UAH_ORYSJ
ID UAH_ORYSJ Reviewed; 484 AA.
AC Q2QMN7; A0A0P0YC33; B9GE33; Q0IM51;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ureidoglycolate hydrolase {ECO:0000303|PubMed:23940254};
DE Short=OsUAH {ECO:0000303|PubMed:23940254};
DE EC=3.5.1.116 {ECO:0000269|PubMed:23940254};
DE Flags: Precursor;
GN Name=UAH {ECO:0000303|PubMed:23940254};
GN OrderedLocusNames=Os12g0597500, LOC_Os12g40550;
GN ORFNames=OsJ_36749 {ECO:0000312|EMBL:EEE53540.1};
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=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
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 [3]
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 [4]
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 [5]
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 [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=(S)-ureidoglycolate + 2 H(+) + H2O = CO2 + glyoxylate + 2
CC NH4(+); Xref=Rhea:RHEA:19809, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57296; EC=3.5.1.116;
CC Evidence={ECO:0000269|PubMed:23940254};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8VXY9};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q8VXY9};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q8VXY9};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q8VXY9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=188 uM for ureidoglycolate {ECO:0000269|PubMed:23940254};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; glyoxylate
CC from (S)-ureidoglycolate: step 1/1. {ECO:0000269|PubMed:23940254}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8VXY9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8VXY9}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF30214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE53540.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA99240.2; -; Genomic_DNA.
DR EMBL; AP008218; BAF30214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014968; BAT17934.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE53540.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015620061.1; XM_015764575.1.
DR AlphaFoldDB; Q2QMN7; -.
DR SMR; Q2QMN7; -.
DR STRING; 4530.OS12T0597500-02; -.
DR PaxDb; Q2QMN7; -.
DR PRIDE; Q2QMN7; -.
DR EnsemblPlants; Os12t0597500-02; Os12t0597500-02; Os12g0597500.
DR GeneID; 4352706; -.
DR Gramene; Os12t0597500-02; Os12t0597500-02; Os12g0597500.
DR KEGG; osa:4352706; -.
DR eggNOG; ENOG502QPR4; Eukaryota.
DR OMA; IWPHGRW; -.
DR OrthoDB; 529725at2759; -.
DR BRENDA; 3.5.1.116; 8948.
DR PlantReactome; R-OSA-1119502; Allantoin degradation.
DR SABIO-RK; Q2QMN7; -.
DR UniPathway; UPA00395; UER00656.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR ExpressionAtlas; Q2QMN7; baseline and differential.
DR Genevisible; Q2QMN7; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0004848; F:ureidoglycolate hydrolase activity; IDA:UniProtKB.
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; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..484
FT /note="Ureidoglycolate hydrolase"
FT /id="PRO_0000423447"
FT REGION 193..194
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 262..265
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 284..399
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 431..432
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 456
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT SITE 307
FT /note="Necessary for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q53389"
SQ SEQUENCE 484 AA; 51716 MW; 4BC65DC32DF37591 CRC64;
MATSAAARFL AALAGAAVLL VLLGGAAGAV VGHDDDAAAA RRTMEEFAGF PASDYRGDGG
GGSGGSSPFY VDSDGLQRQI DELASFSDSP VPSVTRVLYS DKDVQARRYI KGIMNQLGLS
IREDAVGNIF GRWEGSEAGL GAVATGSHVD AIPFSGKYDG VVGVLGALEA IRMLKRSGFQ
PKRSLEVIMF TSEEPTRFGI SCLGSRLMAG SEELARSLKE TVDNQNVSFF DAADSAGYKM
HPEELHNVFL KKDDYFAFVE LHIEQGPILE KEGIKIGVVT AIAAPASIKV EFEGNGGHAG
AVLMPARNDA GLAAAELALA VEKHVLESGS IDTVGTVGIL QLHPGAINSI PSKSHVEIDV
RDIDEKRRNN VIEKVHQSAI EISKNRGVLL SEFKIINQDP PALSDKSVIS AMEFAAKQLN
LEYKLMISRA YHDSLFMARI SPMGMIFIPC YKGYSHKPEE YASPEDMANG VKVLALAMAR
LSLQ
