ID A4Y7Z1_SHEPC Unreviewed; 183 AA.
AC A4Y7Z1;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=Sputcn32_2353 {ECO:0000313|EMBL:ABP76074.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP76074.1};
RN [1] {ECO:0000313|EMBL:ABP76074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP76074.1};
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., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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; CP000681; ABP76074.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y7Z1; -.
DR STRING; 319224.Sputcn32_2353; -.
DR KEGG; spc:Sputcn32_2353; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_0_6; -.
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:ABP76074.1};
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 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 19..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT BINDING 53..56
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-2"
FT SITE 53
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 110
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 111
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ SEQUENCE 183 AA; 20231 MW; 9C22BACD42FE4D02 CRC64;
MVAVNRAVFL DRDGVINKDH GYVHQVDDFE YIEGVFEACL ALKKMGYKLV VVTNQSGIAR
GMYSEDQFHS LTEWMDWNFA DKGVDLDGIY YCPHHAEKGM GEYKVDCDCR KPKPGMLNDA
AKFLKVDLSQ SVMVGDKADD MQAAKAAGVP TRILVRSGKV IADSSDATIV LDSIADVPDY
LKA
//
