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Database: UniProt
Entry: A0A1B0ZSD6_9RHOB
LinkDB: A0A1B0ZSD6_9RHOB
Original site: A0A1B0ZSD6_9RHOB 
ID   A0A1B0ZSD6_9RHOB        Unreviewed;       387 AA.
AC   A0A1B0ZSD6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 13.
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=JL2886_02184 {ECO:0000313|EMBL:ANP37075.1};
OS   Phaeobacter gallaeciensis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Phaeobacter.
OX   NCBI_TaxID=60890 {ECO:0000313|EMBL:ANP37075.1, ECO:0000313|Proteomes:UP000092565};
RN   [1] {ECO:0000313|EMBL:ANP37075.1, ECO:0000313|Proteomes:UP000092565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JL2886 {ECO:0000313|EMBL:ANP37075.1,
RC   ECO:0000313|Proteomes:UP000092565};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) 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; CP015124; ANP37075.1; -; Genomic_DNA.
DR   RefSeq; WP_065271950.1; NZ_CP015124.1.
DR   PATRIC; fig|60890.4.peg.2117; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; GCF_001678945:G1EWY-2101-MONOMER; -.
DR   Proteomes; UP000092565; 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; 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:UP000092565};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092565};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ANP37075.1}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      119    155       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       78    116       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1B0ZSD6}.
SQ   SEQUENCE   387 AA;  41067 MW;  EDCD36D82DF88541 CRC64;
     MSDFLMPSLG ADMEAGTLME QVVAVGQPVT HGDIIAVVET QKGAIEIECY ETGTVTEWLV
     GIGESVPVGT PLARIDTGEA ADGQTVEPAP VPEPEKPKPR AVAEPPQPAP SVPTGTRIVA
     SPAARRLAAE KGVDLSALSV PSGQPIRHAD VAAHITAGGK TAPQDTGLSA MRQAIAAAMS
     RSKREIPHFY LTHQVDLTTL DDFITEMNET RAPEDRVLPP VFYLCAMARA LKKYPEFNGH
     FEGGTFTPAK EAHIGLAIAL RGGGLVAPAL FDVAAQERDG LMAQMRDLIG RVRAGRFKAR
     ELSDATITLT SLGDRGIDGL FGVIYPPQVA IVGIGTPALR PRVVDGKVVP RQIATLTLAA
     DHRVSDGHRG ALFLRAIDRF LQEPETL
//
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