GMHB_THEVO
ID GMHB_THEVO Reviewed; 146 AA.
AC Q97B60;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable 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=TV0598; ORFNames=TVG0590688;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB59740.1; -; Genomic_DNA.
DR AlphaFoldDB; Q97B60; -.
DR SMR; Q97B60; -.
DR STRING; 273116.14324813; -.
DR PRIDE; Q97B60; -.
DR EnsemblBacteria; BAB59740; BAB59740; BAB59740.
DR KEGG; tvo:TVG0590688; -.
DR eggNOG; arCOG07384; Archaea.
DR HOGENOM; CLU_085077_4_1_2; -.
DR OMA; EHQICLE; -.
DR PhylomeDB; Q97B60; -.
DR Proteomes; UP000001017; 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 InterPro; IPR013954; PNK3P.
DR PANTHER; PTHR42891; PTHR42891; 1.
DR Pfam; PF08645; PNK3P; 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 Zinc.
FT CHAIN 1..146
FT /note="Probable D-glycero-D-manno-heptose-1,7-bisphosphate
FT 7-phosphatase"
FT /id="PRO_0000209411"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 15..18
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 49..52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 49
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 99
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 16939 MW; 8A10D3962F54D74F CRC64;
MKTLFIDRDG TINKDCPYCH NPSDLFIYPD AVDLLQRYQD DGFRIIIVTN QSGIGRGYFT
ESQFKEFSDF MNDKLKENGI VISAIYYCPH KPEDSCNCRK PETGLFSEVL EDYKVDIPSS
IVVGDRNEID GEFARRIKLP FRLLRH
