ID A0A411WT41_9BURK Unreviewed; 184 AA.
AC A0A411WT41;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=gmhB {ECO:0000313|EMBL:QBH99817.1};
GN ORFNames=EYF70_02395 {ECO:0000313|EMBL:QBH99817.1}, GCM10007387_40470
GN {ECO:0000313|EMBL:GGY54164.1};
OS Pseudoduganella albidiflava.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=321983 {ECO:0000313|EMBL:QBH99817.1, ECO:0000313|Proteomes:UP000292307};
RN [1] {ECO:0000313|EMBL:GGY54164.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY54164.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [2] {ECO:0000313|EMBL:QBH99817.1, ECO:0000313|Proteomes:UP000292307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17472 {ECO:0000313|EMBL:QBH99817.1,
RC ECO:0000313|Proteomes:UP000292307};
RA Miess H., Frediansyhah A., Gross H.;
RT "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GGY54164.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY54164.1};
RA Sun Q., Kim S.;
RL Submitted (DEC-2022) 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}.
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DR EMBL; BMWV01000010; GGY54164.1; -; Genomic_DNA.
DR EMBL; CP036401; QBH99817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WT41; -.
DR KEGG; mali:EYF70_02395; -.
DR OrthoDB; 9781367at2; -.
DR Proteomes; UP000292307; Chromosome.
DR Proteomes; UP000628442; 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 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, ECO:0000313|EMBL:QBH99817.1};
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 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 94
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 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT SITE 53
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 103
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 104
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ SEQUENCE 184 AA; 19881 MW; 2FF4A87D0372B004 CRC64;
MPQPKLIILD RDGVINHDSP DFIKSPDEWI PIPGSLEAIA RLNQANYRVV IASNQSGIAR
QLFDITTLNA IHAKMHRLAL QVGADIDAVF FCPHAAADNC DCRKPKPGMF AEISKRYQVS
LKGVPTVGDS LRDLQSGFIS GCVPFLVRTG KGEKTEATGG LPPGTLTFPD LAATVQHILK
TPTP
//
