(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BI20_GEOS0

ID   A0A0F6BI20_GEOS0        Unreviewed;       395 AA.
AC   A0A0F6BI20;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=GY4MC1_0222 {ECO:0000313|EMBL:ADP73071.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73071.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73071.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73071.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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; CP002293; ADP73071.1; -; Genomic_DNA.
DR   RefSeq; WP_013399875.1; NC_014650.1.
DR   EnsemblBacteria; ADP73071; ADP73071; GY4MC1_0222.
DR   GeneID; 29237129; -.
DR   KEGG; gmc:GY4MC1_0222; -.
DR   KO; K00627; -.
DR   OMA; RAMAQNM; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; GSP581103:G1GOQ-265-MONOMER; -.
DR   Proteomes; UP000002034; 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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BI20.
DR   SWISS-2DPAGE; A0A0F6BI20.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN       96    133       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   COILED      288    308       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   395 AA;  43677 MW;  D52659F012F635B0 CRC64;
     MRYEFKLPDI GEGLHEAEIV RWFIQEGDEV AADQPIAEIQ TDKAMVEMTT PVAGKVVALA
     GPEGMTVKVG EPLIILEQQK AAIAESRPAQ QKKRVIAAPS VRKRAREMGI PIEEVEGTGE
     GGRVTLADLE RYAKARESAL EPVAPALEAA GRKMDRRHGI TEHEERIPIR GLRKKIAEKM
     VKSAYTAPHV TGMDEIDVTK LVEIRASLAK QLEAEAIKLT YLPFVIKAVT RALKEYPLLN
     AAIDEETNEI VLKKQYHIGI ATATKEGLVV PVIKHADQKS IHDLAVEIAE LSEKARRHAL
     RIDELQGSTF TITNTGANGG WFATPIINYP EVAILGIHAI KRKPVVIGEE IVIRDMMGMS
     LTFDHRVIDG EPAGRFMRAV SHILEHPEQL LLDVR
//

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