FABZ_DECAR
ID FABZ_DECAR Reviewed; 144 AA.
AC Q47F81;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Daro_1753;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ46500.1; -; Genomic_DNA.
DR RefSeq; WP_011287504.1; NC_007298.1.
DR AlphaFoldDB; Q47F81; -.
DR SMR; Q47F81; -.
DR STRING; 159087.Daro_1753; -.
DR EnsemblBacteria; AAZ46500; AAZ46500; Daro_1753.
DR KEGG; dar:Daro_1753; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_0_4; -.
DR OMA; FPGRPLM; -.
DR OrthoDB; 1763197at2; -.
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..144
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000230811"
FT ACT_SITE 47
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ SEQUENCE 144 AA; 16403 MW; 3B41339A7DB27BB1 CRC64;
MDIIEILEHL PHRYPFLLVD RVLEIEPGKS IHAYKNVTIN EPFFVGHFPH HPVMPGVLIM
EALAQAAGIL SFKSMDEKPS PDTVFYFAGI DEARFKKPVM PGDQLHLHIE IERQMRGVWK
YKAEARVDGQ LAASAKLMCA KRDL