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Database: UniProt
Entry: A0A0M8VSP3_9ACTN
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ID   A0A0M8VSP3_9ACTN        Unreviewed;       266 AA.
AC   A0A0M8VSP3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-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=ADL00_08190 {ECO:0000313|EMBL:KOV71510.1};
OS   Streptomyces sp. AS58.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV71510.1, ECO:0000313|Proteomes:UP000037758};
RN   [1] {ECO:0000313|EMBL:KOV71510.1, ECO:0000313|Proteomes:UP000037758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS58 {ECO:0000313|EMBL:KOV71510.1,
RC   ECO:0000313|Proteomes:UP000037758};
RA   Noorani M.;
RL   Submitted (JUL-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:KOV71510.1}.
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DR   EMBL; LGDU01000047; KOV71510.1; -; Genomic_DNA.
DR   RefSeq; WP_053757376.1; NZ_LGDU01000047.1.
DR   AlphaFoldDB; A0A0M8VSP3; -.
DR   PATRIC; fig|1519489.3.peg.1904; -.
DR   OrthoDB; 9772456at2; -.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000037758; 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:SF6; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE; 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};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037758}.
SQ   SEQUENCE   266 AA;  29018 MW;  C1A6C5641D75FB94 CRC64;
     MPDYLDDLRL AHVLADAADA TTTARFKALD LKVDTKPDMT PVSEADRAAE ELIRGQLQRA
     RPRDAILGEE YGVEGTGPRR WVIDPIDGTK NYIRGVPVWA TLISLMEAGE GGYQPVVGLV
     SAPALGRRWW AAKGHGAFTG RSLSSASRLQ VSRVGKLSDA SFAYSSLSGW EERDRLVGFL
     DLTREVWRTR AYGDFWPYMM VAEGSIDMCA EPELSLWDMA ANAIIVTEAG GTFTGLDGRP
     GPHSGDAAAS NGLLHDELLG YLNQRY
//
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