ID   GMHBB_PHOLL             Reviewed;         188 AA.
AC   Q7N8M1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE            EC=3.1.3.82;
DE   AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE            Short=HBP phosphatase;
GN   Name=gmhB1; OrderedLocusNames=plu0698;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate
CC       intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by
CC       removing the phosphate group at the C-7 position. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC         glycero-beta-D-manno-heptose 1-phosphate + phosphate;
CC         Xref=Rhea:RHEA:28518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60208, ChEBI:CHEBI:61593; EC=3.1.3.82;
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC       heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC       glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
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DR   EMBL; BX571861; CAE12993.1; -; Genomic_DNA.
DR   RefSeq; WP_011145074.1; NC_005126.1.
DR   AlphaFoldDB; Q7N8M1; -.
DR   SMR; Q7N8M1; -.
DR   STRING; 243265.plu0698; -.
DR   EnsemblBacteria; CAE12993; CAE12993; plu0698.
DR   GeneID; 24167953; -.
DR   KEGG; plu:plu0698; -.
DR   eggNOG; COG0241; Bacteria.
DR   HOGENOM; CLU_085077_3_0_6; -.
DR   OMA; EHQICLE; -.
DR   OrthoDB; 1472357at2; -.
DR   BioCyc; PLUM243265:PLU_RS03455-MON; -.
DR   UniPathway; UPA00356; UER00438.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004446; Heptose_bisP_phosphatase.
DR   InterPro; IPR006543; Histidinol-phos.
DR   PANTHER; PTHR42891; PTHR42891; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00213; GmhB_yaeD; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase;
KW   Lipopolysaccharide biosynthesis; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..188
FT                   /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000209401"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
SQ   SEQUENCE   188 AA;  20962 MW;  2F9D09664604162E CRC64;
     MTQGIPAVFL DRDGTINIDH GYVHEIDDFQ FIDGVIEAMI ELKKMGYALV LVTNQSGIAR
     GIFDEEQFLQ LTEWMDWSLA DRGVDLDGIY YCPHHPDATE EQYKKSCDCR KPQPGMLLDA
     QRELSIDMTA SFMIGDKLED MQAATLAKIG TKVLVRTGKP VNTEAEQAAN LIINSLADLP
     KAIKGIKK