GMHBA_MYCBO
ID GMHBA_MYCBO Reviewed; 190 AA.
AC Q7U2U1; A0A1R3XVI5; X2BE37;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; OrderedLocusNames=BQ2027_MB0118;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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. {ECO:0000250}.
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 -!- 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 -!- 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; LT708304; SIT98525.1; -; Genomic_DNA.
DR RefSeq; NP_853785.1; NC_002945.3.
DR RefSeq; WP_010950343.1; NC_002945.4.
DR AlphaFoldDB; Q7U2U1; -.
DR SMR; Q7U2U1; -.
DR OMA; WFIGDIL; -.
DR UniPathway; UPA00543; UER00607.
DR Proteomes; UP000001419; 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 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..190
FT /note="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000209396"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 17
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 15..17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 23..28
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 109..110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT SITE 59
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 109
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 110
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
SQ SEQUENCE 190 AA; 20611 MW; 5A4B07E97EA4D462 CRC64;
MVAERAGHQW CLFLDRDGVI NRQVVGDYVR NWRQFEWLPG AARALKKLRA WAPYIVVVTN
QQGVGAGLMS AVDVMVIHRH LQMQLASDGV LIDGFQVCPH HRSQRCGCRK PRPGLVLDWL
RRHPDSEPLL SIVVGDSLSD LELAHNVAAA AGACASVQIG GASSGGVADA SFDSLWEFAV
AVGHARGERG
