ID FABZ_PSEA8 Reviewed; 146 AA.
AC B7V7U3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 08-MAY-2019, entry version 55.
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};
GN OrderedLocusNames=PLES_13901;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L.,
RA Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D.,
RA Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L.,
RA Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants
RT of in vivo competitiveness in the Liverpool epidemic strain of
RT Pseudomonas aeruginosa.";
RL Genome Res. 19:12-23(2009).
CC -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis.
CC Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and
CC long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
CC {ECO:0000255|HAMAP-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;
CC EC=4.2.1.59; 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}.
DR EMBL; FM209186; CAW26118.1; -; Genomic_DNA.
DR RefSeq; WP_003092375.1; NC_011770.1.
DR SMR; B7V7U3; -.
DR PRIDE; B7V7U3; -.
DR EnsemblBacteria; CAW26118; CAW26118; PLES_13901.
DR KEGG; pag:PLES_13901; -.
DR HOGENOM; HOG000277829; -.
DR KO; K02372; -.
DR OMA; FPGRPLM; -.
DR BioCyc; PAER557722:G1GIH-1478-MONOMER; -.
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:0047451; F:3-hydroxyoctanoyl-[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 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 1 146 3-hydroxyacyl-[acyl-carrier-protein]
FT dehydratase FabZ.
FT /FTId=PRO_1000123653.
FT ACT_SITE 49 49 {ECO:0000255|HAMAP-Rule:MF_00406}.
SQ SEQUENCE 146 AA; 16774 MW; BC7D53E61F5E44CB CRC64;
MMDINEIREY LPHRYPFLLV DRVVELDIEG KRIRAYKNVS INEPFFNGHF PEHPIMPGVL
IIEAMAQAAG ILGFKMLDVK PADGTLYYFV GSDKLRFRQP VLPGDQLQLH AKFISVKRSI
WKFDCHATVD DKPVCSAEII CAERKL
//
