GMHBA_ANETH
ID GMHBA_ANETH Reviewed; 179 AA.
AC Q9AGY5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE EC=3.1.3.83;
DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE Short=HBP phosphatase;
GN Name=gmhB; Synonyms=gmhC;
OS Aneurinibacillus thermoaerophilus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=143495;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 12990 / DSM 10155 / LMG 17166;
RX PubMed=11279237; DOI=10.1074/jbc.m100378200;
RA Kneidinger B., Graninger M., Puchberger M., Kosma P., Messner P.;
RT "Biosynthesis of nucleotide-activated D-glycero-D-manno-heptose.";
RL J. Biol. Chem. 276:20935-20944(2001).
RN [2]
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).
CC -!- FUNCTION: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
CC intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by
CC removing the phosphate group at the C-7 position.
CC {ECO:0000269|PubMed:11279237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC glycero-alpha-D-manno-heptose 1-phosphate + phosphate;
CC Xref=Rhea:RHEA:28522, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60207, ChEBI:CHEBI:61574; EC=3.1.3.83;
CC Evidence={ECO:0000269|PubMed:11279237};
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 -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-
CC heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-
CC glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
CC {ECO:0000269|PubMed:11279237}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:11279237}.
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; AF324836; AAK27853.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AGY5; -.
DR SMR; Q9AGY5; -.
DR BioCyc; MetaCyc:MON-15574; -.
DR BRENDA; 3.1.3.83; 344.
DR UniPathway; UPA00543; UER00607.
DR UniPathway; UPA00977; -.
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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0045232; P:S-layer organization; 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 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; 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; Cell wall biogenesis/degradation; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Zinc.
FT CHAIN 1..179
FT /note="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000209384"
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 108..109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 51
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 108
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 109
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
SQ SEQUENCE 179 AA; 20764 MW; 941AAFD10C10239A CRC64;
MKNKALFLDR DGVINVEKNY VHKIEDFEFM DGIFETLRYF QEKGYLLIII TNQAGIGRGY
YTEEQFHILN DWMLSEFEKE GIYITKVYYC PYHPEHGIGK YKRDSFDRKP NPGMILKSQK
EFNIDLSKSI LVGDKESDIQ AGKRAGVNVN IIFSNNKNGD ELDCCKKINS LSELVSLIL
