(data stored in ACNUC7421 zone)

SWISSPROT: A8FP62_SHESH

ID   A8FP62_SHESH            Unreviewed;       387 AA.
AC   A8FP62;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 79.
DE   RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000256|HAMAP-Rule:MF_01620};
DE            EC=2.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01620};
DE   AltName: Full=Acetyl-CoA acyltransferase {ECO:0000256|HAMAP-Rule:MF_01620};
DE   AltName: Full=Beta-ketothiolase {ECO:0000256|HAMAP-Rule:MF_01620};
DE   AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01620};
GN   Name=fadA {ECO:0000256|HAMAP-Rule:MF_01620};
GN   OrderedLocusNames=Ssed_0022 {ECO:0000313|EMBL:ABV34635.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34635.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34635.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34635.1,
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: Catalyzes the final step of fatty acid oxidation in
CC       which acetyl-CoA is released and the CoA ester of a fatty acid two
CC       carbons shorter is formed. {ECO:0000256|HAMAP-Rule:MF_01620,
CC       ECO:0000256|SAAS:SAAS00848546}.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
CC       {ECO:0000256|HAMAP-Rule:MF_01620, ECO:0000256|SAAS:SAAS00848512}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|HAMAP-Rule:MF_01620, ECO:0000256|SAAS:SAAS00848504}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|HAMAP-Rule:MF_01620,
CC       ECO:0000256|SAAS:SAAS00848610}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01620,
CC       ECO:0000256|SAAS:SAAS00848528}.
CC   -!- SIMILARITY: Belongs to the thiolase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01620, ECO:0000256|RuleBase:RU003557,
CC       ECO:0000256|SAAS:SAAS00850636}.
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DR   EMBL; CP000821; ABV34635.1; -; Genomic_DNA.
DR   RefSeq; WP_012004161.1; NC_009831.1.
DR   ProteinModelPortal; A8FP62; -.
DR   STRING; 425104.Ssed_0022; -.
DR   EnsemblBacteria; ABV34635; ABV34635; Ssed_0022.
DR   KEGG; sse:Ssed_0022; -.
DR   eggNOG; ENOG4105CHU; Bacteria.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012239; -.
DR   KO; K00632; -.
DR   OMA; CGGTESM; -.
DR   OrthoDB; POG091H0I7B; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
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; IPR020610; Thiolase_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.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FP62.
DR   SWISS-2DPAGE; A8FP62.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01620,
KW   ECO:0000256|RuleBase:RU003557, ECO:0000256|SAAS:SAAS00850626,
KW   ECO:0000313|EMBL:ABV34635.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01620,
KW   ECO:0000256|SAAS:SAAS00848560};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01620,
KW   ECO:0000256|SAAS:SAAS00848562};
KW   Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01620,
KW   ECO:0000256|SAAS:SAAS00848580};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01620,
KW   ECO:0000256|SAAS:SAAS00848599};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01620,
KW   ECO:0000256|RuleBase:RU003557, ECO:0000256|SAAS:SAAS00850637,
KW   ECO:0000313|EMBL:ABV34635.1}.
FT   DOMAIN        5    254       Thiolase_N. {ECO:0000259|Pfam:PF00108}.
FT   DOMAIN      262    386       Thiolase_C. {ECO:0000259|Pfam:PF02803}.
FT   ACT_SITE     91     91       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01620,
FT                                ECO:0000256|PIRSR:PIRSR000429-1}.
FT   ACT_SITE    343    343       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01620, ECO:0000256|PIRSR:PIRSR000429-
FT                                1}.
FT   ACT_SITE    373    373       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01620, ECO:0000256|PIRSR:PIRSR000429-
FT                                1}.
SQ   SEQUENCE   387 AA;  40943 MW;  204BAD74FF496800 CRC64;
     MKQAVIVDCI RTPMGRSKAG VFRNVRAETL SAELMKALLV RNPQLDPNTI EDVIWGCVQQ
     TLEQGFNIAR NASLLAGLPK QIGGVTVNRL CGSSMDALHQ AARAIMTGQG DTFIIGGVEH
     MGHVPMNHGV DFHPGLANNV AKASGMMGLT AEMLGKMHGI TREQQDEFAV RSHQRAHAAT
     VEGRFANEIH PIEGHDADGA LIKVEHDEVI RPETSMESLS GLRPAFDPAN GTVTAGTSSA
     LSDGASAMLV MEEEKAKALG LPIRARIRSM AVAGCDAAIM GYGPVPATKK ALERANLSID
     DLDVIELNEA FAAQSLPCVK ELGLMDVVDE KINLNGGAIA LGHPLGCSGA RISTTLINLM
     EAKDAKYGLA TMCIGLGQGI ATIFERP
//

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