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Database: UniProt/TrEMBL
Entry: D5BM89_ZUNPS
LinkDB: D5BM89_ZUNPS
Original site: D5BM89_ZUNPS 
ID   D5BM89_ZUNPS            Unreviewed;       539 AA.
AC   D5BM89;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   OrderedLocusNames=ZPR_3923 {ECO:0000313|EMBL:ADF54229.1};
OS   Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF54229.1, ECO:0000313|Proteomes:UP000001654};
RN   [1] {ECO:0000313|EMBL:ADF54229.1, ECO:0000313|Proteomes:UP000001654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC   {ECO:0000313|Proteomes:UP000001654};
RX   PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA   Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B.,
RA   Dang H.Y., Zhou B.C., Yu J., Zhang Y.Z.;
RT   "The complete genome of Zunongwangia profunda SM-A87 reveals its
RT   adaptation to the deep-sea environment and ecological role in
RT   sedimentary organic nitrogen degradation.";
RL   BMC Genomics 11:247-247(2010).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP001650; ADF54229.1; -; Genomic_DNA.
DR   RefSeq; WP_013073313.1; NC_014041.1.
DR   STRING; 655815.ZPR_3923; -.
DR   EnsemblBacteria; ADF54229; ADF54229; ZPR_3923.
DR   KEGG; zpr:ZPR_3923; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H0NG1; -.
DR   BioCyc; ZPRO655815:GI6J-3915-MONOMER; -.
DR   Proteomes; UP000001654; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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; IPR004167; E3-bd.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001654};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:ADF54229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001654};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ADF54229.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      123    198       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   539 AA;  58098 MW;  8C6CA499DE42FB94 CRC64;
     MAEVINMPRL SDTMEEGVVA KWLKQKGDKV AEGDILAEIE TDKATMEFES FYEGTLLHIG
     IEEGETAPVD TLLAIIGEEG EDISGLLNGE GGSTEEAKEE SAAEEETEDD DSASEAGEIP
     EGVEIVKMPR LSDTMEEGTV ASWLKKEGDK VSEGDILAEI ETDKATMEFE SFYEGTLLKI
     GIPEGETAPV DSLLAIIGPE GTDVSNVTGD STGKKAAPKK EEKSEAKEEK KEETTTTSSD
     SSSEGGRIFA SPLAKKMAED KGIDLSKVEG SGENGRIVKK DIESYKPSEA PAPKETKKEA
     ETSVAAPYVP AGEESFEEIK NSQMRKTIAK RLGESKFSAP HYYLTIEVDM ENAMASRKQI
     NEMPDVKVSF NDMVIKASAM ALRKHPQVNS QWTGDAMKIA KHIHMGVAVA VEDGLVVPVL
     KFADQMSMTQ IGGNVKDLAG KARNKKLQPK EMEGSTFTVS NLGMFGITEF TSIINQPNSA
     ILSVGTIVEK PVVKNGEIVV GHTMKLTLAC DHRTVDGATG AAFLKDLKTY IENPVTMLA
//
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