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
//