ID A0A0M0HS39_VIBNE Unreviewed; 391 AA.
AC A0A0M0HS39;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ECO:0000313|EMBL:KOO04879.1};
GN ORFNames=AKJ17_03055 {ECO:0000313|EMBL:KOO04879.1};
OS Vibrio nereis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=693 {ECO:0000313|EMBL:KOO04879.1, ECO:0000313|Proteomes:UP000037515};
RN [1] {ECO:0000313|Proteomes:UP000037515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19584 {ECO:0000313|Proteomes:UP000037515};
RA Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT isolated from the Solomon Islands.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01620};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01620}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|HAMAP-Rule:MF_01620,
CC ECO:0000256|RuleBase:RU003557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO04879.1}.
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DR EMBL; LHPJ01000003; KOO04879.1; -; Genomic_DNA.
DR RefSeq; WP_053394315.1; NZ_LHPJ01000003.1.
DR AlphaFoldDB; A0A0M0HS39; -.
DR STRING; 693.AKJ17_03055; -.
DR PATRIC; fig|693.5.peg.613; -.
DR OrthoDB; 8951704at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000037515; Unassembled WGS sequence.
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; -; 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR NCBIfam; TIGR02445; fadA; 1.
DR PANTHER; PTHR43853:SF11; 3-KETOACYL-COA THIOLASE FADA; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01620};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_01620};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01620}; Reference proteome {ECO:0000313|Proteomes:UP000037515};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01620,
KW ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 8..258
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 266..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620,
FT ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 41191 MW; CBFB88BA5C544DB3 CRC64;
MTLNTRNVVV VDCLRTPMGR SKGGAFRHTR AEDLSAHLMK GILARNPQVN PSEIEDIYWG
CVQQTLEQGF NVARNAALLA GLPIEVGAVT VNRLCGSSMQ ALHDGTRAIM TGDAEICLIG
GVEHMGHVPM NHGVDFHPGM AKNVAKAAGM MGLTAEMLGK LHGISREQQD AFAARSHARA
HAATVEGRFK SEILPIEAHA ADGTLFTLDY DEVIRPETTV EGLSQLRPVF DPANGTVTAG
SSSALSDGAS AMLIMSEEKA NELGLTIRAR IKGMAIAGCD PSIMGYGPVP ATKKALKRAG
LSIEDMDVVE LNEAFAAQSL PCAKDLGLLD VVDEKVNLNG GAIALGHPLG CSGSRISTTL
INLMEAKDAK YGLATMCIGL GQGIATVFER P
//
