(data stored in SCRATCH zone)

SWISSPROT: A8FQC2_SHESH

ID   A8FQC2_SHESH            Unreviewed;       545 AA.
AC   A8FQC2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 74.
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=Ssed_0432 {ECO:0000313|EMBL:ABV35045.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35045.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35045.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35045.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CP000821; ABV35045.1; -; Genomic_DNA.
DR   RefSeq; WP_012140782.1; NC_009831.1.
DR   ProteinModelPortal; A8FQC2; -.
DR   STRING; 425104.Ssed_0432; -.
DR   EnsemblBacteria; ABV35045; ABV35045; Ssed_0432.
DR   KEGG; sse:Ssed_0432; -.
DR   eggNOG; ENOG4107QSN; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281562; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H05OF; -.
DR   BioCyc; SSED425104:GH7Q-454-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178:SF4; PTHR43178:SF4; 1.
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; TIGR01348; PDHac_trf_long; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   3: Inferred from homology;
DR   PRODOM; A8FQC2.
DR   SWISS-2DPAGE; A8FQC2.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ABV35045.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ABV35045.1}.
FT   DOMAIN        4     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      116    190       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   545 AA;  56909 MW;  2145F85E4C8E9C02 CRC64;
     MSELKEVLVP DIGGDDVQVI EICVAVGDQL AAEESIITVE SDKATMDIPA PFAGTLAELK
     IAVGDTVSEG TLIAMMSAQG ASTEVTAATA APEPTPVAPA APVDAAPVPA STATQVIEVK
     VPDIGDAADV EIIEVLVAVG DSIDVDTGLI TLETDKATME VPAPSAGVVK ELKVAVGDKV
     SEGSLVLMLE VGASAPAAIV APVEAPVVAP VAQPAQAATS KPPVPHHPSA GSKPVTGAVH
     ASPAVRRLAR EFGADMTLVK GTGRKGRILK EDVQAFIKYE LSRPKASAAT AVAGGAGGLN
     VIAAPKVDFA KFGEIEEVPL TRIQKISGPN LHRNWVTIPH VTQFDEADIT EMEAFRKQQN
     ELAAKRKTGI KITPLVFMMK AVAKTLQAFP VFNASLSADG ESLIKKKYYH IGVAVDTPNG
     LVVPVVRDVD KKGIHELTQE LTEISIKARD GKLKSADMQG SCFTISSLGG IGGTAFTPIV
     NYPDVAILGV SKSEIKPKWN GKDFEPKLML PLSLSYDHRV IDGAMAARFS VTLSSMLSDI
     RTLIL
//

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