ID A0A7U9BGX6_ECOLX Unreviewed; 190 AA. AC A0A7U9BGX6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. 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}; RN [1] {ECO:0000313|EMBL:EGI38534.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TA271 {ECO:0000313|EMBL:EGI38534.1}; 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 -!- 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|ARBA:ARBA00005628}. 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 UniPathway; UPA00356; UER00438. 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR004682}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. 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 //