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Database: UniProt
Entry: A0A0M9DBI1_9LACO
LinkDB: A0A0M9DBI1_9LACO
Original site: A0A0M9DBI1_9LACO 
ID   A0A0M9DBI1_9LACO        Unreviewed;       259 AA.
AC   A0A0M9DBI1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000256|PIRNR:PIRNR000915};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR000915};
GN   ORFNames=RZ71_13800 {ECO:0000313|EMBL:KOY76582.1};
OS   Apilactobacillus kunkeei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Apilactobacillus.
OX   NCBI_TaxID=148814 {ECO:0000313|EMBL:KOY76582.1, ECO:0000313|Proteomes:UP000037778};
RN   [1] {ECO:0000313|EMBL:KOY76582.1, ECO:0000313|Proteomes:UP000037778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LAko {ECO:0000313|EMBL:KOY76582.1,
RC   ECO:0000313|Proteomes:UP000037778};
RX   PubMed=25953738; DOI=10.1093/gbe/evv079;
RA   Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A.,
RA   Andersson S.G.;
RT   "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing the
RT   Honey Crop and Food Products of Honeybees and Stingless Bees.";
RL   Genome Biol. Evol. 7:1455-1473(2015).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in
CC       vitro. {ECO:0000256|PIRNR:PIRNR000915}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000915-3};
CC       Note=Divalent metal ions. Mg(2+) is the most effective.
CC       {ECO:0000256|PIRSR:PIRSR000915-3};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC       {ECO:0000256|ARBA:ARBA00006696, ECO:0000256|PIRNR:PIRNR000915}.
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:KOY76582.1}.
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DR   EMBL; JXCY01000005; KOY76582.1; -; Genomic_DNA.
DR   RefSeq; WP_053791679.1; NZ_JXCY01000005.1.
DR   AlphaFoldDB; A0A0M9DBI1; -.
DR   PATRIC; fig|148814.8.peg.576; -.
DR   Proteomes; UP000037778; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07530; HAD_Pase_UmpH-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR006354; HAD-SF_hydro_IIA_hyp1.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR   NCBIfam; TIGR01457; HAD-SF-IIA-hyp2; 1.
DR   PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR19288:SF46; HALOACID DEHALOGENASE-LIKE HYDROLASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SFLD; SFLDG01139; C2.A:_Pyridoxal_Phosphate_Phos; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KOY76582.1};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000915, ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000915,
KW   ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037778}.
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        12
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   259 AA;  28334 MW;  D28EF54728317F86 CRC64;
     MTKYKGYFID LDGTIYAGSK RIPAAKRFIE RLQSNGIDFL FVTNNTTKMP EDVVKNLGDN
     HDIHVSVDNV YTAGLATADY VKKDAESNQL DKTAYVVGEK GLITALQNNG FEITDNKPSY
     VIVGLDSSVT YNQLSKAVLL VRDGAKFIGT NPDSNIPTEK GMQPGAGSLV KLVEYATQQK
     PVLIGKPESI IMQNALDKIG LNKSDVVMVG DNYMTDISAG INFGMDTLIV YTGLSTKEQV
     AQKEVQPTHQ IDSLDDWEV
//
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