FABZ_YEREN
ID FABZ_YEREN Reviewed; 178 AA.
AC P32205;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 92.
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};
OS Yersinia enterocolitica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EH902;
RX PubMed=8293817; DOI=10.1016/0014-5793(94)80211-4;
RA Vuorio R., Haerkonen T., Tolvanen M., Vaara M.;
RT "The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of
RT lipid A biosynthesis is conserved in various bacteria.";
RL FEBS Lett. 337:289-292(1994).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA80952.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z25463; CAA80952.1; ALT_INIT; Genomic_DNA.
DR PIR; S35968; S35968.
DR RefSeq; WP_005164036.1; NZ_UHIX01000001.1.
DR AlphaFoldDB; P32205; -.
DR SMR; P32205; -.
DR STRING; 1443113.LC20_01206; -.
DR PATRIC; fig|630.129.peg.3351; -.
DR eggNOG; COG0764; Bacteria.
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 3: Inferred from homology;
KW Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lyase.
FT CHAIN 1..178
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000091767"
FT ACT_SITE 54
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ SEQUENCE 178 AA; 19862 MW; 4C1B6D87847D49BC CRC64;
MTTDTHTLHI EEILDLLPHR FPFLLVDRVL DFEEGKFLRA VKNVSFNEPF FQGHFPGKPI
FPGVLILEAM AQATGILAFK SRGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVEFVKE
RRGLTRFTGV AKVDGEIVCT ATMMCARSKP ATAVVIKSEV TKSEGTKSEV GKPDVKES
