GMHBB_RHOPA
ID GMHBB_RHOPA Reviewed; 180 AA.
AC Q6N2R1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RPA3988 {ECO:0000312|EMBL:CAE29429.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000312|Proteomes:UP000001426};
RN [1] {ECO:0000312|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000312|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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. Also catalyzes the
CC dephosphorylation of D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
CC in vitro. {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 -!- 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; BX572605; CAE29429.1; -; Genomic_DNA.
DR RefSeq; WP_011159524.1; NC_005296.1.
DR AlphaFoldDB; Q6N2R1; -.
DR SMR; Q6N2R1; -.
DR STRING; 258594.RPA3988; -.
DR PRIDE; Q6N2R1; -.
DR DNASU; 2692359; -.
DR EnsemblBacteria; CAE29429; CAE29429; RPA3988.
DR GeneID; 66895105; -.
DR KEGG; rpa:RPA3988; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_2_5; -.
DR OMA; EHQICLE; -.
DR PhylomeDB; Q6N2R1; -.
DR BioCyc; RPAL258594:TX73_RS20355-MON; -.
DR UniPathway; UPA00356; UER00438.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001426; 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.
FT CHAIN 1..180
FT /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT phosphatase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435568"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT ACT_SITE 16
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 14..16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 22..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 56..59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 95
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 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT SITE 56
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT SITE 113
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:P63228"
FT SITE 114
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000250|UniProtKB:P63228"
SQ SEQUENCE 180 AA; 20082 MW; 60572BDA32F9D3C9 CRC64;
MTASAPRRPA AFLDRDGVIN YNDHYVGTRE RLRWMPGIAA AIRQLNAAGY YVFIITNQSG
VARGMFSEDD VRALHRWMLD ELNTQGARID DVRFCPHHVE GTLDAYRVAC EHRKPGPGMI
LDLAKTWPVD MTRSFVIGDS ASDVEAAKAA GIPGFRFEGE DIDVFVKQVL IEMQRAAVSN
