GMHBB_PSEPK
ID GMHBB_PSEPK Reviewed; 175 AA.
AC Q88RS0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase {ECO:0000250|UniProtKB:P63228};
DE EC=3.1.3.82 {ECO:0000269|PubMed:25848029};
DE AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000255|PIRNR:PIRNR004682};
DE Short=HBP phosphatase {ECO:0000250|UniProtKB:P63228};
GN Name=gmhB {ECO:0000250|UniProtKB:P63228};
GN OrderedLocusNames=PP_0059 {ECO:0000312|EMBL:AAN65693.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000312|Proteomes:UP000000556};
RN [1] {ECO:0000312|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000312|EMBL:AAN65693.1, ECO:0000312|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
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:25848029}.
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:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P63228};
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:0000305|PubMed:25848029}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000250|UniProtKB:P63228}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P63228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR004682}.
CC -!- SIMILARITY: Belongs to the gmhB family.
CC {ECO:0000255|PIRNR:PIRNR004682}.
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DR EMBL; AE015451; AAN65693.1; -; Genomic_DNA.
DR RefSeq; NP_742229.1; NC_002947.4.
DR RefSeq; WP_003253129.1; NC_002947.4.
DR AlphaFoldDB; Q88RS0; -.
DR SMR; Q88RS0; -.
DR STRING; 160488.PP_0059; -.
DR ChEMBL; CHEMBL4105992; -.
DR EnsemblBacteria; AAN65693; AAN65693; PP_0059.
DR KEGG; ppu:PP_0059; -.
DR PATRIC; fig|160488.4.peg.64; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_2_0_6; -.
DR OMA; EHQICLE; -.
DR PhylomeDB; Q88RS0; -.
DR BioCyc; PPUT160488:G1G01-62-MON; -.
DR UniPathway; UPA00356; UER00438.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Carbohydrate metabolism; Cytoplasm; Hydrolase;
KW Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..175
FT /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435566"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 15..19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 100..101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT SITE 50
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT SITE 100
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT SITE 101
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250|UniProtKB:P63228"
SQ SEQUENCE 175 AA; 18796 MW; 19D0F5A8413B646E CRC64;
MKLLILDRDG VINYDSDAYI KTLEEWVPIP GSVDAIAQLS KAGWTVAVAT NQSGIARGYY
PLATLEAMHA RLRALVAEQG GEVGHIVYCP HGPDEGCDCR KPKPGMLRAI AEHYQIGLEG
VWFVGDSKGD LEAALAVGAQ PVLVKTGKGE RTLEKGVPET TLIFDDLAAI ARELI
