Ornithine carbamoyltransferase chain I (P04391)

Identification
Name:Ornithine carbamoyltransferase chain I
Synonyms:
  • OTCase-1
Gene Name:argI
Enzyme Class:
Biological Properties
General Function:Involved in carboxyl- or carbamoyltransferase activity
Specific Function:Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Carbamoylphosphate + 1.0Ornithine + 1.0L-Ornithine ↔ 1.0Citrulline + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Carbamoylphosphate + 1.0Ornithine ↔ 1.0Phosphate + 1.0Citrulline
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Ornithine + 1.0Carbamoylphosphate ↔ 1.0Hydrogen ion + 1.0Citrulline + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Ornithine+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Ornithine + 1.0Carbamoylphosphate + 1.0Ornithine → 1.0Phosphate + 1.0Hydrogen ion + 1.0Citrulline
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Carbamoylphosphate + 1.0Ornithine + 1.0L-Ornithine ↔ 1.0Citrulline + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Ornithine + 1.0Carbamoylphosphate ↔ 1.0Hydrogen ion + 1.0Citrulline + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Carbamoylphosphate + 1.0Ornithine → 1.0Inorganic phosphate + 1.0Citrulline
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01096CarbamoylphosphateMetaboCard
ECMDB00904CitrullineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB23898L-OrnithineMetaboCard
ECMDB00214OrnithineMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Component
macromolecular complex
ornithine carbamoyltransferase complex
protein complex
Function
amino acid binding
binding
carboxyl- or carbamoyltransferase activity
carboxylic acid binding
catalytic activity
ornithine carbamoyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b4254
Gene OrientationCounterclockwise
Centisome Percentage:96.46
Left Sequence End4475330
Right Sequence End4476334
Gene Sequence:
>1005 bp
GTGAAACTGGATGAAATCGCTCGGCTGGCGGGAGTGTCGCGGACCACTGCAAGCTATGTT
ATTAACGGCAAAGCGAAGCAATACCGTGTGAGCGACAAAACCGTTGAAAAAGTCATGGCT
GTGGTGCGTGAGCACAATTACCACCCGAACGCCGTGGCAGCTGGGCTTCGTGCTGGACGC
ACACGTTCTATTGGTCTTGTGATCCCCGATCTGGAGAACACCAGCTATACCCGCATCGCT
AACTATCTTGAACGCCAGGCGCGGCAACGGGGTTATCAACTGCTGATTGCCTGCTCAGAA
GATCAGCCAGACAACGAAATGCGGTGCATTGAGCACCTTTTACAGCGTCAGGTTGATGCC
ATTATTGTTTCGACGTCGTTGCCTCCTGAGCATCCTTTTTATCAACGCTGGGCTAACGAC
CCGTTCCCGATTGTCGCGCTGGACCGCGCCCTCGATCGTGAACACTTCACCAGCGTGGTT
GGTGCCGATCAGGATGATGCCGAAATGCTGGCGGAAGAGTTACGTAAGTTTCCCGCCGAG
ACGGTGCTTTATCTTGGTGCGCTACCGGAGCTTTCTGTCAGCTTCCTGCGTGAACAAGGT
TTCCGTACTGCCTGGAAAGATGATCCGCGCGAAGTGCATTTCCTGTATGCCAACAGCTAT
GAGCGGGAGGCGGCTGCCCAGTTATTCGAAAAATGGCTGGAAACGCATCCGATGCCGCAG
GCGCTGTTCACAACGTCGTTTGCGTTGTTGCAAGGAGTGATGGATGTCACGCTGCGTCGC
GACGGCAAACTGCCTTCTGACCTGGCAATTGCCACCTTTGGCGATAACGAACTGCTCGAC
TTCTTACAGTGTCCGGTGCTGGCAGTGGCTCAACGTCACCGCGATGTCGCAGAGCGTGTG
CTGGAGATTGTCCTGGCAAGCCTGGACGAACCGCGTAAGCCAAAACCTGGTTTAACGCGC
ATTAAACGTAATCTCTATCGCCGCGGCGTGCTCAGCCGTAGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:334
Protein Molecular Weight:36907
Protein Theoretical pI:5
PDB File:1DUV
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Ornithine carbamoyltransferase chain I
MSGFYHKHFLKLLDFTPAELNSLLQLAAKLKADKKSGKEEAKLTGKNIALIFEKDSTRTR
CSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEY
ASVPVWNGLTNEFHPTQLLADLLTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALT
GLDLRLVAPQACWPEAALVTECRALAQQNGGNITLTEDVAKGVEGADFIYTDVWVSMGEA
KEKWAERIALLREYQVNSKMMQLTGNPEVKFLHCLPAFHDDQTTLGKKMAEEFGLHGGME
VTDEVFESAASIVFDQAENRMHTIKAVMVATLSK
References
External Links:
ResourceLink
Uniprot ID:P04391
Uniprot Name:OTC1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321961
PDB ID:1DUV
Ecogene ID:EG10069
Ecocyc:EG10069
ColiBase:b4254
Kegg Gene:b4254
EchoBASE ID:EB0067
CCDB:OTC1_ECOLI
BacMap:16132076
General Reference:
  • Bencini, D. A., Houghton, J. E., Hoover, T. A., Foltermann, K. F., Wild, J. R., O'Donovan, G. A. (1983). "The DNA sequence of argI from Escherichia coli K12." Nucleic Acids Res 11:8509-8518. Pubmed: 6369246
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Ha, Y., McCann, M. T., Tuchman, M., Allewell, N. M. (1997). "Substrate-induced conformational change in a trimeric ornithine transcarbamoylase." Proc Natl Acad Sci U S A 94:9550-9555. Pubmed: 9275160
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jin, L., Seaton, B. A., Head, J. F. (1997). "Crystal structure at 2.8 A resolution of anabolic ornithine transcarbamylase from Escherichia coli." Nat Struct Biol 4:622-625. Pubmed: 9253409
  • Kuo, L. C., Miller, A. W., Lee, S., Kozuma, C. (1988). "Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis." Biochemistry 27:8823-8832. Pubmed: 3072022
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646