GMHBB_BORBR
ID GMHBB_BORBR Reviewed; 179 AA.
AC Q7WG29;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE EC=3.1.3.82;
DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE Short=HBP phosphatase;
GN OrderedLocusNames=BB4091;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP MASS SPECTROMETRY, 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH DIVALENT CATIONS AND
RP SUBSTRATE ANALOGS, FUNCTION, AND SUBUNIT.
RX PubMed=20050614; DOI=10.1021/bi902019q;
RA Nguyen H.H., Wang L., Huang H., Peisach E., Dunaway-Mariano D., Allen K.N.;
RT "Structural determinants of substrate recognition in the HAD superfamily
RT member D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
RL Biochemistry 49:1082-1092(2010).
CC -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate
CC (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate
CC by removing the phosphate group at the C-7 position.
CC {ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050615}.
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:20050615};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for beta-HBP (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20050615};
CC KM=280 uM for alpha-HBP (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:20050615};
CC Note=kcat is 22 sec(-1) and 5.9 sec(-1) with beta-HBP and alpha-HBP
CC as substrate, respectively. Thus, the enzyme displays 150-fold more
CC efficiency towards the beta- than the alpha-anomer (PubMed:20050615).
CC {ECO:0000269|PubMed:20050615};
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 {ECO:0000269|PubMed:20050615}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000269|PubMed:20050615}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20050614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=19034; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20050615};
CC -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
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DR EMBL; BX640449; CAE34454.1; -; Genomic_DNA.
DR RefSeq; WP_003814404.1; NC_002927.3.
DR PDB; 3L8H; X-ray; 1.68 A; A/B/C/D=1-179.
DR PDBsum; 3L8H; -.
DR AlphaFoldDB; Q7WG29; -.
DR SMR; Q7WG29; -.
DR STRING; 257310.BB4091; -.
DR EnsemblBacteria; CAE34454; CAE34454; BB4091.
DR GeneID; 56477409; -.
DR GeneID; 66437358; -.
DR KEGG; bbr:BB4091; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_2_0_4; -.
DR OMA; EHQICLE; -.
DR OrthoDB; 1472357at2; -.
DR BRENDA; 3.1.3.82; 227.
DR UniPathway; UPA00356; UER00438.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; Q7WG29; -.
DR Proteomes; UP000001027; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009244; P:lipopolysaccharide core region 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 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Zinc.
FT CHAIN 1..179
FT /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /id="PRO_0000417695"
FT ACT_SITE 7
FT /note="Nucleophile"
FT ACT_SITE 9
FT /note="Proton donor"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20050614,
FT ECO:0007744|PDB:3L8H"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20050614"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20050614,
FT ECO:0007744|PDB:3L8H"
FT BINDING 15..19
FT /ligand="substrate"
FT BINDING 50..53
FT /ligand="substrate"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20050614"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20050614,
FT ECO:0007744|PDB:3L8H"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20050614,
FT ECO:0007744|PDB:3L8H"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20050614,
FT ECO:0007744|PDB:3L8H"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:20050614,
FT ECO:0007744|PDB:3L8H"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20050614"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:3L8H"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20050614"
FT SITE 50
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250"
FT SITE 101
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3L8H"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3L8H"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3L8H"
FT TURN 53..58
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 62..78
FT /evidence="ECO:0007829|PDB:3L8H"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3L8H"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:3L8H"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:3L8H"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:3L8H"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:3L8H"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:3L8H"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:3L8H"
SQ SEQUENCE 179 AA; 19035 MW; B95E1F61A6B3F7AD CRC64;
MKLIILDRDG VVNQDSDAFV KSPDEWIALP GSLQAIARLT QADWTVVLAT NQSGLARGLF
DTATLNAIHD KMHRALAQMG GVVDAIFMCP HGPDDGCACR KPLPGMYRDI ARRYDVDLAG
VPAVGDSLRD LQAAAQAGCA PWLVQTGNGR KTLAQGGLPE GTRVCEDLAA VAEQLLQEA
