ID D8IC98_BRAP9 Unreviewed; 154 AA.
AC D8IC98;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:ADK30771.1};
GN OrderedLocusNames=BP951000_0773 {ECO:0000313|EMBL:ADK30771.1};
OS Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30771.1, ECO:0000313|Proteomes:UP000000332};
RN [1] {ECO:0000313|EMBL:ADK30771.1, ECO:0000313|Proteomes:UP000000332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT "The complete genome sequence of the pathogenic intestinal spirochete
RT Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL PLoS ONE 5:E11455-E11455(2010).
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|HAMAP-Rule:MF_00406}.
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DR EMBL; CP002025; ADK30771.1; -; Genomic_DNA.
DR RefSeq; WP_013243725.1; NC_014330.1.
DR AlphaFoldDB; D8IC98; -.
DR STRING; 759914.BP951000_0773; -.
DR GeneID; 56439342; -.
DR KEGG; bpo:BP951000_0773; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_2_12; -.
DR InParanoid; D8IC98; -.
DR Proteomes; UP000000332; 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:UP000000332}.
FT ACT_SITE 49
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
SQ SEQUENCE 154 AA; 17351 MW; 6AC14FF9250EF9C7 CRC64;
MENINITKIM ELLPHRYPFL LVDKVISIEE GKIHSLKNVT FNEPQFTGHF PESPIMPGVL
MVEALAQTSG IYCYMKLLKP EEIGNKFMFF AKIDNVKFKN PVIPGDVMDM FVTVEAFNGT
LLKTHGEVRV GDSLACSADL GLFLVDREAM KINK
//
