ID   FABZ_BURTA              Reviewed;         160 AA.
AC   Q2SWY7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BTH_I2038;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC39413.1; -; Genomic_DNA.
DR   PDB; 4H4G; X-ray; 2.65 A; A/B/C/D/E/F/G/H/I=1-160.
DR   PDBsum; 4H4G; -.
DR   AlphaFoldDB; Q2SWY7; -.
DR   SMR; Q2SWY7; -.
DR   PRIDE; Q2SWY7; -.
DR   EnsemblBacteria; ABC39413; ABC39413; BTH_I2038.
DR   KEGG; bte:BTH_I2038; -.
DR   HOGENOM; CLU_078912_1_0_4; -.
DR   OMA; FPGRPLM; -.
DR   Proteomes; UP000001930; Chromosome I.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Lyase.
FT   CHAIN           1..160
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_0000242887"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
FT   HELIX           15..21
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   HELIX           68..84
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   STRAND          97..107
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   STRAND          116..127
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:4H4G"
FT   STRAND          142..153
FT                   /evidence="ECO:0007829|PDB:4H4G"
SQ   SEQUENCE   160 AA;  18087 MW;  5A03FC5D9F004913 CRC64;
     MRRTIMSTEK INFDIHKILT LLPHRYPILL VDRVLELEPH KSIKALKNVT VNEPFFTGHF
     PKRPVMPGVL IIEALAQAAA LLTFAEAEPK DPENTLYYFV GIDNARFKRV VEPGDQLILN
     VTFERYIRGI WKFKAVAEVD GKVAAEAELM CTVKTADAAP