FADI_VIBVY
ID FADI_VIBVY Reviewed; 435 AA.
AC Q7MIS4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000255|HAMAP-Rule:MF_01618};
DE EC=2.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01618};
DE AltName: Full=ACSs {ECO:0000255|HAMAP-Rule:MF_01618};
DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000255|HAMAP-Rule:MF_01618};
DE AltName: Full=Acyl-CoA ligase {ECO:0000255|HAMAP-Rule:MF_01618};
DE AltName: Full=Beta-ketothiolase {ECO:0000255|HAMAP-Rule:MF_01618};
DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01618};
GN Name=fadI {ECO:0000255|HAMAP-Rule:MF_01618}; OrderedLocusNames=VV2441;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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_01618}.
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_01618};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000255|HAMAP-Rule:MF_01618}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC (FadI). {ECO:0000255|HAMAP-Rule:MF_01618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01618}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01618}.
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DR EMBL; BA000037; BAC95205.1; -; Genomic_DNA.
DR RefSeq; WP_011150895.1; NC_005139.1.
DR AlphaFoldDB; Q7MIS4; -.
DR SMR; Q7MIS4; -.
DR STRING; 672.VV93_v1c21440; -.
DR EnsemblBacteria; BAC95205; BAC95205; BAC95205.
DR KEGG; vvy:VV2441; -.
DR PATRIC; fig|196600.6.peg.2447; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 330994at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002675; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01618; FadI; 1.
DR InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; TIGR02446; FadI; 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..435
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206453"
FT ACT_SITE 98
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01618"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01618"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01618"
SQ SEQUENCE 435 AA; 46026 MW; 2044264BD28A662F CRC64;
MGKQEVKTRQ GERVAIVAGL RTPFARQSTE FSQVPAVDLG KMVVSDLLAR TDIDPKLIDQ
VVFGQVVQMP EAPNIAREIV LGTGMNIHTD AYSVTRACAT SFQSAVNVAE SIMAGAIDIG
IAGGADSSSV LPIGVSKKLA ASLLALSKTK TLGQKLKVLS GLGLKDLMPV PPAVAEYSTG
LSMGQTAEQM AKTHGITRAE QDALAHRSHT LASQAWRDGK IAGEVMTAFP EPYKKWIAED
NNIRHDSTLE GYAKLRPAFD RQYGSVTAAN STPLTDGAAA VLLMREGRAK ELGMEILGYI
RGYAFSAIGV ESDMLMGPSY ATSKVLQSTG LALSDLTLID MHEAFAAQAL ANVKMFASDK
FAQENLGRSK AMGEIDMDKF NVLGGSIAYG HPFAATGARM MTQTLRELKR RGGGLALNTA
CAAGGLGAAM ILEVE
