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Database: UniProt
Entry: H1ZA22_MYROD
LinkDB: H1ZA22_MYROD
Original site: H1ZA22_MYROD 
ID   H1ZA22_MYROD            Unreviewed;       434 AA.
AC   H1ZA22;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   10-APR-2019, entry version 33.
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=Myrod_2400 {ECO:0000313|EMBL:EHQ43223.1};
OS   Myroides odoratus DSM 2801.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Myroides.
OX   NCBI_TaxID=929704 {ECO:0000313|EMBL:EHQ43223.1, ECO:0000313|Proteomes:UP000005785};
RN   [1] {ECO:0000313|EMBL:EHQ43223.1, ECO:0000313|Proteomes:UP000005785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2801 {ECO:0000313|EMBL:EHQ43223.1,
RC   ECO:0000313|Proteomes:UP000005785};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The draft genome of Myroides odoratus DSM 2801.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CM001437; EHQ43223.1; -; Genomic_DNA.
DR   RefSeq; WP_002990119.1; NZ_CM001437.1.
DR   STRING; 929704.Myrod_2400; -.
DR   EnsemblBacteria; EHQ43223; EHQ43223; Myrod_2400.
DR   OrthoDB; 1626282at2; -.
DR   Proteomes; UP000005785; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
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; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000005785};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005785};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      121    161       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   434 AA;  46267 MW;  83F99FB57170D707 CRC64;
     MAKFELKLPK MGESVAEATI TNWLKNVGDR IEADETVLEI ATDKVDSEVP SEVEGTLVEI
     LFQVDDVVQV GQTIAIIETE GGEVASTPAA TSTPTVAAVE QTVNVAQEAA APVDFSASEK
     FFSPLVKNIA KEEGISLSEL EAIQGTGKEG RVTKNDILAY VEQRGSQPQA AAPVAKAEVA
     KPTAAPAAAA KAVPVSVNGG DEIVEMDRMR KLISGYMVQS VQTSAHVQSF IEVDVTNIVK
     WRDKVKGAFE KREGEKLTFT PIFMEAVAKA LKDFPGMNIS VDGDFIIKKK NINLGMAAAL
     PNGNLIVPVI KNADQLNLVG MAKAVNDLGN RAKAGKLKPD DTQGGTYTVT NVGTFGSVFG
     TPIINQPQVG ILALGAIRKV PAVIETPEGD FIGIRQKMFL SHSYDHRVVD GALGGSFVKR
     VADILEAWDI NREI
//
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