HISN_CHLP8
ID HISN_CHLP8 Reviewed; 259 AA.
AC P56160;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Histidinol-phosphatase;
DE Short=HolPase;
DE EC=3.1.3.15;
DE AltName: Full=Histidinol-phosphate phosphatase;
GN Name=hisN; OrderedLocusNames=Cpar_0733;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8626508; DOI=10.1074/jbc.271.14.8176;
RA Rhie G.-E., Avissar Y.J., Beale S.I.;
RT "Structure and expression of the Chlorobium vibrioforme hemB gene and
RT characterization of its encoded enzyme, porphobilinogen synthase.";
RL J. Biol. Chem. 271:8176-8182(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dephosphorylation of histidinol-phosphate to
CC histidinol, the direct precursor of histidine. {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CP001099; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U38348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP001099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P56160; -.
DR SMR; P56160; -.
DR OMA; WRTRAYG; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000008811; Chromosome.
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 GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR InterPro; IPR011809; His_9_proposed.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR TIGRFAMs; TIGR02067; his_9_HisN; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase; Magnesium;
KW Metal-binding.
FT CHAIN 1..259
FT /note="Histidinol-phosphatase"
FT /id="PRO_0000142584"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 84..87
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 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="L -> LAL (in Ref. 1; U38348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28059 MW; 44EEEE19A48232B2 CRC64;
MTPDLQLALE LAEKAGKLTL DYFGRRSLQV FSKRDDTPVT EADRNAEELI RQGISAKFPD
DGLFGEEFDE HPSGNGRRWI IDPIDGTRSF IHGVPLYGVM IALEVEGAMQ LGVINFPALG
ELYQAERGSG AFMNGSPVQV SAIAENSAST VVFTEKEYLL DPPSNHPVDQ LRIDAGLVRG
WGDCYGHMLV ASGRAEVAVD KIMSPWDCAA VIPIVEEAGG CCFDYRGRQS IIDGEGLVSA
NNAMGRNLIA AIGNGERDR
