FABA_SHIFL
ID FABA_SHIFL Reviewed; 172 AA.
AC P0A6Q5; P18391; Q59383;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase;
DE EC=4.2.1.59;
DE AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA;
DE AltName: Full=Beta-hydroxydecanoyl thioester dehydrase;
DE AltName: Full=Trans-2-decenoyl-[acyl-carrier-protein] isomerase;
DE EC=5.3.3.14;
GN Name=fabA; OrderedLocusNames=SF0954, S1020;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 (By similarity). {ECO:0000250}.
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 -!- 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 -!- 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabA
CC subfamily. {ECO:0000305}.
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DR EMBL; AE005674; AAN42583.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16468.1; -; Genomic_DNA.
DR RefSeq; NP_706876.1; NC_004337.2.
DR RefSeq; WP_000227927.1; NZ_SUPT01000004.1.
DR AlphaFoldDB; P0A6Q5; -.
DR SMR; P0A6Q5; -.
DR STRING; 198214.SF0954; -.
DR DrugBank; DB03813; 2-Decenoyl N-Acetyl Cysteamine.
DR PRIDE; P0A6Q5; -.
DR EnsemblBacteria; AAN42583; AAN42583; SF0954.
DR EnsemblBacteria; AAP16468; AAP16468; S1020.
DR GeneID; 1023905; -.
DR GeneID; 67414158; -.
DR KEGG; sfl:SF0954; -.
DR KEGG; sfx:S1020; -.
DR PATRIC; fig|198214.7.peg.1112; -.
DR HOGENOM; CLU_097925_0_0_6; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..172
FT /note="3-hydroxydecanoyl-[acyl-carrier-protein]
FT dehydratase"
FT /id="PRO_0000091616"
FT ACT_SITE 71
FT /evidence="ECO:0000250"
FT VARIANT 76
FT /note="P -> L (in allele FABA6; TS)"
FT VARIANT 102
FT /note="G -> D (in allele FABA2; TS)"
FT CONFLICT 18
FT /note="R -> H (in Ref. 2; AAP16468)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="M -> I (in Ref. 2; AAP16468)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="G -> C (in Ref. 2; AAP16468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 18969 MW; DFC508352D2DCF2C CRC64;
MVDKRESYTK EDLLASGRGE LFGAKGPQLP APNMLMMDRV VKMTETGGNF DKGYVEAELD
INPDLWFFGC HFIGDPVMPG CLGLDAMWQL VGFYLGWLGG EGKGRALGVG EVKFTGQVLP
TAKKVTYRIH FKRIVNRRLI MGLADGEVLV DGRLIYTASD LKVGLFQDTS AF
