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Q8GXV5 (UGHY_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ureidoglycine aminohydrolase

EC=3.5.3.-
Gene names
Name:UGLYAH
Synonyms:UGHY, YlbA
Ordered Locus Names:At4g17050
ORF Names:dl4555w, FCAALL.343
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.8

Catalytic activity

(S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH3. Ref.1 Ref.7

Cofactor

Manganese. Ref.1 Ref.8

Subunit structure

Homooctamer. Ref.8

Subcellular location

Endoplasmic reticulum Ref.1.

Biophysicochemical properties

Kinetic parameters:

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

KM=1.77 mM for (S)-2-ureidoglycine Ref.8

Sequence caution

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 298278Ureidoglycine aminohydrolase
PRO_0000423444

Regions

Compositional bias139 – 1424Poly-Ser
Compositional bias243 – 2464Poly-Leu

Sites

Metal binding2351Manganese
Metal binding2371Manganese
Metal binding2411Manganese
Metal binding2751Manganese
Binding site2351Substrate
Binding site2751Substrate
Binding site2871Substrate
Binding site2911Substrate

Experimental info

Mutagenesis2211H → A: Decreased activity. Ref.8
Mutagenesis2351E → A: Loss of manganese binding and loss of activity. Ref.8
Mutagenesis2351E → Q: No effect on manganese binding, but loss of activity. Ref.8
Mutagenesis2371H → A: Loss of activity. Ref.8
Mutagenesis2411H → A: Loss of activity. Ref.8
Mutagenesis2521Y → F: No effect on the affinity for the substrate, but decreased activity. Ref.8
Mutagenesis2751Q → A: Loss of activity. Ref.8
Mutagenesis2871Y → A or F: Loss of activity. Ref.8
Mutagenesis2911K → A: Loss of activity. Ref.8
Mutagenesis2911K → R: Increased affinity for the substrate, but decreased activity. Ref.8
Sequence conflict1381T → S in BAD44550. Ref.6
Sequence conflict2241D → G in BAD43635. Ref.6

Secondary structure

................................................ 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8GXV5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 50CED7DBA1C40A99

FASTA29833,673
        10         20         30         40         50         60 
MRSLYLIVFI VISLVKASKS DDGFCSAPSI VESDEKTNPI YWKATNPTLS PSHLQDLPGF 

        70         80         90        100        110        120 
TRSVYKRDHA LITPESHVYS PLPDWTNTLG AYLITPATGS HFVMYLAKMK EMSSSGLPPQ 

       130        140        150        160        170        180 
DIERLIFVVE GAVTLTNTSS SSKKLTVDSY AYLPPNFHHS LDCVESATLV VFERRYEYLG 

       190        200        210        220        230        240 
SHTTELIVGS TDKQPLLETP GEVFELRKLL PMSVAYDFNI HTMDFQPGEF LNVKEVHYNQ 

       250        260        270        280        290 
HGLLLLEGQG IYRLGDNWYP VQAGDVIWMA PFVPQWYAAL GKTRSRYLLY KDVNRNPL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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: FUNCTION, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 36-298 IN COMPLEX WITH SUBSTRATE AND COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-221; GLU-235; HIS-237; HIS-241; TYR-252; GLN-275; TYR-287 AND LYS-291, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRH71438.
RefSeqNP_193438.2. NM_117809.5.
UniGeneAt.44735.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ8GXV5.
SMRQ8GXV5. Positions 39-298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G17050.1-P.

Proteomic databases

PRIDEQ8GXV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G17050.1; AT4G17050.1; AT4G17050.
GeneID827413.
KEGGath:AT4G17050.

Organism-specific databases

TAIRAT4G17050.

Phylogenomic databases

eggNOGCOG3257.
HOGENOMHOG000219622.
InParanoidQ8GXV5.
KOK14977.
OMADWINTLG.
PhylomeDBQ8GXV5.

Enzyme and pathway databases

BioCycARA:GQT-2347-MONOMER.

Gene expression databases

GenevestigatorQ8GXV5.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF07883. Cupin_2. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

PROQ8GXV5.

Entry information

Entry nameUGHY_ARATH
AccessionPrimary (citable) accession number: Q8GXV5
Secondary accession number(s): O23549, Q67XN1, Q680J5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names