Carbamoyl-phosphate synthase large chain (P00968)

Identification
Name:Carbamoyl-phosphate synthase large chain
Synonyms:
  • Carbamoyl-phosphate synthetase ammonia chain
Gene Name:carB
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
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
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01096CarbamoylphosphateMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB00595Hydrogen carbonateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
carbamoyl-phosphate synthase activity
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
purine nucleoside binding
Process
metabolic process
nitrogen compound metabolic process
Gene Properties
Blattner:b0033
Gene OrientationClockwise
Centisome Percentage:0.66
Left Sequence End30817
Right Sequence End34038
Gene Sequence:
>3222 bp
ATGCCAAAACGTACAGATATAAAAAGTATCCTGATTCTGGGTGCGGGCCCGATTGTTATC
GGTCAGGCGTGTGAGTTTGACTACTCTGGCGCGCAAGCGTGTAAAGCCCTGCGTGAAGAG
GGTTACCGCGTCATTCTGGTGAACTCCAACCCGGCGACCATCATGACCGACCCGGAAATG
GCTGATGCAACCTACATCGAGCCGATTCACTGGGAAGTTGTACGCAAGATTATTGAAAAA
GAGCGCCCGGACGCGGTGCTGCCAACGATGGGCGGTCAGACGGCGCTGAACTGCGCGCTG
GAGCTGGAACGTCAGGGCGTGTTGGAAGAGTTCGGTGTCACCATGATTGGTGCCACTGCC
GATGCGATTGATAAAGCAGAAGACCGCCGTCGTTTCGACGTAGCGATGAAGAAAATTGGT
CTGGAAACCGCGCGTTCCGGTATCGCACACACGATGGAAGAAGCGCTGGCGGTTGCCGCT
GACGTGGGCTTCCCGTGCATTATTCGCCCATCCTTTACCATGGGCGGTAGCGGCGGCGGT
ATCGCTTATAACCGTGAAGAGTTTGAAGAAATTTGCGCCCGCGGTCTGGATCTCTCTCCG
ACCAAAGAGTTGCTGATTGATGAGTCGCTGATCGGCTGGAAAGAGTACGAGATGGAAGTG
GTGCGTGATAAAAACGACAACTGCATCATCGTCTGCTCTATCGAAAACTTCGATGCGATG
GGCATCCACACCGGTGACTCCATCACTGTCGCGCCAGCCCAAACGCTGACCGACAAAGAA
TATCAAATCATGCGTAACGCCTCGATGGCGGTGCTGCGTGAAATCGGCGTTGAAACCGGT
GGTTCCAACGTTCAGTTTGCGGTGAACCCGAAAAACGGTCGTCTGATTGTTATCGAAATG
AACCCACGCGTGTCCCGTTCTTCGGCGCTGGCGTCGAAAGCGACCGGTTTCCCGATTGCT
AAAGTGGCGGCGAAACTGGCGGTGGGTTACACCCTCGACGAACTGATGAACGACATCACT
GGCGGACGTACTCCGGCCTCCTTCGAGCCGTCCATCGACTATGTGGTTACTAAAATTCCT
CGCTTCAACTTCGAAAAATTCGCCGGTGCTAACGACCGTCTGACCACTCAGATGAAATCG
GTTGGCGAAGTGATGGCGATTGGTCGCACGCAGCAGGAATCCCTGCAAAAAGCGCTGCGC
GGCCTGGAAGTCGGTGCGACTGGATTCGACCCGAAAGTGAGCCTGGATGACCCGGAAGCG
TTAACCAAAATCCGTCGCGAACTGAAAGACGCAGGCGCAGATCGTATCTGGTACATCGCC
GATGCGTTCCGTGCGGGCCTGTCTGTGGACGGCGTCTTCAACCTGACCAACATTGACCGC
TGGTTCCTGGTACAGATTGAAGAGCTGGTGCGTCTGGAAGAGAAAGTGGCGGAAGTGGGC
ATCACTGGCCTGAACGCTGACTTCCTGCGCCAGCTGAAACGCAAAGGCTTTGCCGATGCG
CGCTTGGCAAAACTGGCGGGCGTACGCGAAGCGGAAATCCGTAAGCTGCGTGACCAGTAT
GACCTGCACCCGGTTTATAAGCGCGTGGATACCTGTGCGGCAGAGTTCGCCACCGACACC
GCTTACATGTACTCCACTTATGAAGAAGAGTGCGAAGCGAATCCGTCTACCGACCGTGAA
AAAATCATGGTGCTTGGCGGCGGCCCGAACCGTATCGGTCAGGGTATCGAATTCGACTAC
TGTTGCGTACACGCCTCGCTGGCGCTGCGCGAAGACGGTTACGAAACCATTATGGTTAAC
TGTAACCCGGAAACCGTCTCCACCGACTACGACACTTCCGACCGCCTCTACTTCGAGCCG
GTAACTCTGGAAGATGTGCTGGAAATCGTGCGTATCGAGAAGCCGAAAGGCGTTATCGTC
CAGTACGGCGGTCAGACCCCGCTGAAACTGGCGCGCGCGCTGGAAGCTGCTGGCGTACCG
GTTATCGGCACCAGCCCGGATGCTATCGACCGTGCAGAAGACCGTGAACGCTTCCAGCAT
GCGGTTGAGCGTCTGAAACTGAAACAACCGGCGAACGCCACCGTTACCGCTATTGAAATG
GCGGTAGAGAAGGCGAAAGAGATTGGCTACCCGCTGGTGGTACGTCCGTCTTACGTTCTC
GGCGGTCGGGCGATGGAAATCGTCTATGACGAAGCTGACCTGCGTCGCTACTTCCAGACG
GCGGTCAGCGTGTCTAACGATGCGCCAGTGTTGCTGGACCACTTCCTCGATGACGCGGTA
GAAGTTGACGTGGATGCCATCTGCGACGGCGAAATGGTGCTGATTGGCGGCATCATGGAG
CATATTGAGCAGGCGGGCGTGCACTCCGGTGACTCCGCATGTTCTCTGCCAGCCTACACC
TTAAGTCAGGAAATTCAGGATGTGATGCGCCAGCAGGTGCAGAAACTGGCCTTCGAATTG
CAGGTGCGCGGCCTGATGAACGTGCAGTTTGCGGTGAAAAACAACGAAGTCTACCTGATT
GAAGTTAACCCGCGTGCGGCGCGTACCGTTCCGTTCGTCTCCAAAGCCACCGGCGTACCG
CTGGCAAAAGTGGCGGCGCGCGTGATGGCTGGCAAATCGCTGGCTGAGCAGGGCGTAACC
AAAGAAGTTATCCCGCCGTACTACTCGGTGAAAGAAGTGGTGCTGCCGTTCAATAAATTC
CCGGGCGTTGACCCGCTGTTAGGGCCAGAAATGCGCTCTACCGGGGAAGTCATGGGCGTG
GGCCGCACCTTCGCTGAAGCGTTTGCCAAAGCGCAGCTGGGCAGCAACTCCACCATGAAG
AAACACGGTCGTGCGCTGCTTTCCGTGCGCGAAGGCGATAAAGAACGCGTGGTGGACCTG
GCGGCAAAACTGCTGAAACAGGGCTTCGAGCTGGATGCGACCCACGGCACGGCGATTGTG
CTGGGCGAAGCAGGTATCAACCCGCGTCTGGTAAACAAGGTGCATGAAGGCCGTCCGCAC
ATTCAGGACCGTATCAAGAATGGCGAATATACCTACATCATCAACACCACCTCAGGCCGT
CGTGCGATTGAAGACTCCCGCGTGATTCGTCGCAGTGCGCTGCAATATAAAGTGCATTAC
GACACCACCCTGAACGGCGGCTTTGCCACCGCGATGGCGCTGAATGCCGATGCGACTGAA
AAAGTAATTTCGGTGCAGGAAATGCACGCACAGATCAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:1073
Protein Molecular Weight:117841
Protein Theoretical pI:5
PDB File:1KEE
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Carbamoyl-phosphate synthase large chain
MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEM
ADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLEEFGVTMIGATA
DAIDKAEDRRRFDVAMKKIGLETARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGSGGG
IAYNREEFEEICARGLDLSPTKELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAM
GIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEM
NPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIP
RFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATGFDPKVSLDDPEA
LTKIRRELKDAGADRIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVG
ITGLNADFLRQLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDT
AYMYSTYEEECEANPSTDREKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVN
CNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARALEAAGVP
VIGTSPDAIDRAEDRERFQHAVERLKLKQPANATVTAIEMAVEKAKEIGYPLVVRPSYVL
GGRAMEIVYDEADLRRYFQTAVSVSNDAPVLLDHFLDDAVEVDVDAICDGEMVLIGGIME
HIEQAGVHSGDSACSLPAYTLSQEIQDVMRQQVQKLAFELQVRGLMNVQFAVKNNEVYLI
EVNPRAARTVPFVSKATGVPLAKVAARVMAGKSLAEQGVTKEVIPPYYSVKEVVLPFNKF
PGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKHGRALLSVREGDKERVVDL
AAKLLKQGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTSGR
RAIEDSRVIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISVQEMHAQIK
References
External Links:
ResourceLink
Uniprot ID:P00968
Uniprot Name:CARB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321915
PDB ID:1KEE
Ecogene ID:EG10135
Ecocyc:EG10135
ColiBase:b0033
Kegg Gene:b0033
EchoBASE ID:EB0133
CCDB:CARB_ECOLI
BacMap:16128027
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
  • 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
  • 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