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Database: UniProt
Entry: A0A1G1LQE3_9BACT
LinkDB: A0A1G1LQE3_9BACT
Original site: A0A1G1LQE3_9BACT 
ID   A0A1G1LQE3_9BACT        Unreviewed;       431 AA.
AC   A0A1G1LQE3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   05-JUN-2019, entry version 10.
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=A2Z88_03830 {ECO:0000313|EMBL:OGX07377.1};
OS   Omnitrophica WOR_2 bacterium GWA2_47_8.
OC   Bacteria; Candidatus Omnitrophica.
OX   NCBI_TaxID=1801840 {ECO:0000313|EMBL:OGX07377.1};
RN   [1] {ECO:0000313|EMBL:OGX07377.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGX07377.1}.
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DR   EMBL; MHFY01000089; OGX07377.1; -; Genomic_DNA.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      137    174       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       84    122       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G1LQE3}.
FT   COILED      321    341       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   431 AA;  47199 MW;  EC4FF58F6FDBED12 CRC64;
     MLTEFKLPEL GENIKGGTLV RVAVKVGDAV KKNQTLIEVE TDKATIDVPS TVDGVIKEIL
     VKEGSEIKIG QTIMKIDAGA RQPQEAVGEV SPSLPAKLGG QPPKEEKKVP ASVPQSKAAA
     PAPAVVGIDT NDHKDVPAAP SVRRFAREIG INISEVPGSG PGGRISIDDV KTYSKMLNSG
     AIARTGSAGV AAAPLPNFAK FGEVERKPMN NIRKKTAEHL SQAWMTIPHV TQFDKTDITE
     LERLRKRYST KEKRLTITPF IMKVMASALK NFPQFNTSID MATNEIIYKK YFNIGVAVDT
     DRGLIVPVVR DVDKKNILQI SDELTEIAEK ARNKKTTLEE MQGGCFTLTN LGGIGGTYFP
     PIVNWPEVAI LGISRAQMEP VYVDNQFVPR FILPLSLSYD HRVIDGADGA RFLRWICDAI
     QQPFLMELEK N
//
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