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Protein

(S)-ureidoglycine aminohydrolase

Gene

UGLYAH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the catabolism of purine nucleotides. Can use (S)-2-ureidoglycine as substrate, but not allantoate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea.3 Publications

Catalytic activityi

(S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH3.3 Publications

Cofactori

Mn2+1 Publication

Kineticsi

kcat is 761 sec(-1) for (S)-2-ureidoglycine.

  1. KM=1.77 mM for (S)-2-ureidoglycine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi235 – 2351Manganese1 Publication
    Binding sitei235 – 2351Substrate1 Publication
    Metal bindingi237 – 2371Manganese1 Publication
    Metal bindingi241 – 2411Manganese1 Publication
    Metal bindingi275 – 2751Manganese1 Publication
    Binding sitei275 – 2751Substrate1 Publication
    Binding sitei287 – 2871Substrate1 Publication
    Binding sitei291 – 2911Substrate1 Publication

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • sequence-specific DNA binding transcription factor activity Source: TAIR
    • ureidoglycine aminohydrolase activity Source: TAIR

    GO - Biological processi

    • allantoin catabolic process Source: TAIR
    • purine nucleobase catabolic process Source: TAIR
    • regulation of transcription, DNA-templated Source: TAIR
    • ureide catabolic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Purine metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:GQT-2347-MONOMER.
    BRENDAi3.5.3.26. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    (S)-ureidoglycine aminohydrolase (EC:3.5.3.26)
    Short name:
    AtUGLYAH
    Gene namesi
    Name:UGLYAH
    Synonyms:UGHY, YlbA
    Ordered Locus Names:At4g17050
    ORF Names:dl4555w, FCAALL.343
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G17050.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi221 – 2211H → A: Decreased activity. 1 Publication
    Mutagenesisi235 – 2351E → A: Loss of manganese binding and loss of activity. 1 Publication
    Mutagenesisi235 – 2351E → Q: No effect on manganese binding, but loss of activity. 1 Publication
    Mutagenesisi237 – 2371H → A: Loss of activity. 1 Publication
    Mutagenesisi241 – 2411H → A: Loss of activity. 1 Publication
    Mutagenesisi252 – 2521Y → F: No effect on the affinity for the substrate, but decreased activity. 1 Publication
    Mutagenesisi275 – 2751Q → A: Loss of activity. 1 Publication
    Mutagenesisi287 – 2871Y → A or F: Loss of activity. 1 Publication
    Mutagenesisi291 – 2911K → A: Loss of activity. 1 Publication
    Mutagenesisi291 – 2911K → R: Increased affinity for the substrate, but decreased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 298278(S)-ureidoglycine aminohydrolasePRO_0000423444Add
    BLAST

    Proteomic databases

    PRIDEiQ8GXV5.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT4G17050.1.

    Structurei

    Secondary structure

    1
    298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi42 – 443Combined sources
    Helixi51 – 544Combined sources
    Beta strandi67 – 726Combined sources
    Helixi74 – 763Combined sources
    Beta strandi85 – 9410Combined sources
    Helixi96 – 983Combined sources
    Beta strandi101 – 1099Combined sources
    Beta strandi111 – 1144Combined sources
    Beta strandi122 – 13110Combined sources
    Beta strandi133 – 1364Combined sources
    Beta strandi143 – 1453Combined sources
    Beta strandi149 – 1535Combined sources
    Beta strandi160 – 1656Combined sources
    Beta strandi167 – 1759Combined sources
    Beta strandi187 – 1904Combined sources
    Helixi191 – 1933Combined sources
    Beta strandi204 – 2107Combined sources
    Beta strandi217 – 2259Combined sources
    Beta strandi241 – 2477Combined sources
    Beta strandi249 – 2546Combined sources
    Beta strandi257 – 2626Combined sources
    Beta strandi266 – 2694Combined sources
    Beta strandi275 – 2839Combined sources
    Beta strandi285 – 2928Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E2QX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P36-298[»]
    4E2SX-ray2.59A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P36-298[»]
    ProteinModelPortaliQ8GXV5.
    SMRiQ8GXV5. Positions 39-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi139 – 1424Poly-Ser
    Compositional biasi243 – 2464Poly-Leu

    Sequence similaritiesi

    Belongs to the UGHY family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3257.
    HOGENOMiHOG000219622.
    InParanoidiQ8GXV5.
    KOiK14977.
    OMAiRFIFVVQ.
    PhylomeDBiQ8GXV5.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR013096. Cupin_2.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PfamiPF07883. Cupin_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8GXV5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRSLYLIVFI VISLVKASKS DDGFCSAPSI VESDEKTNPI YWKATNPTLS
    60 70 80 90 100
    PSHLQDLPGF TRSVYKRDHA LITPESHVYS PLPDWTNTLG AYLITPATGS
    110 120 130 140 150
    HFVMYLAKMK EMSSSGLPPQ DIERLIFVVE GAVTLTNTSS SSKKLTVDSY
    160 170 180 190 200
    AYLPPNFHHS LDCVESATLV VFERRYEYLG SHTTELIVGS TDKQPLLETP
    210 220 230 240 250
    GEVFELRKLL PMSVAYDFNI HTMDFQPGEF LNVKEVHYNQ HGLLLLEGQG
    260 270 280 290
    IYRLGDNWYP VQAGDVIWMA PFVPQWYAAL GKTRSRYLLY KDVNRNPL
    Length:298
    Mass (Da):33,673
    Last modified:March 1, 2003 - v1
    Checksum:i50CED7DBA1C40A99
    GO

    Sequence cautioni

    The sequence CAB10485.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence CAB80976.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381T → S in BAD44550 (Ref. 6) Curated
    Sequence conflicti224 – 2241D → G in BAD43635 (Ref. 6) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    GQ303359 mRNA. Translation: ADH04164.1.
    Z97342 Genomic DNA. Translation: CAB10485.1. Sequence problems.
    AL161545 Genomic DNA. Translation: CAB80976.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE83843.1.
    AK118019 mRNA. Translation: BAC42652.1.
    AK176787 mRNA. Translation: BAD44550.1.
    AK175872 mRNA. Translation: BAD43635.1.
    PIRiH71438.
    RefSeqiNP_193438.2. NM_117809.5.
    UniGeneiAt.44735.

    Genome annotation databases

    EnsemblPlantsiAT4G17050.1; AT4G17050.1; AT4G17050.
    GeneIDi827413.
    KEGGiath:AT4G17050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    GQ303359 mRNA. Translation: ADH04164.1.
    Z97342 Genomic DNA. Translation: CAB10485.1. Sequence problems.
    AL161545 Genomic DNA. Translation: CAB80976.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE83843.1.
    AK118019 mRNA. Translation: BAC42652.1.
    AK176787 mRNA. Translation: BAD44550.1.
    AK175872 mRNA. Translation: BAD43635.1.
    PIRiH71438.
    RefSeqiNP_193438.2. NM_117809.5.
    UniGeneiAt.44735.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4E2QX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P36-298[»]
    4E2SX-ray2.59A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P36-298[»]
    ProteinModelPortaliQ8GXV5.
    SMRiQ8GXV5. Positions 39-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT4G17050.1.

    Proteomic databases

    PRIDEiQ8GXV5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G17050.1; AT4G17050.1; AT4G17050.
    GeneIDi827413.
    KEGGiath:AT4G17050.

    Organism-specific databases

    TAIRiAT4G17050.

    Phylogenomic databases

    eggNOGiCOG3257.
    HOGENOMiHOG000219622.
    InParanoidiQ8GXV5.
    KOiK14977.
    OMAiRFIFVVQ.
    PhylomeDBiQ8GXV5.

    Enzyme and pathway databases

    BioCyciARA:GQT-2347-MONOMER.
    BRENDAi3.5.3.26. 399.

    Miscellaneous databases

    PROiQ8GXV5.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR013096. Cupin_2.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PfamiPF07883. Cupin_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria."
      Serventi F., Ramazzina I., Lamberto I., Puggioni V., Gatti R., Percudani R.
      ACS Chem. Biol. 5:203-214(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
    2. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
      Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
      , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
      Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    7. "Ureide catabolism in Arabidopsis thaliana and Escherichia coli."
      Werner A.K., Romeis T., Witte C.P.
      Nat. Chem. Biol. 6:19-21(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    8. "Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana."
      Shin I., Percudani R., Rhee S.
      J. Biol. Chem. 287:18796-18805(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 36-298 IN COMPLEX WITH SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF HIS-221; GLU-235; HIS-237; HIS-241; TYR-252; GLN-275; TYR-287 AND LYS-291, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiUGHY_ARATH
    AccessioniPrimary (citable) accession number: Q8GXV5
    Secondary accession number(s): O23549, Q67XN1, Q680J5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 18, 2013
    Last sequence update: March 1, 2003
    Last modified: July 22, 2015
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.