FABZ_ECOL6
ID FABZ_ECOL6 Reviewed; 151 AA.
AC P0A6Q7; P21774;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ;
DE EC=4.2.1.59;
DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase;
DE Short=(3R)-hydroxymyristoyl-ACP dehydrase;
DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase;
GN Name=fabZ; OrderedLocusNames=c0217;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes
CC the dehydration of short chain beta-hydroxyacyl-ACPs and long chain
CC saturated and unsaturated beta-hydroxyacyl-ACPs (By similarity).
CC {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 -!- SUBUNIT: Oligomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN78709.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN78709.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000210739.1; NC_004431.1.
DR AlphaFoldDB; P0A6Q7; -.
DR SMR; P0A6Q7; -.
DR STRING; 199310.c0217; -.
DR EnsemblBacteria; AAN78709; AAN78709; c0217.
DR GeneID; 67416256; -.
DR KEGG; ecc:c0217; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_0_6; -.
DR OMA; FPGRPLM; -.
DR Proteomes; UP000001410; 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-EC.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00406; FabZ; 1.
DR InterPro; IPR013114; FabA_FabZ.
DR InterPro; IPR010084; FabZ.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR30272; PTHR30272; 1.
DR Pfam; PF07977; FabA; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR01750; fabZ; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lyase.
FT CHAIN 1..151
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000091674"
FT ACT_SITE 54
FT /evidence="ECO:0000250"
SQ SEQUENCE 151 AA; 17033 MW; 91F514A7319C2FB1 CRC64;
MTTNTHTLQI EEILELLPHR FPFLLVDRVL DFEEGRFLRA VKNVSVNEPF FQGHFPGKPI
FPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVTFEKT
RRGLTRFKGV ALVDGKVVCE ATMMCARSRE A