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Database: UniProt
Entry: Q07RN4_RHOP5
LinkDB: Q07RN4_RHOP5
Original site: Q07RN4_RHOP5 
ID   Q07RN4_RHOP5            Unreviewed;       177 AA.
AC   Q07RN4;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|ARBA:ARBA00031828, ECO:0000256|PIRNR:PIRNR004682};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682};
GN   OrderedLocusNames=RPE_1450 {ECO:0000313|EMBL:ABJ05400.1};
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ05400.1};
RN   [1] {ECO:0000313|EMBL:ABJ05400.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53 {ECO:0000313|EMBL:ABJ05400.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR004682}.
CC   -!- SIMILARITY: Belongs to the gmhB family.
CC       {ECO:0000256|PIRNR:PIRNR004682}.
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DR   EMBL; CP000463; ABJ05400.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07RN4; -.
DR   STRING; 316055.RPE_1450; -.
DR   KEGG; rpe:RPE_1450; -.
DR   eggNOG; COG0241; Bacteria.
DR   HOGENOM; CLU_085077_3_2_5; -.
DR   OrthoDB; 9814110at2; -.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07503; HAD_HisB-N; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR   NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR   PANTHER; PTHR42891; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR   PANTHER; PTHR42891:SF1; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; HAD-like; 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, ECO:0000313|EMBL:ABJ05400.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004682-4};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   ACT_SITE        15
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         138
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   SITE            55
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT   SITE            112
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT   SITE            113
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ   SEQUENCE   177 AA;  19546 MW;  1B3A4DCC35F7BA1E CRC64;
     MTARVPRPAA FLDRDGVINY NDHYVGSRDR FRWMPGVASA IRRLNDAGYY VFVISNQSGV
     ARGMFSEDDV RALHVWMLAE LASQGARIDD LRFCPYHPDG IVEAYRRVSD DRKPGPGMIL
     DLMANWPVER ERSFVIGDSP IDIEAAAAAG IAGHLFAGGD LDVFVADVLN KTQFAAS
//
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