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FABA_YERPG
ID   FABA_YERPG              Reviewed;         172 AA.
AC   A9R7H1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
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};
GN   OrderedLocusNames=YpAngola_A1942;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX87138.1; -; Genomic_DNA.
DR   RefSeq; WP_002220006.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R7H1; -.
DR   SMR; A9R7H1; -.
DR   GeneID; 66842115; -.
DR   KEGG; ypg:YpAngola_A1942; -.
DR   PATRIC; fig|349746.12.peg.2918; -.
DR   OMA; FDCHFKG; -.
DR   UniPathway; UPA00094; -.
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_1000201230"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
SQ   SEQUENCE   172 AA;  18810 MW;  19037054D0A721EC CRC64;
     MVDKRESYTK EDLEASGRGE LFGAGGPPLP AGNMLMMDRI VKMIEDGGSH NKGYVEAELD
     INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
     DAKKVTYRIN FKRVIMRKLI MGVADGEVLV DGKVIYTATD LKVGLFKDTN AF
 
 
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