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Database: UniProt
Entry: A0A132MND0_9ACTN
LinkDB: A0A132MND0_9ACTN
Original site: A0A132MND0_9ACTN 
ID   A0A132MND0_9ACTN        Unreviewed;       261 AA.
AC   A0A132MND0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidinol-phosphatase {ECO:0000256|ARBA:ARBA00013085};
DE            EC=3.1.3.15 {ECO:0000256|ARBA:ARBA00013085};
DE   AltName: Full=Histidinol-phosphate phosphatase {ECO:0000256|ARBA:ARBA00033209};
GN   ORFNames=LI90_1005 {ECO:0000313|EMBL:KWW99370.1}, TH66_09805
GN   {ECO:0000313|EMBL:KWX04176.1}, TR74_20550
GN   {ECO:0000313|EMBL:KWX06906.1};
OS   Carbonactinospora thermoautotrophica.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Carbonactinosporaceae; Carbonactinospora.
OX   NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99370.1, ECO:0000313|Proteomes:UP000070188};
RN   [1] {ECO:0000313|Proteomes:UP000070598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBT1 {ECO:0000313|Proteomes:UP000070598};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KWX04176.1, ECO:0000313|Proteomes:UP000070659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBT1 {ECO:0000313|EMBL:KWX04176.1,
RC   ECO:0000313|Proteomes:UP000070659};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000070188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA   Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KWW99370.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|EMBL:KWW99370.1};
RA   MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA   Woodward J., Friesen M., Prell J.;
RT   "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT   of multiple isolates of Streptomyces thermoautotrophicus.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC         Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001216};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000256|ARBA:ARBA00004970}.
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:KWW99370.1}.
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DR   EMBL; LAXD01000001; KWW99370.1; -; Genomic_DNA.
DR   EMBL; JYIJ01000016; KWX04176.1; -; Genomic_DNA.
DR   EMBL; JYIK01001083; KWX06906.1; -; Genomic_DNA.
DR   RefSeq; WP_066884706.1; NZ_LAXD01000001.1.
DR   AlphaFoldDB; A0A132MND0; -.
DR   STRING; 1469144.LI90_1005; -.
DR   PATRIC; fig|1469144.10.peg.1122; -.
DR   OrthoDB; 9772456at2; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000070188; Unassembled WGS sequence.
DR   Proteomes; UP000070598; Unassembled WGS sequence.
DR   Proteomes; UP000070659; Unassembled WGS sequence.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR020583; Inositol_monoP_metal-BS.
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.
DR   PROSITE; PS00629; IMP_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KWW99370.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070188}.
SQ   SEQUENCE   261 AA;  28221 MW;  544067D7F7B2886C CRC64;
     MPGFDDDLRL AHVLADAADD TTLARFKAID LRVDTKPDMT PVTDADRTVE ERIRATLGRV
     RPRDAVVGEE FGAEGSSRRS WIIDPIDGTK NFVRGVPVWA TLIALMVDDE PVVGLVSAPA
     LGRRWWAAEG HGAWTGRSLS TATRCQVSQV AALEDASFAY SEITEWEKAG RLEGFLDLNR
     ACWRSRAYGD FWSHMLVAEG AVDVSAEPEV ALWDLAALAV IVMEAGGRFT SLDGTPGPGG
     GSAVCSNGLL HDQALRFLAP R
//
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