FABA_SALEP
ID FABA_SALEP Reviewed; 172 AA.
AC B5QZF7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00405};
DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00405};
DE AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA {ECO:0000255|HAMAP-Rule:MF_00405};
DE AltName: Full=Beta-hydroxydecanoyl thioester dehydrase {ECO:0000255|HAMAP-Rule:MF_00405};
DE AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase {ECO:0000255|HAMAP-Rule:MF_00405};
DE EC=5.3.3.14 {ECO:0000255|HAMAP-Rule:MF_00405};
GN Name=fabA {ECO:0000255|HAMAP-Rule:MF_00405}; OrderedLocusNames=SEN0932;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00405};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_00405}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00405}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00405}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00405}.
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DR EMBL; AM933172; CAR32515.1; -; Genomic_DNA.
DR RefSeq; WP_000227928.1; NC_011294.1.
DR AlphaFoldDB; B5QZF7; -.
DR SMR; B5QZF7; -.
DR KEGG; set:SEN0932; -.
DR HOGENOM; CLU_097925_0_0_6; -.
DR OMA; FDCHFKG; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000613; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[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 HAMAP; MF_00405; FabA; 1.
DR InterPro; IPR010083; FabA.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR30272; PTHR30272; 1.
DR PANTHER; PTHR30272:SF8; PTHR30272:SF8; 1.
DR Pfam; PF07977; FabA; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR01749; fabA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Lyase.
FT CHAIN 1..172
FT /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT dehydratase"
FT /id="PRO_1000201200"
FT ACT_SITE 71
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
SQ SEQUENCE 172 AA; 19047 MW; DFD69583E5C0782C CRC64;
MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF DKGYVEAELD
INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
TARKVTYRIH FKRIVNRRLI MGLADGEVLV DGRLIYTAHD LKVGLFQDTS AF
