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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

  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 catabolic process Source: TAIR
  3. regulation of transcription, DNA-templated Source: TAIR
  4. 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

Endoplasmic reticulum 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-SubCell
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.

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 – 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.
OMAiFTMYLAN.
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:February 28, 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-P.

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.
OMAiFTMYLAN.
PhylomeDBiQ8GXV5.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8GXV5.

Gene expression databases

GenevestigatoriQ8GXV5.

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(2009) [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(1997) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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 (AUG-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(2009) [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(2011) [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 17, 2013
Last sequence update: February 28, 2003
Last modified: March 31, 2015
This is version 81 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.