GenomeNet

Database: UniProt/SWISS-PROT
Entry: FABZ_PSEA8
LinkDB: FABZ_PSEA8
Original site: FABZ_PSEA8 
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
//
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