Sequence of AOTC_XANCP
EC Number:2.1.3.9
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
N-acetylornithine carbamoyltransferase
Q8P8J2
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
339
37873
Reaction
carbamoyl phosphate + N2-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline
Other sequences found for EC No. 2.1.3.9
General information:
Sequence
0 MSLKHFLNTQ DWSRAELDAL LTQAALFKRN KLGSELKGKS IALVFFNPSM RTRTSFELGA
60 FQLGGHAVVL QPGKDAWPIE FNLGTVMDGD TEEHIAEVAR VLGRYVDLIG VRAFPKFVDW
120 SKDREDQVLK SFAKYSPVPV INMETITHPC QELAHALALQ EHFGTPDLRG KKYVLTWTYH
180 PKPLNTAVAN SALTIATRMG MDVTLLCPTP DYILDERYMD WAAQNVAESG GSLQVSHDID
240 SAYAGADVVY AKSWGALPFF GNWEPEKPIR DQYQHFIVDE RKMALTNNGV FSHCLPLRRN
300 VKATDAVMDS PNCIAIDEAE NRLHVQKAIM AALVGQSRP
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
514311
da Silva A.C.R.,Ferro J.A.,Reinach F.C.,Farah C.S.,Furlan L.R.,Quaggio R.B.,Monteiro-Vitorello C.B.,Van Sluys M.A.,Almeida N.F. Jr.,Alves L.M.C.,do Amaral A.M.,Bertolini M.C.,Camargo L.E.A.,Camarotte G.,Cannavan F.,Cardozo J.,Chambergo F.,Ciapina L.P.,Cicarelli R.M.B.,Coutinho L.L.,Cursino-Santos J.R.,El-Dorry H.,Faria J.B.,Ferreira A.J.S.,Ferreira R.C.C.,Ferro M.I.T.,Formighieri E.F.,Franco M.C.,Greggio C.C.,Gruber A.,Katsuyama A.M.,Kishi L.T.,Leite R.P.,Lemos E.G.M.,Lemos M.V.F.,Locali E.C.,Machado M.A.,Madeira A.M.B.N.,Martinez-Rossi N.M.,Martins E.C.,Meidanis J.,Menck C.F.M.,Miyaki C.Y.,Moon D.H.,Moreira L.M.,Novo M.T.M.,Okura V.K.,Oliveira M.C.,Oliveira V.R.,Pereira H.A.,Rossi A.,Sena J.A.D.,Silva C.,de Souza R.F.,Spinola L.A.F.,Takita M.A.,Tamura R.E.,Teixeira E.C.,Tezza R.I.D.,Trindade dos Santos M.,Truffi D.,Tsai S.M.,White F.F.,Setubal J.C.,Kitajima J.P.
Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.
Nature
417
459-463
2002
514312
Morizono H.,Cabrera-Luque J.,Shi D.,Gallegos R.,Yamaguchi S.,Yu X.,Allewell N.M.,Malamy M.H.,Tuchman M.
Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis.
J. Bacteriol.
188
2974-2982
2006
514313
Shi D.,Morizono H.,Yu X.,Roth L.,Caldovic L.,Allewell N.M.,Malamy M.H.,Tuchman M.
Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria.
J. Biol. Chem.
280
14366-14369
2005
514314
Shi D.,Yu X.,Roth L.,Morizono H.,Tuchman M.,Allewell N.M.
Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.
Proteins
64
532-542
2006
514315
Shi D.,Yu X.,Cabrera-Luque J.,Chen T.Y.,Roth L.,Morizono H.,Allewell N.M.,Tuchman M.
A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase.
Protein Sci.
16
1689-1699
2007
514316
Li Y.,Yu X.,Ho J.,Fushman D.,Allewell N.M.,Tuchman M.,Shi D.
Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.
Biochemistry
49
6887-6895
2010
