ALN_ARATH
ID ALN_ARATH Reviewed; 506 AA.
AC Q94AP0; Q8LCA4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Allantoinase;
DE Short=AtALN;
DE EC=3.5.2.5;
GN Name=ALN; OrderedLocusNames=At4g04955; ORFNames=T1J1;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=14976234; DOI=10.1104/pp.103.034637;
RA Yang J., Han K.H.;
RT "Functional characterization of allantoinase genes from Arabidopsis and a
RT nonureide-type legume black locust.";
RL Plant Physiol. 134:1039-1049(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16496096; DOI=10.1007/s00425-006-0236-x;
RA Todd C.D., Polacco J.C.;
RT "AtAAH encodes a protein with allantoate amidohydrolase activity from
RT Arabidopsis thaliana.";
RL Planta 223:1108-1113(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23940254; DOI=10.1104/pp.113.224261;
RA Werner A.K., Medina-Escobar N., Zulawski M., Sparkes I.A., Cao F.Q.,
RA Witte C.P.;
RT "The ureide-degrading reactions of purine ring catabolism employ three
RT amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice.";
RL Plant Physiol. 163:672-681(2013).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=24182190; DOI=10.1111/pce.12218;
RA Watanabe S., Matsumoto M., Hakomori Y., Takagi H., Shimada H., Sakamoto A.;
RT "The purine metabolite allantoin enhances abiotic stress tolerance through
RT synergistic activation of abscisic acid metabolism.";
RL Plant Cell Environ. 37:1022-1036(2014).
CC -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC allantoate by hydrolytic cleavage of the five-member hydantoin ring.
CC Catalyzes the first step of the ureide allantoin degradation followed
CC by the sequential activity of AAH, UGLYAH and UAH which allows a
CC complete purine breakdown without the intermediate generation of urea.
CC {ECO:0000269|PubMed:14976234, ECO:0000269|PubMed:16496096,
CC ECO:0000269|PubMed:23940254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-allantoin + H2O = allantoate + H(+); Xref=Rhea:RHEA:17029,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678,
CC ChEBI:CHEBI:17536; EC=3.5.2.5;
CC Evidence={ECO:0000269|PubMed:23940254};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.47 mM for allantoin {ECO:0000269|PubMed:23940254};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC from (S)-allantoin: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are unable to grow on a medium containing
CC allantoin as the sole nitrogen source, accumulate allantoin and have
CC increased tolerance to drought and osmotic stresses.
CC {ECO:0000269|PubMed:16496096, ECO:0000269|PubMed:23940254,
CC ECO:0000269|PubMed:24182190}.
CC -!- MISCELLANEOUS: In Arabidopsis the intermediary metabolite allantoin
CC plays a role in abiotic stress tolerance via activation of abscisic
CC acid (ABA) metabolism. {ECO:0000305|PubMed:23940254}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Allantoinase family. {ECO:0000305}.
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DR EMBL; AF128393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE82448.1; -; Genomic_DNA.
DR EMBL; AY045901; AAK76575.1; -; mRNA.
DR EMBL; AY113948; AAM44996.1; -; mRNA.
DR EMBL; AY086706; AAM63760.1; -; mRNA.
DR RefSeq; NP_567276.1; NM_116734.3.
DR AlphaFoldDB; Q94AP0; -.
DR SMR; Q94AP0; -.
DR STRING; 3702.AT4G04955.1; -.
DR PaxDb; Q94AP0; -.
DR PRIDE; Q94AP0; -.
DR ProteomicsDB; 244970; -.
DR EnsemblPlants; AT4G04955.1; AT4G04955.1; AT4G04955.
DR GeneID; 825836; -.
DR Gramene; AT4G04955.1; AT4G04955.1; AT4G04955.
DR KEGG; ath:AT4G04955; -.
DR Araport; AT4G04955; -.
DR TAIR; locus:505006432; AT4G04955.
DR eggNOG; KOG2584; Eukaryota.
DR HOGENOM; CLU_015572_4_1_1; -.
DR InParanoid; Q94AP0; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q94AP0; -.
DR BioCyc; ARA:AT4G04955-MON; -.
DR BRENDA; 3.5.2.5; 399.
DR SABIO-RK; Q94AP0; -.
DR UniPathway; UPA00395; UER00653.
DR PRO; PR:Q94AP0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AP0; baseline and differential.
DR Genevisible; Q94AP0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0004038; F:allantoinase activity; IDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:TAIR.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IMP:TAIR.
DR GO; GO:0010136; P:ureide catabolic process; IMP:TAIR.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Purine metabolism; Reference proteome; Zinc.
FT CHAIN 1..506
FT /note="Allantoinase"
FT /id="PRO_0000430041"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 195
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT CONFLICT 426
FT /note="G -> R (in Ref. 4; AAM63760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 55432 MW; 09018BBE5CAB5428 CRC64;
MERTLLQWRL LPLLALIVAL FSFFFASPRS LQGNNKCSLL PHDHYWISSK RIVTPNGLIS
GSVEVKGGII VSVVKEVDWH KSQRSRVKVI DYGEAVLMPG LIDVHVHLDD PGRSEWEGFP
SGTKAAAAGG ITTLVDMPLN SFPSTVSPET LKLKIEAAKN RIHVDVGFWG GLVPDNALNS
SALESLLDAG VLGLKSFMCP SGINDFPMTN ITHIKEGLSV LAKYKRPLLV HAEIERDLEI
EDGSENDPRS YLTYLKTRPT SWEEGAIRNL LSVTENTRIG GSAEGAHLHI VHLSDASSSL
DLIKEAKGKG DSVTVETCPH YLAFSAEEIP EGDTRFKCSP PIRDAANREK LWEALMEGDI
DMLSSDHSPT KPELKLMSDG NFLKAWGGIS SLQFVLPITW SYGKKYGVTL EQVTSWWSDR
PSKLAGLHSK GAVTVGKHAD LVVWEPEAEF DVDEDHPIHF KHPSISAYLG RRLSGKVVST
FVRGNLVFGE GKHASDACGS LQLATT
