ID UGHY_ARATH Reviewed; 298 AA. AC Q8GXV5; O23549; Q67XN1; Q680J5; DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 126. DE RecName: Full=(S)-ureidoglycine aminohydrolase {ECO:0000303|PubMed:20038185}; DE Short=AtUGLYAH; DE EC=3.5.3.26 {ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:20038185, ECO:0000269|PubMed:22493446}; DE Flags: Precursor; GN Name=UGLYAH; Synonyms=UGHY, YlbA; OrderedLocusNames=At4g17050; GN ORFNames=dl4555w, FCAALL.343; 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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND RP SUBCELLULAR LOCATION. RX PubMed=20038185; DOI=10.1021/cb900248n; RA Serventi F., Ramazzina I., Lamberto I., Puggioni V., Gatti R., RA Percudani R.; RT "Chemical basis of nitrogen recovery through the ureide pathway: formation RT and hydrolysis of S-ureidoglycine in plants and bacteria."; RL ACS Chem. Biol. 5:203-214(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9461215; DOI=10.1038/35140; RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E., RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.; RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis RT thaliana."; RL Nature 391:485-488(1998). RN [3] 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., RA Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND CATALYTIC ACTIVITY. 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 [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 36-298 IN COMPLEX WITH SUBSTRATE RP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF RP HIS-221; GLU-235; HIS-237; HIS-241; TYR-252; GLN-275; TYR-287 AND LYS-291, RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22493446; DOI=10.1074/jbc.m111.331819; RA Shin I., Percudani R., Rhee S.; RT "Structural and functional insights into (S)-ureidoglycine aminohydrolase, RT key enzyme of purine catabolism in Arabidopsis thaliana."; RL J. Biol. Chem. 287:18796-18805(2012). CC -!- FUNCTION: Involved in the catabolism of purine nucleotides. Can use CC (S)-2-ureidoglycine as substrate, but not allantoate. The sequential CC activity of AAH, UGLYAH and UAH allows a complete purine breakdown CC without the intermediate generation of urea. CC {ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:20038185, CC ECO:0000269|PubMed:22493446}. 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:19935661, ECO:0000269|PubMed:20038185, CC ECO:0000269|PubMed:22493446}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:20038185, ECO:0000269|PubMed:22493446}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.77 mM for (S)-2-ureidoglycine {ECO:0000269|PubMed:22493446}; CC Note=kcat is 761 sec(-1) for (S)-2-ureidoglycine.; CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:22493446}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:20038185}. CC -!- SIMILARITY: Belongs to the UGHY family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB10485.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB80976.1; Type=Erroneous gene model prediction; Evidence={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; GQ303359; ADH04164.1; -; mRNA. DR EMBL; Z97342; CAB10485.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161545; CAB80976.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE83843.1; -; Genomic_DNA. DR EMBL; AK118019; BAC42652.1; -; mRNA. DR EMBL; AK176787; BAD44550.1; -; mRNA. DR EMBL; AK175872; BAD43635.1; -; mRNA. DR PIR; H71438; H71438. DR RefSeq; NP_193438.2; NM_117809.6. DR PDB; 4E2Q; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=36-298. DR PDB; 4E2S; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=36-298. DR PDBsum; 4E2Q; -. DR PDBsum; 4E2S; -. DR AlphaFoldDB; Q8GXV5; -. DR SMR; Q8GXV5; -. DR STRING; 3702.Q8GXV5; -. DR iPTMnet; Q8GXV5; -. DR PaxDb; 3702-AT4G17050-1; -. DR ProteomicsDB; 245264; -. DR EnsemblPlants; AT4G17050.1; AT4G17050.1; AT4G17050. DR GeneID; 827413; -. DR Gramene; AT4G17050.1; AT4G17050.1; AT4G17050. DR KEGG; ath:AT4G17050; -. DR Araport; AT4G17050; -. DR TAIR; AT4G17050; UGLYAH. DR eggNOG; ENOG502QS1M; Eukaryota. DR HOGENOM; CLU_056083_1_0_1; -. DR InParanoid; Q8GXV5; -. DR OMA; DVRHDMH; -. DR OrthoDB; 553275at2759; -. DR PhylomeDB; Q8GXV5; -. DR BioCyc; ARA:AT4G17050-MONOMER; -. DR BioCyc; MetaCyc:AT4G17050-MONOMER; -. DR BRENDA; 3.5.3.26; 399. DR PRO; PR:Q8GXV5; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q8GXV5; baseline and differential. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0071522; F:ureidoglycine aminohydrolase activity; IDA:TAIR. DR GO; GO:0000256; P:allantoin catabolic process; IDA:TAIR. DR GO; GO:0006145; P:purine nucleobase catabolic process; IDA:TAIR. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:TAIR. DR GO; GO:0010136; P:ureide catabolic process; IDA:TAIR. DR CDD; cd02212; cupin_UGlyAH_C; 1. DR CDD; cd02211; cupin_UGlyAH_N; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR InterPro; IPR017627; UGHY. DR InterPro; IPR044697; UGlyAH_cupin_C. DR InterPro; IPR044704; UGlyAH_cupin_N. DR NCBIfam; TIGR03214; ura-cupin; 1. DR PANTHER; PTHR34571; (S)-UREIDOGLYCINE AMINOHYDROLASE; 1. DR PANTHER; PTHR34571:SF1; (S)-UREIDOGLYCINE AMINOHYDROLASE; 1. DR Pfam; PF07883; Cupin_2; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 1: Evidence at protein level; KW 3D-structure; Endoplasmic reticulum; Hydrolase; Manganese; Metal-binding; KW Purine metabolism; Reference proteome; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..298 FT /note="(S)-ureidoglycine aminohydrolase" FT /id="PRO_0000423444" FT DOMAIN 222..288 FT /note="Cupin type-2" FT /evidence="ECO:0000255" FT BINDING 235 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 237 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 241 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 275 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 287 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22493446" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 221 FT /note="H->A: Decreased activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 235 FT /note="E->A: Loss of manganese binding and loss of FT activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 235 FT /note="E->Q: No effect on manganese binding, but loss of FT activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 237 FT /note="H->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 241 FT /note="H->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 252 FT /note="Y->F: No effect on the affinity for the substrate, FT but decreased activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 275 FT /note="Q->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 287 FT /note="Y->A,F: Loss of activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 291 FT /note="K->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:22493446" FT MUTAGEN 291 FT /note="K->R: Increased affinity for the substrate, but FT decreased activity." FT /evidence="ECO:0000269|PubMed:22493446" FT CONFLICT 138 FT /note="T -> S (in Ref. 6; BAD44550)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="D -> G (in Ref. 6; BAD43635)" FT /evidence="ECO:0000305" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:4E2Q" FT HELIX 51..54 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 67..72 FT /evidence="ECO:0007829|PDB:4E2Q" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 85..94 FT /evidence="ECO:0007829|PDB:4E2Q" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 101..109 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 122..131 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 160..165 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 167..175 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:4E2Q" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 217..225 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 257..262 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 275..283 FT /evidence="ECO:0007829|PDB:4E2Q" FT STRAND 285..292 FT /evidence="ECO:0007829|PDB:4E2Q" SQ SEQUENCE 298 AA; 33673 MW; 50CED7DBA1C40A99 CRC64; MRSLYLIVFI VISLVKASKS DDGFCSAPSI VESDEKTNPI YWKATNPTLS PSHLQDLPGF TRSVYKRDHA LITPESHVYS PLPDWTNTLG AYLITPATGS HFVMYLAKMK EMSSSGLPPQ DIERLIFVVE GAVTLTNTSS SSKKLTVDSY AYLPPNFHHS LDCVESATLV VFERRYEYLG SHTTELIVGS TDKQPLLETP GEVFELRKLL PMSVAYDFNI HTMDFQPGEF LNVKEVHYNQ HGLLLLEGQG IYRLGDNWYP VQAGDVIWMA PFVPQWYAAL GKTRSRYLLY KDVNRNPL //