FADI_VIBC3
ID FADI_VIBC3 Reviewed; 435 AA.
AC A5F2P1; C3LZ56;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 83.
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}; Synonyms=hadHB;
GN OrderedLocusNames=VC0395_A0564, VC395_1060;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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=ABQ21909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACP09072.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000627; ABQ21909.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001235; ACP09072.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000517924.1; NZ_JAACZH010000005.1.
DR AlphaFoldDB; A5F2P1; -.
DR SMR; A5F2P1; -.
DR STRING; 345073.VC395_1060; -.
DR EnsemblBacteria; ABQ21909; ABQ21909; VC0395_A0564.
DR KEGG; vco:VC0395_A0564; -.
DR KEGG; vcr:VC395_1060; -.
DR PATRIC; fig|345073.21.peg.1028; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000249; Chromosome 2.
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; Transferase.
FT CHAIN 1..435
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000323534"
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; 46384 MW; 9CAB6A8D6A705328 CRC64;
MGKQEVRTRS GERVAIVAGL RTPFARQSTE FGQVPAVDLG KMVVQEMMAR TAIDPKLIEQ
VVFGQVVQMP EAPNIAREIV LGTGMSINTD AYSVTRACAT SFQAAVNVAE SIMAGSIDIG
IAGGADSSSV LPIGVSKKLA ASLLALSKTK TVGQKLKLLS NLSFKDLMPV PPAVAEYSTG
LSMGQTAEQM AKSYAISRAE QDALAHRSHT LAAQAWTEGK IRDEVMTAFP EPYKKWLDMD
NNIRMDSKLE SYAKLRPAFD RQYGSVTAAN STPLTDGAAA IMLMREGKAK ELGLEIMGYI
RSYAFAAIGV EKDMLMGPSY ATPIALDRAG ITLNDLTLID MHEAFAAQTL ANLKMFASDK
FAQEQLGRAQ AIGEVDMSKF NVLGGSLAYG HPFAATGARM ITQTLRELKR RGGGLALNTA
CAAGGLGAAM ILEVE
