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Database: UniProt
Entry: A0A2S9KG44_9BURK
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Original site: A0A2S9KG44_9BURK 
ID   A0A2S9KG44_9BURK        Unreviewed;       196 AA.
AC   A0A2S9KG44;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=C6P61_06950 {ECO:0000313|EMBL:PRD69394.1};
OS   Malikia spinosa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Malikia.
OX   NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD69394.1, ECO:0000313|Proteomes:UP000238326};
RN   [1] {ECO:0000313|EMBL:PRD69394.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=83 {ECO:0000313|EMBL:PRD69394.1};
RA   Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT   "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT   mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT   serpentinized springs.";
RL   Submitted (MAR-2018) 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}.
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:PRD69394.1}.
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DR   EMBL; PVLR01000016; PRD69394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9KG44; -.
DR   Proteomes; UP000238326; 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   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; TIGR00213; GmhB_yaeD; 1.
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; PF00702; Hydrolase; 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   Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT   ACT_SITE        21
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   ACT_SITE        23
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         29..32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         120..121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   SITE            63
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT   SITE            120
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT   SITE            121
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ   SEQUENCE   196 AA;  20616 MW;  818E70CD21C404AB CRC64;
     MRAGDGTEAS AATPRKAAFL DRDGVINRDR AYVSRWEDFE FVPGAVDAMR RLKKAGYALV
     VVTNQSGIAR GYYSEAQYQA LTAAMQQALL DAGAAVDAVY HCPHHPKGKV AELAIDCDCR
     KPAPGMILRA AKELNLSLAD SILVGDKPSD IEAARAAGVG RAYIVQSDNA ESTTGLAGAD
     AAHADLQSCV AALLPD
//
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