GMHBA_BACTN
ID GMHBA_BACTN Reviewed; 156 AA.
AC Q8AAI7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=BT_0477;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP AND PATHWAY.
RX PubMed=20050615; DOI=10.1021/bi902018y;
RA Wang L., Huang H., Nguyen H.H., Allen K.N., Mariano P.S.,
RA Dunaway-Mariano D.;
RT "Divergence of biochemical function in the HAD superfamily: D-glycero-D-
RT manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
RL Biochemistry 49:1072-1081(2010).
CC -!- FUNCTION: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
CC (alpha-HBP) intermediate into D-glycero-alpha-D-manno-heptose 1-
CC phosphate by removing the phosphate group at the C-7 position.
CC {ECO:0000269|PubMed:20050615}.
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:20050615};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for alpha-HBP (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20050615};
CC KM=86 uM for beta-HBP (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20050615};
CC Note=kcat is 29 sec(-1) and 13 sec(-1) with alpha-HBP and beta-HBP as
CC substrate, respectively. Thus, the enzyme displays 6-fold more
CC efficiency towards the alpha- than the beta-anomer (PubMed:20050615).
CC {ECO:0000269|PubMed:20050615};
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:20050615}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:20050615}.
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; AE015928; AAO75584.1; -; Genomic_DNA.
DR RefSeq; NP_809390.1; NC_004663.1.
DR RefSeq; WP_011107287.1; NC_004663.1.
DR AlphaFoldDB; Q8AAI7; -.
DR SMR; Q8AAI7; -.
DR STRING; 226186.BT_0477; -.
DR PaxDb; Q8AAI7; -.
DR PRIDE; Q8AAI7; -.
DR DNASU; 1071787; -.
DR EnsemblBacteria; AAO75584; AAO75584; BT_0477.
DR GeneID; 60926437; -.
DR KEGG; bth:BT_0477; -.
DR PATRIC; fig|226186.12.peg.477; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_1_1_10; -.
DR InParanoid; Q8AAI7; -.
DR OMA; DHPMRKP; -.
DR BRENDA; 3.1.3.83; 709.
DR UniPathway; UPA00543; UER00607.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; 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; TIGR01662; HAD-SF-IIIA; 1.
DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Carbohydrate metabolism; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..156
FT /note="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000424235"
FT ACT_SITE 17
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 19
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 17..19
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 61..64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 61
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 156 AA; 18105 MW; 7820655F6CA51EE8 CRC64;
MRLQDIDVTG FETLLLDRDG VVNRLRPDDY VKKWEEFEFL PGVLEILKAW NTHFKYIFIV
TNQRGVGKEI MSEEDLKHIH ERMISEVKNY GGRIDRIYYC TALTDSDINR KPGIGMFLQI
LRDYPDIDKA KCLMIGDSDS DIKFAKNCGI VGIKVI
