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Database: UniProt
Entry: A0A192D6A5_9SPHN
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ID   A0A192D6A5_9SPHN        Unreviewed;       158 AA.
AC   A0A192D6A5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000256|HAMAP-Rule:MF_00406};
DE            EC=4.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00406};
DE   AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000256|HAMAP-Rule:MF_00406};
DE            Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000256|HAMAP-Rule:MF_00406};
DE   AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000256|HAMAP-Rule:MF_00406};
GN   Name=fabZ {ECO:0000256|HAMAP-Rule:MF_00406};
GN   ORFNames=A9D12_10565 {ECO:0000313|EMBL:ANK13309.1};
OS   Erythrobacter neustonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1112 {ECO:0000313|EMBL:ANK13309.1, ECO:0000313|Proteomes:UP000078263};
RN   [1] {ECO:0000313|EMBL:ANK13309.1, ECO:0000313|Proteomes:UP000078263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9434 {ECO:0000313|EMBL:ANK13309.1,
RC   ECO:0000313|Proteomes:UP000078263};
RA   Shi X.-L., Wu Y.-H., Cheng H., Xu L., Zhang X.-Q., Wang C.-S., Xu X.-W.;
RT   "Compelete Genome Sequence of Bacteriochlorophyll-Synthesizing Bacterium
RT   Porphyrobacter neustonensis DSM 9434.";
RL   Submitted (MAY-2016) 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.
CC       {ECO:0000256|ARBA:ARBA00025049, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00406};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00406}.
CC   -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC       subfamily. {ECO:0000256|ARBA:ARBA00009174, ECO:0000256|HAMAP-
CC       Rule:MF_00406}.
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DR   EMBL; CP016033; ANK13309.1; -; Genomic_DNA.
DR   RefSeq; WP_068351647.1; NZ_CP016033.1.
DR   AlphaFoldDB; A0A192D6A5; -.
DR   STRING; 1112.A9D12_10565; -.
DR   KEGG; pns:A9D12_10565; -.
DR   Proteomes; UP000078263; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[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   CDD; cd01288; FabZ; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   HAMAP; MF_00406; FabZ; 1.
DR   InterPro; IPR013114; FabA_FabZ.
DR   InterPro; IPR010084; FabZ.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   NCBIfam; TIGR01750; fabZ; 1.
DR   PANTHER; PTHR30272; 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE; 1.
DR   PANTHER; PTHR30272:SF1; 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE FABZ; 1.
DR   Pfam; PF07977; FabA; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00406};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW   Rule:MF_00406};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00406};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00406};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00406};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078263}.
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   158 AA;  17313 MW;  33CD8EBABAC4AAF1 CRC64;
     MNDTGSMPAE VLDYDIVKIL KALPHRYPLL LVDRVKAIQL GERIHAVKAV SMNEQFFQGH
     FPGAPIMPGV LQIEALAQAA GILGIETMEL AGTGKLVIFM GIENAKFRSP VTPGCLLDLH
     VEFTQRRSRV YKFKGIASVE GKTTCEVEFT AMMTDPPA
//
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