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FABZ_SALPA
ID   FABZ_SALPA              Reviewed;         151 AA.
AC   Q5PD74;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=SPA0234;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76263.1; -; Genomic_DNA.
DR   RefSeq; WP_000210741.1; NC_006511.1.
DR   AlphaFoldDB; Q5PD74; -.
DR   SMR; Q5PD74; -.
DR   EnsemblBacteria; AAV76263; AAV76263; SPA0234.
DR   GeneID; 66754751; -.
DR   KEGG; spt:SPA0234; -.
DR   HOGENOM; CLU_078912_1_0_6; -.
DR   OMA; FPGRPLM; -.
DR   Proteomes; UP000008185; 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: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..151
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_0000091724"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   151 AA;  16999 MW;  71151E0D3B3C85BB CRC64;
     MTTNTHTLQI EEILELLPHR FPFLLVDRVL DFEEGRFLRA VKNVSVNEPF FQGHFPGKPI
     LPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVTFEKT
     RRGLTRFKGV ALVDGKVVCE ATMMCARSRE A
 
 
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