UGHY_ARATH
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 03-AUG-2022, entry version 120.
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};
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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.AT4G17050.1; -.
DR iPTMnet; Q8GXV5; -.
DR PaxDb; Q8GXV5; -.
DR PRIDE; Q8GXV5; -.
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; locus:2130459; AT4G17050.
DR eggNOG; ENOG502QS1M; Eukaryota.
DR HOGENOM; CLU_056083_1_0_1; -.
DR InParanoid; Q8GXV5; -.
DR OMA; DVRHDMH; -.
DR OrthoDB; 980218at2759; -.
DR PhylomeDB; Q8GXV5; -.
DR BioCyc; ARA:AT4G17050-MON; -.
DR BioCyc; MetaCyc:AT4G17050-MON; -.
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 transcription, DNA-templated; 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; -; 1.
DR InterPro; IPR013096; Cupin_2.
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 Pfam; PF07883; Cupin_2; 1.
DR SUPFAM; SSF51182; SSF51182; 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 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
