HISN_CORGL
ID HISN_CORGL Reviewed; 260 AA.
AC Q8NS80; Q6M6Y3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Histidinol-phosphatase;
DE Short=HolPase {ECO:0000303|PubMed:16901339};
DE EC=3.1.3.15 {ECO:0000305|PubMed:16901339};
DE AltName: Full=Histidinol-phosphate phosphatase;
GN Name=hisN {ECO:0000303|PubMed:16901339}; OrderedLocusNames=Cgl0799, cg0910;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP IDENTIFICATION, FUNCTION IN HISTIDINE BIOSYNTHESIS, PROBABLE CATALYTIC
RP ACTIVITY, GENE NAME, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16901339; DOI=10.1186/1471-2164-7-205;
RA Mormann S., Lomker A., Ruckert C., Gaigalat L., Tauch A., Puhler A.,
RA Kalinowski J.;
RT "Random mutagenesis in Corynebacterium glutamicum ATCC 13032 using an
RT IS6100-based transposon vector identified the last unknown gene in the
RT histidine biosynthesis pathway.";
RL BMC Genomics 7:205-205(2006).
CC -!- FUNCTION: Catalyzes the dephosphorylation of histidinol-phosphate to
CC histidinol, the direct precursor of histidine.
CC {ECO:0000305|PubMed:16901339}.
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:16901339};
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:16901339}.
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:16901339}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAB98192.1; -; Genomic_DNA.
DR EMBL; BX927150; CAF19505.1; -; Genomic_DNA.
DR RefSeq; NP_600028.1; NC_003450.3.
DR RefSeq; WP_011013898.1; NC_006958.1.
DR AlphaFoldDB; Q8NS80; -.
DR SMR; Q8NS80; -.
DR STRING; 196627.cg0910; -.
DR KEGG; cgb:cg0910; -.
DR KEGG; cgl:Cgl0799; -.
DR PATRIC; fig|196627.13.peg.781; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_4_0_11; -.
DR OMA; WRTRAYG; -.
DR BioCyc; MetaCyc:G18NG-10362-MON; -.
DR BRENDA; 3.1.3.15; 960.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000000582; 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: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..260
FT /note="Histidinol-phosphatase"
FT /id="PRO_0000404324"
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 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 27893 MW; C2B32618972C62B8 CRC64;
MSKYADDLAL ALELAELADS ITLDRFEASD LEVSSKPDMT PVSDADLATE EALREKIATA
RPADSILGEE FGGDVEFSGR QWIIDPIDGT KNYVRGVPVW ATLIALLDNG KPVAGVISAP
ALARRWWASE GAGAWRTFNG SSPRKLSVSQ VSKLDDASLS FSSLSGWAER DLRDQFVSLT
DTTWRLRGYG DFFSYCLVAE GAVDIAAEPE VSLWDLAPLS ILVTEAGGKF TSLAGVDGPH
GGDAVATNGI LHDETLDRLK
