ID A0A1J0VQH3_9NOCA Unreviewed; 297 AA.
AC A0A1J0VQH3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=HAD family hydrolase {ECO:0000313|EMBL:APE34276.1};
GN ORFNames=BOX37_10270 {ECO:0000313|EMBL:APE34276.1};
OS Nocardia mangyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=2213200 {ECO:0000313|EMBL:APE34276.1, ECO:0000313|Proteomes:UP000183810};
RN [1] {ECO:0000313|EMBL:APE34276.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y48 {ECO:0000313|EMBL:APE34276.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; CP018082; APE34276.1; -; Genomic_DNA.
DR RefSeq; WP_071927457.1; NZ_CP018082.1.
DR AlphaFoldDB; A0A1J0VQH3; -.
DR KEGG; nsl:BOX37_10270; -.
DR Proteomes; UP000183810; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF96; D-GLYCEROL 3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:APE34276.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000183810}.
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 16
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 190
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 297 AA; 30964 MW; F7D71117AC01C10A CRC64;
MNRLRDRYEA LLLDLDGTLY RGPAVIDGGP KALAPEGDSA QRLVYVTNNA ARGPGAVAGH
LAELGYPATA ADVVTSAQAA ARMLALRLTP RDRVLVVGTE DLVAEVEAVG LSPIRRFGDT
PPAAVVQGHS PTTAWPDLAE AAYALRAGAL WIAANTDRTL PNERGLAPGN GSMVAALRTA
SDREPLVAGK PYAPLMEDAI ERARTRNALV VGDRLDTDVE GANGLGLDSL LVLTGVSTLD
EVITAPDAQV PTYIATSLDA LNADVVSGPV APSAVAELLR QYPGRAVRVR AADSEIR
//