ID   A0A1H0N0E6_9PSEU        Unreviewed;       263 AA.
AC   A0A1H0N0E6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=NagD protein {ECO:0000313|EMBL:SDO85840.1};
GN   ORFNames=SAMN05421507_104187 {ECO:0000313|EMBL:SDO85840.1};
OS   Lentzea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=641025 {ECO:0000313|EMBL:SDO85840.1, ECO:0000313|Proteomes:UP000199691};
RN   [1] {ECO:0000313|EMBL:SDO85840.1, ECO:0000313|Proteomes:UP000199691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6609 {ECO:0000313|EMBL:SDO85840.1,
RC   ECO:0000313|Proteomes:UP000199691};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNIX01000004; SDO85840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0N0E6; -.
DR   STRING; 641025.SAMN05421507_104187; -.
DR   Proteomes; UP000199691; Unassembled WGS sequence.
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        7
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        9
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   263 AA;  28756 MW;  DB4DCF1F8152626A CRC64;
     MWHYLMDMDG VLVHEEHLIP GADEFVAELR ASETPFLVLT NNSIYTPRDL RARLQRTGLD
     IPEQSIWTSA LATARFLDSQ RPNGSAFVIG EAGLTTALHE IGYVLTDRDP DYVVLGETRT
     YSFTAITKAI RLVEEGAKFI ATNPDATGPS REGSLPATGA VAALIERATG REPYYVGKPN
     PLMMRSALRA LGSHSEQALM IGDRMDTDVR SGLEAGLSTI LVLSGVFSAE TAEMFPYRPT
     RVLKSIAELV GHSADPFGDW TDR
//