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Conserved domains on  [gi|290998938|ref|XP_002682037|]
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dihydrolipoamide succinyltransferase [Naegleria gruberi]

Protein Classification

dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex( domain architecture ID 1007828)

dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2)

CATH:  2.40.50.100
EC:  2.3.1.61
Gene Ontology:  GO:0004149|GO:0045252|GO:0006099
PubMed:  9278141|12023822
SCOP:  4002909

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00144 super family cl36517
dihydrolipoamide succinyltransferase; Provisional
 1-369 0e+00

dihydrolipoamide succinyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00144:

Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 595.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   1 MIKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPT 80
Cdd:PTZ00144  46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  81 ATPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKP-TQSSAPTTSANGLA---RTERRVKMTRIRAKIAERL 156
Cdd:PTZ00144 126 AAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPpEPAPAAKPPPTPVAradPRETRVPMSRMRQRIAERL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 157 KQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAASIALTEVPAVNGVIDGNEVVYRDYVDISV 236
Cdd:PTZ00144 206 KASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKH-GVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISV 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 237 AVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAT 316
Cdd:PTZ00144 285 AVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAI 364

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 290998938 317 KNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLLF 369
Cdd:PTZ00144 365 KKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
 
Name Accession Description Interval E-value
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 1-369 0e+00

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 595.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   1 MIKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPT 80
Cdd:PTZ00144  46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  81 ATPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKP-TQSSAPTTSANGLA---RTERRVKMTRIRAKIAERL 156
Cdd:PTZ00144 126 AAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPpEPAPAAKPPPTPVAradPRETRVPMSRMRQRIAERL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 157 KQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAASIALTEVPAVNGVIDGNEVVYRDYVDISV 236
Cdd:PTZ00144 206 KASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKH-GVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISV 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 237 AVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAT 316
Cdd:PTZ00144 285 AVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAI 364

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 290998938 317 KNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLLF 369
Cdd:PTZ00144 365 KKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 2-368 3.90e-172

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 485.39  E-value: 3.90e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938    2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKK--EEAKPTQSSAPTTSANG------------------------ 135
Cdd:TIGR01347  83 APPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRlaKEHGIDLSAVPGTGVTGrvtkediikkteapasaqppaaaa 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  136 -------LARTERRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAAS 208
Cdd:TIGR01347 163 aaaapaaATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKH-GVKLGFMSFFVKAVV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  209 IALTEVPAVNGVIDGNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTI 288
Cdd:TIGR01347 242 AALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTI 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  289 SNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:TIGR01347 322 TNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 156-367 1.45e-96

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 285.98  E-value: 1.45e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  156 LKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHDglKLGFMGAFCKAASIALTEVPAVNGVIDGN--EVVYRDYVD 233
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET--KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  234 ISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGM 313
Cdd:pfam00198  79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 290998938  314 HATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKML 367
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 2-73 1.37e-23

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 92.85  E-value: 1.37e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:cd06849    3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 2-73 3.40e-22

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 88.97  E-value: 3.40e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:COG0508    5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
 
Name Accession Description Interval E-value
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 1-369 0e+00

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 595.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   1 MIKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPT 80
Cdd:PTZ00144  46 VIKVPTMGDSISEGTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEIDTGGAPP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  81 ATPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKP-TQSSAPTTSANGLA---RTERRVKMTRIRAKIAERL 156
Cdd:PTZ00144 126 AAAPAAAAAAKAEKTTPEKPKAAAPTPEPPAASKPTPPAAAKPpEPAPAAKPPPTPVAradPRETRVPMSRMRQRIAERL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 157 KQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAASIALTEVPAVNGVIDGNEVVYRDYVDISV 236
Cdd:PTZ00144 206 KASQNTCAMLTTFNECDMSALMELRKEYKDDFQKKH-GVKLGFMSAFVKASTIALKKMPIVNAYIDGDEIVYRNYVDISV 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 237 AVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAT 316
Cdd:PTZ00144 285 AVATPTGLVVPVIRNCENKSFAEIEKELADLAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAI 364

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 290998938 317 KNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLLF 369
Cdd:PTZ00144 365 KKRPVVVGNEIVIRPIMYLALTYDHRLIDGRDAVTFLKKIKDLIEDPARMLLD 417
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
2-368 4.96e-179

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 502.83  E-value: 4.96e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:PRK05704   5 IKVPTLPESVTEATIATWHKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRIDEGAAAGA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  82 TPAAAASTPSTTTTTTTTASTPSTPTPTATP-----------------------------------TPTPKKEEAKPTQS 126
Cdd:PRK05704  85 AAAAAAAAAAAAAAPAQAQAAAAAEQSNDALspaarklaaengldasavkgtgkggrvtkedvlaaLAAAAAAPAAPAAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 127 SAPTTSANGLARTERRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKA 206
Cdd:PRK05704 165 APAAAPAPLGARPEERVPMTRLRKTIAERLLEAQNTTAMLTTFNEVDMTPVMDLRKQYKDAFEKKH-GVKLGFMSFFVKA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 207 ASIALTEVPAVNGVIDGNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTF 286
Cdd:PRK05704 244 VVEALKRYPEVNASIDGDDIVYHNYYDIGIAVGTPRGLVVPVLRDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTF 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 287 TISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKM 366
Cdd:PRK05704 324 TITNGGVFGSLMSTPIINPPQSAILGMHKIKERPVAVNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERL 403


                 ..
gi 290998938 367 LL 368
Cdd:PRK05704 404 LL 405
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 2-368 3.90e-172

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 485.39  E-value: 3.90e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938    2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:TIGR01347   3 IKVPELAESITEGTVAEWHKKVGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKK--EEAKPTQSSAPTTSANG------------------------ 135
Cdd:TIGR01347  83 APPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARRlaKEHGIDLSAVPGTGVTGrvtkediikkteapasaqppaaaa 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  136 -------LARTERRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAAS 208
Cdd:TIGR01347 163 aaaapaaATRPEERVKMTRLRQRIAERLKEAQNSTAMLTTFNEVDMSAVMELRKRYKEEFEKKH-GVKLGFMSFFVKAVV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  209 IALTEVPAVNGVIDGNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTI 288
Cdd:TIGR01347 242 AALKRFPEVNAEIDGDDIVYKDYYDISVAVSTDRGLVVPVVRNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTI 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  289 SNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:TIGR01347 322 TNGGVFGSLMSTPIINPPQSAILGMHGIKERPVAVNGQIEIRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLL 401
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 4-368 9.08e-125

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 367.16  E-value: 9.08e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   4 VPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTATP 83
Cdd:PLN02226  96 VPHMGESITDGTLATFLKKPGERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPGTKVAIISKSEDAASQV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  84 AAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEeaKPTQSSAPTTSANGL----ARTERRVKMTRIRAKIAERLKQA 159
Cdd:PLN02226 176 TPSQKIPETTDPKPSPPAEDKQKPKVESAPVAEKPK--APSSPPPPKQSAKEPqlppKERERRVPMTRLRKRVATRLKDS 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 160 QNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAASIALTEVPAVNGVIDGNEVVYRDYVDISVAVA 239
Cdd:PLN02226 254 QNTFALLTTFNEVDMTNLMKLRSQYKDAFYEKH-GVKLGLMSGFIKAAVSALQHQPVVNAVIDGDDIIYRDYVDISIAVG 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 240 TPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNR 319
Cdd:PLN02226 333 TSKGLVVPVIRGADKMNFAEIEKTINGLAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSR 412

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 290998938 320 PIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:PLN02226 413 PMVVGGSVVPRPMMYVALTYDHRLIDGREAVYFLRRVKDVVEDPQRLLL 461
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 2-368 2.63e-103

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 310.57  E-value: 2.63e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:PRK11856   5 FKMPDLGEGMTEGEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVIEEEGEAEA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTP--------------------------------------------- 116
Cdd:PRK11856  85 AAAAEAAPEAPAPEPAPAAAAAAAAAPAAAAAPAApaaaaakaspavrklarelgvdlstvkgsgpggritkedveaaaa 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 117 KKEEAKPTQSSAPTTSANGLARTERRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKvnqddfQERHDGLK 196
Cdd:PRK11856 165 AAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESKREIPHFTLTDEVDVTALLALRK------QLKAIGVK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 197 LGFMGAFCKAASIALTEVPAVNGVIDGNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAI 276
Cdd:PRK11856 239 LTVTDFLIKAVALALKKFPELNASWDDDAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 277 SLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRV 356
Cdd:PRK11856 319 KPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVDGEIVVRKVMPLSLSFDHRVIDGADAARFLKAL 398

                        410
                 ....*....|..
gi 290998938 357 KELIEDPEKMLL 368
Cdd:PRK11856 399 KELLENPALLLL 410
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 156-367 1.45e-96

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 285.98  E-value: 1.45e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  156 LKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERHDglKLGFMGAFCKAASIALTEVPAVNGVIDGN--EVVYRDYVD 233
Cdd:pfam00198   1 MTESKQTIPHFTLTDEVDVTELLALREELKEDAADEET--KLTFLPFLVKAVALALKKFPELNASWDGEegEIVYKKYVN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  234 ISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGM 313
Cdd:pfam00198  79 IGIAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 290998938  314 HATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKML 367
Cdd:pfam00198 159 GRIRKRPVVVDGEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 2-368 4.58e-85

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 267.84  E-value: 4.58e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   2 IKVPSMGDsISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:PRK11855 122 VKVPDIGE-ITEVEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPA 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPK-------------------------------------KE----- 119
Cdd:PRK11855 201 AAAAPAAAAPAAAAAAAPAPAPAAAAAPAAAAPAAAaapgkaphaspavrrlarelgvdlsqvkgtgkkgritKEdvqaf 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 120 ------EAKPTQSSAPTTSANGLA------------RTERRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELR 181
Cdd:PRK11855 281 vkgamsAAAAAAAAAAAAGGGGLGllpwpkvdfskfGEIETKPLSRIKKISAANLHRSWVTIPHVTQFDEADITDLEALR 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 182 KVNQDDFQErhDGLKLGFMGAFCKAASIALTEVPAVNGVID--GNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQ 259
Cdd:PRK11855 361 KQLKKEAEK--AGVKLTMLPFFIKAVVAALKEFPVFNASLDedGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLE 438

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 260 IERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTY 339
Cdd:PRK11855 439 IAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGTAFTPIINAPEVAILGVGKSQMKPVWDGKEFVPRLMLPLSLSY 518

                        410       420
                 ....*....|....*....|....*....
gi 290998938 340 DHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:PRK11855 519 DHRVIDGATAARFTNYLKQLLADPRRMLL 547
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 2-362 1.06e-70

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 231.44  E-value: 1.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938    2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:TIGR02927 129 VKMPELGESVTEGTVTSWLKAVGDTVEVDEPLLEVSTDKVDTEIPSPVAGTLLEIRAPEDDTVEVGTVLAIIGDANAAPA 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKPTQSSAPTTSANG-------------------------- 135
Cdd:TIGR02927 209 EPAEEEAPAPSEAGSEPAPDPAARAPHAAPDPPAPAPAPAKTAAPAAAAPVSSGdsgpyvtplvrklakdkgvdlstvkg 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  136 ------------LARTE-------------------------------------RRVKMTRIRAKIAERLKQAQNTYAML 166
Cdd:TIGR02927 289 tgvggrirkqdvLAAAKaaeearaaaaapaaaaapaapaaaakpaepdtaklrgTTQKMNRIRQITADKTIESLQTSAQL 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  167 TTFNEIDMKKIMELRKVNQDDFQERHdGLKLGFMGAFCKAASIALTEVPAVNGVI--DGNEVVYRDYVDISVAVATPNGL 244
Cdd:TIGR02927 369 TQVHEVDMTRVAALRARAKNDFLEKN-GVNLTFLPFFVQAVTEALKAHPNVNASYnaETKEVTYHDVEHVGIAVDTPRGL 447

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  245 VVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAI- 323
Cdd:TIGR02927 448 LVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFDTPILNPPQAAILGTGAIVKRPRVIk 527

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 290998938  324 ----GDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIED 362
Cdd:TIGR02927 528 dedgGESIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEE 570
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 2-368 2.76e-66

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 221.03  E-value: 2.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   2 IKVPSMGDSisSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:PRK11854 209 VNVPDIGGD--EVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFEVEGAAPA 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKPTQS----------------------------------- 126
Cdd:PRK11854 287 AAPAKQEAAAPAPAAAKAEAPAAAPAAKAEGKSEFAENDAYVHATplvrrlarefgvnlakvkgtgrkgrilkedvqayv 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 127 --------SAPTTSANGLARTER---------------RVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKV 183
Cdd:PRK11854 367 kdavkraeAAPAAAAAGGGGPGLlpwpkvdfskfgeieEVELGRIQKISGANLHRNWVMIPHVTQFDKADITELEAFRKQ 446

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 184 -NQDDFQERHdGLKLGFMGAFCKAASIALTEVPAVNGVI--DGNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQI 260
Cdd:PRK11854 447 qNAEAEKRKL-GVKITPLVFIMKAVAAALEQMPRFNSSLseDGQRLTLKKYVNIGIAVDTPNGLVVPVFKDVNKKGIIEL 525

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 261 ERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYD 340
Cdd:PRK11854 526 SRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAILGVSKSAMEPVWNGKEFAPRLMLPLSLSYD 605

                        410       420
                 ....*....|....*....|....*...
gi 290998938 341 HRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:PRK11854 606 HRVIDGADGARFITIINDRLSDIRRLVL 633
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 2-368 2.67e-61

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 203.10  E-value: 2.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938    2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAIL--ANAKDtVEVGKDIAIIDTDGKP 79
Cdd:TIGR01349   2 ITMPALSPTMTTGNLAKWLKKEGDKVNPGDVIAEIETDKATMEFEAVEEGYLAKILvpEGTKD-VPVNKPIAVLVEEKED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   80 TATPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKPTQSSAPTTSANG--------LARTE----------- 140
Cdd:TIGR01349  81 VADAFKNYKLESSASPAPKPSEIAPTAPPSAPKPSPAPQKQSPEPSSPAPLSDKESgdrifaspLAKKLakekgidlsav 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  141 -------RRVK-----------------------------------------MTRIRAKIAERLKQAQNTYAMLTTFNEI 172
Cdd:TIGR01349 161 agsgpngRIVKkdiesfvpqspasanqqaaattpatypaaapvstgsyedvpLSNIRKIIAKRLLESKQTIPHYYVSIEC 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  173 DMKKIMELRKVNQDDFQERHdglKLGFMGAFCKAASIALTEVPAVNGVIDGNEVVYRDYVDISVAVATPNGLVVPVVRNC 252
Cdd:TIGR01349 241 NVDKLLALRKELNAMASEVY---KLSVNDFIIKASALALREVPEANSSWTDNFIRRYKNVDISVAVATPDGLITPIVRNA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  253 ESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQ---VVV 329
Cdd:TIGR01349 318 DAKGLSTISNEIKDLAKRARNNKLKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVEDVAVVDNDEekgFAV 397

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 290998938  330 RPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:TIGR01349 398 ASIMSVTLSCDHRVIDGAVGAEFLKSFKKYLENPIEMLL 436
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 2-368 1.96e-54

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 187.77  E-value: 1.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938    2 IKVPSMGDsISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDGKPTA 81
Cdd:TIGR01348 119 VTVPDIGD-IEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLSVAGSTPA 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   82 TPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPK-------------------------------------------- 117
Cdd:TIGR01348 198 TAPAPASAQPAAQSPAATQPEPAAAPAAAKAQAPAPqqagtqnpakvdhaapavrrlarefgvdlsavkgtgikgrilre 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  118 ------KEEAKPTQSSAPTTSANGLAR------------TERRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIME 179
Cdd:TIGR01348 278 dvqrfvKEPSVRAQAAAASAAGGAPGAlpwpnvdfskfgEVEEVDMSRIRKISGANLTRNWTMIPHVTHFDKADITEMEA 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  180 LRKvnQDDFQERHDGLKLGFMGAFCKAASIALTEVPAVNGVID--GNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSI 257
Cdd:TIGR01348 358 FRK--QQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNASLDlgGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGI 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  258 AQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVAL 337
Cdd:TIGR01348 436 TELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGTAFTPIVNAPEVAILGVSKSGMEPVWNGKEFEPRLMLPLSL 515

                         410       420       430
                  ....*....|....*....|....*....|.
gi 290998938  338 TYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:TIGR01348 516 SYDHRVIDGADAARFTTYICESLADIRRLLL 546
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 118-364 1.14e-51

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 174.21  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 118 KEEAKPTQSSAPT-TSANGLARTE-RRVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQeRHDGL 195
Cdd:PRK11857  52 AASVSSAQQAAKTaAPAAAPPKLEgKREKVAPIRKAIARAMTNSWSNVAYVNLVNEIDMTKLWDLRKSVKDPVL-KTEGV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 196 KLGFMGAFCKAASIALTEVPAVNGVID--GNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARK 273
Cdd:PRK11857 131 KLTFLPFIAKAILIALKEFPIFAAKYDeaTSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKAARE 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 274 NAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFL 353
Cdd:PRK11857 211 RKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIVKNGQIVAGKVMHLTVAADHRWIDGATIGRFA 290

                        250
                 ....*....|.
gi 290998938 354 KRVKELIEDPE 364
Cdd:PRK11857 291 SRVKELLEKPE 301
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 2-368 2.35e-49

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 173.89  E-value: 2.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVL-KAILANAKDTVEVGKDIAIIdTDGKPT 80
Cdd:PLN02744 115 IGMPSLSPTMTEGNIARWLKKEGDKVSPGEVLCEVETDKATVEMECMEEGYLaKIVKGDGAKEIKVGEVIAIT-VEEEED 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  81 ATPAAAASTPSTTTTTTTTASTPSTPTPTATPTPTPKKEEAKPTQSSAPTTS-----ANGLART---------------- 139
Cdd:PLN02744 194 IGKFKDYKPSSSAAPAAPKAKPSPPPPKEEEVEKPASSPEPKASKPSAPPSSgdrifASPLARKlaednnvplssikgtg 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 140 --ERRVKM---------------------------------TRIRAKIAERLKQAQNT--YAMLTTFNEIDmkKIMELR- 181
Cdd:PLN02744 274 pdGRIVKAdiedylasggkgatappstdskapaldytdipnTQIRKVTASRLLQSKQTipHYYLTVDTRVD--KLMALRs 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 182 KVNQddFQERHDGLKLGFMGAFCKAASIALTEVPAVNGVIDGNEVvyRDY--VDISVAVATPNGLVVPVVRNCESKSIAQ 259
Cdd:PLN02744 352 QLNS--LQEASGGKKISVNDLVIKAAALALRKVPQCNSSWTDDYI--RQYhnVNINVAVQTENGLYVPVVKDADKKGLST 427

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 260 IERDISNLGEKARKNAISLDDMQGGTFTISN-GGVFGSLMGTPIINPPQSAILGMHATKNR--PIAIGDQVVVRPMMYVA 336
Cdd:PLN02744 428 IAEEVKQLAQKARENSLKPEDYEGGTFTVSNlGGPFGIKQFCAIINPPQSAILAVGSAEKRviPGSGPDQYNFASFMSVT 507

                        410       420       430
                 ....*....|....*....|....*....|..
gi 290998938 337 LTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:PLN02744 508 LSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 142-368 1.65e-41

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 148.51  E-value: 1.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 142 RVKMTRIRAKIAERLKQAQNTYAMLTTFNEIDMKKIMELRKVNQDDFQERhDGLKLGFMGAFCKAASIALTEVPAVNGVI 221
Cdd:PRK14843 120 RIPMTPMRKVIAQRMVESYLTAPTFTLNYEVDMTEMLALRKKVLEPIMEA-TGKKTTVTDLLSLAVVKTLMKHPYINASL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 222 --DGNEVVYRDYVDISVAVATPNGLVVPVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMG 299
Cdd:PRK14843 199 teDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKLAPSELQNSTFTISNLGMFGVQSF 278

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 290998938 300 TPIINPPQSAILGMHATKNRPIAIGDQVVVRPMMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:PRK14843 279 GPIINQPNSAILGVSSTIEKPVVVNGEIVIRPIMSLGLTIDHRVVDGMAGAKFMKDLKELIETPISMLI 347
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 171-368 9.27e-41

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 148.33  E-value: 9.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 171 EIDMKKIMELRkvnqDDFQE--RHDGLKLGFMGAFCKAASIALTEVPAVNGVIDG--NEVVYRDYVDISVAVATPNGLVV 246
Cdd:PLN02528 215 EINVDALVELK----ASFQEnnTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFNEetSEIRLKGSHNIGVAMATEHGLVV 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938 247 PVVRNCESKSIAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAIlgmhatknrpIAIGD- 325
Cdd:PLN02528 291 PNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGSPVLNLPEVAI----------IALGRi 360

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 290998938 326 QVVVRP----------MMYVALTYDHRIIDGREAVTFLKRVKELIEDPEKMLL 368
Cdd:PLN02528 361 QKVPRFvddgnvypasIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLML 413
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 2-73 1.37e-23

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 92.85  E-value: 1.37e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:cd06849    3 IKMPDLGESMTEGTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 2-73 3.40e-22

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 88.97  E-value: 3.40e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:COG0508    5 IKMPDLGESMTEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 112-359 1.70e-16

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 81.09  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  112 PTPTPKKEEAKPTQSSAPTTSANGLARTERRVKMTRIRAkIAERLkqAQNTYAML-----TTFNEIDMKKIMELRKV-Nq 185
Cdd:PRK12270   84 PKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRG-AAAAV--AKNMDASLevptaTSVRAVPAKLLIDNRIViN- 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  186 dDFQERHDGLKLGFMGAFCKAASIALTEVPAVN---GVIDGN-EVVYRDYVDISVA--VATPNG---LVVPVVRNCESKS 256
Cdd:PRK12270  160 -NHLKRTRGGKVSFTHLIGYALVQALKAFPNMNrhyAEVDGKpTLVTPAHVNLGLAidLPKKDGsrqLVVPAIKGAETMD 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290998938  257 IAQIERDISNLGEKARKNAISLDDMQGGTFTISNGGVFGSLMGTPIINPPQSAILGMHA---------TKNRPIAigdQV 327
Cdd:PRK12270  239 FAQFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAmeypaefqgASEERLA---EL 315

                         250       260       270
                  ....*....|....*....|....*....|..
gi 290998938  328 VVRPMMYVALTYDHRIIDGREAVTFLKRVKEL 359
Cdd:PRK12270  316 GISKVMTLTSTYDHRIIQGAESGEFLRTIHQL 347
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 2-73 1.96e-14

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 67.62  E-value: 1.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290998938    2 IKVPSMGDSISSGEInEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:pfam00364   3 IKSPMIGESVREGVV-EWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 2-74 4.46e-13

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 70.42  E-value: 4.46e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 290998938   2 IKVPSMGdsISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIID 74
Cdd:PRK11854   5 IKVPDIG--ADEVEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 1-77 5.98e-13

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 69.20  E-value: 5.98e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 290998938   1 MIKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIIDTDG 77
Cdd:PRK14875   4 PITMPKWGLSMTEGKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVVADAE 80
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 2-73 3.22e-07

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 47.44  E-value: 3.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:cd06663    2 ILIPDLAQHLGDGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 13-73 9.12e-06

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 42.79  E-value: 9.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 290998938  13 SGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:cd06850    7 PGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 2-77 3.29e-05

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 45.68  E-value: 3.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 290998938   2 IKVPSMGDSISSGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAIL-ANAKDTVEVGKDIAIIDTDG 77
Cdd:PRK11892   5 ILMPALSPTMEEGTLAKWLKKEGDKVKSGDVIAEIETDKATMEVEAVDEGTLGKILvPEGTEGVKVNTPIAVLLEEG 81
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 22-74 3.37e-04

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 40.26  E-value: 3.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 290998938  22 KPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAIID 74
Cdd:COG0511   84 KVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
13-67 3.97e-03

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 39.14  E-value: 3.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 290998938  13 SGEINEWVKKPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVG 67
Cdd:PRK14040 532 AGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVG 586
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 22-73 6.46e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 38.29  E-value: 6.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 290998938  22 KPGQACVEDEVICTIDTDKVSVEIRAPEAGVLKAILANAKDTVEVGKDIAII 73
Cdd:PRK09282 539 KEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
 
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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