ID D8MNG3_ERWBE Unreviewed; 186 AA.
AC D8MNG3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 Name=hisB {ECO:0000313|EMBL:CAX58370.1};
GN OrderedLocusNames=EbC_08390 {ECO:0000313|EMBL:CAX58370.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX58370.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX58370.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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; FP236843; CAX58370.1; -; Genomic_DNA.
DR RefSeq; WP_013200873.1; NC_014306.1.
DR AlphaFoldDB; D8MNG3; -.
DR STRING; 634500.EbC_08390; -.
DR KEGG; ebi:EbC_08390; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_0_6; -.
DR Proteomes; UP000008793; 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};
KW Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR004682-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
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 186 AA; 20762 MW; 0BDCEDAAF441AC1D CRC64;
MTDKVPAIFL DRDGTMNEDH GYVHEIDNFQ FIDGAIEAMQ ELKKMGYALV MVTNQSGIAR
GIFSEDTFMQ LTEWMDWSLA DRDVDLDGIY FCPHHPEGVI EEYRQQCDCR KPEPGMLLSA
QKELNIDMAA SYMVGDKIDD MLAGKAAGVG IKVLVRSGKP ITEEGEKAAD WVINSLADLP
ARIKQG
//
