ID A0A0J8YKF5_9GAMM Unreviewed; 172 AA.
AC A0A0J8YKF5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase {ECO:0000256|HAMAP-Rule:MF_00405};
DE EC=4.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00405};
DE AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA {ECO:0000256|HAMAP-Rule:MF_00405};
DE AltName: Full=Beta-hydroxydecanoyl thioester dehydrase {ECO:0000256|HAMAP-Rule:MF_00405};
DE AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase {ECO:0000256|HAMAP-Rule:MF_00405};
DE EC=5.3.3.14 {ECO:0000256|HAMAP-Rule:MF_00405};
GN Name=fabA {ECO:0000256|HAMAP-Rule:MF_00405};
GN ORFNames=AI28_21030 {ECO:0000313|EMBL:KMV69925.1};
OS bacteria symbiont BFo1 of Frankliniella occidentalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae.
OX NCBI_TaxID=1628855 {ECO:0000313|EMBL:KMV69925.1, ECO:0000313|Proteomes:UP000037152};
RN [1] {ECO:0000313|EMBL:KMV69925.1, ECO:0000313|Proteomes:UP000037152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFo1 {ECO:0000313|EMBL:KMV69925.1,
RC ECO:0000313|Proteomes:UP000037152};
RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT occidentalis [Pergande]).";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for the introduction of cis unsaturation into fatty
CC acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-
CC (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can
CC catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with
CC saturated chain lengths up to 16:0, being most active on intermediate
CC chain length. {ECO:0000256|HAMAP-Rule:MF_00405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-decenoyl-[ACP] = (3Z)-decenoyl-[ACP];
CC Xref=Rhea:RHEA:23568, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9927,
CC ChEBI:CHEBI:78467, ChEBI:CHEBI:78798; EC=5.3.3.14;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000256|ARBA:ARBA00001055, ECO:0000256|HAMAP-
CC Rule:MF_00405};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|HAMAP-Rule:MF_00405}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00405}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00405}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC subfamily. {ECO:0000256|ARBA:ARBA00006714, ECO:0000256|HAMAP-
CC Rule:MF_00405}.
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:KMV69925.1}.
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DR EMBL; JMSO01000144; KMV69925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8YKF5; -.
DR PATRIC; fig|1628855.3.peg.4244; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000037152; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008693; F:(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0034017; F:trans-2-decenoyl-acyl-carrier-protein isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01287; FabA; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR HAMAP; MF_00405; FabA; 1.
DR InterPro; IPR010083; FabA.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
DR NCBIfam; TIGR01749; fabA; 1.
DR PANTHER; PTHR30272; 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE; 1.
DR PANTHER; PTHR30272:SF8; 3-HYDROXYDECANOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE; 1.
DR Pfam; PF07977; FabA; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00405};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_00405};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_00405};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00405};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00405};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00405};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00405, ECO:0000313|EMBL:KMV69925.1}.
FT ACT_SITE 71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00405"
SQ SEQUENCE 172 AA; 18798 MW; 7607AA04F87F512E CRC64;
MVDKRDSYTK EDLIASGRGE LFGAEGPPLP SGNMLMMDRV VKMSEDGGNY GKGFVEAELD
INPDLWFFSC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGA EGKGRALGVG EVKFTGQVLP
SAKKVSYRIH FKRVINRKLV MGVADGEVLV DGHVIYTATD LKVGLFKDTT AF
//
