HISN_STRCO
ID HISN_STRCO Reviewed; 266 AA.
AC Q9K4B1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histidinol-phosphatase;
DE Short=HolPase;
DE EC=3.1.3.15 {ECO:0000305|PubMed:17851715};
DE AltName: Full=Histidinol-phosphate phosphatase;
GN Name=hisN {ECO:0000303|PubMed:17851715}; OrderedLocusNames=SCO5208;
GN ORFNames=SC7E4.05c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP IDENTIFICATION, FUNCTION IN HISTIDINE BIOSYNTHESIS, PHOSPHATASE ACTIVITY,
RP GENE NAME, PATHWAY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-118.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=17851715; DOI=10.1007/s00284-007-9014-7;
RA Marineo S., Cusimano M.G., Limauro D., Coticchio G., Puglia A.M.;
RT "The histidinol phosphate phosphatase involved in histidine biosynthetic
RT pathway is encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2).";
RL Curr. Microbiol. 56:6-13(2008).
CC -!- FUNCTION: Catalyzes the dephosphorylation of histidinol-phosphate to
CC histidinol, the direct precursor of histidine.
CC {ECO:0000305|PubMed:17851715}.
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:0000305|PubMed:17851715};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC {ECO:0000269|PubMed:17851715}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit an auxotrophy for
CC histidine, but can grow on minimal medium supplemented with histidinol.
CC {ECO:0000269|PubMed:17851715}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AL939122; CAB94593.1; -; Genomic_DNA.
DR RefSeq; NP_629355.1; NC_003888.3.
DR RefSeq; WP_003973764.1; NZ_VNID01000008.1.
DR AlphaFoldDB; Q9K4B1; -.
DR SMR; Q9K4B1; -.
DR STRING; 100226.SCO5208; -.
DR GeneID; 1100649; -.
DR KEGG; sco:SCO5208; -.
DR PATRIC; fig|100226.15.peg.5292; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_4_0_11; -.
DR InParanoid; Q9K4B1; -.
DR OMA; WRTRAYG; -.
DR PhylomeDB; Q9K4B1; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR InterPro; IPR011809; His_9_proposed.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR TIGRFAMs; TIGR02067; his_9_HisN; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..266
FT /note="Histidinol-phosphatase"
FT /id="PRO_0000404325"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 118
FT /note="G->R: Requires histidine to grow."
FT /evidence="ECO:0000269|PubMed:17851715"
SQ SEQUENCE 266 AA; 29084 MW; 9C2802DB177B243E CRC64;
MPDYLDDLRL AHVLADAADA ATMDRFKALD LKVETKPDMT PVSEADKAAE ELIRGHLSRA
RPRDSVHGEE FGVAGTGPRR WVIDPIDGTK NYVRGVPVWA TLIALMEAKE GGYQPVVGLV
SAPALGRRWW AVEDHGAFTG RSLTSAHRLH VSQVSTLSDA SFAYSSLSGW EEQGRLDGFL
DLTREVWRTR AYGDFWPYMM VAEGSVDLCA EPELSLWDMA ANAIIVTEAG GTFTGLDGRP
GPHSGNAAAS NGRLHDELLG YLNQRY
