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Database: UniProt/TrEMBL
Entry: F4CDI4_SPHS2
LinkDB: F4CDI4_SPHS2
Original site: F4CDI4_SPHS2 
ID   F4CDI4_SPHS2            Unreviewed;       548 AA.
AC   F4CDI4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 40.
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=Sph21_1150 {ECO:0000313|EMBL:ADZ77719.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77719.1, ECO:0000313|Proteomes:UP000007808};
RN   [1] {ECO:0000313|Proteomes:UP000007808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21 {ECO:0000313|Proteomes:UP000007808};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Siebers A.K., Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002584; ADZ77719.1; -; Genomic_DNA.
DR   RefSeq; WP_013664447.1; NC_015277.1.
DR   STRING; 743722.Sph21_1150; -.
DR   EnsemblBacteria; ADZ77719; ADZ77719; Sph21_1150.
DR   KEGG; shg:Sph21_1150; -.
DR   PATRIC; fig|743722.3.peg.1231; -.
DR   eggNOG; ENOG4105C7S; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H0NG1; -.
DR   BioCyc; SSP743722:GH04-1142-MONOMER; -.
DR   Proteomes; UP000007808; 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; IPR036625; E3-bd_dom_sf.
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   ECO:0000313|EMBL:ADZ77719.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007808};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:ADZ77719.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007808};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ADZ77719.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      128    203       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   548 AA;  58904 MW;  C25CB6418719C135 CRC64;
     MAEVVRMPKM SDTMTEGVIA KWHKKVGDKV SSGDLIAEVE TDKATMDFES YQEGTLLYIG
     PKEGEAVPID AVIAVLGEEG EDYQALLNGN GGASPSTKED KKEEEAPAQE ETEDEDEGEE
     VSAESLGATV ITMPLLSDTM TEGVIAEWHF KVGDKIKSDD VIADVETDKA TMEVTAYAEG
     TLLYIGVEKG QAAKVNDIIA IVGKEGTDVT PLLKQKSSKP KKQEAPKKEE ASTSAANEPS
     QAESKEVTSS DSSRVKASPL ARKIAKEKGI DLNELKGSAE NGRIIKKDVE SFTPAAKQKT
     EAPAAAPSAE SKSVTIPQFI GEERFTEKPV TQMRKTIAKR LSESLFTAPH FYVTVKVDMD
     SAISARNKIN EVAPVKVSFN DLVIKAVAVA LKQHPNVNSS WLGDKIRYNE HVNIGVAIAV
     DEGLLVPVVR FADGKTLSHI SAEVKDFAQR AKAKKLQPKD WEGSTFTVSN LGMFGVDEFT
     AIINPPDSCI LAIGGIQQVP VVKNGAVVPG NIMKITLSCD HRVVDGATGA AFLQTVKSLL
     EEPVRLLV
//
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