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Q8GXV5

- UGHY_ARATH

UniProt

Q8GXV5 - UGHY_ARATH

Protein

(S)-ureidoglycine aminohydrolase

Gene

UGLYAH

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    Manganese.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

    1. metal ion binding Source: UniProtKB-KW
    2. sequence-specific DNA binding transcription factor activity Source: TAIR
    3. ureidoglycine aminohydrolase activity Source: TAIR

    GO - Biological processi

    1. allantoin catabolic process Source: TAIR
    2. purine nucleobase metabolic process Source: UniProtKB-KW
    3. regulation of transcription, DNA-templated Source: TAIR

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Purine metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:GQT-2347-MONOMER.

    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: Chromosome 4

    Organism-specific databases

    TAIRiAT4G17050.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8GXV5.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT4G17050.1-P.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiDWINTLG.
    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

    MRSLYLIVFI VISLVKASKS DDGFCSAPSI VESDEKTNPI YWKATNPTLS    50
    PSHLQDLPGF TRSVYKRDHA LITPESHVYS PLPDWTNTLG AYLITPATGS 100
    HFVMYLAKMK EMSSSGLPPQ DIERLIFVVE GAVTLTNTSS SSKKLTVDSY 150
    AYLPPNFHHS LDCVESATLV VFERRYEYLG SHTTELIVGS TDKQPLLETP 200
    GEVFELRKLL PMSVAYDFNI HTMDFQPGEF LNVKEVHYNQ HGLLLLEGQG 250
    IYRLGDNWYP VQAGDVIWMA PFVPQWYAAL GKTRSRYLLY KDVNRNPL 298
    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.
    The sequence CAB80976.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381T → S in BAD44550. 1 PublicationCurated
    Sequence conflicti224 – 2241D → G in BAD43635. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi H71438.
    RefSeqi NP_193438.2. NM_117809.5.
    UniGenei At.44735.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4E2Q X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 36-298 [» ]
    4E2S X-ray 2.59 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 36-298 [» ]
    ProteinModelPortali Q8GXV5.
    SMRi Q8GXV5. Positions 39-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G17050.1-P.

    Proteomic databases

    PRIDEi Q8GXV5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G17050.1 ; AT4G17050.1 ; AT4G17050 .
    GeneIDi 827413.
    KEGGi ath:AT4G17050.

    Organism-specific databases

    TAIRi AT4G17050.

    Phylogenomic databases

    eggNOGi COG3257.
    HOGENOMi HOG000219622.
    InParanoidi Q8GXV5.
    KOi K14977.
    OMAi DWINTLG.
    PhylomeDBi Q8GXV5.

    Enzyme and pathway databases

    BioCyci ARA:GQT-2347-MONOMER.

    Miscellaneous databases

    PROi Q8GXV5.

    Gene expression databases

    Genevestigatori Q8GXV5.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    InterProi IPR013096. Cupin_2.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    Pfami PF07883. Cupin_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 77 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