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Database: UniProt
Entry: A0A1S6HSM0_9GAMM
LinkDB: A0A1S6HSM0_9GAMM
Original site: A0A1S6HSM0_9GAMM 
ID   A0A1S6HSM0_9GAMM        Unreviewed;       183 AA.
AC   A0A1S6HSM0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=Sps_03381 {ECO:0000313|EMBL:AQS38511.1};
OS   Shewanella psychrophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225848 {ECO:0000313|EMBL:AQS38511.1, ECO:0000313|Proteomes:UP000189545};
RN   [1] {ECO:0000313|EMBL:AQS38511.1, ECO:0000313|Proteomes:UP000189545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP2 {ECO:0000313|EMBL:AQS38511.1,
RC   ECO:0000313|Proteomes:UP000189545};
RA   Xu G., Jian H.;
RT   "Complete genome sequence of Shewanella psychrophila WP2, a deep sea
RT   bacterium isolated from west Pacific sediment.";
RL   Submitted (MAR-2016) 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; CP014782; AQS38511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6HSM0; -.
DR   STRING; 225848.Sps_03381; -.
DR   KEGG; spsw:Sps_03381; -.
DR   OrthoDB; 9781367at2; -.
DR   Proteomes; UP000189545; Chromosome.
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; 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:AQS38511.1};
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        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT   BINDING         8..10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         16..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         50..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         91
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         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         134
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT   SITE            50
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT   SITE            107
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT   SITE            108
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ   SEQUENCE   183 AA;  20245 MW;  43D3637260B249D9 CRC64;
     MSPAVFLDRD GVINIDHGYV HQVDDFEYVE GVFDACRSLK EMGYKLAVVT NQSGIARGMY
     SEDQFHTLTE WMDWNFVDKG VELDGIYYCP HHAEKGVGDY KQDCDCRKPK PGMMLTAAKF
     LKIDLSQSVM VGDKRDDMLA AQAAGIPTRI LVRTGKSVTD EAIAAASVVL DSIAQVPGYL
     KSL
//
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