ID A0A7U9BGX6_ECOLX Unreviewed; 190 AA. AC A0A7U9BGX6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|ARBA:ARBA00018214, 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|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: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: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 REGION 11..13 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT REGION 19..22 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT REGION 53..56 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" FT REGION 110..111 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2" 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 METAL 11 FT /note="Magnesium" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 13 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 92 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 94 FT /note="Zinc; via pros nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 107 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 109 FT /note="Zinc" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 136 FT /note="Magnesium" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT METAL 137 FT /note="Magnesium" FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4" FT BINDING 137 FT /note="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 //