ID A0A0C5FQ96_9ACTN Unreviewed; 259 AA.
AC A0A0C5FQ96;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=HAD family hydrolase {ECO:0000313|EMBL:AJP02172.1};
GN ORFNames=TU94_12435 {ECO:0000313|EMBL:AJP02172.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP02172.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP02172.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP02172.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) 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; CP010849; AJP02172.1; -; Genomic_DNA.
DR RefSeq; WP_044381771.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5FQ96; -.
DR STRING; 477245.TU94_12435; -.
DR KEGG; scw:TU94_12435; -.
DR PATRIC; fig|477245.3.peg.2634; -.
DR HOGENOM; CLU_043473_1_1_11; -.
DR OrthoDB; 9810449at2; -.
DR Proteomes; UP000032234; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:AJP02172.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000915-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000915-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000032234}.
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; 27901 MW; 1E8D6824D5C83C8F CRC64;
MADRKPIESW LTDMDGVLIH EGVPIPGADA FLKRLRESGK PFLVLTNNSM YTPRDLHARL
RRMGLEVPIE AIWTSALATA KFLDDQRPGG SAYVIGEAGL TTALHDIGYV LTDHDPDYVV
LGETRTYSFE AMTKAVRLIN GGARFICTNP DETGPSTEGP LPATGAVAAL ITKATGKQPY
FAGKPNPLMM RTGLNAIGAH SETSAMIGDR MDTDVLAGIE AGMQTFLVLT GLTAPGRIED
FPYRPSQVVD SIADLVDRI
//
