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FABA_CAUVN
ID   FABA_CAUVN              Reviewed;         170 AA.
AC   B8GVZ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=CCNA_03836;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(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; CP001340; ACL97301.1; -; Genomic_DNA.
DR   RefSeq; WP_010921547.1; NC_011916.1.
DR   RefSeq; YP_002519209.1; NC_011916.1.
DR   AlphaFoldDB; B8GVZ8; -.
DR   SMR; B8GVZ8; -.
DR   PRIDE; B8GVZ8; -.
DR   EnsemblBacteria; ACL97301; ACL97301; CCNA_03836.
DR   GeneID; 7332684; -.
DR   KEGG; ccs:CCNA_03836; -.
DR   PATRIC; fig|565050.3.peg.3741; -.
DR   HOGENOM; CLU_097925_0_0_5; -.
DR   OMA; FDCHFKG; -.
DR   OrthoDB; 1379832at2; -.
DR   PhylomeDB; B8GVZ8; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001364; 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..170
FT                   /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT                   dehydratase"
FT                   /id="PRO_1000201174"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
SQ   SEQUENCE   170 AA;  18759 MW;  2316A43A815E2A19 CRC64;
     MQKNAYTFEE LLACGRGEMF GPGNAQLPAP PMLMFDRIVR IEAEGGKYGK GYVEAEFDIR
     PDLWFFDCHF IGDPVMPGCL GLDAMWQLVG FFLGWSGGPG RGRALGVGEV KFTGQVTPDI
     KKVVYKIDLK RVIMRKLVMG IADGVLEADG KVIYETSDLK VGLFTPEQMA
 
 
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