ID   A0A1C4YM00_MICEC        Unreviewed;       259 AA.
AC   A0A1C4YM00;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NagD protein {ECO:0000313|EMBL:SCF21793.1};
GN   ORFNames=GA0070618_4139 {ECO:0000313|EMBL:SCF21793.1};
OS   Micromonospora echinospora (Micromonospora purpurea).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF21793.1, ECO:0000313|Proteomes:UP000198253};
RN   [1] {ECO:0000313|EMBL:SCF21793.1, ECO:0000313|Proteomes:UP000198253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF21793.1,
RC   ECO:0000313|Proteomes:UP000198253};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000256|PIRNR:PIRNR000915}.
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DR   EMBL; LT607413; SCF21793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4YM00; -.
DR   InParanoid; A0A1C4YM00; -.
DR   OrthoDB; 9810449at2; -.
DR   Proteomes; UP000198253; Chromosome i.
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   3: Inferred from homology;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3}.
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        15
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   259 AA;  27882 MW;  84F674056AAD25D0 CRC64;
     MIERKPVASW LTDMDGVLVH EGQPVPGAPE FVNRLRASGK PFLVLTNNSI YTPRDLVARL
     NRMGFEVPEH AIWTAALATA QFLADQRPGG TAYVIGEAGL TTALHAVGYV LTDFEPDYVV
     LGETRTYSFE AITKAVRLIN GGARFICTNP DVTGPSVEGA LPAAGSVAAM ISKATGVEPY
     FVGKPNPMMM RSALNTIEAH SESTAMIGDR MDTDILCGLE AGLETILVLT GISTRAEAER
     YPYRPSRIVN SVLDLIDEI
//