ID A0A176YPD0_9BRAD Unreviewed; 173 AA.
AC A0A176YPD0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AYJ54_15725 {ECO:0000313|EMBL:OAF08186.1};
OS Bradyrhizobium centrolobii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAF08186.1, ECO:0000313|Proteomes:UP000076959};
RN [1] {ECO:0000313|EMBL:OAF08186.1, ECO:0000313|Proteomes:UP000076959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10245 {ECO:0000313|EMBL:OAF08186.1,
RC ECO:0000313|Proteomes:UP000076959};
RA Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (MAR-2016) 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:OAF08186.1}.
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DR EMBL; LUUB01000063; OAF08186.1; -; Genomic_DNA.
DR RefSeq; WP_063701613.1; NZ_LUUB01000063.1.
DR AlphaFoldDB; A0A176YPD0; -.
DR STRING; 1505087.AYJ54_15725; -.
DR OrthoDB; 9786735at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000076959; 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}.
FT ACT_SITE 71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00405"
SQ SEQUENCE 173 AA; 19179 MW; 2683DB512BD0EE7B CRC64;
MLNRRNGYEY EDLLTCARGE MFGPGNAQLP LPPMLMFDRI TEISDAGGEF GKGLVRAELD
VKPDLWFFGC HFKNDPVMPG CLGLDALWQM VGFYLGWIGG EGRGRALGLS ELKFGGQVLT
EARKVVYNVD IKRVMRSKLV LGIADGWLSV DDTIIYRAKD LKVGLFKQGT TLG
//
