N-acetylornithine carbamoyltransferase
Details
- Name
- N-acetylornithine carbamoyltransferase
- Kind
- protein
- Synonyms
- 2.1.3.9
- AOTCase
- Gene Name
- argF'
- UniProtKB Entry
- Q8P8J2Swiss-Prot
- Organism
- Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
- NCBI Taxonomy ID
- 190485
- Amino acid sequence
>lcl|BSEQ0011080|N-acetylornithine carbamoyltransferase MSLKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSMRTRTSFELGA FQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVARVLGRYVDLIGVRAFPKFVDW SKDREDQVLKSFAKYSPVPVINMETITHPCQELAHALALQEHFGTPDLRGKKYVLTWTYH PKPLNTAVANSALTIATRMGMDVTLLCPTPDYILDERYMDWAAQNVAESGGSLQVSHDID SAYAGADVVYAKSWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRN VKATDAVMDSPNCIAIDEAENRLHVQKAIMAALVGQSRP
- Number of residues
- 339
- Molecular Weight
- 37872.96
- Theoretical pI
- 6.59
- GO Classification
- Functionsamino acid binding / aspartate carbamoyltransferase activity / N-acetylornithine carbamoyltransferase activityProcesses'de novo' pyrimidine nucleobase biosynthetic process / arginine biosynthetic processComponentscytoplasm
- General Function
- Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine.
- Specific Function
- amino acid binding
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011081|N-acetylornithine carbamoyltransferase (argF') ATGTCACTGAAGCACTTCTTGAACACCCAGGACTGGAGCCGCGCCGAACTGGATGCGCTG TTGACCCAGGCCGCGTTGTTCAAACGCAACAAGCTGGGAAGCGAGCTGAAGGGCAAGTCG ATCGCGCTGGTGTTCTTCAACCCGTCCATGCGGACCCGCACCAGCTTCGAGCTGGGCGCG TTCCAGCTGGGTGGGCATGCGGTGGTGCTGCAGCCGGGCAAGGATGCGTGGCCGATCGAA TTCAACCTGGGCACGGTGATGGACGGCGATACCGAGGAGCACATCGCCGAGGTGGCGCGC GTGCTGGGGCGCTACGTCGACCTGATCGGAGTGCGTGCGTTCCCGAAGTTCGTCGACTGG TCCAAGGACCGCGAAGACCAGGTGCTCAAGAGCTTTGCCAAGTATTCGCCGGTGCCGGTG ATCAACATGGAGACCATTACCCACCCGTGCCAGGAGCTGGCGCACGCGCTGGCGCTGCAG GAGCATTTCGGCACCCCGGACCTGCGCGGCAAGAAGTACGTGTTGACCTGGACCTACCAC CCCAAGCCGTTGAACACCGCGGTAGCCAATTCGGCACTGACCATCGCCACGCGCATGGGC ATGGACGTGACCCTGCTGTGCCCGACCCCGGACTACATCCTGGACGAGCGCTACATGGAC TGGGCGGCGCAGAACGTGGCCGAAAGCGGTGGCTCGCTGCAGGTCAGCCACGACATCGAC AGTGCCTATGCCGGCGCCGATGTGGTGTACGCCAAGAGCTGGGGCGCGTTGCCGTTCTTC GGCAACTGGGAGCCGGAAAAGCCGATCCGCGACCAGTACCAGCATTTCATCGTCGACGAA CGCAAGATGGCGCTGACCAACAACGGCGTGTTTTCGCACTGCCTGCCGCTGCGTCGCAAC GTCAAGGCTACTGATGCGGTGATGGATTCGCCCAATTGCATCGCCATCGACGAGGCCGAA AACCGCCTGCATGTGCAGAAGGCGATCATGGCAGCGCTGGTGGGTCAGAGCCGCCCGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q8P8J2 UniProtKB Entry Name AOTC_XANCP GenBank Protein ID 21113385 GenBank Gene ID AE012332 PDB ID(s) 3KZC, 3KZK, 3KZM, 3KZN, 3KZO, 3L02, 3L04, 3L05, 3L06, 3M4J, 3M4N, 3M5C, 3M5D KEGG ID xcc:XCC2249 NCBI Gene ID 998828 - General References
- da Silva AC, Ferro JA, Reinach FC, Farah CS, Furlan LR, Quaggio RB, Monteiro-Vitorello CB, Van Sluys MA, Almeida NF, Alves LM, do Amaral AM, Bertolini MC, Camargo LE, Camarotte G, Cannavan F, Cardozo J, Chambergo F, Ciapina LP, Cicarelli RM, Coutinho LL, Cursino-Santos JR, El-Dorry H, Faria JB, Ferreira AJ, Ferreira RC, Ferro MI, Formighieri EF, Franco MC, Greggio CC, Gruber A, Katsuyama AM, Kishi LT, Leite RP, Lemos EG, Lemos MV, Locali EC, Machado MA, Madeira AM, Martinez-Rossi NM, Martins EC, Meidanis J, Menck CF, Miyaki CY, Moon DH, Moreira LM, Novo MT, Okura VK, Oliveira MC, Oliveira VR, Pereira HA, Rossi A, Sena JA, Silva C, de Souza RF, Spinola LA, Takita MA, Tamura RE, Teixeira EC, Tezza RI, Trindade dos Santos M, Truffi D, Tsai SM, White FF, Setubal JC, Kitajima JP: Comparison of the genomes of two Xanthomonas pathogens with differing host specificities. Nature. 2002 May 23;417(6887):459-63. [Article]
- Shi D, Morizono H, Yu X, Roth L, Caldovic L, Allewell NM, Malamy MH, 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. 2005 Apr 15;280(15):14366-9. Epub 2005 Feb 24. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details N-Acetyl-L-Citrulline experimental unknown target Details N-(3-carboxypropanoyl)-L-norvaline experimental unknown target Details