GMHB_THEVB
ID GMHB_THEVB Reviewed; 196 AA.
AC Q8DH26;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=D-glycero-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE EC=3.1.3.-;
DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE Short=HBP phosphatase;
GN Name=gmhB; OrderedLocusNames=tlr2134;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- FUNCTION: Converts the D-glycero-D-manno-heptose 1,7-bisphosphate
CC intermediate into D-glycero-D-manno-heptose 1-phosphate by removing the
CC phosphate group at the C-7 position. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glycero-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-
CC D-manno-heptose 1-phosphate + phosphate; Xref=Rhea:RHEA:48504,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:59957,
CC ChEBI:CHEBI:60002;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
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DR EMBL; BA000039; BAC09686.1; -; Genomic_DNA.
DR RefSeq; NP_682924.1; NC_004113.1.
DR RefSeq; WP_011057968.1; NC_004113.1.
DR AlphaFoldDB; Q8DH26; -.
DR SMR; Q8DH26; -.
DR STRING; 197221.22295861; -.
DR EnsemblBacteria; BAC09686; BAC09686; BAC09686.
DR KEGG; tel:tlr2134; -.
DR PATRIC; fig|197221.4.peg.2236; -.
DR eggNOG; COG0241; Bacteria.
DR OMA; EHQICLE; -.
DR OrthoDB; 1472357at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..196
FT /note="D-glycero-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000209407"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51..54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112..113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 51
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 113
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 21487 MW; 5AE0D21609685CBD CRC64;
MPRPAVFLDR DGVLNQEVGY IHRLEDLQLI PGVAQAVRRL NDAGWFCCLA SNQSGPARDY
YSIDHVHALH HRLQELLAAS AGAVLDAVYF CPDLSRPEGG VVADYAGWTT WRKPNTGMLV
AAAWDHDLDL SRSVMVGDKA TDIDLARNAG CYGILVQTGF GDRVLEGSYQ HASQPDYIAE
DLAAAVEWIC THLAPR
