PYRP2_ARATH
ID PYRP2_ARATH Reviewed; 373 AA.
AC Q9LDD5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase, chloroplastic {ECO:0000303|PubMed:27490826};
DE Short=AtPyrP2 {ECO:0000303|PubMed:27490826};
DE EC=3.1.3.104 {ECO:0000269|PubMed:27490826};
DE AltName: Full=5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase {ECO:0000305|PubMed:27490826};
DE Short=ARPP phosphatase {ECO:0000305|PubMed:27490826};
DE AltName: Full=Haloacid dehalogenase-like hydrolase domain-containing protein {ECO:0000305};
DE Flags: Precursor;
GN Name=PYRP2 {ECO:0000303|PubMed:27490826};
GN OrderedLocusNames=At4g11570 {ECO:0000312|Araport:AT4G11570};
GN ORFNames=F25E4.190 {ECO:0000312|EMBL:AAL25585.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=27490826; DOI=10.1111/tpj.13291;
RA Sa N., Rawat R., Thornburg C., Walker K.D., Roje S.;
RT "Identification and characterization of the missing phosphatase on the
RT riboflavin biosynthesis pathway in Arabidopsis thaliana.";
RL Plant J. 88:705-716(2016).
CC -!- FUNCTION: Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D-
CC ribitylamino)uracil, also known as ARPP, but has no activity toward
CC flavin mononucleotide (FMN) (PubMed:27490826).
CC {ECO:0000269|PubMed:27490826}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-
CC (D-ribitylamino)uracil + phosphate; Xref=Rhea:RHEA:25197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58421; EC=3.1.3.104;
CC Evidence={ECO:0000269|PubMed:27490826};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:27490826};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=127 uM for 5-amino-6-(5-phospho-D-ribitylamino)uracil
CC {ECO:0000269|PubMed:27490826};
CC Vmax=0.21 umol/min/mg enzyme {ECO:0000269|PubMed:27490826};
CC Note=kcat is 0.13 sec(-1) for 5-amino-6-(5-phospho-D-
CC ribitylamino)uracil. {ECO:0000269|PubMed:27490826};
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:27490826};
CC Temperature dependence:
CC Optimum temperature is 40-50 degrees Celsius.
CC {ECO:0000269|PubMed:27490826};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27490826}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:27490826}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL050399; CAB82162.1; -; Genomic_DNA.
DR EMBL; AL161532; CAB78200.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83025.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83026.1; -; Genomic_DNA.
DR EMBL; AY058171; AAL25585.1; -; mRNA.
DR EMBL; AY098974; AAM19984.1; -; mRNA.
DR EMBL; BT000932; AAN41332.1; -; mRNA.
DR PIR; T10577; T10577.
DR RefSeq; NP_192894.1; NM_117226.3.
DR RefSeq; NP_849359.1; NM_179028.2.
DR AlphaFoldDB; Q9LDD5; -.
DR SMR; Q9LDD5; -.
DR STRING; 3702.AT4G11570.2; -.
DR PaxDb; Q9LDD5; -.
DR PRIDE; Q9LDD5; -.
DR ProteomicsDB; 236603; -.
DR EnsemblPlants; AT4G11570.1; AT4G11570.1; AT4G11570.
DR EnsemblPlants; AT4G11570.2; AT4G11570.2; AT4G11570.
DR GeneID; 826761; -.
DR Gramene; AT4G11570.1; AT4G11570.1; AT4G11570.
DR Gramene; AT4G11570.2; AT4G11570.2; AT4G11570.
DR KEGG; ath:AT4G11570; -.
DR Araport; AT4G11570; -.
DR TAIR; locus:2123141; AT4G11570.
DR eggNOG; KOG2914; Eukaryota.
DR HOGENOM; CLU_055359_1_0_1; -.
DR InParanoid; Q9LDD5; -.
DR OMA; PPAFMLR; -.
DR OrthoDB; 747123at2759; -.
DR PhylomeDB; Q9LDD5; -.
DR BRENDA; 3.1.3.104; 399.
DR PRO; PR:Q9LDD5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9LDD5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0043726; F:5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity; IEA:RHEA.
DR GO; GO:0043621; F:protein self-association; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Plastid; Reference proteome;
KW Riboflavin biosynthesis; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..373
FT /note="5-amino-6-(5-phospho-D-ribitylamino)uracil
FT phosphatase, chloroplastic"
FT /id="PRO_0000439663"
SQ SEQUENCE 373 AA; 42204 MW; BF75146D1D4F25B2 CRC64;
MAEAIGAVSL VGHRPSIVRI TVKNELKTQK SQSIVRFPVK VDYSAKGVLS HLMTQSVKKN
RMSVFPIRAL AMELTKEKKK DDRLPKTWNY LDSGADDKPS LWPPENKADK PSLHNPLLRQ
ERMGCGWLGA IFEWEGVLIE DNPDLDNQSW LTLAQEEGKS PPPAFMLRRV EGMKNEQAIS
EVLCWSRDPV QVRRMAKRKE EIFKALHGGV YRLRDGSQEF VNVLMNNKIP MALVSTRPRE
TLENAVGSIG IRKFFSVIVA SEDVYRGKPD PEMFIYAAQL LDFIPERCIV FGNSNQTIEA
AHDGRMKCVA VASKHPIYEL GAAELVVRRL DELSIIDLKK LADTDLTEFE PELEMEKEDE
RELPSSAVAV DDF
