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Database: UniProt
Entry: A0A2W0HI24_9BACI
LinkDB: A0A2W0HI24_9BACI
Original site: A0A2W0HI24_9BACI 
ID   A0A2W0HI24_9BACI        Unreviewed;       168 AA.
AC   A0A2W0HI24;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=CR205_13025 {ECO:0000313|EMBL:PYZ96622.1};
OS   Alteribacter lacisalsi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX   NCBI_TaxID=2045244 {ECO:0000313|EMBL:PYZ96622.1, ECO:0000313|Proteomes:UP000248066};
RN   [1] {ECO:0000313|EMBL:PYZ96622.1, ECO:0000313|Proteomes:UP000248066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSP-3 {ECO:0000313|EMBL:PYZ96622.1,
RC   ECO:0000313|Proteomes:UP000248066};
RA   Wang H.;
RT   "Bacillus sp. nov., a halophilic bacterium isolated from a Yangshapao
RT   Lake.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRSR:PIRSR004682-4};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004682-4};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PYZ96622.1}.
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DR   EMBL; PDOF01000002; PYZ96622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W0HI24; -.
DR   OrthoDB; 9801899at2; -.
DR   Proteomes; UP000248066; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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   InterPro; IPR013954; PNK3P.
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; PF08645; PNK3P; 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};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004682-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248066};
KW   Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   ACT_SITE        7
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   ACT_SITE        9
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
SQ   SEQUENCE   168 AA;  18867 MW;  9E119B1EE210C103 CRC64;
     MKAAFFDRDG TIIEDYPDHE WTHITQPVFK DGAIHVLKEV TRKGYAIIII TNQYIIEEGY
     ITLDQYNDIN SQMVEELGRH GINIHDIYYC PHARTGNCAC IKPRTGMIEK ALSIHPGINL
     NESFMIGDSA ADVELAINLG IKGFGIGIGS AYRNVHEINT IKELTTFL
//
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