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Q8GXV5 (Q8GXV5_ARATH) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesSubmitted name:
Ureidoglycine aminohydrolase EMBL ADH04164.1
Gene names
Name:UGLYAH EMBL AEE83843.1
Synonyms:ylbA EMBL ADH04164.1
Ordered Locus Names:AT4G17050 EMBL AEE83843.1, At4g17050 TAIR At4g17050
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome] EMBL BAC42652.1
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

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References

[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
EU, CSHL and WU Arabidopsis Sequencing Project
Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portatelle 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., Dirske W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Kotter 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., 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., Blocker H., Scharfe M., Grimm M., Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-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., Mundlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Montfort 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., Sehkon 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., 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., Hoffmann J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Arabidopsis thaliana full-length cDNA."
Seki M., Iida K., Satou M., Sakurai T., Akiyama K., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"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.
[4]TAIR10
Swarbreck D., Lamesch P., Wilks C., Huala E.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		GQ303359 mRNA. Translation: ADH04164.1.
CP002687 Genomic DNA. Translation: AEE83843.1.
AK118019 mRNA. Translation: BAC42652.1.
IPIIPI00541898.
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[»]
SMRQ8GXV5. Positions 39-298.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT4G17050.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRAt4g17050.

Phylogenomic databases

InParanoidQ8GXV5.
KOK14977.
OMAGSTDKQP.
ProtClustDBCLSN2690303.

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. RmlC_like_cupin. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ8GXV5_ARATH
AccessionPrimary (citable) accession number: Q8GXV5
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·Ontologies·Sequences·References·Cross-refs·Entry info