ID A0A149VZC0_9PROT Unreviewed; 151 AA.
AC A0A149VZC0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:KXW58571.1};
GN ORFNames=FEMY_09700 {ECO:0000313|EMBL:KXW58571.1};
OS Ferrovum myxofaciens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=416213 {ECO:0000313|EMBL:KXW58571.1, ECO:0000313|Proteomes:UP000075653};
RN [1] {ECO:0000313|EMBL:KXW58571.1, ECO:0000313|Proteomes:UP000075653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-31 {ECO:0000313|EMBL:KXW58571.1,
RC ECO:0000313|Proteomes:UP000075653};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z-31.";
RL Submitted (JAN-2016) 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:KXW58571.1}.
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DR EMBL; LRRD01000013; KXW58571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A149VZC0; -.
DR STRING; 1789004.FEMY_09700; -.
DR PATRIC; fig|1789004.3.peg.985; -.
DR Proteomes; UP000075653; 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:UP000075653}.
FT ACT_SITE 50
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
SQ SEQUENCE 151 AA; 17146 MW; 35CE142A2107E2B3 CRC64;
MSGMDINEIM EYLPHRYPFL MVDRVLEVTP GKSIVAIKNV SRNEEYFQGH FPHHPVMPGV
LIIESLAQAA ALLSFKTEGI KPDGKIVTYF VGIDQARFRN PVFPGDQLRL EVSLLRHSYK
IWKFSAKAWV EDRVAAEAQL MCAEKNLVES A
//
