FABA_CROS8
ID FABA_CROS8 Reviewed; 172 AA.
AC A7MEX0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, 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=ESA_02394;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(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; CP000783; ABU77640.1; -; Genomic_DNA.
DR RefSeq; WP_004385423.1; NC_009778.1.
DR AlphaFoldDB; A7MEX0; -.
DR SMR; A7MEX0; -.
DR EnsemblBacteria; ABU77640; ABU77640; ESA_02394.
DR GeneID; 45716077; -.
DR GeneID; 56731164; -.
DR KEGG; esa:ESA_02394; -.
DR HOGENOM; CLU_097925_0_0_6; -.
DR OMA; FDCHFKG; -.
DR OrthoDB; 1379832at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000260; 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_1000049824"
FT ACT_SITE 71
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00405"
SQ SEQUENCE 172 AA; 18932 MW; F35C6A4F4C29B564 CRC64;
MVDKRESYTK EDLLASGRGE LFGANGPQLP APNMLMMDRV VKMTETGGNF DKGYVEAELD
INPDMWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
SAKKVTYRIH FKRVVNRRLV MGIADGEVLV DGKQIYTATD LKVGLFQDTS AF
