FABZ_POLSJ
ID FABZ_POLSJ Reviewed; 145 AA.
AC Q12A42;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 25-MAY-2022, entry version 81.
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=Bpro_2684;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABE44600.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000316; ABE44600.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011483598.1; NC_007948.1.
DR AlphaFoldDB; Q12A42; -.
DR SMR; Q12A42; -.
DR STRING; 296591.Bpro_2684; -.
DR EnsemblBacteria; ABE44600; ABE44600; Bpro_2684.
DR KEGG; pol:Bpro_2684; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_0_4; -.
DR OMA; FPGRPLM; -.
DR OrthoDB; 1763197at2; -.
DR Proteomes; UP000001983; 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..145
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000340795"
FT ACT_SITE 47
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ SEQUENCE 145 AA; 16312 MW; C1B533B8C31A441E CRC64;
MDIHQILKQL PHRYPILLVD RVLEIEKGKR IKALKNVTMN EPFFMGHFPH HPVMPGVLML
EAMAQAAALL AFETLGVTPD DKTVYYFAGI DGARFKRPVE PGDQLIMDVT LERMKAGIFK
FKGVTRVGEA IACEAELMCT MRTIA