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FABA_ALKEH
ID   FABA_ALKEH              Reviewed;         176 AA.
AC   Q0A8W4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=Mlg_1374;
OS   Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
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   Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA   Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA   Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI56723.1; -; Genomic_DNA.
DR   RefSeq; WP_011629118.1; NC_008340.1.
DR   AlphaFoldDB; Q0A8W4; -.
DR   SMR; Q0A8W4; -.
DR   EnsemblBacteria; ABI56723; ABI56723; Mlg_1374.
DR   KEGG; aeh:Mlg_1374; -.
DR   eggNOG; COG0764; Bacteria.
DR   HOGENOM; CLU_097925_0_0_6; -.
DR   OMA; FDCHFKG; -.
DR   OrthoDB; 1379832at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001962; 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..176
FT                   /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT                   dehydratase"
FT                   /id="PRO_0000267720"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
SQ   SEQUENCE   176 AA;  19520 MW;  0C416AB285406173 CRC64;
     MTRQESYNFD ELLLSGHGRL FGPGNPQLPA PQMLMFHRIT QMSEEGGAYD KGQVIAELDL
     DPDLWFFRCH FPGDPVMPGC LGLDALWQLV GFYLGWIGGS GKGRALGCGE VKFSGQILPE
     HKKVTYEIAF KRVINRRLVM GIADGWVSVD GEQIYTAKDL KVGLFQDPGD LSRSQG
 
 
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