Ornithine carbamoyltransferase chain I

Details

Name
Ornithine carbamoyltransferase chain I
Synonyms
  • 2.1.3.3
  • OTCase-1
Gene Name
argI
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016594|Ornithine carbamoyltransferase chain I
MSGFYHKHFLKLLDFTPAELNSLLQLAAKLKADKKSGKEEAKLTGKNIALIFEKDSTRTR
CSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEY
ASVPVWNGLTNEFHPTQLLADLLTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALT
GLDLRLVAPQACWPEAALVTECRALAQQNGGNITLTEDVAKGVEGADFIYTDVWVSMGEA
KEKWAERIALLREYQVNSKMMQLTGNPEVKFLHCLPAFHDDQTTLGKKMAEEFGLHGGME
VTDEVFESAASIVFDQAENRMHTIKAVMVATLSK
Number of residues
334
Molecular Weight
36906.845
Theoretical pI
5.43
GO Classification
Functions
amino acid binding / metal ion binding / ornithine carbamoyltransferase activity
Processes
arginine biosynthetic process / primary metabolic process / urea cycle
Components
cytoplasm
General Function
Ornithine carbamoyltransferase activity
Specific Function
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016595|Ornithine carbamoyltransferase chain I (argI)
ATGTCCGGGTTTTATCATAAGCATTTCCTGAAATTACTCGATTTCACGCCAGCTGAACTC
AACAGCCTGCTGCAGTTAGCCGCGAAGCTGAAAGCCGATAAGAAAAGCGGTAAAGAAGAA
GCCAAACTCACTGGTAAAAACATCGCGCTCATCTTCGAAAAAGACTCGACTCGTACCCGA
TGCTCTTTCGAAGTTGCCGCATATGACCAGGGTGCTCGCGTTACTTATCTCGGCCCAAGC
GGCAGCCAGATTGGTCATAAAGAGTCGATTAAAGACACTGCCCGCGTGCTTGGTCGCATG
TATGACGGTATTCAGTATCGCGGCTATGGTCAGGAGATTGTCGAAACACTGGCGGAATAC
GCTAGCGTGCCGGTATGGAATGGCCTGACCAATGAGTTCCATCCCACGCAGCTGCTGGCG
GATCTTCTCACCATGCAGGAGCATTTGCCCGGCAAAGCGTTCAACGAAATGACGCTGGTC
TATGCAGGTGACGCGCGTAACAACATGGGCAATTCGATGCTCGAAGCTGCGGCGCTTACC
GGTCTGGATTTGCGTCTGGTCGCGCCACAAGCGTGCTGGCCGGAAGCTGCGCTGGTTACG
GAATGCCGCGCCCTGGCACAGCAAAATGGTGGGAATATTACGCTGACTGAAGATGTCGCG
AAGGGAGTTGAAGGTGCTGACTTTATCTATACCGATGTGTGGGTGTCGATGGGGGAAGCA
AAAGAGAAATGGGCGGAACGGATTGCATTGCTGCGTGAATATCAGGTGAACAGCAAGATG
ATGCAGTTGACCGGTAACCCGGAGGTCAAATTCCTCCACTGCCTGCCCGCGTTTCATGAC
GACCAAACGACGCTTGGCAAGAAAATGGCGGAAGAATTTGGCCTACATGGCGGTATGGAA
GTCACTGATGAGGTCTTCGAATCTGCCGCCAGCATTGTTTTTGATCAGGCGGAAAACCGT
ATGCATACTATCAAAGCGGTGATGGTCGCGACGCTCAGTAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04391
UniProtKB Entry NameOTC1_ECOLI
GenBank Protein ID145344
GenBank Gene IDJ02842
General References
  1. Kuo LC, Miller AW, Lee S, Kozuma C: Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis. Biochemistry. 1988 Nov 29;27(24):8823-32. [Article]
  2. Bencini DA, Houghton JE, Hoover TA, Foltermann KF, Wild JR, O'Donovan GA: The DNA sequence of argI from Escherichia coli K12. Nucleic Acids Res. 1983 Dec 10;11(23):8509-18. [Article]
  3. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  7. Legrain C, Halleux P, Stalon V, Glansdorff N: The dual genetic control of ornithine carbamolytransferase in Escherichia coli. A case of bacterial hybrid enzymes. Eur J Biochem. 1972 May;27(1):93-102. [Article]
  8. Legrain C, Stalon V, Glansdorff N: Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary significance and the isolation of lambdaargF and lambdaargI transducing bacteriophages. J Bacteriol. 1976 Oct;128(1):35-8. [Article]
  9. Kuo LC, Lipscomb WN, Kantrowitz ER: Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2250-4. [Article]
  10. Kuo LC, Seaton BA: X-ray diffraction analysis on single crystals of recombinant Escherichia coli ornithine transcarbamoylase. J Biol Chem. 1989 Sep 25;264(27):16246-8. [Article]
  11. Lee S, Shen WH, Miller AW, Kuo LC: Zn2+ regulation of ornithine transcarbamoylase. I. Mechanism of action. J Mol Biol. 1990 Jan 5;211(1):255-69. [Article]
  12. Kuo LC, Caron C, Lee S, Herzberg W: Zn2+ regulation of ornithine transcarbamoylase. II. Metal binding site. J Mol Biol. 1990 Jan 5;211(1):271-80. [Article]
  13. Murata LB, Schachman HK: Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase. Protein Sci. 1996 Apr;5(4):709-18. [Article]
  14. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  15. Jin L, Seaton BA, Head JF: Crystal structure at 2.8 A resolution of anabolic ornithine transcarbamylase from Escherichia coli. Nat Struct Biol. 1997 Aug;4(8):622-5. [Article]
  16. Ha Y, McCann MT, Tuchman M, Allewell NM: Substrate-induced conformational change in a trimeric ornithine transcarbamoylase. Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9550-5. [Article]
  17. Langley DB, Templeton MD, Fields BA, Mitchell RE, Collyer CA: Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism. J Biol Chem. 2000 Jun 30;275(26):20012-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02965Ndelta-(N'-Sulphodiaminophosphinyl)-L-OrnithineexperimentalunknownDetails