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Q8GXV5

- UGHY_ARATH

UniProt

Q8GXV5 - UGHY_ARATH

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Protein

Ureidoglycine aminohydrolase

Gene
UGLYAH, UGHY, YlbA, At4g17050, dl4555w, FCAALL.343
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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 + NH3.2 Publications

Cofactori

Manganese.2 Publications

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 – 2351Manganese
Binding sitei235 – 2351Substrate
Metal bindingi237 – 2371Manganese
Metal bindingi241 – 2411Manganese
Metal bindingi275 – 2751Manganese
Binding sitei275 – 2751Substrate
Binding sitei287 – 2871Substrate
Binding sitei291 – 2911Substrate

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
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Ureidoglycine aminohydrolase (EC:3.5.3.-)
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
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 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 298278Ureidoglycine 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.

Family & Domainsi

Compositional bias

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

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.

Sequence conflict

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

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

« 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: 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.

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: September 3, 2014
This is version 76 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

External Data

Dasty 3

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