FADI_VIBCH
ID FADI_VIBCH Reviewed; 435 AA.
AC Q9KT59;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 109.
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=VC_1046;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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_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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF94205.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94205.1; ALT_INIT; Genomic_DNA.
DR PIR; E82248; E82248.
DR RefSeq; NP_230691.2; NC_002505.1.
DR RefSeq; WP_000517921.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KT59; -.
DR SMR; Q9KT59; -.
DR STRING; 243277.VC_1046; -.
DR DNASU; 2614316; -.
DR EnsemblBacteria; AAF94205; AAF94205; VC_1046.
DR GeneID; 57739727; -.
DR GeneID; 66939735; -.
DR KEGG; vch:VC_1046; -.
DR PATRIC; fig|243277.26.peg.998; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OMA; MTAFPEP; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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_0000206449"
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; 46354 MW; 600CA5A5DCBF7270 CRC64;
MGKQEVRTRS GERVAIVAGL RTPFARQSTE FGQVPAVDLG KMVVQEMMAR TAIDPKLIEQ
VVFGQVVQMP EAPNIAREIV LGTGMSINTD AYSVTRACAT SFQAAVNVAE SIMAGSIDIG
IAGGADSSSV LPIGVSKKLA ASLLALSKTK TVGQKLKLLS NLSFKDLMPV PPAVAEYSTG
LSMGQTAEQM AKSYAISRAE QDALAHRSHT LAAQAWAEGK IRDEVMTAFP EPYKKWLDMD
NNIRMDSKLE SYAKLRPAFD RQYGSVTAAN STPLTDGAAA IMLMREGKAK ELGLEIMGYI
RSYAFAAIGV EKDMLMGPSY ATPIALDRAG ITLNDLTLID MHEAFAAQTL ANLKMFASDK
FAQEQLGRAQ AIGEVDMSKF NVLGGSLAYG HPFAATGARM ITQTLRELKR RGGGLALNTA
CAAGGLGAAM ILEVE
