FABZ_HELPY
ID FABZ_HELPY Reviewed; 159 AA.
AC O25928;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=HP_1376;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08419.1; -; Genomic_DNA.
DR PIR; H64691; H64691.
DR RefSeq; NP_208167.1; NC_000915.1.
DR RefSeq; WP_000438056.1; NC_018939.1.
DR PDB; 2GLL; X-ray; 2.20 A; A/B/C/D/E/F=1-158.
DR PDB; 2GLM; X-ray; 2.60 A; A/B/C/D/E/F=1-158.
DR PDB; 2GLP; X-ray; 2.42 A; A/B/C/D/E/F=1-158.
DR PDB; 2GLV; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
DR PDBsum; 2GLL; -.
DR PDBsum; 2GLM; -.
DR PDBsum; 2GLP; -.
DR PDBsum; 2GLV; -.
DR AlphaFoldDB; O25928; -.
DR SMR; O25928; -.
DR IntAct; O25928; 1.
DR STRING; 85962.C694_07100; -.
DR BindingDB; O25928; -.
DR DrugBank; DB07445; N'-[(1E)-(3,5-DIBROMO-2,4-DIHYDROXYPHENYL)METHYLENE]NICOTINOHYDRAZIDE.
DR PaxDb; O25928; -.
DR EnsemblBacteria; AAD08419; AAD08419; HP_1376.
DR KEGG; hpy:HP_1376; -.
DR PATRIC; fig|85962.47.peg.1473; -.
DR eggNOG; COG0764; Bacteria.
DR OMA; FPGRPLM; -.
DR PhylomeDB; O25928; -.
DR EvolutionaryTrace; O25928; -.
DR PRO; PR:O25928; -.
DR Proteomes; UP000000429; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Reference proteome.
FT CHAIN 1..159
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000091688"
FT ACT_SITE 58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:2GLL"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2GLL"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2GLL"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2GLL"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2GLL"
FT HELIX 67..87
FT /evidence="ECO:0007829|PDB:2GLL"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:2GLL"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:2GLL"
FT STRAND 118..141
FT /evidence="ECO:0007829|PDB:2GLL"
FT STRAND 144..157
FT /evidence="ECO:0007829|PDB:2GLL"
SQ SEQUENCE 159 AA; 18196 MW; 715B6FBED872AE32 CRC64;
MEQSHQNLQS QFFIEHILQI LPHRYPMLLV DRIIELQANK KIVAYKNITF NEDVFNGHFP
NKPIFPGVLI VEGMAQTGGF LAFTSLWGFD PEIAKTKIVY FMTIDKVKFR IPVTPGDRLE
YHLEVLKHKG MIWQVGGTAQ VDGKVVAEAE LKAMIAERD
