(data stored in ACNUC7421 zone)

SWISSPROT: Q4ZZ35_PSEU2

ID   Q4ZZ35_PSEU2            Unreviewed;       557 AA.
AC   Q4ZZ35;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 101.
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=Psyr_0517 {ECO:0000313|EMBL:AAY35587.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35587.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35587.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35587.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={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; CP000075; AAY35587.1; -; Genomic_DNA.
DR   RefSeq; WP_011266457.1; NC_007005.1.
DR   RefSeq; YP_233625.1; NC_007005.1.
DR   STRING; 205918.Psyr_0517; -.
DR   EnsemblBacteria; AAY35587; AAY35587; Psyr_0517.
DR   GeneID; 3365993; -.
DR   KEGG; psb:Psyr_0517; -.
DR   PATRIC; fig|205918.7.peg.537; -.
DR   eggNOG; ENOG4107QSN; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281562; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   BioCyc; PSYR205918:G1G4J-518-MONOMER; -.
DR   Proteomes; UP000000426; 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; 3.30.559.10; -; 1.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178:SF2; PTHR43178:SF2; 3.
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.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZ35.
DR   SWISS-2DPAGE; Q4ZZ35.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:AAY35587.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:AAY35587.1}.
FT   DOMAIN        2     75       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      127    201       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      257    294       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   557 AA;  57278 MW;  99B5234E42258E61 CRC64;
     MSELIRVPDI GNGEGEVIEL MVKVGDRIEA DQSVLTLESD KASMEIPAPK AGVIKTMKVK
     LGDRLKEGDE LFELEVEGEA AAAAAPAAEP APAPAPAPAP AAAEKPAEAA PAPAAAAEPA
     PAASASVQDI HVPDIGSSGK AKIIELMVKV GDSIQADQSL ITLESDKASM EIPSPAAGVV
     ESIEVKLDQE VGTGDLILKL KVEGAAPAAA PAPAASAPAA APAKAEAAAP AAPAPKAEAA
     PAPAAPAAPA KDGAKVHAGP AVRQLAREFG VELNAVSATG PHGRVLKEDV QAYVKTMMQK
     AKEAPAGGAS GGSGIPPIPE VDFSRFGEIE EVPMTRLMQL GASGLHRSWL NIPHVTQFDQ
     ADITDLEAFR VAQKGAAEKA GVKLTVLPLL LKSCAHLLKE LPDFNASLAP SGKAVIRKKY
     VHIGFAVDTP DGLLVPVIRD VDQKSLLQLA AEAAALAEKA RNKKLTANDM QGACFTISSL
     GHIGGTGFTP IVNAPEVAIL GVSKATIQPV WDGKAFQPKL MLPLSLSYDH RVINGAAAAR
     FTKRLSELLA DIRTILL
//

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