(data stored in ACNUC1104 zone)

SWISSPROT: D3UWH0_XENBS

ID   D3UWH0_XENBS            Unreviewed;       150 AA.
AC   D3UWH0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000256|HAMAP-Rule:MF_00406};
DE            EC=4.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00406};
DE   AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000256|HAMAP-Rule:MF_00406};
DE            Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000256|HAMAP-Rule:MF_00406};
DE   AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000256|HAMAP-Rule:MF_00406};
GN   Name=fabZ {ECO:0000256|HAMAP-Rule:MF_00406,
GN   ECO:0000313|EMBL:CBJ79744.1};
GN   OrderedLocusNames=XBJ1_0600 {ECO:0000313|EMBL:CBJ79744.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79744.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79744.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79744.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|HAMAP-Rule:MF_00406, ECO:0000256|SAAS:SAAS00371087}.
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:0000256|HAMAP-Rule:MF_00406,
CC         ECO:0000256|SAAS:SAAS01122688};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00406,
CC       ECO:0000256|SAAS:SAAS00064863}.
CC   -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00406,
CC       ECO:0000256|SAAS:SAAS00829032}.
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DR   EMBL; FN667741; CBJ79744.1; -; Genomic_DNA.
DR   RefSeq; WP_012987198.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0600; -.
DR   EnsemblBacteria; CBJ79744; CBJ79744; XBJ1_0600.
DR   GeneID; 8830222; -.
DR   KEGG; xbo:XBJ1_0600; -.
DR   PATRIC; fig|406818.4.peg.553; -.
DR   eggNOG; ENOG4108YXN; Bacteria.
DR   eggNOG; COG0764; LUCA.
DR   HOGENOM; HOG000277829; -.
DR   KO; K02372; -.
DR   OMA; FPGRPLM; -.
DR   BioCyc; XBOV406818:XBJ1_RS02610-MONOMER; -.
DR   Proteomes; UP000002045; 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: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;
DR   PRODOM; D3UWH0.
DR   SWISS-2DPAGE; D3UWH0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00406,
KW   ECO:0000256|SAAS:SAAS00064829};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00406,
KW   ECO:0000256|SAAS:SAAS00064858};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00406,
KW   ECO:0000256|SAAS:SAAS00448566};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00406,
KW   ECO:0000256|SAAS:SAAS00448576};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00406, ECO:0000256|SAAS:SAAS00448581,
KW   ECO:0000313|EMBL:CBJ79744.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       16    141       FabA. {ECO:0000259|Pfam:PF07977}.
FT   ACT_SITE     53     53       {ECO:0000256|HAMAP-Rule:MF_00406}.
SQ   SEQUENCE   150 AA;  16879 MW;  18A98ED0513DF84B CRC64;
     MSDNRTLQIE EILDLLPHRY PFLLVDRVLD FEEGKFLRAV KNVSFNEPFF QGHFPGKPIF
     PGVLILEAMA QATGILAFKS VGSLAPGELY YFAAIDGARF KRPVLPGDQM VLEVEFIKER
     RGVARFKGVA KVDGEVACEA EMMCARRREA
//

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