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FADA_PSEAE
ID   FADA_PSEAE              Reviewed;         391 AA.
AC   Q9HZJ3;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE            EC=2.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01620};
DE   AltName: Full=Acetyl-CoA acyltransferase {ECO:0000255|HAMAP-Rule:MF_01620};
DE   AltName: Full=Beta-ketothiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE   AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01620};
GN   Name=fadA {ECO:0000255|HAMAP-Rule:MF_01620}; OrderedLocusNames=PA3013;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in which
CC       acetyl-CoA is released and the CoA ester of a fatty acid two carbons
CC       shorter is formed. {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01620};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC       (FadA). {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01620}.
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DR   EMBL; AE004091; AAG06401.1; -; Genomic_DNA.
DR   PIR; F83269; F83269.
DR   RefSeq; NP_251703.1; NC_002516.2.
DR   RefSeq; WP_003113978.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZJ3; -.
DR   SMR; Q9HZJ3; -.
DR   STRING; 287.DR97_4924; -.
DR   PaxDb; Q9HZJ3; -.
DR   PRIDE; Q9HZJ3; -.
DR   EnsemblBacteria; AAG06401; AAG06401; PA3013.
DR   GeneID; 880523; -.
DR   KEGG; pae:PA3013; -.
DR   PATRIC; fig|208964.12.peg.3161; -.
DR   PseudoCAP; PA3013; -.
DR   HOGENOM; CLU_031026_2_3_6; -.
DR   InParanoid; Q9HZJ3; -.
DR   OMA; DYYWGMG; -.
DR   PhylomeDB; Q9HZJ3; -.
DR   BioCyc; MetaCyc:MON-17590; -.
DR   BioCyc; PAER208964:G1FZ6-3065-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   HAMAP; MF_01620; FadA; 1.
DR   InterPro; IPR012805; FadA.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   TIGRFAMs; TIGR02445; fadA; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..391
FT                   /note="3-ketoacyl-CoA thiolase"
FT                   /id="PRO_0000206378"
FT   ACT_SITE        95
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ   SEQUENCE   391 AA;  41643 MW;  D04065FACB7E8A73 CRC64;
     MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AETMSAHLIS KLLERNPKVD PAEVEDVIWG
     CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIQ TGNGDVFVIG
     GVEHMGHVGM MHGVDPNPHL SLYAAKASGM MGLTAEMLGK MHGISREAQD KFGARSHQLA
     WKATQEGKFK DEIIPMEGYD ENGFLKVFDF DETIRPETTV ETLAELKPAF NPKGGTVTAG
     TSSQITDGAS CMIVMSAQRA QDLGIQPMAV IRSMAVAGVD PAIMGYGPVP STNKALKRAG
     LTIADIDFVE LNEAFAAQAL PVLKDLKLLD KMDEKVNLHG GAIALGHPFG CSGARISGTL
     LNVMKQNGGT LGVSTMCVGL GQGITTVFER I
 
 
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