ID V2VQ85_9GAMM Unreviewed; 162 AA.
AC V2VQ85;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=P253_00721 {ECO:0000313|EMBL:ESK49864.1};
OS Acinetobacter indicus CIP 110367.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1341679 {ECO:0000313|EMBL:ESK49864.1, ECO:0000313|Proteomes:UP000018415};
RN [1] {ECO:0000313|EMBL:ESK49864.1, ECO:0000313|Proteomes:UP000018415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110367 {ECO:0000313|EMBL:ESK49864.1,
RC ECO:0000313|Proteomes:UP000018415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter indicus CIP 110367.";
RL Submitted (OCT-2013) 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}.
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:ESK49864.1}.
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DR EMBL; AYET01000001; ESK49864.1; -; Genomic_DNA.
DR AlphaFoldDB; V2VQ85; -.
DR PATRIC; fig|1341679.3.peg.705; -.
DR eggNOG; COG0764; Bacteria.
DR HOGENOM; CLU_078912_1_2_6; -.
DR Proteomes; UP000018415; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018415}.
FT ACT_SITE 62
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
SQ SEQUENCE 162 AA; 18084 MW; 97F2D85DAA158620 CRC64;
MMTESNTPTF TKPELPMHIQ TIREYLPHRY PFLLVDRIVD VTDNGIVGYK NVSINEEFLQ
GHFPEYPIMP GVLIVEALAQ VSGVLGFIMN NQKPTAGALF LFAGAEKVRF KKQVVAGDQL
VLKSELVMQK RGIYKYNCIA TVDGIVAATA EIMISHQKTE QA
//
