ID A0A097R118_HAFAL Unreviewed; 172 AA.
AC A0A097R118;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=AT03_08505 {ECO:0000313|EMBL:AIU72428.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU72428.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU72428.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU72428.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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}.
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DR EMBL; CP009706; AIU72428.1; -; Genomic_DNA.
DR RefSeq; WP_025801007.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R118; -.
DR GeneID; 78450163; -.
DR KEGG; hav:AT03_08505; -.
DR PATRIC; fig|1453496.5.peg.1699; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_097925_0_0_6; -.
DR OrthoDB; 9786735at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000029986; Chromosome.
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:AIU72428.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029986}.
FT ACT_SITE 71
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00405"
SQ SEQUENCE 172 AA; 18863 MW; E9CA11EFDE9BC326 CRC64;
MVDKRESYTK EDLEASGRGE LFGAGGPPLP SGNMLMMDRV VKMTEDGGNY NKGYVEAELD
INPDLWFFGC HFVGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
TAKKVTYRIH FKRVINRRLI MGMADGEVLV DGQVIYNASD LKVGLFKDTS AF
//