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D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC 3.1.3.82) (D,D-heptose 1,7-bisphosphate phosphatase) (HBP phosphatase)

 GMHBB_BORBR             Reviewed;         179 AA.
Q7WG29;
13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-APR-2018, entry version 97.
RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
EC=3.1.3.82;
AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
Short=HBP phosphatase;
OrderedLocusNames=BB4091;
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
(Alcaligenes bronchisepticus).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257310;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
PubMed=12910271; DOI=10.1038/ng1227;
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC
PARAMETERS, MASS SPECTROMETRY, AND PATHWAY.
PubMed=20050615; DOI=10.1021/bi902018y;
Wang L., Huang H., Nguyen H.H., Allen K.N., Mariano P.S.,
Dunaway-Mariano D.;
"Divergence of biochemical function in the HAD superfamily: D-glycero-
D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).";
Biochemistry 49:1072-1081(2010).
[3]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH DIVALENT
CATIONS AND SUBSTRATE ANALOGS, FUNCTION, AND SUBUNIT.
PubMed=20050614; DOI=10.1021/bi902019q;
Nguyen H.H., Wang L., Huang H., Peisach E., Dunaway-Mariano D.,
Allen K.N.;
"Structural determinants of substrate recognition in the HAD
superfamily member D-glycero-D-manno-heptose-1,7-bisphosphate
phosphatase (GmhB).";
Biochemistry 49:1082-1092(2010).
-!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-
bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-
heptose 1-phosphate by removing the phosphate group at the C-7
position. {ECO:0000269|PubMed:20050614,
ECO:0000269|PubMed:20050615}.
-!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1,7-
bisphosphate + H(2)O = D-glycero-beta-D-manno-heptose 1-phosphate
+ phosphate. {ECO:0000269|PubMed:20050615}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.9 uM for beta-HBP (at pH 7.5 and 25 degrees Celsius)
{ECO:0000269|PubMed:20050615};
KM=280 uM for alpha-HBP (at pH 7.5 and 25 degrees Celsius)
{ECO:0000269|PubMed:20050615};
Note=kcat is 22 sec(-1) and 5.9 sec(-1) with beta-HBP and alpha-
HBP as substrate, respectively. Thus, the enzyme displays 150-
fold more efficiency towards the beta- than the alpha-anomer
(PubMed:20050615). {ECO:0000269|PubMed:20050615};
-!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
{ECO:0000269|PubMed:20050615}.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
biosynthesis. {ECO:0000269|PubMed:20050615}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20050614}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=19034; Method=Electrospray; Range=1-179;
Evidence={ECO:0000269|PubMed:20050615};
-!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
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EMBL; BX640449; CAE34454.1; -; Genomic_DNA.
RefSeq; WP_003814404.1; NC_002927.3.
PDB; 3L8H; X-ray; 1.68 A; A/B/C/D=1-179.
PDBsum; 3L8H; -.
ProteinModelPortal; Q7WG29; -.
SMR; Q7WG29; -.
STRING; 257310.BB4091; -.
EnsemblBacteria; CAE34454; CAE34454; BB4091.
KEGG; bbr:BB4091; -.
eggNOG; ENOG4108ZI0; Bacteria.
eggNOG; COG0241; LUCA.
HOGENOM; HOG000016503; -.
KO; K03273; -.
OMA; EHQICLE; -.
OrthoDB; POG091H01YE; -.
BRENDA; 3.1.3.82; 227.
UniPathway; UPA00356; UER00438.
UniPathway; UPA00958; -.
EvolutionaryTrace; Q7WG29; -.
Proteomes; UP000001027; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006549; HAD-SF_hydro_IIIA.
InterPro; IPR023214; HAD_sf.
InterPro; IPR004446; Heptose_bisP_phosphatase.
InterPro; IPR006543; Histidinol-phos.
PANTHER; PTHR42891; PTHR42891; 1.
PIRSF; PIRSF004682; GmhB; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm;
Hydrolase; Magnesium; Metal-binding; Zinc.
CHAIN 1 179 D-glycero-beta-D-manno-heptose-1,7-
bisphosphate 7-phosphatase.
/FTId=PRO_0000417695.
REGION 15 19 Substrate binding.
REGION 50 53 Substrate binding.
ACT_SITE 7 7 Nucleophile.
ACT_SITE 9 9 Proton donor.
METAL 7 7 Magnesium. {ECO:0000244|PDB:3L8H,
ECO:0000269|PubMed:20050614}.
METAL 9 9 Magnesium; via carbonyl oxygen.
{ECO:0000244|PDB:3L8H,
ECO:0000269|PubMed:20050614}.
METAL 89 89 Zinc. {ECO:0000244|PDB:3L8H,
ECO:0000269|PubMed:20050614}.
METAL 91 91 Zinc; via pros nitrogen.
{ECO:0000244|PDB:3L8H,
ECO:0000269|PubMed:20050614}.
METAL 97 97 Zinc. {ECO:0000244|PDB:3L8H,
ECO:0000269|PubMed:20050614}.
METAL 99 99 Zinc. {ECO:0000244|PDB:3L8H,
ECO:0000269|PubMed:20050614}.
METAL 126 126 Magnesium. {ECO:0000244|PDB:3L8H}.
BINDING 7 7 Substrate. {ECO:0000269|PubMed:20050614}.
BINDING 57 57 Substrate. {ECO:0000269|PubMed:20050614}.
BINDING 100 100 Substrate. {ECO:0000269|PubMed:20050614}.
BINDING 129 129 Substrate. {ECO:0000269|PubMed:20050614}.
SITE 50 50 Stabilizes the phosphoryl group.
{ECO:0000250}.
SITE 100 100 Contributes to substrate recognition.
{ECO:0000250}.
SITE 101 101 Stabilizes the phosphoryl group.
{ECO:0000250}.
STRAND 3 6 {ECO:0000244|PDB:3L8H}.
TURN 9 11 {ECO:0000244|PDB:3L8H}.
HELIX 23 25 {ECO:0000244|PDB:3L8H}.
HELIX 32 41 {ECO:0000244|PDB:3L8H}.
STRAND 45 51 {ECO:0000244|PDB:3L8H}.
TURN 53 58 {ECO:0000244|PDB:3L8H}.
HELIX 62 78 {ECO:0000244|PDB:3L8H}.
STRAND 85 89 {ECO:0000244|PDB:3L8H}.
STRAND 98 100 {ECO:0000244|PDB:3L8H}.
HELIX 105 114 {ECO:0000244|PDB:3L8H}.
STRAND 122 127 {ECO:0000244|PDB:3L8H}.
HELIX 128 137 {ECO:0000244|PDB:3L8H}.
STRAND 140 145 {ECO:0000244|PDB:3L8H}.
TURN 146 148 {ECO:0000244|PDB:3L8H}.
HELIX 149 155 {ECO:0000244|PDB:3L8H}.
STRAND 162 167 {ECO:0000244|PDB:3L8H}.
HELIX 168 177 {ECO:0000244|PDB:3L8H}.
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


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