ID FABZ_XYLF2 Reviewed; 160 AA. AC B2I7P0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 26-FEB-2020, entry version 63. 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=XfasM23_0320; OS Xylella fastidiosa (strain M23). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405441; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23; RX PubMed=20601474; DOI=10.1128/jb.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) RT causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(2010). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001011; ACB91768.1; -; Genomic_DNA. DR RefSeq; WP_004089335.1; NC_010577.1. DR SMR; B2I7P0; -. DR PRIDE; B2I7P0; -. DR EnsemblBacteria; ACB91768; ACB91768; XfasM23_0320. DR KEGG; xfn:XfasM23_0320; -. DR HOGENOM; CLU_078912_1_2_6; -. DR KO; K02372; -. DR OMA; FPGRPLM; -. DR BioCyc; XFAS405441:G1GBK-360-MONOMER; -. DR Proteomes; UP000001698; 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 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..160 FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase FT FabZ" FT /id="PRO_1000197306" FT ACT_SITE 63 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406" SQ SEQUENCE 160 AA; 17996 MW; 4319B5AE2FDA745E CRC64; MSDSPTTAHT RLELPIDIIR IQALLPHRYP FLLVDRILEL DQKQKRIVAQ KNVSINEPFF QGHFPEHPVM PGVLIIEALA QAGGVMTQLN LSHNGHSSLL FYMVRVDNAR FNKQVVPGDI LILDMTMKRR IRNMGCYYGE ARVNGEVVAC ADIMCAGVKS //