ID A8UYT7_9AQUI Unreviewed; 397 AA.
AC A8UYT7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=HG1285_12172 {ECO:0000313|EMBL:EDP74423.1};
OS Hydrogenivirga sp. 128-5-R1-1.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP74423.1, ECO:0000313|Proteomes:UP000005981};
RN [1] {ECO:0000313|EMBL:EDP74423.1, ECO:0000313|Proteomes:UP000005981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP74423.1,
RC ECO:0000313|Proteomes:UP000005981};
RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP74423.1}.
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DR EMBL; ABHJ01000020; EDP74423.1; -; Genomic_DNA.
DR AlphaFoldDB; A8UYT7; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000005981; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:EDP74423.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000005981};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EDP74423.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 327..354
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 397 AA; 45492 MW; A4990B7417A853E6 CRC64;
MEYEITMPRL TDTMETGLIV RWLKKEGEAV EKGEPIVEVE TEKAIQEVPS FKNGILKKIL
AQEGDEVEVG KPIAILELSE EKTVSQIQTS QEKVISEKTE PVNLQKNTAQ TYQKQTTKKE
EFKPEEKDKT VKSVEHVEEK HVKLAGGSAS PAAKKLSSQL GIDLKKLQEE GKIPAPAHEE
DIWLYFYSKY FTQDALEEIK GYKIDLKNIV EELGENITKE KLLKYLKEKG AYKLLDISQT
QKRLIEHLTK SATLPVYHIY ETLDLKYIEH NEEFTLTTYL VKIFADVMQE HYRTRIYYDN
GKYRLYPSSN IAIAVAVDEE LFSPVIKNAS EKTLKQIQEE INQIKEKAKE KSFKVEDFED
GTFGISNLGM FGIQMFDAVI PYNYSGIAAV GAEERKK
//
