FABZ_HELPH
ID FABZ_HELPH Reviewed; 159 AA.
AC Q1CRN3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000255|HAMAP-Rule:MF_00406};
DE EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00406};
DE AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00406};
DE Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000255|HAMAP-Rule:MF_00406};
DE AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000255|HAMAP-Rule:MF_00406};
GN Name=fabZ {ECO:0000255|HAMAP-Rule:MF_00406}; OrderedLocusNames=HPAG1_1322;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00406}.
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_00406};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00406}.
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DR EMBL; CP000241; ABF85389.1; -; Genomic_DNA.
DR RefSeq; WP_000438051.1; NC_008086.1.
DR AlphaFoldDB; Q1CRN3; -.
DR SMR; Q1CRN3; -.
DR EnsemblBacteria; ABF85389; ABF85389; HPAG1_1322.
DR KEGG; hpa:HPAG1_1322; -.
DR HOGENOM; CLU_078912_1_0_7; -.
DR OMA; FPGRPLM; -.
DR OrthoDB; 1763197at2; -.
DR Proteomes; UP000008835; 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..159
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000301898"
FT ACT_SITE 58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ SEQUENCE 159 AA; 18168 MW; F7EB7DBB8603200F CRC64;
MEQSHQNLQS QFFIEHILQI LPHRYPMLLV DRIIELQANK KIAAYKNITF NEDVFNGHFP
NKPIFPGVLI VEGMAQSGGF LAFTSLWGFD PEIAKTKIVY FMTIDKVKFR IPVTPGDRLE
YHLEVLKHKG MIWQVGGTAQ VDGKVVAEAE LKAMIAERE
