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P0A6F1 (CARA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. 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 small chain

EC=6.3.5.5
Alternative name(s):
Carbamoyl-phosphate synthetase glutamine chain
Gene names
Name:carA
Synonyms:pyrA
Ordered Locus Names:b0032, JW0030
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
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_01209

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP-Rule MF_01209

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule MF_01209

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 CarA family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Pyrimidine biosynthesis
   DomainGlutamine amidotransferase
   LigandATP-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

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from mutant phenotype PubMed 5319709. Source: EcoliWiki

arginine biosynthetic process

Inferred from mutant phenotype PubMed 5319709. Source: EcoliWiki

carbamoyl phosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

glutamine catabolic process

Inferred from electronic annotation. Source: InterPro

glutamine metabolic process

Inferred from mutant phenotype PubMed 1827118. Source: EcoliWiki

   Cellular_componentcarbamoyl-phosphate synthase complex

Inferred from direct assay PubMed 4358555. Source: EcoCyc

cytoplasm

Inferred from direct assay PubMed 2682645. Source: EcoliWiki

cytosol

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein binding

Inferred from physical interaction Ref.13Ref.15PubMed 12130656PubMed 15690043PubMed 23582331PubMed 24561554Ref.11. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Carbamoyl-phosphate synthase small chain HAMAP-Rule MF_01209
PRO_0000112274

Regions

Domain193 – 380188Glutamine amidotransferase type-1
Region1 – 189189CPSase HAMAP-Rule MF_01209

Sites

Active site2691Nucleophile By similarity
Active site3531 By similarity
Active site3551 By similarity

Secondary structure

............................................................................ 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6F1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 60BC26366417443F

FASTA38241,431
        10         20         30         40         50         60 
MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI 

        70         80         90        100        110        120 
GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS YLKRHNIVAI ADIDTRKLTR 

       130        140        150        160        170        180 
LLREKGAQNG CIIAGDNPDA ALALEKARAF PGLNGMDLAK EVTTAEAYSW TQGSWTLTGG 

       190        200        210        220        230        240 
LPEAKKEDEL PFHVVAYDFG AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN 

       250        260        270        280        290        300 
GPGDPAPCDY AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV 

       310        320        330        340        350        360 
EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF QGHPEASPGP 

       370        380 
HDAAPLFDHF IELIEQYRKT AK 

« Hide

References

« Hide 'large scale' references
[1]"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].
[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]"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] OF 361-382.
[7]"A whole genome approach to in vivo DNA-protein interactions in E. coli."
Wang M.X., Church G.M.
Nature 360:606-610(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
Strain: K12.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[9]"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.
[10]"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).
[11]"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).
[12]"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).
[13]"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).
[14]"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).
[15]"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: AAA23538.1.
U00096 Genomic DNA. Translation: AAC73143.1.
AP009048 Genomic DNA. Translation: BAB96601.1.
X70017 Genomic DNA. Translation: CAA49615.1.
PIRSYECCS. A01128.
B85484.
RefSeqNP_414573.1. NC_000913.3.
YP_488338.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9XX-ray1.80B/D/F/H2-380[»]
1BXRX-ray2.10B/D/F/H1-382[»]
1C30X-ray2.00B/D/F/H1-382[»]
1C3OX-ray2.10B/D/F/H1-382[»]
1CE8X-ray2.10B/D/F/H1-380[»]
1CS0X-ray2.00B/D/F/H1-382[»]
1JDBX-ray2.10C/F/I/L1-382[»]
1KEEX-ray2.10B/D/F/H1-382[»]
1M6VX-ray2.10B/D/F/H1-382[»]
1T36X-ray2.10B/D/F/H1-382[»]
ProteinModelPortalP0A6F1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35412N.
IntActP0A6F1. 16 interactions.
STRING511145.b0032.

Protein family/group databases

MEROPSC26.954.

2D gel databases

SWISS-2DPAGEP0A6F1.

Proteomic databases

PaxDbP0A6F1.
PRIDEP0A6F1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73143; AAC73143; b0032.
BAB96601; BAB96601; BAB96601.
GeneID12934451.
949025.
KEGGecj:Y75_p0032.
eco:b0032.
PATRIC32115157. VBIEscCol129921_0030.

Organism-specific databases

EchoBASEEB0132.
EcoGeneEG10134. carA.

Phylogenomic databases

eggNOGCOG0505.
HOGENOMHOG000038087.
KOK01956.
OMAKTIKMKF.
OrthoDBEOG61ZTH6.
PhylomeDBP0A6F1.

Enzyme and pathway databases

BioCycEcoCyc:CARBPSYN-SMALL.
ECOL316407:JW0030-MONOMER.
MetaCyc:CARBPSYN-SMALL.
SABIO-RKP0A6F1.
UniPathwayUPA00068; UER00171.
UPA00070; UER00115.

Gene expression databases

GenevestigatorP0A6F1.

Family and domain databases

Gene3D3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPMF_01209. CPSase_S_chain.
InterProIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6F1.
PROP0A6F1.

Entry information

Entry nameCARA_ECOLI
AccessionPrimary (citable) accession number: P0A6F1
Secondary accession number(s): P00907
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 98 of the entry and version 1 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