UGHY_ORYSJ
ID UGHY_ORYSJ Reviewed; 309 AA.
AC Q7F1K9; A0A0P0X6Z2;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable (S)-ureidoglycine aminohydrolase {ECO:0000303|PubMed:23940254};
DE Short=OsUGLYAH {ECO:0000303|PubMed:23940254};
DE EC=3.5.3.26 {ECO:0000269|PubMed:23940254};
DE Flags: Precursor;
GN Name=UGLYAH; Synonyms=UGHY; OrderedLocusNames=Os07g0495000, LOC_Os07g31270;
GN ORFNames=OJ1058_B11.119, OsJ_24321;
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, AND CATALYTIC ACTIVITY.
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)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH4(+);
CC Xref=Rhea:RHEA:25241, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57296, ChEBI:CHEBI:59947; EC=3.5.3.26;
CC Evidence={ECO:0000269|PubMed:23940254};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8GXV5};
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:Q8GXV5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8GXV5}.
CC -!- SIMILARITY: Belongs to the UGHY family. {ECO:0000305}.
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DR EMBL; AP003864; BAC83197.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21606.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01587.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67206.1; -; Genomic_DNA.
DR EMBL; AK060721; BAG87551.1; -; mRNA.
DR EMBL; AK073883; BAG93690.1; -; mRNA.
DR EMBL; AK119204; BAG99577.1; -; mRNA.
DR RefSeq; XP_015644616.1; XM_015789130.1.
DR AlphaFoldDB; Q7F1K9; -.
DR SMR; Q7F1K9; -.
DR STRING; 4530.OS07T0495000-01; -.
DR PaxDb; Q7F1K9; -.
DR PRIDE; Q7F1K9; -.
DR EnsemblPlants; Os07t0495000-01; Os07t0495000-01; Os07g0495000.
DR GeneID; 4343286; -.
DR Gramene; Os07t0495000-01; Os07t0495000-01; Os07g0495000.
DR KEGG; osa:4343286; -.
DR eggNOG; ENOG502QS1M; Eukaryota.
DR HOGENOM; CLU_056083_1_0_1; -.
DR InParanoid; Q7F1K9; -.
DR OMA; PPLYWKV; -.
DR OrthoDB; 980218at2759; -.
DR PlantReactome; R-OSA-1119502; Allantoin degradation.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q7F1K9; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071522; F:ureidoglycine aminohydrolase 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 CDD; cd02212; cupin_UGlyAH_C; 1.
DR CDD; cd02211; cupin_UGlyAH_N; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR044697; UGlyAH_cupin_C.
DR InterPro; IPR044704; UGlyAH_cupin_N.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding;
KW Purine metabolism; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..309
FT /note="Probable (S)-ureidoglycine aminohydrolase"
FT /id="PRO_0000423445"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GXV5"
SQ SEQUENCE 309 AA; 34106 MW; AF85E94E1EFB888A CRC64;
MMLPRLLLLV VASALPLASV AAGAVGVGEG FCSAEPSAAS GGCSGVRPPL YWKATNPTLA
PAHLQDLPGF TRSVYKRDHA LITPESHVFS PLPDWINTLG AYLISPAIGA HFTMYLAKMH
DGSKSALPPK GVERLIFVLQ GSILLSEESG NTHTLLVDSY AYLPANMKHS VISDEVTTLV
IFERRYTTIE GYHPDLIVGS TDKQPLLETP GEVFELRKLL PTSLPYDFNI HIMDFQPGEY
LNVKEVHYNQ HGLLLLEGQG IYRLGDSWYP VQSGDTIWMA PFVPQWYAAL GKTKTRYLLY
KDVNRDPLI
