AAH_ORYSJ
ID AAH_ORYSJ Reviewed; 491 AA.
AC Q655X8; A0A0P0WZU4; B9FQD8;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable allantoate deiminase;
DE EC=3.5.3.9;
DE AltName: Full=Allantoate amidohydrolase;
DE Short=OsAAH;
DE Flags: Precursor;
GN Name=AAH; OrderedLocusNames=Os06g0665500, LOC_Os06g45480;
GN ORFNames=OsJ_22281, P0473H04.24;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP IDENTIFICATION.
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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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. The
CC sequential activity of AAH, UGLYAH and UAH allows a complete purine
CC breakdown without the intermediate generation of urea.
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;
CC Evidence={ECO:0000269|PubMed:23940254};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=83 uM for allantoate {ECO:0000269|PubMed:23940254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AP003628; BAD45389.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20218.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99030.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE66180.1; -; Genomic_DNA.
DR EMBL; AK073262; BAG93368.1; -; mRNA.
DR RefSeq; XP_015644100.1; XM_015788614.1.
DR AlphaFoldDB; Q655X8; -.
DR SMR; Q655X8; -.
DR STRING; 4530.OS06T0665500-01; -.
DR PaxDb; Q655X8; -.
DR PRIDE; Q655X8; -.
DR EnsemblPlants; Os06t0665500-01; Os06t0665500-01; Os06g0665500.
DR GeneID; 4341777; -.
DR Gramene; Os06t0665500-01; Os06t0665500-01; Os06g0665500.
DR KEGG; osa:4341777; -.
DR eggNOG; ENOG502QSJ5; Eukaryota.
DR HOGENOM; CLU_024588_1_0_1; -.
DR InParanoid; Q655X8; -.
DR OMA; WTLDTDS; -.
DR OrthoDB; 529725at2759; -.
DR PlantReactome; R-OSA-1119502; Allantoin degradation.
DR SABIO-RK; Q655X8; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q655X8; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0047652; F:allantoate deiminase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000256; P:allantoin catabolic process; TAS:UniProtKB.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IEA:EnsemblPlants.
DR GO; GO:0010136; P:ureide catabolic process; IEA:EnsemblPlants.
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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..491
FT /note="Probable allantoate deiminase"
FT /id="PRO_0000423443"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 414..415
FT /note="VR -> FP (in Ref. 4; EEE66180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 52716 MW; 7F631B0C1FBEE731 CRC64;
MALLLSYPRR HPSIHLLILS AYALFLLPIL DGLELGGDGL YREILRDETV LRLKELGKIS
DGEGYLERTF LSPASIRASA VIISWMKDAG LTTWIDQMGN IHGRFEPTNS TKEALLIGSH
MDTVIDAGMY DGALGIISAI SALKVLKVTG RLQRLTRPVE VIAFSDEEGV RFQTTFLGSA
AVAGTLPESI LQVSDKSGTT VQDVLKLNSL EGTANALGEV RYSPESVGSY VEVHIEQGPV
LEALRYPLGV VKGIAGQTRL KVIINGSQGH AGTVPMKLRR DPMVAAAELV LTLETLCKEP
NKFLTYDEEC GCFTEESLAG LVCTVGELLT WPSASNVIPG QVNFTVDIRA MDDKVRETIV
TSFSRLVLQR CDDRLVDCAV EQKHAAAATP CDAELTSRLE RATRSTISSM AAGVRRAGGE
TPVLMSGAGH DAMAMARLTK VGMLFVRCRG GVSHSPEESV MDDDVWAAGL ALVNFIDQNA
VDAAAATAAE S
