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
- Functionsamino acid binding / metal ion binding / ornithine carbamoyltransferase activityProcessesarginine biosynthetic process / primary metabolic process / urea cycleComponentscytoplasm
- 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
Resource Link UniProtKB ID P04391 UniProtKB Entry Name OTC1_ECOLI GenBank Protein ID 145344 GenBank Gene ID J02842 - General References
- 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]
- 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]
- 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]
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- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]