ID N0B4H8_9BACI Unreviewed; 255 AA.
AC N0B4H8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Sugar phosphatase of the HAD superfamily protein {ECO:0000313|EMBL:AGK55481.1};
GN ORFNames=B1NLA3E_18685 {ECO:0000313|EMBL:AGK55481.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK55481.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK55481.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK55481.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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. NagD family.
CC {ECO:0000256|ARBA:ARBA00006696}.
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DR EMBL; CP005586; AGK55481.1; -; Genomic_DNA.
DR RefSeq; WP_015595523.1; NC_021171.1.
DR AlphaFoldDB; N0B4H8; -.
DR STRING; 666686.B1NLA3E_18685; -.
DR KEGG; baci:B1NLA3E_18685; -.
DR eggNOG; COG0647; Bacteria.
DR HOGENOM; CLU_043473_1_1_9; -.
DR OrthoDB; 9810449at2; -.
DR Proteomes; UP000013300; Chromosome.
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; IPR006354; HAD-SF_hydro_IIA_hyp1.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01460; HAD-SF-IIA; 1.
DR NCBIfam; TIGR01457; HAD-SF-IIA-hyp2; 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:UP000013300}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-2"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000915-3"
SQ SEQUENCE 255 AA; 28022 MW; 786FD38587E123B8 CRC64;
MKKYSGYLID LDGTMYRGTE RIIEAVQFVK RLHEKQIPYL FVTNNSSRTP EQVAEKLREF
DIPAKAQQVF TTSQATANFI NEQNPAARVY VIGEEGIQTA LEQKNFQKAG EDADFVVAGI
DRDISYEKLA VACLAVRNGA TFISTNGDIA IPTERGLLPG NGALTSVITV STQTKPIFIG
KPESIIMEQA LKVLGTKKEE TLMVGDNYDT DILAGMNAGL DTLLVHTGVT SKEHLKGYSN
QPTFVVDSLA DWLEI
//
