FABZ_YERPA
ID FABZ_YERPA Reviewed; 176 AA.
AC Q1CAM3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
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}; OrderedLocusNames=YPA_0531;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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}.
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DR EMBL; CP000308; ABG12499.1; -; Genomic_DNA.
DR RefSeq; WP_002217656.1; NZ_CP009906.1.
DR PDB; 5BUX; X-ray; 1.90 A; A/B=1-176.
DR PDBsum; 5BUX; -.
DR AlphaFoldDB; Q1CAM3; -.
DR SMR; Q1CAM3; -.
DR EnsemblBacteria; ABG12499; ABG12499; YPA_0531.
DR GeneID; 66844579; -.
DR KEGG; ypa:YPA_0531; -.
DR OMA; FPGRPLM; -.
DR Proteomes; UP000001971; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lyase.
FT CHAIN 1..176
FT /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT FabZ"
FT /id="PRO_0000301938"
FT ACT_SITE 54
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:5BUX"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:5BUX"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5BUX"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:5BUX"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:5BUX"
FT HELIX 63..82
FT /evidence="ECO:0007829|PDB:5BUX"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:5BUX"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:5BUX"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:5BUX"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:5BUX"
SQ SEQUENCE 176 AA; 19631 MW; 3A1602C0A93DD2E2 CRC64;
MTTDTHTLHI EEILDLLPHR FPFLLVDRVL DFEEGKFLRA VKNVSFNEPF FQGHFPGKPI
FPGVLILEAM AQATGILAFK SRGKLEPGEL YYFAGIDEAR FKRPVVPGDQ MIMEVEFVKE
RRGLTRFTGV AKVDGEIVCT ATMMCARSKP AAPAESVVVK PDVVKPDVVN PVVKES