ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00968


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CARB_ECOLI
Primary accession number P00968
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 108)
Name and origin of the protein
Protein name Carbamoyl-phosphate synthase large chain
Synonyms EC 6.3.5.5
Carbamoyl-phosphate synthetase ammonia chain
Gene name
Name: carB
Synonyms: pyrA
OrderedLocusNames: b0033, JW0031
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-2.
STRAIN=K12;
PubMed=6308632 [NCBI, ExPASy, EBI, Israel, Japan]
Nyunoya H., Lusty C.J.;
"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(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6377309 [NCBI, ExPASy, EBI, Israel, Japan]
Bouvier J., Patte J.-C., Stragier P.;
"Multiple regulatory signals in the control region of the Escherichia coli carAB operon.";
Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/20.13.3305; PubMed=1630901 [NCBI, ExPASy, EBI, Israel, Japan]
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, 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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
PubMed=6330744 [NCBI, ExPASy, EBI, Israel, Japan]
Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M., Charlier D.R.M., Glansdorff N., Pierard A.;
"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(1984).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1021/bi970503q; PubMed=9174345 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I.;
"Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product.";
Biochemistry 36:6305-6316(1997).
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1021/bi9807761; PubMed=9636022 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M., Holden H.M.;
"Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis.";
Biochemistry 37:8825-8831(1998).
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1107/S0907444998006234; PubMed=10089390 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.;
"The structure of carbamoyl phosphate synthetase determined to 2.1-A resolution.";
Acta Crystallogr. D 55:8-24(1999).
[10]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1021/bi982517h; PubMed=10029528 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M.;
"Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding.";
Biochemistry 38:2347-2357(1999).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1021/bi991741j; PubMed=10587438 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Huang X., Raushel F.M., Holden H.M.;
"The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway.";
Biochemistry 38:16158-16166(1999).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1074/jbc.274.32.22502; PubMed=10428826 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M.;
"The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase.";
J. Biol. Chem. 274:22502-22507(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J01597; AAA23539.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01500; CAA24744.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73144.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96602.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01198; SYECCP.
RefSeq AP_000697.1; -.
NP_414574.1; -.
3D structure databases
PDB
1A9X; X-ray; 1.80 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1BXR; X-ray; 2.10 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1C30; X-ray; 2.00 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1C3O; X-ray; 2.10 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1CE8; X-ray; 2.10 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1CS0; X-ray; 2.00 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1JDB; X-ray; 2.10 A; B/E/H/K=1-1073.[ExPASy / RCSB / EBI]
1KEE; X-ray; 2.10 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1M6V; X-ray; 2.10 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
1T36; X-ray; 2.10 A; A/C/E/G=1-1073.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A9X; -.
1BXR; -.
1C30; -.
1C3O; -.
1CE8; -.
1CS0; -.
1JDB; -.
1KEE; -.
1M6V; -.
1T36; -.
ModBase P00968.
Protein-protein interaction databases
DIP DIP:1025N; -.
IntAct P00968; -.
Enzyme and pathway databases
BioCyc EcoCyc:CARBPSYN-LARGE; -.
MetaCyc:CARBPSYN-LARGE; -.
2D gel databases
ECO2DBASE E133.0; 6TH EDITION.
Organism-specific databases
EchoBASE EB0133; -.
EcoGene EG10135; carB.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
HAMAP MF_01210; -; 1.
PBIL [Tree]
InterPro IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR005483; CarbamoylP_synth_lsu.
IPR005479; CarbamoylP_synth_lsu_ATP-bd.
IPR006275; CarbamoylP_synth_lsu_Gln-dep.
IPR005481; CarbamoylP_synth_lsu_N.
IPR005480; CarbamoylP_synth_lsu_oligo.
IPR011607; MGS.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
Pfam PF00289; CPSase_L_chain; 2.
PF02786; CPSase_L_D2; 3.
PF02787; CPSase_L_D3; 1.
PF02142; MGS; 1.
Pfam graphical view of domain structure.
PRINTS PR00098; CPSASE.
TIGRFAMs TIGR01369; CPSaseII_lrg; 1.
PROSITE PS50975; ATP_GRASP; 2.
PS00866; CPSASE_1; 2.
PS00867; CPSASE_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00968.
ProtoNet P00968.
Genome annotation databases
GeneID 944775; -.
GenomeReviews U00096_GR; b0033.
AP009048_GR; JW0031.
KEGG ecj:JW0031; -.
eco:b0033; -.
Phylogenomic databases
HOGENOM P00968; -.
Other
LinkHub P00968; -.
Genome annotation databases
CMR P00968; b0033.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Manganese; Metal-binding; Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed. 
CHAIN   2   1073  1072     Carbamoyl-phosphate synthase large chain. PRO_0000145004
DOMAIN   133    328  196     ATP-grasp 1. 
DOMAIN   679    870  192     ATP-grasp 2. 
NP_BIND   159    216  58     ATP (By similarity). 
NP_BIND   705    762  58     ATP (By similarity). 
REGION   2    403  402     Carboxyphosphate synthetic domain. 
REGION   404    553  150     Oligomerization domain. 
REGION   554    936  383     Carbamoyl phosphate synthetic domain. 
REGION   937   1073  137     Allosteric domain. 
METAL   285    285        Manganese 1. 
METAL   299    299        Manganese 1. 
METAL   299    299        Manganese 2. 
METAL   301    301        Manganese 2. 
METAL   829    829        Manganese 3. 
METAL   841    841        Manganese 3. 
METAL   841    841        Manganese 4 (By similarity). 
METAL   843    843        Manganese 4 (By similarity). 
STRAND   9     13  5      
HELIX   25     40  16      
STRAND   43     47  5      
HELIX   54     56  3      
HELIX   58     60  3      
STRAND   61     65  5      
HELIX   71     81  11      
STRAND   84     87  4      
STRAND   89     91  3      
HELIX   92    104  13      
HELIX   107    111  5      
HELIX   120    127  8      
HELIX   129    138  10      
STRAND   145    151  7      
HELIX   152    162  11      
STRAND   164    170  7      
TURN   175    178  4      
STRAND   180    184  5      
HELIX   185    198  14      
STRAND   204    208  5      
STRAND   213    222  10      
STRAND   228    238  11      
HELIX   244    246  3      
STRAND   249    252  4      
HELIX   258    275  18      
STRAND   279    288  10      
TURN   290    292  3      
STRAND   295    303  9      
HELIX   306    315  10      
HELIX   319    327  9      
HELIX   332    334  3      
TURN   338    342  5      
STRAND   344    346  3      
STRAND   353    361  9      
HELIX   364    366  3      
STRAND   382    390  9      
HELIX   391    401  11      
STRAND   402    405  4      
STRAND   407    409  3      
HELIX   420    429  10      
HELIX   435    444  10      
HELIX   449    456  8      
HELIX   460    479  20      
HELIX   481    483  3      
HELIX   486    494  9      
HELIX   499    505  7      
HELIX   510    519  10      
STRAND   525    528  4      
STRAND   541    547  7      
STRAND   557    559  3      
STRAND   561    565  5      
HELIX   576    591  16      
STRAND   595    599  5      
STRAND   612    617  6      
HELIX   623    633  11      
STRAND   636    639  4      
STRAND   641    643  3      
HELIX   645    648  4      
HELIX   651    656  6      
HELIX   666    673  8      
HELIX   675    685  11      
STRAND   692    694  3      
HELIX   698    708  11      
STRAND   710    715  6      
STRAND   725    728  4      
HELIX   731    740  10      
STRAND   751    754  4      
STRAND   760    768  9      
STRAND   773    783  11      
HELIX   789    791  3      
STRAND   794    797  4      
HELIX   803    819  17      
STRAND   824    832  9      
STRAND   837    843  7      
HELIX   850    857  8      
HELIX   861    869  9      
HELIX   874    877  4      
STRAND   886    894  9      
HELIX   896    899  4      
STRAND   915    923  9      
HELIX   924    934  11      
STRAND   941    948  8      
HELIX   951    954  4      
HELIX   957    966  10      
STRAND   970    973  4      
HELIX   975    982  8      
TURN   983    985  3      
TURN   994    996  3      
STRAND   998   1000  3      
HELIX   1001   1007  7      
STRAND   1011   1015  5      
HELIX   1020   1025  6      
HELIX   1027   1035  9      
STRAND   1039   1043  5      
HELIX   1044   1054  11      
HELIX   1065   1070  6