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Sequence of UAH_ARATH

EC Number:3.5.1.116

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ureidoglycolate amidohydrolase
Q8VXY9
Arabidopsis thaliana
476
51487
Reaction
(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2
Other sequences found for EC No. 3.5.1.116

EC Number:3.5.1.116

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
ureidoglycolate amidohydrolase
Q8VXY9
Arabidopsis thaliana
476
51487
Reaction
(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2
Other sequences found for EC No. 3.5.1.116

General information:

Sequence
show sequence in fasta format
  0 MESLKRFLCS IALLLISLLL PSSLAQQQQH ESIRTMEDFS GYPIHEPGQF GSINLASSLS
 60 VDAPGLQNQI DELSSFSDAP SPSVTRVLYT DKDVSARRYV KNLMALAGLT VREDAVGNIF
120 GKWDGLEPNL PAVATGSHID AIPYSGKYDG VVGVLGAIEA INVLKRSGFK PKRSLEIILF
180 TSEEPTRFGI SCLGSRLLAG SKELAEALKT TVVDGQNVSF IEAARSAGYA EDKDDDLSSV
240 FLKKGSYFAF LELHIEQGPI LEDEGLDIGV VTAIAAPASL KVEFEGNGGH AGAVLMPYRN
300 DAGLAAAELA LAVEKHVLES ESIDTVGTVG ILELHPGAIN SIPSKSHLEI DTRDIDEARR
360 NTVIKKIQES ANTIAKKRKV KLSEFKIVNQ DPPALSDKLV IKKMAEAATE LNLSHKMMIS
420 RAYHDSLFMA RISPMGMIFI PCYKGYSHKP EEYSSPEDMA NGVKVLSLTL AKLSLD
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
372052
Asamizu E.,Sato S.,Kaneko T.,Nakamura Y.,Kotani H.,Miyajima N.,Tabata S.
Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones.
DNA Res.
5
379-391
1998
372053
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
372054
Yamada K.,Lim J.,Dale J.M.,Chen H.,Shinn P.,Palm C.J.,Southwick A.M.,Wu H.C.,Kim C.J.,Nguyen M.,Pham P.K.,Cheuk R.F.,Karlin-Newmann G.,Liu S.X.,Lam B.,Sakano H.,Wu T.,Yu G.,Miranda M.,Quach H.L.,Tripp M.,Chang C.H.,Lee J.M.,Toriumi M.J.,Chan M.M.,Tang C.C.,Onodera C.S.,Deng J.M.,Akiyama K.,Ansari Y.,Arakawa T.,Banh J.,Banno F.,Bowser L.,Brooks S.Y.,Carninci P.,Chao Q.,Choy N.,Enju A.,Goldsmith A.D.,Gurjal M.,Hansen N.F.,Hayashizaki Y.,Johnson-Hopson C.,Hsuan V.W.,Iida K.,Karnes M.,Khan S.,Koesema E.,Ishida J.,Jiang P.X.,Jones T.,Kawai J.,Kamiya A.,Meyers C.,Nakajima M.,Narusaka M.,Seki M.,Sakurai T.,Satou M.,Tamse R.,Vaysberg M.,Wallender E.K.,Wong C.,Yamamura Y.,Yuan S.,Shinozaki K.,Davis R.W.,Theologis A.,Ecker J.R.
Empirical analysis of transcriptional activity in the Arabidopsis genome.
Science
302
842-846
2003
372056
Werner A.K.,Romeis T.,Witte C.P.
Ureide catabolism in Arabidopsis thaliana and Escherichia coli.
Nat. Chem. Biol.
6
19-21
2010
372057
Werner A.K.,Medina-Escobar N.,Zulawski M.,Sparkes I.A.,Cao F.Q.,Witte C.P.
The ureide-degrading reactions of purine ring catabolism employ three amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice.
Plant Physiol.
163
672-681
2013
372058
Shin I.,Han K.,Rhee S.
Structural insights into the substrate specificity of (s)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase.
J. Mol. Biol.
426
3028-3040
2014