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FABZ_KLEP7
ID   FABZ_KLEP7              Reviewed;         151 AA.
AC   A6T4Y2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=KPN78578_01920; ORFNames=KPN_00193;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR75653.1; -; Genomic_DNA.
DR   RefSeq; WP_004145858.1; NC_009648.1.
DR   AlphaFoldDB; A6T4Y2; -.
DR   SMR; A6T4Y2; -.
DR   STRING; 272620.KPN_00193; -.
DR   jPOST; A6T4Y2; -.
DR   EnsemblBacteria; ABR75653; ABR75653; KPN_00193.
DR   GeneID; 61331326; -.
DR   GeneID; 64296972; -.
DR   GeneID; 66605391; -.
DR   KEGG; kpn:KPN_00193; -.
DR   HOGENOM; CLU_078912_1_0_6; -.
DR   OMA; FPGRPLM; -.
DR   Proteomes; UP000000265; 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; Reference proteome.
FT   CHAIN           1..151
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_1000049848"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   151 AA;  17025 MW;  E20B4493F6DC1551 CRC64;
     MTTDTHTLHI EEILELLPHR YPFLLVDRVL DFEEGRFLRA VKNVSVNEPF FQGHFPGKPI
     LPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVTFEKT
     RRGLTRFKGV ALVDGKVVCE ATMMCARSRE A
 
 
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