GMHB_CHLTE
ID GMHB_CHLTE Reviewed; 199 AA.
AC Q8KAY7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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=CT2011;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006470; AAM73229.1; -; Genomic_DNA.
DR RefSeq; NP_662887.1; NC_002932.3.
DR RefSeq; WP_010933667.1; NC_002932.3.
DR AlphaFoldDB; Q8KAY7; -.
DR SMR; Q8KAY7; -.
DR STRING; 194439.CT2011; -.
DR EnsemblBacteria; AAM73229; AAM73229; CT2011.
DR KEGG; cte:CT2011; -.
DR PATRIC; fig|194439.7.peg.1822; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_2_10; -.
DR OMA; EHQICLE; -.
DR OrthoDB; 1472357at2; -.
DR Proteomes; UP000001007; 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..199
FT /note="D-glycero-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000209387"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 18..22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 53..56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 110
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 22675 MW; 28A7CCF105CDE85E CRC64;
MESAKVLFLD RDGTINRDIG RYVSSREEFI LIDRADEAIA IAREAGFRIV LITNQAGIAR
GIVTPQDVED VNDYLNELLA ERQTSFDRCY YCPAHPNYPH PEYDRFIDHR KPSPRMVEQA
IADLREEGFE VDRSASFFIG DKLIDVECGQ RAGLKTILVR TGHNEESLCE QHQIFPDHVA
DDLYQAVTGY ILGQPTSRD
