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Database: UniProt
Entry: A0A0G9GZP5_9GAMM
LinkDB: A0A0G9GZP5_9GAMM
Original site: A0A0G9GZP5_9GAMM 
ID   A0A0G9GZP5_9GAMM        Unreviewed;       157 AA.
AC   A0A0G9GZP5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=Y882_15875 {ECO:0000313|EMBL:KLD62424.1};
OS   Dyella japonica DSM 16301.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1440762 {ECO:0000313|EMBL:KLD62424.1, ECO:0000313|Proteomes:UP000035481};
RN   [1] {ECO:0000313|EMBL:KLD62424.1, ECO:0000313|Proteomes:UP000035481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16301 {ECO:0000313|EMBL:KLD62424.1,
RC   ECO:0000313|Proteomes:UP000035481};
RX   PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA   Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT   "A phylogenomic and molecular marker based taxonomic framework for the
RT   order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT   Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT   within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT   containing the genus Rhodanobacter and its closest relatives.";
RL   Antonie Van Leeuwenhoek 107:467-485(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLD62424.1}.
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DR   EMBL; JPLA01000045; KLD62424.1; -; Genomic_DNA.
DR   RefSeq; WP_046972869.1; NZ_JPLA01000045.1.
DR   AlphaFoldDB; A0A0G9GZP5; -.
DR   STRING; 1440762.Y882_15875; -.
DR   PATRIC; fig|1440762.4.peg.2899; -.
DR   OrthoDB; 9772788at2; -.
DR   Proteomes; UP000035481; Unassembled WGS sequence.
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}.
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   157 AA;  17316 MW;  6DEAA6EDA4B65A98 CRC64;
     MSDLTVPFHL PVNVEQIQQL LPHRYPFLLV DRVIELVPDK SAVAIKNVTI NEPFFQGHFP
     GHPVMPGVLI VEAMAQAAGL LTQISSRLKG TTGSPLFYLA KVDNARFNAP VVPGDQLRLE
     VELKRLLRSM GLFEARTIVN GKEVASCELM CAARSDK
//
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