ID G9PD95_9ACTO Unreviewed; 596 AA.
AC G9PD95;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=HMPREF0045_00374 {ECO:0000313|EMBL:EHM89709.1};
OS Actinomyces graevenitzii C83.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=435830 {ECO:0000313|EMBL:EHM89709.1, ECO:0000313|Proteomes:UP000003822};
RN [1] {ECO:0000313|EMBL:EHM89709.1, ECO:0000313|Proteomes:UP000003822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C83 {ECO:0000313|EMBL:EHM89709.1,
RC ECO:0000313|Proteomes:UP000003822};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinomyces graevenitzii C83.";
RL Submitted (OCT-2011) 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:EHM89709.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACRN01000001; EHM89709.1; -; Genomic_DNA.
DR RefSeq; WP_005984972.1; NZ_JH470338.1.
DR AlphaFoldDB; G9PD95; -.
DR STRING; 435830.HMPREF0045_00374; -.
DR PATRIC; fig|435830.3.peg.367; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000003822; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR014276; 2-oxoglutarate_DH_E2.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000003822};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EHM89709.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 131..206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 274..311
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 94..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 60259 MW; 1835A1AF8C9FCA5F CRC64;
MSHSVEMPAL GESVTEGTVS SWYKAVGEHV EADEPLVSVA TDKVDTDVPS PVSGVVEQIL
VPEDETVDVG TVIAIIGDGS GLGGAAEAAP APVAESAPAP AAPAPAPVAA EPTPAPAAPA
ATPAHSDDTA GTEVTMPALG ESVTEGTVSS WYKAVGDTIE ADEPLVSVAT DKVDTDVPSP
VSGVVIKLLV PEDETVDVGT PIAIIGAPGA APAAPAPAPV AAEPTPAPAP AVPAPVAPAA
PAPVAQAPAP AVVTEPAPAA VAEPAPSVVT NSAYVTPLVR KLAREKGVDL STVTGSGVGG
RIRKEDVEAK AAQIAAEKAA QEAAAKAAAQ AAAQAPAPAA PAPVSAKPAA AKPAVDTTLR
GKTEKMSRLR QVISTRMIES LQTSAQLTTV VEVDVTRIAS LRARAKNAFL AANGTKLTFL
PFFVQAATEA LKAHPKINAS INGKEVTYHA VEHIGIAVDT PRGLLVPVVK NAGDLNIPGL
AKRINDLAAR TRDNQVNPQE LSGSTFTITN TGSGGALFDT PIINQPEVAI LGLGAITKQP
RVVRDADGNE TIGIRSVCYL ALSYDHRLVD GADAARYLMT VKKRLEEGDF AGELGL
//