HIS7_ARATH
ID HIS7_ARATH Reviewed; 346 AA.
AC Q6NPM8; A0A1P8B6U8; F4JV95; Q67Y38; Q9T021;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Bifunctional phosphatase IMPL2, chloroplastic;
DE AltName: Full=Histidinol-phosphatase;
DE AltName: Full=Histidinol-phosphate phosphatase;
DE Short=HPP;
DE EC=3.1.3.15 {ECO:0000269|PubMed:20023146};
DE AltName: Full=Inositol-phosphate phosphatase;
DE EC=3.1.3.25 {ECO:0000269|PubMed:19339506, ECO:0000269|PubMed:20023146};
DE AltName: Full=L-galactose 1-phosphate phosphatase;
DE EC=3.1.3.93 {ECO:0000269|PubMed:19339506};
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 7;
DE AltName: Full=Protein MYO-INOSITOL MONOPHOSPHATASE-LIKE 2;
DE Flags: Precursor;
GN Name=HISN7; Synonyms=IMPL2; OrderedLocusNames=At4g39120; ORFNames=T22F8.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-346.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547652; DOI=10.1007/s00726-005-0247-0;
RA Stepansky A., Leustek T.;
RT "Histidine biosynthesis in plants.";
RL Amino Acids 30:127-142(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17434988; DOI=10.1104/pp.107.096511;
RA Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.;
RT "Genetic dissection of histidine biosynthesis in Arabidopsis.";
RL Plant Physiol. 144:890-903(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19339506; DOI=10.1104/pp.108.135129;
RA Torabinejad J., Donahue J.L., Gunesekera B.N., Allen-Daniels M.J.,
RA Gillaspy G.E.;
RT "VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate
RT biosynthesis in plants.";
RL Plant Physiol. 150:951-961(2009).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20960216; DOI=10.1007/s10265-010-0381-y;
RA Sato Y., Yazawa K., Yoshida S., Tamaoki M., Nakajima N., Iwai H., Ishii T.,
RA Satoh S.;
RT "Expression and functions of myo-inositol monophosphatase family genes in
RT seed development of Arabidopsis.";
RL J. Plant Res. 124:385-394(2011).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-195, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20023146; DOI=10.1104/pp.109.150805;
RA Petersen L.N., Marineo S., Mandala S., Davids F., Sewell B.T., Ingle R.A.;
RT "The missing link in plant histidine biosynthesis: Arabidopsis myoinositol
RT monophosphatase-like2 encodes a functional histidinol-phosphate
RT phosphatase.";
RL Plant Physiol. 152:1186-1196(2010).
CC -!- FUNCTION: Phosphatase required for histidine production. Acts also on
CC L-galactose 1-phosphate (L-Gal 1-P), D-myoinositol 3-phosphate (D-Ins
CC 3-P) and D-myoinositol 1-phosphate (D-Ins 1-P).
CC {ECO:0000269|PubMed:19339506, ECO:0000269|PubMed:20023146,
CC ECO:0000269|PubMed:20960216}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:19339506, ECO:0000269|PubMed:20023146};
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:0000269|PubMed:20023146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-galactose 1-phosphate + H2O = L-galactose + phosphate;
CC Xref=Rhea:RHEA:26349, ChEBI:CHEBI:15377, ChEBI:CHEBI:37619,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:75522; EC=3.1.3.93;
CC Evidence={ECO:0000269|PubMed:19339506};
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 -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20023146}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. High expression in roots. Expressed in
CC pistil and seed endosperm. {ECO:0000269|PubMed:20023146,
CC ECO:0000269|PubMed:20960216}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages. Detected in
CC globular to heart stage embryos. {ECO:0000269|PubMed:20023146,
CC ECO:0000269|PubMed:20960216}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. {ECO:0000269|PubMed:19339506,
CC ECO:0000269|PubMed:20023146, ECO:0000269|PubMed:20960216}.
CC -!- MISCELLANEOUS: No redundancy with IMPL1 or VTC4.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ANM67312.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC43548.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43627.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80575.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL050351; CAB43627.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161594; CAB80575.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE87019.2; -; Genomic_DNA.
DR EMBL; CP002687; ANM67312.1; ALT_INIT; Genomic_DNA.
DR EMBL; BT010891; AAR24669.1; -; mRNA.
DR EMBL; AK175533; BAD43296.1; -; mRNA.
DR EMBL; AK176630; BAD44393.1; -; mRNA.
DR EMBL; AK220687; BAD93756.1; -; mRNA.
DR EMBL; AK118971; BAC43548.1; ALT_INIT; mRNA.
DR PIR; T08560; T08560.
DR RefSeq; NP_001320164.1; NM_001342523.1.
DR RefSeq; NP_195623.3; NM_120072.5.
DR AlphaFoldDB; Q6NPM8; -.
DR SMR; Q6NPM8; -.
DR STRING; 3702.AT4G39120.1; -.
DR PaxDb; Q6NPM8; -.
DR PRIDE; Q6NPM8; -.
DR ProteomicsDB; 230246; -.
DR EnsemblPlants; AT4G39120.1; AT4G39120.1; AT4G39120.
DR GeneID; 830067; -.
DR Gramene; AT4G39120.1; AT4G39120.1; AT4G39120.
DR KEGG; ath:AT4G39120; -.
DR Araport; AT4G39120; -.
DR eggNOG; KOG2951; Eukaryota.
DR HOGENOM; CLU_044118_4_1_1; -.
DR InParanoid; Q6NPM8; -.
DR OMA; WRTRAYG; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; Q6NPM8; -.
DR BioCyc; ARA:AT4G39120-MON; -.
DR BioCyc; MetaCyc:AT4G39120-MON; -.
DR BRENDA; 3.1.3.15; 399.
DR BRENDA; 3.1.3.25; 399.
DR UniPathway; UPA00031; UER00013.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q6NPM8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6NPM8; baseline and differential.
DR Genevisible; Q6NPM8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IGI:UniProtKB.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052834; F:inositol monophosphate phosphatase activity; IGI:UniProtKB.
DR GO; GO:0010347; F:L-galactose-1-phosphate phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IGI:UniProtKB.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
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; Chloroplast; Histidine biosynthesis; Hydrolase;
KW Magnesium; Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..346
FT /note="Bifunctional phosphatase IMPL2, chloroplastic"
FT /id="PRO_0000383678"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 263..265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 195
FT /note="G->R: Loss of histidinol-phosphatase activity."
FT /evidence="ECO:0000269|PubMed:20023146"
SQ SEQUENCE 346 AA; 38235 MW; 2DA4939BB947517E CRC64;
MLAQSHFFSK SFDLIPPQSP ALRSANPSLR ISSSYSNSRL SFLSSSAIAV PVSRRRFCLT
MASNSKRPNI SNESPSELSD TELDRFAAVG NALADASGEV IRKYFRKKFD IVDKDDMSPV
TIADQMAEEA MVSIIFQNLP SHAIYGEEKG WRCKEESADY VWVLDPIDGT KSFITGKPVF
GTLIALLYKG KPILGLIDQP ILKERWIGMN GRRTKLNGED ISTRSCPKLS QAYLYTTSPH
LFSEEAEKAY SRVRDKVKVP LYGCDCYAYA LLASGFVDLV IESGLKPYDF LALVPVIEGA
GGTITDWTGK RFLWEASSSA VATSFNVVAA GDSDIHQQAL ESLEWH
