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Database: UniProt
Entry: A8Z6A0_SULMW
LinkDB: A8Z6A0_SULMW
Original site: A8Z6A0_SULMW 
ID   A8Z6A0_SULMW            Unreviewed;       371 AA.
AC   A8Z6A0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=aceF {ECO:0000313|EMBL:ABS30651.1};
GN   OrderedLocusNames=SMGWSS_255 {ECO:0000313|EMBL:ABS30651.1};
OS   Sulcia muelleri (strain GWSS).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Candidatus Sulcia.
OX   NCBI_TaxID=444179 {ECO:0000313|EMBL:ABS30651.1, ECO:0000313|Proteomes:UP000000781};
RN   [1] {ECO:0000313|EMBL:ABS30651.1, ECO:0000313|Proteomes:UP000000781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GWSS {ECO:0000313|EMBL:ABS30651.1,
RC   ECO:0000313|Proteomes:UP000000781};
RX   PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA   McCutcheon J.P., Moran N.A.;
RT   "Parallel genomic evolution and metabolic interdependence in an
RT   ancient symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
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; CP000770; ABS30651.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABS30651; ABS30651; SMGWSS_255.
DR   KEGG; smg:SMGWSS_255; -.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   Proteomes; UP000000781; 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;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABS30651.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000781};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000781};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABS30651.1}.
FT   DOMAIN        2     79       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      100    137       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   371 AA;  41482 MW;  1933533ABDB8BE91 CRC64;
     MAEVIFMPRL SDTMVVGTVV KWHKKIGDKI LEGDILAEIE TDKAIQELEA EYNSTLLYIG
     IKEGESAPVN SNSVLAILGS ENEDISSLLK QNKINYKRIL ISPLAKKLAF DKGISLDNIK
     GTGINGRIIK KDIERYIDNN LDKTISSNEV NHSNIRKIIS KRLINSKIES PHYSLFIEVI
     MDNLIKLRDS INEKKYLDKI SFNDLIVKAS ALAIKENPKI NSSWTEKSIL YHNNINIGIA
     VALEDGLIVP VINQVNEKSL RQISFEIKEK VIKAKEKKIQ SNELEGSTFT VSNLGMFGID
     SFTSIINQPN SCILSVGSIK KKPIINNDKI VIGHTTKFTL TCDHRIIDGA VGSDYLKSLK
     KLLQEPLNII I
//
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