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Database: UniProt
Entry: Q820A3_NITEU
LinkDB: Q820A3_NITEU
Original site: Q820A3_NITEU 
ID   Q820A3_NITEU            Unreviewed;       453 AA.
AC   Q820A3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   05-JUN-2019, entry version 111.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=aceF {ECO:0000313|EMBL:CAD84271.1};
GN   OrderedLocusNames=NE0360 {ECO:0000313|EMBL:CAD84271.1};
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 /
OS   NBRC 14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410 {ECO:0000313|EMBL:CAD84271.1, ECO:0000313|Proteomes:UP000001416};
RN   [1] {ECO:0000313|EMBL:CAD84271.1, ECO:0000313|Proteomes:UP000001416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298
RC   {ECO:0000313|Proteomes:UP000001416};
RX   PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J., Larimer F., Regala W., Land M., Hauser L.,
RA   Hooper A., Klotz M., Norton J., Sayavedra-Soto L., Arciero D.,
RA   Hommes N., Whittaker M., Arp D.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and
RT   obligate chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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 1 lipoyl cofactor 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; AL954747; CAD84271.1; -; Genomic_DNA.
DR   RefSeq; WP_011110995.1; NC_004757.1.
DR   STRING; 228410.NE0360; -.
DR   EnsemblBacteria; CAD84271; CAD84271; NE0360.
DR   KEGG; neu:NE0360; -.
DR   eggNOG; ENOG4107QSN; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281562; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   PhylomeDB; Q820A3; -.
DR   BioCyc; NEUR228410:ALW85_RS01900-MONOMER; -.
DR   Proteomes; UP000001416; 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; 2.
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   TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:CAD84271.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001416};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:CAD84271.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001416};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:CAD84271.1}.
FT   DOMAIN        6     80       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      155    192       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       84    142       Disordered. {ECO:0000256|MobiDB-lite:
FT                                Q820A3}.
FT   COMPBIAS     84    112       Polar. {ECO:0000256|MobiDB-lite:Q820A3}.
SQ   SEQUENCE   453 AA;  48876 MW;  8EBF550B0D1958FA CRC64;
     MQVAEVKKVL VPDIGDFEDI PVIEIMVKPG DSVQVEDPLI VLESDKATVE VPSPYSGIIR
     EIRVQMGSKV SKDSEILTME VVSAESDNKT TSSQPQPSAG SQPAQPTRPI ETGAGQSEEE
     PAAKPAATTT KPATPSAPIQ IPDHTIDQHN KIIPHASPSV RRFARELGVD LSKVVGTGPK
     QRILKEDVQA FVKQALTGGR NARGGTLDLL PWPHVDFAKF GPIELKSLSR IREISGANLH
     RNWVMIPHVT QFDEADVTDL EALRKNHNET RQNNGTKLTI LAFLIKAVTA ALKKFPEFNA
     SLDNSTTESQ LIIKRYYHLG FAADTPNGLV VPVIRDADQK GVIGIAEELT RLSSLAREGK
     LKPGDMQGAS FTISSLGGIG GTGFTPIINA PEVAILGVSR ASLKPVYQNG QFVPRLVLPL
     SLSYDHRVID GASAARFTAH LASILADMRL ALF
//
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