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Database: UniProt
Entry: A0A0M1J8S1_9GAMM
LinkDB: A0A0M1J8S1_9GAMM
Original site: A0A0M1J8S1_9GAMM 
ID   A0A0M1J8S1_9GAMM        Unreviewed;       412 AA.
AC   A0A0M1J8S1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
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=TI04_09430 {ECO:0000313|EMBL:KOR29105.1};
OS   Achromatium sp. WMS2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Achromatium.
OX   NCBI_TaxID=1604835 {ECO:0000313|EMBL:KOR29105.1};
RN   [1] {ECO:0000313|EMBL:KOR29105.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMS2 {ECO:0000313|EMBL:KOR29105.1};
RX   PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA   Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT   "Metabolic diversity and ecological niches of Achromatium populations
RT   revealed with single-cell genomic sequencing.";
RL   Front. Microbiol. 6:822-822(2015).
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOR29105.1}.
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DR   EMBL; JXSN01000235; KOR29105.1; -; Genomic_DNA.
DR   EnsemblBacteria; KOR29105; KOR29105; TI04_09430.
DR   PATRIC; fig|1604835.3.peg.1172; -.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx.
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   PANTHER; PTHR43178:SF2; PTHR43178:SF2; 2.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        4     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      121    158       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   412 AA;  44502 MW;  EEB95EAEBF6324DB CRC64;
     MPSIQEVRLP DMGGVTKAEI VEILVTPGQF VQLDSSLLTL ESDKATIEIP APVTGTVVEI
     LVTIGNSVQS GDILLRIDVA ADASEVILPQ ASMQAPPQPA PNISKPPVLA KPSDYYTPKP
     HASPSVRSFA RELGVDLSLV TGTGRHGYIM HTDIQAFVKN RLSQAPTPAP APGIDFSRFG
     PVHTQPLSRL RQRSGSHLQH AWSSIPHVTQ FDSADITDLE TFRQLHKNDF AHQSLRLTIL
     PFVLRACANA LQAAPIFNSY LTADGTSIVT REYINIGIAV ATDTGLIVPV IKDVVTQSIS
     QLAASIQQLS SKAKANKLMP DDLQGGCFSV SNLGNGSGSH FTPIINAPEA AILGISKAQI
     QPVWNQDSNQ FVPRLLLPLS LSYDHRIIDG TDGTKFISRI RELLQDIRHL LL
//
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