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Database: UniProt
Entry: A0A448PGD1_9ACTO
LinkDB: A0A448PGD1_9ACTO
Original site: A0A448PGD1_9ACTO 
ID   A0A448PGD1_9ACTO        Unreviewed;       254 AA.
AC   A0A448PGD1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=UMP phosphatase {ECO:0000313|EMBL:VEI13966.1};
GN   Name=nagD_2 {ECO:0000313|EMBL:VEI13966.1};
GN   ORFNames=NCTC13354_01692 {ECO:0000313|EMBL:VEI13966.1};
OS   Trueperella bialowiezensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Trueperella.
OX   NCBI_TaxID=312285 {ECO:0000313|EMBL:VEI13966.1, ECO:0000313|Proteomes:UP000269542};
RN   [1] {ECO:0000313|EMBL:VEI13966.1, ECO:0000313|Proteomes:UP000269542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13354 {ECO:0000313|EMBL:VEI13966.1,
RC   ECO:0000313|Proteomes:UP000269542};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; LR134476; VEI13966.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448PGD1; -.
DR   KEGG; tbw:NCTC13354_01692; -.
DR   OrthoDB; 9810449at2; -.
DR   Proteomes; UP000269542; Chromosome 1.
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; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01460; HAD-SF-IIA; 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   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269542}.
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   254 AA;  27438 MW;  18D03794D63A428C CRC64;
     MSKAWLIDMD GVLVHEGIAL DGAKEFLGKL EEKGLPHLIL TNNSIFTTRD LSARLATSGL
     EVPPERIWTS ALATARFLAN QTDNKRAYVV GEAGLTTALY EEGFIMTADS PEFVVLGETR
     TYSFESITKA IRLIQSGARF IATNPDATGP SAEGDIPATG AVAAMIETAT GKRPFFVGKP
     NPIMLRNGLN KINAHSEHTA IVGDRMDTDI QAGVETGLTT HLVLTGSTKK EDISLYPYRP
     DFVHNSIANV IEHV
//
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