ID A0A7U9BGX6_ECOLX Unreviewed; 190 AA. AC A0A7U9BGX6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 12-OCT-2022, entry version 6. DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|PIRNR:PIRNR004682}; DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682}; GN ORFNames=ECLG_03711 {ECO:0000313|EMBL:EGI38534.1}; OS Escherichia coli TA271. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656443 {ECO:0000313|EMBL:EGI38534.1, ECO:0000313|Proteomes:UP000004645}; RN [1] {ECO:0000313|EMBL:EGI38534.1, ECO:0000313|Proteomes:UP000004645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TA271 {ECO:0000313|EMBL:EGI38534.1, RC ECO:0000313|Proteomes:UP000004645}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli TA271."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001226}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR004682-4}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, CC ECO:0000256|PIRSR:PIRSR004682-4}; 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:0000256|ARBA:ARBA00004708}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|PIRNR:PIRNR004682}. CC -!- SIMILARITY: Belongs to the gmhB family. CC {ECO:0000256|PIRNR:PIRNR004682}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL884249; EGI38534.1; -; Genomic_DNA. DR SMR; A0A7U9BGX6; -. DR UniPathway; UPA00356; UER00438. DR Proteomes; UP000004645; Unassembled WGS sequence. 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:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 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; TIGR00213; GmhB_yaeD; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PIRNR:PIRNR004682}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR004682}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR004682}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR004682-4}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR004682-4}; Zinc {ECO:0000256|PIRSR:PIRSR004682-4}. FT ACT_SITE 11 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1" FT ACT_SITE 13 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1" FT BINDING 11..13 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT BINDING 11 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 19..22 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT BINDING 53..56 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 110..111 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT BINDING 136 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 137 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 137 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT SITE 53 FT /note="Stabilizes the phosphoryl group" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3" FT SITE 110 FT /note="Contributes to substrate recognition" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3" FT SITE 111 FT /note="Stabilizes the phosphoryl group" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3" SQ SEQUENCE 190 AA; 21138 MW; 331B34A2313B5874 CRC64; MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMLLSA RDYLHIDMAA SYMVGDKLED MQAAAAANVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP QAIKKQQKPA //