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Database: UniProt
Entry: A0A0R1HLC9_9LACO
LinkDB: A0A0R1HLC9_9LACO
Original site: A0A0R1HLC9_9LACO 
ID   A0A0R1HLC9_9LACO        Unreviewed;       171 AA.
AC   A0A0R1HLC9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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   ORFNames=FC96_GL000579 {ECO:0000313|EMBL:KRK47308.1};
OS   Secundilactobacillus kimchicus JCM 15530.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1302272 {ECO:0000313|EMBL:KRK47308.1, ECO:0000313|Proteomes:UP000050911};
RN   [1] {ECO:0000313|EMBL:KRK47308.1, ECO:0000313|Proteomes:UP000050911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15530 {ECO:0000313|EMBL:KRK47308.1,
RC   ECO:0000313|Proteomes:UP000050911};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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|ARBA:ARBA00001055, ECO:0000256|HAMAP-
CC         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:KRK47308.1}.
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DR   EMBL; AZCX01000010; KRK47308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1HLC9; -.
DR   STRING; 1302272.FC96_GL000579; -.
DR   PATRIC; fig|1302272.5.peg.577; -.
DR   Proteomes; UP000050911; 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:UP000050911}.
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   171 AA;  18855 MW;  2AB554FA1A629D23 CRC64;
     MFKLNYHVEY LKTSTQAKGR LKQLAILSAQ EIMELIPNRY PILFMDYVDE LEPGESIVAT
     KNVTINEEFF QGHFPGNPVM PGVLIIESLA QAASILILKS PEFAGKTAYL GAIKDARFHQ
     IVRPGDVLKL HVAFTKRRSN MGVVHTEATV GDNVAAKADL TFIVAPNTAS N
//
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