Carbamoyl-phosphate synthase small chain (P0A6F1)

Identification
Name:Carbamoyl-phosphate synthase small chain
Synonyms:
  • Carbamoyl-phosphate synthetase glutamine chain
Gene Name:carA
Enzyme Class:
Biological Properties
General Function:Involved in glutamine catabolic process
Specific Function:2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 2.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
2.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Hydrogen carbonate → 2.0ADP + 1.0Carbamoylphosphate + 1.0L-Glutamate + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Hydrogen carbonate + 1.0Water ↔ 2.0ADP + 1.0Phosphate + 1.0L-Glutamate + 1.0Carbamoylphosphate
ReactionCard
2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb ↔ 2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Hydrogen carbonate + 1.0Water + 1.0Ammonia + 1.0Carbamic acid + 1.0Carboxyphosphate ↔ 2.0ADP + 1.0Phosphate + 1.0L-Glutamate + 1.0Carbamoylphosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb → 2.0Adenosine diphosphate+1.0Thumb+1.0L-Glutamic acid+2.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
1.0Hydrogen carbonate + 1.0Water + 1.0L-Glutamine + 2.0Adenosine triphosphate → 2.0Adenosine diphosphate + 1.0Phosphate + 1.0L-Glutamic acid + 2.0Hydrogen ion + 1.0Carbamoylphosphate + 2.0ADP + 1.0L-Glutamate
ReactionCard
EcoCyc Reactions:
2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 2.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
2.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water + 1.0Hydrogen carbonate → 2.0ADP + 1.0Carbamoylphosphate + 1.0L-Glutamate + 2.0Hydrogen ion + 1.0Phosphate
ReactionCard
Complex Reactions:
2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
2.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Carbonic acid + 1.0Water → 2.0ADP + 1.0Inorganic phosphate + 1.0L-Glutamate + 1.0Carbamoylphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01096CarbamoylphosphateMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbamoyl-phosphate synthase activity
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
Process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
glutamine metabolic process
metabolic process
nitrogen compound metabolic process
Gene Properties
Blattner:b0032
Gene OrientationClockwise
Centisome Percentage:0.64
Left Sequence End29651
Right Sequence End30799
Gene Sequence:
>1149 bp
TTGATTAAGTCAGCGCTATTGGTTCTGGAAGACGGAACCCAGTTTCACGGTCGGGCCATA
GGGGCAACAGGTTCGGCGGTTGGGGAAGTCGTTTTCAATACTTCAATGACCGGTTATCAA
GAAATCCTCACTGATCCTTCCTATTCTCGTCAAATCGTTACTCTTACTTATCCCCATATT
GGCAATGTCGGCACCAATGACGCCGATGAAGAATCTTCTCAGGTACATGCACAAGGTCTG
GTGATTCGCGACCTGCCGCTGATTGCCAGCAACTTCCGTAATACCGAAGACCTCTCTTCT
TACCTGAAACGCCATAACATCGTGGCGATTGCCGATATCGATACCCGTAAGCTGACGCGT
TTACTGCGCGAGAAAGGCGCACAGAATGGCTGCATTATCGCGGGCGATAACCCGGATGCG
GCGCTGGCGTTAGAAAAAGCCCGCGCGTTCCCAGGTCTGAATGGCATGGATCTGGCAAAA
GAAGTGACCACCGCAGAAGCCTATAGCTGGACACAAGGGAGCTGGACGTTGACCGGTGGC
CTGCCAGAAGCGAAAAAAGAAGACGAGCTGCCGTTCCACGTCGTGGCTTATGATTTTGGT
GCCAAGCGCAACATCCTGCGGATGCTGGTGGATAGAGGCTGTCGCCTGACCATCGTTCCG
GCGCAAACTTCTGCGGAAGATGTGCTGAAAATGAATCCAGACGGCATCTTCCTCTCCAAC
GGTCCTGGCGACCCGGCCCCGTGCGATTACGCCATTACCGCCATCCAGAAATTCCTCGAA
ACCGATATTCCGGTATTCGGCATCTGTCTCGGTCATCAGCTGCTGGCGCTGGCGAGCGGT
GCGAAGACTGTCAAAATGAAATTTGGTCACCACGGCGGCAACCATCCGGTTAAAGATGTG
GAGAAAAACGTGGTAATGATCACCGCCCAGAACCACGGTTTTGCGGTGGACGAAGCAACA
TTACCTGCAAACCTGCGTGTCACGCATAAATCCCTGTTCGACGGTACGTTACAGGGCATT
CATCGCACCGATAAACCGGCATTCAGCTTCCAGGGGCACCCTGAAGCCAGCCCTGGTCCA
CACGACGCCGCGCCGTTGTTCGACCACTTTATCGAGTTAATTGAGCAGTACCGTAAAACC
GCTAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:382
Protein Molecular Weight:41431
Protein Theoretical pI:6
PDB File:1CE8
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Carbamoyl-phosphate synthase small chain
MIKSALLVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHI
GNVGTNDADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTR
LLREKGAQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGG
LPEAKKEDELPFHVVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNPDGIFLSN
GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDV
EKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGP
HDAAPLFDHFIELIEQYRKTAK
References
External Links:
ResourceLink
Uniprot ID:P0A6F1
Uniprot Name:CARA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321914
PDB ID:1CE8
Ecogene ID:EG10134
Ecocyc:EG10134
ColiBase:b0032
Kegg Gene:b0032
EchoBASE ID:EB0132
CCDB:CARA_ECOLI
BacMap:16128026
General Reference:
  • 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
  • Bouvier, J., Patte, J. C., Stragier, P. (1984). "Multiple regulatory signals in the control region of the Escherichia coli carAB operon." Proc Natl Acad Sci U S A 81:4139-4143. Pubmed: 6377309
  • 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
  • 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
  • Nyunoya, H., Lusty, C. J. (1983). "The carB gene of Escherichia coli: a duplicated gene coding for the large subunit of carbamoyl-phosphate synthetase." Proc Natl Acad Sci U S A 80:4629-4633. Pubmed: 6308632
  • Piette, J., Nyunoya, H., Lusty, C. J., Cunin, R., Weyens, G., Crabeel, M., Charlier, D., Glansdorff, N., Pierard, A. (1984). "DNA sequence of the carA gene and the control region of carAB: tandem promoters, respectively controlled by arginine and the pyrimidines, regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia coli K-12." Proc Natl Acad Sci U S A 81:4134-4138. Pubmed: 6330744
  • Thoden, J. B., Holden, H. M., Wesenberg, G., Raushel, F. M., Rayment, I. (1997). "Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product." Biochemistry 36:6305-6316. Pubmed: 9174345
  • Thoden, J. B., Huang, X., Raushel, F. M., Holden, H. M. (1999). "The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway." Biochemistry 38:16158-16166. Pubmed: 10587438
  • Thoden, J. B., Miran, S. G., Phillips, J. C., Howard, A. J., Raushel, F. M., Holden, H. M. (1998). "Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis." Biochemistry 37:8825-8831. Pubmed: 9636022
  • Thoden, J. B., Raushel, F. M., Benning, M. M., Rayment, I., Holden, H. M. (1999). "The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution." Acta Crystallogr D Biol Crystallogr 55:8-24. Pubmed: 10089390
  • Thoden, J. B., Raushel, F. M., Wesenberg, G., Holden, H. M. (1999). "The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase." J Biol Chem 274:22502-22507. Pubmed: 10428826
  • Thoden, J. B., Wesenberg, G., Raushel, F. M., Holden, H. M. (1999). "Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding." Biochemistry 38:2347-2357. Pubmed: 10029528
  • Wang, M. X., Church, G. M. (1992). "A whole genome approach to in vivo DNA-protein interactions in E. coli." Nature 360:606-610. Pubmed: 1334233
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901