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Database: UniProt
Entry: J2FX51_9SPHN
LinkDB: J2FX51_9SPHN
Original site: J2FX51_9SPHN 
ID   J2FX51_9SPHN            Unreviewed;       297 AA.
AC   J2FX51;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Histidinol-phosphate phosphatase HisN, inositol monophosphatase family {ECO:0000313|EMBL:EJL21795.1};
GN   ORFNames=PMI02_04976 {ECO:0000313|EMBL:EJL21795.1};
OS   Novosphingobium sp. AP12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1144305 {ECO:0000313|EMBL:EJL21795.1, ECO:0000313|Proteomes:UP000007515};
RN   [1] {ECO:0000313|EMBL:EJL21795.1, ECO:0000313|Proteomes:UP000007515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP12 {ECO:0000313|EMBL:EJL21795.1,
RC   ECO:0000313|Proteomes:UP000007515};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJL21795.1}.
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DR   EMBL; AKKE01000159; EJL21795.1; -; Genomic_DNA.
DR   AlphaFoldDB; J2FX51; -.
DR   STRING; 1144305.PMI02_04976; -.
DR   PATRIC; fig|1144305.3.peg.4596; -.
DR   eggNOG; COG0483; Bacteria.
DR   Proteomes; UP000007515; Unassembled WGS sequence.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01641; Bacterial_IMPase_like_1; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR011809; His_9_proposed.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   NCBIfam; TIGR02067; his_9_HisN; 1.
DR   PANTHER; PTHR43200:SF26; BIFUNCTIONAL PHOSPHATASE IMPL2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43200; PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007515}.
SQ   SEQUENCE   297 AA;  32258 MW;  D114E1534014D5C0 CRC64;
     MQENPQVPLD FELSYKRGHV RRTLTASAAC RQSSAMKIEQ DIALALRLAD AAGEAIRPHF
     RTGLSGDRKD DASPVTVADR AAEEAMRRIL KAECPRDAII GEEFGTEAGS SNRTWVLDPI
     DGTVSFLGGR PIFGTLIALL VDGWPVLGII DQPILRERWV GASGHPTTFN GQEVRTRPCR
     ELSDAMMATT GPQYFDDHQG DHFMALAAKT DHKRLMFGGD CYNYGLLASG HIDLVCEAGL
     KLHDWAALVP IVEGAGGTMC DWNGEPLNID STGGEVLAIG DPARLEDMVE AMACHHH
//
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