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P00968 (CARB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbamoyl-phosphate synthase large chain

EC=6.3.5.5
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene names
Name:carB
Synonyms:pyrA
Ordered Locus Names:b0033, JW0031
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1073 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP-Rule MF_01210_A

Cofactor

Binds 4 manganese ions per subunit.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP-Rule MF_01210_A

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule MF_01210_A

Subunit structure

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4.

Sequence similarities

Belongs to the CarB family.

Contains 2 ATP-grasp domains.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Pyrimidine biosynthesis
   DomainRepeat
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

arginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

biofilm formation

Inferred from mutant phenotype PubMed 22359582. Source: CACAO

cellular amino acid biosynthetic process

Inferred from mutant phenotype PubMed 1737023. Source: EcoliWiki

pyrimidine nucleobase biosynthetic process

Inferred from mutant phenotype PubMed 1737023. Source: EcoliWiki

   Cellular_componentcarbamoyl-phosphate synthase complex

Inferred from direct assay PubMed 4358555. Source: EcoCyc

   Molecular_functionATP binding

Inferred from direct assay PubMed 1737023. Source: EcoCyc

amino acid binding

Inferred from direct assay PubMed 7648201. Source: EcoliWiki

carbamoyl-phosphate synthase (ammonia) activity

Inferred from direct assay PubMed 3549732. Source: EcoliWiki

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from direct assay PubMed 229896. Source: EcoliWiki

nucleotide binding

Inferred from direct assay PubMed 7648201. Source: EcoliWiki

protein binding

Inferred from physical interaction Ref.11Ref.13PubMed 12130656PubMed 15690043PubMed 23582331PubMed 24561554Ref.9. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

carAP0A6F111EBI-546118,EBI-546107

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 10731072Carbamoyl-phosphate synthase large chain HAMAP-Rule MF_01210_A
PRO_0000145004

Regions

Domain133 – 328196ATP-grasp 1
Domain679 – 870192ATP-grasp 2
Nucleotide binding159 – 21658ATP By similarity
Nucleotide binding705 – 76258ATP By similarity
Region2 – 403402Carboxyphosphate synthetic domain HAMAP-Rule MF_01210_A
Region404 – 553150Oligomerization domain HAMAP-Rule MF_01210_A
Region554 – 936383Carbamoyl phosphate synthetic domain HAMAP-Rule MF_01210_A
Region937 – 1073137Allosteric domain HAMAP-Rule MF_01210_A

Sites

Metal binding2851Manganese 1
Metal binding2991Manganese 1
Metal binding2991Manganese 2
Metal binding3011Manganese 2
Metal binding8291Manganese 3
Metal binding8411Manganese 3
Metal binding8411Manganese 4 By similarity
Metal binding8431Manganese 4 By similarity

Secondary structure

.................................................................................................................................................................................................. 1073
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00968 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A09D019CBDFF8D2B

FASTA1,073117,842
        10         20         30         40         50         60 
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM 

        70         80         90        100        110        120 
ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA 

       130        140        150        160        170        180 
DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG 

       190        200        210        220        230        240 
IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM 

       250        260        270        280        290        300 
GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM 

       310        320        330        340        350        360 
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP 

       370        380        390        400        410        420 
RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA 

       430        440        450        460        470        480 
LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG 

       490        500        510        520        530        540 
ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT 

       550        560        570        580        590        600 
AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 

       610        620        630        640        650        660 
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP 

       670        680        690        700        710        720 
VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL 

       730        740        750        760        770        780 
GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME 

       790        800        810        820        830        840 
HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI 

       850        860        870        880        890        900 
EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF 

       910        920        930        940        950        960 
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL 

       970        980        990       1000       1010       1020 
AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR 

      1030       1040       1050       1060       1070 
RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK 

« Hide

References

« Hide 'large scale' references
[1]"The carB gene of Escherichia coli: a duplicated gene coding for the large subunit of carbamoyl-phosphate synthetase."
Nyunoya H., Lusty C.J.
Proc. Natl. Acad. Sci. U.S.A. 80:4629-4633(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-2.
Strain: K12.
[2]"Multiple regulatory signals in the control region of the Escherichia coli carAB operon."
Bouvier J., Patte J.-C., Stragier P.
Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[4]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"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."
Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M., Charlier D.R.M., Glansdorff N., Pierard A.
Proc. Natl. Acad. Sci. U.S.A. 81:4134-4138(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[7]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[8]"Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product."
Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I.
Biochemistry 36:6305-6316(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]"Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis."
Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M., Holden H.M.
Biochemistry 37:8825-8831(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[10]"The structure of carbamoyl phosphate synthetase determined to 2.1-A resolution."
Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.
Acta Crystallogr. D 55:8-24(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[11]"Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding."
Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M.
Biochemistry 38:2347-2357(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[12]"The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway."
Thoden J.B., Huang X., Raushel F.M., Holden H.M.
Biochemistry 38:16158-16166(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[13]"The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase."
Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M.
J. Biol. Chem. 274:22502-22507(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01597 Genomic DNA. Translation: AAA23539.1.
V01500 Genomic DNA. Translation: CAA24744.1.
U00096 Genomic DNA. Translation: AAC73144.1.
AP009048 Genomic DNA. Translation: BAB96602.1.
PIRSYECCP. A01198.
RefSeqNP_414574.1. NC_000913.3.
YP_488339.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9XX-ray1.80A/C/E/G1-1073[»]
1BXRX-ray2.10A/C/E/G1-1073[»]
1C30X-ray2.00A/C/E/G1-1073[»]
1C3OX-ray2.10A/C/E/G1-1073[»]
1CE8X-ray2.10A/C/E/G1-1073[»]
1CS0X-ray2.00A/C/E/G1-1073[»]
1JDBX-ray2.10B/E/H/K1-1073[»]
1KEEX-ray2.10A/C/E/G1-1073[»]
1M6VX-ray2.10A/C/E/G1-1073[»]
1T36X-ray2.10A/C/E/G1-1073[»]
ProteinModelPortalP00968.
SMRP00968. Positions 1-1073.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-1025N.
IntActP00968. 13 interactions.
MINTMINT-1255866.
STRING511145.b0033.

Proteomic databases

PaxDbP00968.
PRIDEP00968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73144; AAC73144; b0033.
BAB96602; BAB96602; BAB96602.
GeneID12930732.
944775.
KEGGecj:Y75_p0033.
eco:b0033.
PATRIC32115159. VBIEscCol129921_0031.

Organism-specific databases

EchoBASEEB0133.
EcoGeneEG10135. carB.

Phylogenomic databases

eggNOGCOG0458.
HOGENOMHOG000234582.
KOK01955.
OMAGSDRIWY.
OrthoDBEOG6J1DC6.
PhylomeDBP00968.

Enzyme and pathway databases

BioCycEcoCyc:CARBPSYN-LARGE.
ECOL316407:JW0031-MONOMER.
MetaCyc:CARBPSYN-LARGE.
SABIO-RKP00968.
UniPathwayUPA00068; UER00171.
UPA00070; UER00115.

Gene expression databases

GenevestigatorP00968.

Family and domain databases

Gene3D1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
HAMAPMF_01210_A. CPSase_L_chain_A.
MF_01210_B. CPSase_L_chain_B.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSPR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00968.
PROP00968.

Entry information

Entry nameCARB_ECOLI
AccessionPrimary (citable) accession number: P00968
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene