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FABZ_MARMS
ID   FABZ_MARMS              Reviewed;         145 AA.
AC   A6VUT3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Mmwyl1_1283;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000749; ABR70212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VUT3; -.
DR   SMR; A6VUT3; -.
DR   STRING; 400668.Mmwyl1_1283; -.
DR   EnsemblBacteria; ABR70212; ABR70212; Mmwyl1_1283.
DR   KEGG; mmw:Mmwyl1_1283; -.
DR   eggNOG; COG0764; Bacteria.
DR   HOGENOM; CLU_078912_1_2_6; -.
DR   OMA; FPGRPLM; -.
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   3: Inferred from homology;
KW   Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Lyase.
FT   CHAIN           1..145
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_1000080440"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   145 AA;  16415 MW;  B18378B3A96539C8 CRC64;
     MMDVNEIRQY LPHRYPFLLV DRIVEINLND SIIAYKNVTI NEPFFNGHFP NHPVMPGVLI
     IEAMAQAAGV LGFKSMDKKP EDGSIYYFVG ADNARFKRPV VPGDRLQLEA KIIAEKRGIW
     KFECRATVDG QLACSATIMC ADRKI
 
 
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