FABZ_CAMJJ
ID FABZ_CAMJJ Reviewed; 146 AA.
AC A1VXZ7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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};
GN OrderedLocusNames=CJJ81176_0300;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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. {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; CP000538; EAQ73095.1; -; Genomic_DNA.
DR RefSeq; WP_002857452.1; NC_008787.1.
DR PDB; 3D6X; X-ray; 2.59 A; A/B/C/D/E/F=1-146.
DR PDBsum; 3D6X; -.
DR AlphaFoldDB; A1VXZ7; -.
DR SMR; A1VXZ7; -.
DR STRING; 354242.CJJ81176_0300; -.
DR EnsemblBacteria; EAQ73095; EAQ73095; CJJ81176_0300.
DR KEGG; cjj:CJJ81176_0300; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_2_7; -.
DR OMA; FPGRPLM; -.
DR EvolutionaryTrace; A1VXZ7; -.
DR Proteomes; UP000000646; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lyase.
FT CHAIN 1..146
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000301885"
FT ACT_SITE 48
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:3D6X"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3D6X"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3D6X"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3D6X"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3D6X"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:3D6X"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:3D6X"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:3D6X"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:3D6X"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:3D6X"
SQ SEQUENCE 146 AA; 16440 MW; EFFA2656B12563A5 CRC64;
MIDVMQIQEI LPHRYPFLLV DKITELKVKE VVLGYKNISI SDHVFMGHFP GHPIYPGVLI
LEGMAQTGGV LAFESMEDKV DPKSKVVYFT GIDGAKFRNP VRPGDRLDYE MSVVKNRGNM
WIFKGQAFVD GNLVAEAELK AMIVDK