AAH_ARATH
ID AAH_ARATH Reviewed; 525 AA.
AC O49434;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Allantoate deiminase;
DE EC=3.5.3.9;
DE AltName: Full=Allantoate amidohydrolase;
DE Short=AtAAH;
DE Flags: Precursor;
GN Name=AAH; OrderedLocusNames=At4g20070; ORFNames=F18F4.170;
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;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, SUBUNIT, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18065556; DOI=10.1104/pp.107.110809;
RA Werner A.K., Sparkes I.A., Romeis T., Witte C.P.;
RT "Identification, biochemical characterization, and subcellular localization
RT of allantoate amidohydrolases from Arabidopsis and soybean.";
RL Plant Physiol. 146:418-430(2008).
RN [6]
RP FUNCTION.
RX PubMed=19935661; DOI=10.1038/nchembio.265;
RA Werner A.K., Romeis T., Witte C.P.;
RT "Ureide catabolism in Arabidopsis thaliana and Escherichia coli.";
RL Nat. Chem. Biol. 6:19-21(2010).
RN [7]
RP FUNCTION, AND DISRUPTION 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).
CC -!- FUNCTION: Involved in the catabolism of purine nucleotides. Can use
CC allantoate as substrate, but not Nalpha-carbamoyl-L-Asp, Nalpha-
CC carbamoyl-L-Ala or Nalpha-carbamoyl-Gly. The sequential activity of
CC AAH, UGLYAH and UAH allows a complete purine breakdown without the
CC intermediate generation of urea. {ECO:0000269|PubMed:16496096,
CC ECO:0000269|PubMed:18065556, ECO:0000269|PubMed:19935661,
CC ECO:0000269|PubMed:23940254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 +
CC NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59947; EC=3.5.3.9; Evidence={ECO:0000269|PubMed:16496096,
CC ECO:0000269|PubMed:18065556};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18065556};
CC -!- ACTIVITY REGULATION: Inhibited by borate, fluoride, L-Asn and L-Asp,
CC but not by phenylphosphorodiamidate. {ECO:0000269|PubMed:18065556}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 27.2 sec(-1) for allantoate.
CC {ECO:0000269|PubMed:18065556};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18065556}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:18065556}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves,
CC flowers, siliques and seeds. {ECO:0000269|PubMed:16496096}.
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 and accumulate allantoate.
CC {ECO:0000269|PubMed:16496096, ECO:0000269|PubMed:18065556,
CC ECO:0000269|PubMed:23940254}.
CC -!- SIMILARITY: Belongs to the peptidase M20A 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; AL021637; CAA16615.2; -; Genomic_DNA.
DR EMBL; AL161552; CAB79007.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84269.1; -; Genomic_DNA.
DR EMBL; BT025334; ABF57290.1; -; mRNA.
DR PIR; F85227; F85227.
DR RefSeq; NP_193740.1; NM_118126.4.
DR AlphaFoldDB; O49434; -.
DR SMR; O49434; -.
DR STRING; 3702.AT4G20070.1; -.
DR MEROPS; M20.A07; -.
DR PaxDb; O49434; -.
DR PRIDE; O49434; -.
DR ProteomicsDB; 245079; -.
DR EnsemblPlants; AT4G20070.1; AT4G20070.1; AT4G20070.
DR GeneID; 827752; -.
DR Gramene; AT4G20070.1; AT4G20070.1; AT4G20070.
DR KEGG; ath:AT4G20070; -.
DR Araport; AT4G20070; -.
DR TAIR; locus:2119732; AT4G20070.
DR eggNOG; ENOG502QSJ5; Eukaryota.
DR HOGENOM; CLU_024588_6_1_1; -.
DR InParanoid; O49434; -.
DR OMA; WTLDTDS; -.
DR OrthoDB; 529725at2759; -.
DR PhylomeDB; O49434; -.
DR BioCyc; ARA:AT4G20070-MON; -.
DR BioCyc; MetaCyc:AT4G20070-MON; -.
DR BRENDA; 3.5.3.9; 399.
DR PRO; PR:O49434; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49434; baseline and differential.
DR Genevisible; O49434; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0047652; F:allantoate deiminase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IDA:TAIR.
DR GO; GO:0010136; P:ureide catabolic process; IDA:TAIR.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..53
FT /evidence="ECO:0000255"
FT CHAIN 54..525
FT /note="Allantoate deiminase"
FT /id="PRO_0000315838"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 56524 MW; 8744B53F4C28ADE0 CRC64;
MAVPHPSSSS SRSHPFLSHV YHTSFHHHHH HNHPSLVLFW CLVFSLLSPL ALSSSSSSSS
SSSDSSSSSS SHISLGIGET EGTKHDLHQA ILRDEAVARL HELGQVSDAA THLERTFMSP
ASIRAIPLIR GWMEDAGLST WVDYMGNVHG RVEPKNGSSQ ALLIGSHMDT VIDAGKYDGS
LGIISAISAL KVLKIDGRLG ELKRPVEVIA FSDEEGVRFQ STFLGSAALA GIMPVSRLEV
TDKSGISVQD ALKENSIDIT DENLMQLKYD PASVWGYVEV HIEQGPVLEW VGYPLGVVKG
IAGQTRLKVT VKGSQGHAGT VPMSMRQDPM TGAAELIVLL ESVCKNPKDY LSCNVQCNED
TVESLANSLV CTVGEISTWP SASNVIPGQV TFTVDLRTID DVGRKAILHD LSTRMYQICD
KRSLLCSIER KHDADAVMSD PQLSLQLKSA AQSALKKMTG EVQDEVPVLM SGAGHDAMAM
AHLTKVGMLF VRCRGGISHS PAEHVLDDDV GAAGLAILEF LESQM
