(data stored in ACNUC7421 zone)

SWISSPROT: FABZ_ECODH

ID   FABZ_ECODH              Reviewed;         151 AA.
AC   B1XD49;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 54.
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=ECDH10B_0160;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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: A (3R)-3-hydroxyacyl-[acyl-carrier protein] =
CC       a trans-2-enoyl-[acyl-carrier protein] + H(2)O.
CC       {ECO:0000255|HAMAP-Rule:MF_00406}.
CC   -!- SUBUNIT: Oligomer. {ECO:0000255|HAMAP-Rule:MF_00406}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}.
CC   -!- PTM: The N-terminus is blocked. {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; CP000948; ACB01358.1; -; Genomic_DNA.
DR   RefSeq; WP_000210739.1; NC_010473.1.
DR   ProteinModelPortal; B1XD49; -.
DR   SMR; B1XD49; -.
DR   EnsemblBacteria; ACB01358; ACB01358; ECDH10B_0160.
DR   KEGG; ecd:ECDH10B_0160; -.
DR   eggNOG; ENOG4108YXN; Bacteria.
DR   eggNOG; COG0764; LUCA.
DR   HOGENOM; HOG000277829; -.
DR   KO; K02372; -.
DR   OMA; FPGRPLM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00406; FabZ; 1.
DR   InterPro; IPR013114; FabA_FabZ.
DR   InterPro; IPR010084; FabZ.
DR   InterPro; IPR029069; HotDog_dom.
DR   Pfam; PF07977; FabA; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   TIGRFAMs; TIGR01750; fabZ; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XD49.
DR   SWISS-2DPAGE; B1XD49.
KW   Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Lyase.
FT   CHAIN         1    151       3-hydroxyacyl-[acyl-carrier-protein]
FT                                dehydratase FabZ.
FT                                /FTId=PRO_1000197296.
FT   ACT_SITE     54     54       {ECO:0000255|HAMAP-Rule:MF_00406}.
SQ   SEQUENCE   151 AA;  17033 MW;  91F514A7319C2FB1 CRC64;
     MTTNTHTLQI EEILELLPHR FPFLLVDRVL DFEEGRFLRA VKNVSVNEPF FQGHFPGKPI
     FPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVTFEKT
     RRGLTRFKGV ALVDGKVVCE ATMMCARSRE A
//

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