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Database: UniProt
Entry: G9PD95_9ACTO
LinkDB: G9PD95_9ACTO
Original site: G9PD95_9ACTO 
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}.
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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
//
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