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Database: UniProt
Entry: A0A1R4GQU2_9MICC
LinkDB: A0A1R4GQU2_9MICC
Original site: A0A1R4GQU2_9MICC 
ID   A0A1R4GQU2_9MICC        Unreviewed;       263 AA.
AC   A0A1R4GQU2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Hypothetical NagD-like phosphatase, Actinobacterial subfamily {ECO:0000313|EMBL:SJM70484.1};
GN   ORFNames=FM101_12485 {ECO:0000313|EMBL:SJM70484.1};
OS   Arthrobacter rhombi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=71253 {ECO:0000313|EMBL:SJM70484.1, ECO:0000313|Proteomes:UP000195913};
RN   [1] {ECO:0000313|EMBL:SJM70484.1, ECO:0000313|Proteomes:UP000195913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B Ar 00.02 {ECO:0000313|EMBL:SJM70484.1,
RC   ECO:0000313|Proteomes:UP000195913};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUHW01000040; SJM70484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4GQU2; -.
DR   Proteomes; UP000195913; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195913}.
FT   ACT_SITE        17
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   ACT_SITE        19
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ   SEQUENCE   263 AA;  28678 MW;  AB5902A5D2116357 CRC64;
     MSTDDRTPAD IECWLTDMDG VLVHENKAIP GAAELIERWV STSKRFLVLT NNSIYTPRDL
     CARLEAAGLV IPEENIWTSA MATAEFLRRQ SPGGKAFVIG EAGLTTALHD AGFILTDRNP
     DFVVLGETRT YSFEAITRAI RLISQGARFI TTNPDATGPS PEGVMPATGA VAALISQATE
     RQPYVVGKPN PMMFRSALNR IQAHSETTAM IGDRMDTDIV AGMEAGLYTV LVHSGITQPE
     DIERFPFRPD TVFPSVAELL PRL
//
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