GMHBB_HAEIN
ID GMHBB_HAEIN Reviewed; 184 AA.
AC P46452;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE EC=3.1.3.82 {ECO:0000269|PubMed:25848029};
DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE Short=HBP phosphatase;
GN Name=gmhB; OrderedLocusNames=HI_0621.1;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION.
RA Koonin E.V., Rudd K.E.;
RL Submitted (SEP-1995) to UniProtKB.
RN [3]
RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA Valvano M.A., Messner P., Kosma P.;
RT "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT heptose precursors of bacterial glycoproteins and cell surface
RT polysaccharides.";
RL Microbiology 148:1979-1989(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
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 in vitro. Also
CC catalyzes the dephosphorylation of D-glycero-alpha-D-manno-heptose 1,7-
CC bisphosphate, phospho-serine and fructose-1,6-biphosphate in vitro.
CC {ECO:0000269|PubMed:25848029}.
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 Evidence={ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
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; LOS core biosynthesis.
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; L42023; AAC22281.1; -; Genomic_DNA.
DR RefSeq; NP_438781.1; NC_000907.1.
DR RefSeq; WP_005694551.1; NC_000907.1.
DR AlphaFoldDB; P46452; -.
DR SMR; P46452; -.
DR STRING; 71421.HI_0621.1; -.
DR EnsemblBacteria; AAC22281; AAC22281; HI_0621.1.
DR KEGG; hin:HI_0621.1; -.
DR PATRIC; fig|71421.8.peg.647; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_0_6; -.
DR OMA; EHQICLE; -.
DR PhylomeDB; P46452; -.
DR BioCyc; HINF71421:G1GJ1-644-MON; -.
DR BRENDA; 3.1.3.82; 2529.
DR UniPathway; UPA00356; UER00438.
DR UniPathway; UPA00976; -.
DR Proteomes; UP000000579; 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:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
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; TIGR00213; GmhB_yaeD; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..184
FT /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000209392"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 8..10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 16..19
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 106..107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 50
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 106
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 107
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
SQ SEQUENCE 184 AA; 20810 MW; 49D1D56DA6DF3DBD CRC64;
MNKAIFLDRD GTLNIDYGYV HEIDNFKFID GVIDALRELK KMGYMLVLVT NQSGIARGYF
SEDQFLQLTE WMDWSLAEQD VDLDGIYYCP HHSEGKGEYK EDCDCRKPKS GMLLQAIKEL
KIDPTQSIMV GDKVEDLKAG IGAKVKMNVL VRTGKPVTGE GEGIADYVLD SIVDLPRILK
RLKK
