       180
                 ....*....|....*....|....*...
gi 308825554 170 NKMIEYIKTGINHKGFSLIEGISSCPTY 197
Cdd:cd03375  161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 9-237 1.72e-79

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: 241.59  E-value: 1.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554    9 IWCPGCG-HGILmRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVTGD 87
Cdd:TIGR02177   2 DWCPGCGdFGIL-SALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   88 GDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARSTAY 167
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  168 HANKMIEYIKTGINHKGFSLIEGISSCPTyYGRKNKKGGAVDLLNHLKDTFVDIKVKDklsPEKLENKMF 237
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVT-YNKINTYEWYRERVYKLDEEGYDPIVRE---PEEFEEKAA 226
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
10-197 7.71e-75

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 229.82  E-value: 7.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  10 WCPGCGH-GILmRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVTGDG 88
Cdd:NF041171   5 WCPGCGNfGIL-TAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  89 DASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARSTAYH 168
Cdd:NF041171  84 DLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYD 163

                        170       180
                 ....*....|....*....|....*....
gi 308825554 169 ANKMIEYIKTGINHKGFSLIEGISSCPTY 197
Cdd:NF041171 164 VKHLKELIKAAIKHKGLAFIDVLQPCPTY 192
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
42-189 2.06e-41

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 139.26  E-value: 2.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   42 GIGCSSR-ASGYMDFN--------TLHTTHGRALAFATGVKFANPDLHVIVVTGDGDASAIGgNHLIHACRRNIDITTIV 112
Cdd:pfam02775   1 DIGCHQMwAAQYYRFRpprryltsGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308825554  113 FNNNIYGMTGGQfspTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATyVARSTAYhaNKMIEYIKTGINHKGFSLIE 189
Cdd:pfam02775  80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARVESP--EELEEALKEALEHDGPALID 150
 
Name Accession Description Interval E-value
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 1-266 2.86e-140

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 396.17  E-value: 2.86e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   1 MRTDRLPHIWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLH 80
Cdd:PRK05778  11 LRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK05778  91 VIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 161 VARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKNKKGGAVDLLNHLKDTFVDIKV------------KDKLS 228
Cdd:PRK05778 171 VARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTKSPAYMREYYKKRVYKLKLeedydptdrdkaAEKML 250

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 308825554 229 PEKLENKMFMGEFHNSVEPEYTAEYDKIIELFSTGGEE 266
Cdd:PRK05778 251 EEELGGKIPIGVFYKNERPTFEERLEKLIEPLLELPPA 288
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 2-258 1.70e-138

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 391.13  E-value: 1.70e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   2 RTDRLPHiWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHV 81
Cdd:PRK11867  12 RNDQEPR-WCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLANPDLTV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  82 IVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYV 161
Cdd:PRK11867  91 IVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALGAGATFV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 162 ARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYgrknkkggAVDLLNHLKDTFVDIKVKDKLSPEKLENKMFMGEF 241
Cdd:PRK11867 171 ARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFN--------NVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEE 242

                        250       260
                 ....*....|....*....|....*.
gi 308825554 242 HNSV---------EPEYTAEYDKIIE 258
Cdd:PRK11867 243 GDPIptgifyqveRPTYEEAVRAQIE 268
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 6-258 2.25e-119

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: 341.74  E-value: 2.25e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   6 LPHIWCPGCGHGILMRAIAVAIEDLkLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVT 85
Cdd:COG1013   11 PGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVFG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  86 GDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARST 165
Cdd:COG1013   90 GDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVARAS 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 166 AYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKnkkggAVDLLNHLKDTFVDIKVKDKLSPEKL----ENKMFMGEF 241
Cdd:COG1013  170 VGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRD-----PSKTIEWAKEGMWPLYEYDPGEKLRLtyepKDKIPVGEF 244

                        250
                 ....*....|....*..
gi 308825554 242 HNsVEPEYTAEYDKIIE 258
Cdd:COG1013  245 LK-NQGRFEELIEEIQK 260
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 10-197 2.49e-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: 333.72  E-value: 2.49e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  10 WCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVTGDGD 89
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  90 ASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARSTAYHA 169
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                        170       180
                 ....*....|....*....|....*...
gi 308825554 170 NKMIEYIKTGINHKGFSLIEGISSCPTY 197
Cdd:cd03375  161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
1-258 8.51e-109

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 315.52  E-value: 8.51e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   1 MRTDRLPHIWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLH 80
Cdd:PRK09628   9 LRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK09628  89 VIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASF 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 161 VARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKNKKGGAVDLLNHLKDTFVDIKVKDKLSPEKLENKMFMGE 240
Cdd:PRK09628 169 VARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKNKMGEAVQMLKWIESRTVSKRKFDALSPEERVGKFPTGI 248

                        250
                 ....*....|....*....
gi 308825554 241 FHNSVEP-EYTAEYDKIIE 258
Cdd:PRK09628 249 LKHDTDRkEYCEAYEEVIE 267
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 9-237 1.72e-79

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: 241.59  E-value: 1.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554    9 IWCPGCG-HGILmRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVTGD 87
Cdd:TIGR02177   2 DWCPGCGdFGIL-SALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   88 GDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARSTAY 167
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  168 HANKMIEYIKTGINHKGFSLIEGISSCPTyYGRKNKKGGAVDLLNHLKDTFVDIKVKDklsPEKLENKMF 237
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVT-YNKINTYEWYRERVYKLDEEGYDPIVRE---PEEFEEKAA 226
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 1-197 9.80e-77

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 234.27  E-value: 9.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   1 MRTDRLPhIWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLH 80
Cdd:PRK11866   1 YAVKRPP-IWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK11866  80 VIGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATF 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 308825554 161 VARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTY 197
Cdd:PRK11866 160 VARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTF 196
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
10-197 7.71e-75

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 229.82  E-value: 7.71e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  10 WCPGCGH-GILmRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLHVIVVTGDG 88
Cdd:NF041171   5 WCPGCGNfGIL-TAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  89 DASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATYVARSTAYH 168
Cdd:NF041171  84 DLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYD 163

                        170       180
                 ....*....|....*....|....*....
gi 308825554 169 ANKMIEYIKTGINHKGFSLIEGISSCPTY 197
Cdd:NF041171 164 VKHLKELIKAAIKHKGLAFIDVLQPCPTY 192
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 1-197 2.78e-63

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 199.62  E-value: 2.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   1 MRTDRLPHIWCPGCGHGILMRAIAVAIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLHTTHGRALAFATGVKFANPDLH 80
Cdd:PRK11869   1 MRPEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK11869  81 VIAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 308825554 161 VARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTY 197
Cdd:PRK11869 161 VARTFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSF 197
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
42-189 2.06e-41

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 139.26  E-value: 2.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   42 GIGCSSR-ASGYMDFN--------TLHTTHGRALAFATGVKFANPDLHVIVVTGDGDASAIGgNHLIHACRRNIDITTIV 112
Cdd:pfam02775   1 DIGCHQMwAAQYYRFRpprryltsGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308825554  113 FNNNIYGMTGGQfspTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATyVARSTAYhaNKMIEYIKTGINHKGFSLIE 189
Cdd:pfam02775  80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARVESP--EELEEALKEALEHDGPALID 150
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 8-205 2.16e-22

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


Pssm-ID: 238976 [Multi-domain]  Cd Length: 237  Bit Score: 92.16  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   8 HIWCPGCGHGILMRAIAVAiedLKLDKDKVcIVSGIGCSSRASGYMDFN-----TLHTTHGRALAFATGVK--------- 73
Cdd:cd02018    5 HGACAGCGEVTAVRVVLAA---LPAPEDTV-IANSTGCSSVYASTAPFNswavpWVNSLFEDANAVASGLKrglkarfpk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  74 FANPDLH--VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICS 151
Cdd:cd02018   81 DRELDKKkdVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308825554 152 LAKGAGATYVAR-STAYhaNKMIEYIKTG--INHKGFSLIEGISSCPTYYGRKNKKG 205
Cdd:cd02018  161 IAATHGCVYVARlSPAL--KKHFLKVVKEaiSRTDGPTFIHAYTPCITEWGIGSGKS 215
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 5-195 4.45e-22

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: 90.03  E-value: 4.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   5 RLPHIwCPGCGHgilmRAIAVAIEdlKLDKDKVCIVSGIGCSSRaSGYMDFNTLHTT--HGRALAFATGVKFANPDLHVI 82
Cdd:cd02008    2 RPPGL-CPGCPH----RPSFYALR--KAFKKDSIVSGDIGCYTL-GALPPLNAIDTCtcMGASIGVAIGMAKASEDKKVV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  83 VVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTapfgnidKAFDICSLAKGAGATYVA 162
Cdd:cd02008   74 AVIGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPT-------TVIDIEALVRAIGVKRVV 146

                        170       180       190
                 ....*....|....*....|....*....|...
gi 308825554 163 RSTAYHANKMIEYIKTGINHKGFSLIegISSCP 195
Cdd:cd02008  147 VVDPYDLKAIREELKEALAVPGVSVI--IAKRP 177
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 11-196 3.36e-21

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: 89.22  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  11 CPGCGHGILMRAIAVAIEDlkldkdKVCIVSGIGCSSRASG---YMDFNT--LHTTHGRALAFATGVKFA------NPDL 79
Cdd:cd03376    8 CAGCGAALALRHVLKALGP------DTVVVNPTGCLEVITTpypYTAWRVpwIHVAFENAAAVASGIEAAlkalgrGKDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  80 HVIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAP-----FGNIDKAFDICSLAK 154
Cdd:cd03376   82 TVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPvgkvsFGKKQPKKDLPLIMA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 308825554 155 GAGATYVARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPT 196
Cdd:cd03376  162 AHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPT 203
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 37-189 2.61e-18

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 79.61  E-value: 2.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  37 VCIVSGIGCSSRASGYMDF---------NTLHTTHGRALAFATGVKFANPDLHVIVVTGDGDASAiGGNHLIHACRRNID 107
Cdd:cd00568   14 AIVVNDAGNSAYWAYRYLPlrrgrrfltSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMM-TGQELATAVRYGLP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 108 ITTIVFNNNIYGMTGGQFSPTTPKGDRGTTapFGNIdkafDICSLAKGAGATYV-ARSTAyhanKMIEYIKTGINHKGFS 186
Cdd:cd00568   93 VIVVVFNNGGYGTIRMHQEAFYGGRVSGTD--LSNP----DFAALAEAYGAKGVrVEDPE----DLEAALAEALAAGGPA 162


                 ...
gi 308825554 187 LIE 189
Cdd:cd00568  163 LIE 165
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
8-196 1.09e-17

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 80.52  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   8 HIWCPGCGHGILMRAIAVAIedlkldKDKVCIVSGIGCSSRASGYM-----DFNTLHTTHGRALAFATGVKFA----NPD 78
Cdd:PRK11864  18 NAACPGCGAPLGLRYLLKAL------GEKTVLVIPASCSTVIQGDTpksplTVPVLHTAFAATAAVASGIEEAlkarGEK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  79 LHVIVV-TGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAG 157
Cdd:PRK11864  92 GVIVVGwAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHK 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 308825554 158 ATYVARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPT 196
Cdd:PRK11864 172 VPYVATASIAYPEDFIRKLKKAKEIRGFKFIHLLAPCPP 210
PRK11865 PRK11865
pyruvate synthase subunit beta;
8-205 2.26e-17

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 79.76  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   8 HIWCPGCGHGILMRAIAVAiedlkLDKDKVcIVSGIGCSSRASGYMDFNT-----LHTTHGRALAFATGVKFA----NPD 78
Cdd:PRK11865  18 HRACAGCGAAIAMRLALKA-----LGKNTV-IVVATGCLEVITTPYPETAwnvpwIHVAFENAAAVASGIERAvkalGKK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  79 LHVIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFD-----ICSLA 153
Cdd:PRK11865  92 VNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRGEDrpkknMPLIM 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 308825554 154 KGAGATYVARSTAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKNKKG 205
Cdd:PRK11865 172 AAHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPTGWGFPPEKT 223
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 63-189 1.15e-12

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: 64.54  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGdaSAIGGNH-LIHACRRNIDITTIVFNNNIYG---MTGGQFSPTTPKGDRGttA 138
Cdd:cd02002   52 GWGLPAAVGAALANPDRKVVAIIGDG--SFMYTIQaLWTAARYGLPVTVVILNNRGYGalrSFLKRVGPEGPGENAP--D 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308825554 139 PFGNIDKAFDICSLAKGAGATYVARSTayhANKMIEYIKTGINHKGFSLIE 189
Cdd:cd02002  128 GLDLLDPGIDFAAIAKAFGVEAERVET---PEELDEALREALAEGGPALIE 175
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 18-161 6.15e-11

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: 62.10  E-value: 6.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  18 ILMRAIAVAIEDLkLDKDKVcIVSGIGCSSR-ASGYMDF---NTLHTTHGR-----ALAFATGVKFANPDLHVIVVTGDG 88
Cdd:COG0028  363 IKPQRVIAALREA-LPDDAI-VVTDVGQHQMwAARYLRFrrpRRFLTSGGLgtmgyGLPAAIGAKLARPDRPVVAITGDG 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  89 DASaIGGNHLIHACRRNIDITTIVFNNNIYGM--------TGGQFSPTTpkgdrgttapFGNIdkafDICSLAKGAGATY 160
Cdd:COG0028  441 GFQ-MNLQELATAVRYGLPVKVVVLNNGGLGMvrqwqelfYGGRYSGTD----------LPNP----DFAKLAEAFGAKG 505


                 .
gi 308825554 161 V 161
Cdd:COG0028  506 E 506
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 63-146 1.51e-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: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGDA-------SAIGG---NHLIHacrrnidittIVFNNNIYGMTGGQfsPTTpkg 132
Cdd:cd03371   51 GHASQIALGIALARPDRKVVCIDGDGAAlmhmgglATIGGlapANLIH----------IVLNNGAHDSVGGQ--PTV--- 115

                         90
                 ....*....|....
gi 308825554 133 drGTTAPFGNIDKA 146
Cdd:cd03371  116 --SFDVSLPAIAKA 127
PRK08266 PRK08266
hypothetical protein; Provisional
 50-119 2.09e-08

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 54.63  E-value: 2.09e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  50 SGYMDfntlhtTHGRALAFATGVKFANPDLHVIVVTGDGdASAIGGNHLIHACRRNIDITTIVFNNNIYG 119
Cdd:PRK08266 398 CGYQG------TLGYGFPTALGAKVANPDRPVVSITGDG-GFMFGVQELATAVQHNIGVVTVVFNNNAYG 460
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 61-147 1.54e-07

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: 49.84  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  61 THGRALAFATGVKFANPDLHVIVVTGDGdasAIG--GNHLIHACRRNIDITTIVFNNN-IYGMTGGQ---FSPTTPKGDR 134
Cdd:cd02004   49 TLGVGLGYAIAAALARPDKRVVLVEGDG---AFGfsGMELETAVRYNLPIVVVVGNNGgWYQGLDGQqlsYGLGLPVTTL 125

                         90
                 ....*....|...
gi 308825554 135 GTTAPFGNIDKAF 147
Cdd:cd02004  126 LPDTRYDLVAEAF 138
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
 59-198 4.20e-07

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: 48.82  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  59 HTTHGRALAFATGVKFANPDLHVIVVTGDGdASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSpttPKGDRGTTA 138
Cdd:cd02010   47 LATMGVALPGAIGAKLVYPDRKVVAVSGDG-GFMMNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQE---KEYGRDSGV 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554 139 PFGNIdkafDICSLAKGAGATYVARStayHANKMIEYIKTGINHKGFSLIEgissCPTYY 198
Cdd:cd02010  123 DFGNP----DFVKYAESFGAKGYRIE---SADDLLPVLERALAADGVHVID----CPVDY 171
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
 48-120 4.56e-07

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: 48.68  E-value: 4.56e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308825554  48 RASGYMDFNT--LHTTHGRALAFATGVKFANPDLHVIVVTGDGdASAIGGNHLIHACRRNIDITTIVFNNNIYGM 120
Cdd:cd02014   37 RMNGKQRFILsgLLATMGNGLPGAIAAKLAYPDRQVIALSGDG-GFAMLMGDLITAVKYNLPVIVVVFNNSDLGF 110
PRK06163 PRK06163
hypothetical protein; Provisional
 34-157 1.45e-06

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 47.52  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  34 KDKVCIVSGIGCSSR---ASGY--MDFNTLHTThGRALAFATGVKFANPDLHVIVVTGDGDASAIGGNHLIHACRRNIDI 108
Cdd:PRK06163  27 KDEEAVIGGIGNTNFdlwAAGQrpQNFYMLGSM-GLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNL 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 308825554 109 TTIVFNNNIYGMTGGQFSPTTpkgdrgttapfgnidKAFDICSLAKGAG 157
Cdd:PRK06163 106 TIIVMDNGVYQITGGQPTLTS---------------QTVDVVAIARGAG 139
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 81-194 2.20e-06

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: 48.61  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554    81 VIVVTGDGDASAIGGNHLIHACRRNIDITTIVFNNNIYGMTGGQFSPTTPKGDRGTTAPFGNIDKAFDICSLAKGAGATY 160
Cdd:TIGR02176  954 VWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVY 1033

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 308825554   161 VArSTAYHANKM--IEYIKTGINHKGFSLIEGISSC 194
Cdd:TIGR02176 1034 VA-QVSMGANMQqtLKAFREAEAYDGPSIVIAYSPC 1068
PRK06154 PRK06154
thiamine pyrophosphate-requiring protein;
60-119 3.88e-06

thiamine pyrophosphate-requiring protein;


Pssm-ID: 235718 [Multi-domain]  Cd Length: 565  Bit Score: 47.50  E-value: 3.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308825554  60 TTH-GRALAFATGVKFANPDLHVIVVTGDGdasAIG--GNHLIHACRRNIDITTIVFNNNIYG 119
Cdd:PRK06154 430 TTQlGYGLGLAMGAKLARPDALVINLWGDA---AFGmtGMDFETAVRERIPILTILLNNFSMG 489
Ppyr-DeCO2ase TIGR03297
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ...
 22-146 3.97e-06

phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).


Pssm-ID: 274508 [Multi-domain]  Cd Length: 361  Bit Score: 47.35  E-value: 3.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   22 AIAVAIEDLKldkDKVCIVSGIGCSSR-------ASGYMDFNTLHT--THGRALAFATGVKFANPDLHVIVVTGDGDA-- 90
Cdd:TIGR03297 177 AIAAILDHLP---DNTVIVSTTGKTSRelyelrdRIGQGHARDFLTvgSMGHASQIALGLALARPDQRVVCLDGDGAAlm 253

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308825554   91 -----SAIG---GNHLIHacrrnidittIVFNNNIYGMTGGQfsPTTpkgdrGTTAPFGNIDKA 146
Cdd:TIGR03297 254 hmgglATIGtqgPANLIH----------VLFNNGAHDSVGGQ--PTV-----SQHLDFAQIAKA 300
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 61-120 4.38e-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: 4.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308825554  61 THGRALAFATGVKFANPDLHVIVVTGDGdasaiG----GNHLIHACRRNIDITTIVFNNNIYGM 120
Cdd:cd02015   51 TMGFGLPAAIGAKVARPDKTVICIDGDG-----SfqmnIQELATAAQYNLPVKIVILNNGSLGM 109
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
63-160 4.79e-06

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 47.30  E-value: 4.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGdaSAIGGN----HLIhACRRNIDITTIVFNNNIYGMTGGQFSPTTPKG--DRGT 136
Cdd:PRK08327 433 GWALGAALGAKLATPDRLVIATVGDG--SFIFGVpeaaHWV-AERYGLPVLVVVFNNGGWLAVKEAVLEVYPEGyaARKG 509

                         90       100
                 ....*....|....*....|....
gi 308825554 137 TAPFGNIDKAFDICSLAKGAGATY 160
Cdd:PRK08327 510 TFPGTDFDPRPDFAKIAEAFGGYG 533
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 81-194 2.28e-05

Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.


Pssm-ID: 239472  Cd Length: 365  Bit Score: 44.90  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  81 VIVVTGDGDASAIGGNHLIH--ACRRNIDIttIVFNNNIYGMTGGQFSPTTPkgdRGTTAPF---GNIDKAFDICSLAKG 155
Cdd:cd03377  154 VWIIGGDGWAYDIGYGGLDHvlASGENVNI--LVLDTEVYSNTGGQASKATP---LGAVAKFaaaGKRTGKKDLGMIAMS 228

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 308825554 156 AGATYVArSTAYHANKM--IEYIKTGINHKGFSLIEGISSC 194
Cdd:cd03377  229 YGNVYVA-QIALGANDNqtLKAFREAEAYDGPSLIIAYSPC 268
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 63-161 2.29e-05

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 45.14  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGdasaiGGNH----LIHACRRNIDITTIVFNNNIYGMtggQFSPTTPK-GDRGTT 137
Cdd:PRK06112 440 GWGVPMAIGAKVARPGAPVICLVGDG-----GFAHvwaeLETARRMGVPVTIVVLNNGILGF---QKHAETVKfGTHTDA 511

                         90       100
                 ....*....|....*....|....
gi 308825554 138 APFGNIDKAfdicSLAKGAGATYV 161
Cdd:PRK06112 512 CHFAAVDHA----AIARACGCDGV 531
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
 63-189 2.80e-05

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 44.95  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGDAS-AIGGnhLIHACRRNIDITTIVFNNNIYGMTGGqFSPTTPKGD-RGTTAPf 140
Cdd:PRK07092 410 GYGLPAAVGVALAQPGRRVIGLIGDGSAMySIQA--LWSAAQLKLPVTFVILNNGRYGALRW-FAPVFGVRDvPGLDLP- 485

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308825554 141 gnidkAFDICSLAKGAG--ATYVARSTAYHANkmieyIKTGINHKGFSLIE 189
Cdd:PRK07092 486 -----GLDFVALARGYGceAVRVSDAAELADA-----LARALAADGPVLVE 526
PRK08322 PRK08322
acetolactate synthase large subunit;
61-120 3.77e-05

acetolactate synthase large subunit;


Pssm-ID: 236239 [Multi-domain]  Cd Length: 547  Bit Score: 44.43  E-value: 3.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308825554  61 THGRALAFATGVKFANPDLHVIVVTGDgdasaiGG---N--HLIHACRRNIDITTIVFNNNIYGM 120
Cdd:PRK08322 407 TMGAGLPSAIAAKLVHPDRKVLAVCGD------GGfmmNsqELETAVRLGLPLVVLILNDNAYGM 465
PRK06546 PRK06546
pyruvate dehydrogenase; Provisional
 58-120 5.44e-05

pyruvate dehydrogenase; Provisional


Pssm-ID: 180614 [Multi-domain]  Cd Length: 578  Bit Score: 44.21  E-value: 5.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308825554  58 LHTTHGRALAFATGVKFANPDLHVIVVTGDGDASAIGGNhLIHACRRNIDITTIVFNNNIYGM 120
Cdd:PRK06546 406 RHGSMANALPHAIGAQLADPGRQVISMSGDGGLSMLLGE-LLTVKLYDLPVKVVVFNNSTLGM 467
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 26-166 7.43e-05

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: 42.09  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  26 AIEDLKLDKDKVCIVSGIGCSSRASGYMDFNTLH----TTHGRALAFATGVKFANPDlHVIVVTGDGD----------AS 91
Cdd:cd02001    4 AIAEIIEASGDTPIVSTTGYASRELYDVQDRDGHfymlGSMGLAGSIGLGLALGLSR-KVIVVDGDGSllmnpgvlltAG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 308825554  92 AIGGNHLIHacrrnidittIVFNNNIYGMTGGQFSPTTpkgdrgttapfgnidkAFDICSLAKGAGATYVARSTA 166
Cdd:cd02001   83 EFTPLNLIL----------VVLDNRAYGSTGGQPTPSS----------------NVNLEAWAAACGYLVLSAPLL 131
PRK08979 PRK08979
acetolactate synthase 3 large subunit;
61-120 1.23e-04

acetolactate synthase 3 large subunit;


Pssm-ID: 181602 [Multi-domain]  Cd Length: 572  Bit Score: 42.89  E-value: 1.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308825554  61 THGRALAFATGVKFANPDLHVIVVTGDGdasAIGGN--HLIHACRRNIDITTIVFNNNIYGM 120
Cdd:PRK08979 422 TMGFGLPAAMGVKFAMPDETVVCVTGDG---SIQMNiqELSTALQYDIPVKIINLNNRFLGM 480
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
 63-119 1.54e-04

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 42.68  E-value: 1.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGdASAIGGNHLIHACRRNIDITTIVFNNNIYG 119
Cdd:PRK07525 438 GYAFPAIIGAKIACPDRPVVGFAGDG-AWGISMNEVMTAVRHNWPVTAVVFRNYQWG 493
PRK12474 PRK12474
hypothetical protein; Provisional
 63-191 2.08e-04

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 42.17  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGDASAIGGNHLIHAcRRNIDITTIVFNNNIYGMTGGQFSPTtpkgdrGTTAPFGN 142
Cdd:PRK12474 392 GQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMA-RENLDVTVVIFANRSYAILNGELQRV------GAQGAGRN 464

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 308825554 143 IDKAFDI-------CSLAKGAGatyVARSTAYHANKMIEYIKTGINHKGFSLIEGI 191
Cdd:PRK12474 465 ALSMLDLhnpelnwMKIAEGLG---VEASRATTAEEFSAQYAAAMAQRGPRLIEAM 517
PRK06882 PRK06882
acetolactate synthase 3 large subunit;
61-120 4.54e-04

acetolactate synthase 3 large subunit;


Pssm-ID: 168717 [Multi-domain]  Cd Length: 574  Bit Score: 41.44  E-value: 4.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308825554  61 THGRALAFATGVKFANPDLHVIVVTGDGdasAIGGN--HLIHACRRNIDITTIVFNNNIYGM 120
Cdd:PRK06882 422 TMGFGLPAAIGVKFAHPEATVVCVTGDG---SIQMNiqELSTAKQYDIPVVIVSLNNRFLGM 480
PRK07586 PRK07586
acetolactate synthase large subunit;
63-118 1.14e-03

acetolactate synthase large subunit;


Pssm-ID: 236063 [Multi-domain]  Cd Length: 514  Bit Score: 39.83  E-value: 1.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGdaSAIggnHLIHA----CRRNIDITTIVFNNNIY 118
Cdd:PRK07586 388 GQGLPLATGAAVACPDRKVLALQGDG--SAM---YTIQAlwtqARENLDVTTVIFANRAY 442
PRK13029 PRK13029
indolepyruvate ferredoxin oxidoreductase family protein;
3-210 1.81e-03

indolepyruvate ferredoxin oxidoreductase family protein;


Pssm-ID: 237278 [Multi-domain]  Cd Length: 1186  Bit Score: 39.77  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554    3 TDRLPHiWCPGCGHGILMR----AIAVAiedlkldkdkvcivsGIGCSSRASgYMDFNTLHTTH--GRALAFATGVKFAN 76
Cdd:PRK13029  450 TERKPW-FCSGCPHNTSTRvpegSRALA---------------GIGCHYMAM-WMDRSTEGFSQmgGEGVAWIGQMPFSR 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554   77 PDlHVIVVTGDGDASAIGgnHL-----IHAcrrNIDITTIVFNNNIYGMTGGQfsPttpkgdrgttapfgnIDKAFDICS 151
Cdd:PRK13029  513 RR-HVFQNLGDGTYFHSG--LLairqaIAA---GVNITYKILYNDAVAMTGGQ--P---------------VDGVLTVPQ 569

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308825554  152 LAKGAGATYVAR--------------------STAYHANKMIEYIKTGINHKGFSLIEGISSCPTYYGRKNKKGGAVDL 210
Cdd:PRK13029  570 IARQVHAEGVRRivvvtdepgkyrgvarlpagVTVHHRDELDAVQRELREVPGVSVLIYDQTCATEKRRRRKRGTYPDP 648
PRK08527 PRK08527
acetolactate synthase large subunit;
61-120 3.09e-03

acetolactate synthase large subunit;


Pssm-ID: 181458 [Multi-domain]  Cd Length: 563  Bit Score: 38.54  E-value: 3.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308825554  61 THGRALAFATGVKFANPDLHVIVVTGDGdasAIGGN--HLIHACRRNIDITTIVFNNNIYGM 120
Cdd:PRK08527 415 TMGYGLPAALGAKLAVPDKVVINFTGDG---SILMNiqELMTAVEYKIPVINIILNNNFLGM 473
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
 63-119 4.71e-03

TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 443161 [Multi-domain]  Cd Length: 545  Bit Score: 38.22  E-value: 4.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308825554  63 GRALAFATGVKFANPDLHVIVVTGDGDA-------SAIGgnhlihacRRNIDITTIVFNNNIYG 119
Cdd:COG3961  411 GYTLPAALGAALAAPDRRVILLVGDGAFqltaqelSTML--------RYGLKPIIFVLNNDGYT 466
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
 69-119 5.93e-03

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 37.93  E-value: 5.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308825554  69 ATGVKFANPDLHVIVVTGDGDAsAIGGNHLIHACRRNIDITTIVFNNNIYG 119
Cdd:PRK08199 424 AIAAKLLFPERTVVAFAGDGCF-LMNGQELATAVQYGLPIIVIVVNNGMYG 473
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 22-166 8.74e-03

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: 36.11  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308825554  22 AIAVAIEDLKldkdKVCIVSGIGCSSRASGYMDFNTLH----TTHGRALAFATGVKFANPDlHVIVVTGDGDA------- 90
Cdd:cd03372    4 AIKTLIADLK----DELVVSNIGFPSKELYAAGDRPLNfymlGSMGLASSIGLGLALAQPR-KVIVIDGDGSLlmnlgal 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308825554  91 SAIGGNhlihaCRRNIDIttIVFNNNIYGMTGGQFSPTtpkgdrgttapfgniDKAFDICSLAKGAGATYVARSTA 166
Cdd:cd03372   79 ATIAAE-----KPKNLII--VVLDNGAYGSTGNQPTHA---------------GKKTDLEAVAKACGLDNVATVAS 132
PRK09259 PRK09259
putative oxalyl-CoA decarboxylase; Validated
 80-129 9.41e-03

putative oxalyl-CoA decarboxylase; Validated


Pssm-ID: 236433 [Multi-domain]  Cd Length: 569  Bit Score: 37.27  E-value: 9.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 308825554  80 HVIVVTGDgdaSAIG--GNHLIHACRRNIDITTIVFNNN-IYGMT------GGQFSPTT 129
Cdd:PRK09259 443 PVVAIEGD---SAFGfsGMEVETICRYNLPVTVVIFNNGgIYRGDdvnlsgAGDPSPTV 498
 
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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