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FABA_SHEDO
ID   FABA_SHEDO              Reviewed;         171 AA.
AC   Q12LD1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Sden_2465;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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: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; CP000302; ABE55745.1; -; Genomic_DNA.
DR   RefSeq; WP_011496896.1; NC_007954.1.
DR   AlphaFoldDB; Q12LD1; -.
DR   SMR; Q12LD1; -.
DR   STRING; 318161.Sden_2465; -.
DR   EnsemblBacteria; ABE55745; ABE55745; Sden_2465.
DR   KEGG; sdn:Sden_2465; -.
DR   eggNOG; COG0764; Bacteria.
DR   HOGENOM; CLU_097925_0_0_6; -.
DR   OMA; FDCHFKG; -.
DR   OrthoDB; 1379832at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001982; 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; Reference proteome.
FT   CHAIN           1..171
FT                   /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT                   dehydratase"
FT                   /id="PRO_0000267750"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
SQ   SEQUENCE   171 AA;  18759 MW;  81E497897E3FE175 CRC64;
     MEKANSFTKE QLIACGQGEL LGANSPKLPI DNMLMVDRIV RINEDGGAFG KGEIIAELDI
     NPTLWFFDCH FKGDPVMPGC LGLDAMWQLV GFYLGWEGAQ GKGRALGVGE VKFTGQVLPD
     AKKVTYKLNI KRKIHRKLVM GIADATMEVD GREIYSATDL KVGIFSDTST F
 
 
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