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P0A6F1

- CARA_ECOLI

UniProt

P0A6F1 - CARA_ECOLI

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Protein

Carbamoyl-phosphate synthase small chain

Gene

carA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei269 – 2691NucleophileBy similarity
Active sitei353 – 3531By similarity
Active sitei355 – 3551By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: EcoliWiki
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  3. arginine biosynthetic process Source: EcoliWiki
  4. carbamoyl phosphate biosynthetic process Source: InterPro
  5. glutamine catabolic process Source: InterPro
  6. glutamine metabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CARBPSYN-SMALL.
ECOL316407:JW0030-MONOMER.
MetaCyc:CARBPSYN-SMALL.
SABIO-RKP0A6F1.
UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Protein family/group databases

MEROPSiC26.954.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase small chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase glutamine chain
Gene namesi
Name:carA
Synonyms:pyrA
Ordered Locus Names:b0032, JW0030
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10134. carA.

Subcellular locationi

GO - Cellular componenti

  1. carbamoyl-phosphate synthase complex Source: EcoCyc
  2. cytoplasm Source: EcoliWiki
  3. cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Carbamoyl-phosphate synthase small chainPRO_0000112274Add
BLAST

Proteomic databases

PaxDbiP0A6F1.
PRIDEiP0A6F1.

2D gel databases

SWISS-2DPAGEP0A6F1.

Expressioni

Gene expression databases

GenevestigatoriP0A6F1.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
carBP0096811EBI-546107,EBI-546118
yejGP0AD212EBI-546107,EBI-1127956

Protein-protein interaction databases

DIPiDIP-35412N.
IntActiP0A6F1. 16 interactions.
STRINGi511145.b0032.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi14 – 196Combined sources
Beta strandi23 – 3311Combined sources
Helixi39 – 435Combined sources
Helixi46 – 483Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 593Combined sources
Helixi67 – 693Combined sources
Beta strandi71 – 744Combined sources
Beta strandi77 – 815Combined sources
Helixi98 – 1047Combined sources
Beta strandi108 – 1136Combined sources
Helixi115 – 12511Combined sources
Beta strandi128 – 13710Combined sources
Helixi140 – 14910Combined sources
Beta strandi153 – 1553Combined sources
Helixi159 – 1624Combined sources
Beta strandi168 – 1703Combined sources
Turni177 – 1793Combined sources
Helixi187 – 1893Combined sources
Beta strandi192 – 2009Combined sources
Helixi203 – 2119Combined sources
Beta strandi214 – 2207Combined sources
Helixi225 – 2295Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi242 – 2454Combined sources
Helixi249 – 25810Combined sources
Turni259 – 2624Combined sources
Beta strandi265 – 2684Combined sources
Helixi270 – 2789Combined sources
Beta strandi283 – 29917Combined sources
Turni300 – 3034Combined sources
Beta strandi304 – 31613Combined sources
Helixi318 – 3203Combined sources
Beta strandi325 – 3317Combined sources
Turni332 – 3343Combined sources
Beta strandi337 – 35216Combined sources
Beta strandi357 – 3593Combined sources
Turni362 – 3643Combined sources
Helixi365 – 37915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A6F1.
SMRiP0A6F1. Positions 2-380.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6F1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini193 – 380188Glutamine amidotransferase type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189CPSaseAdd
BLAST

Sequence similaritiesi

Belongs to the CarA family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0505.
HOGENOMiHOG000038087.
InParanoidiP0A6F1.
KOiK01956.
OMAiKTIKMKF.
OrthoDBiEOG61ZTH6.
PhylomeDBiP0A6F1.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6F1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR
60 70 80 90 100
QIVTLTYPHI GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS
110 120 130 140 150
YLKRHNIVAI ADIDTRKLTR LLREKGAQNG CIIAGDNPDA ALALEKARAF
160 170 180 190 200
PGLNGMDLAK EVTTAEAYSW TQGSWTLTGG LPEAKKEDEL PFHVVAYDFG
210 220 230 240 250
AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN GPGDPAPCDY
260 270 280 290 300
AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV
310 320 330 340 350
EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF
360 370 380
QGHPEASPGP HDAAPLFDHF IELIEQYRKT AK
Length:382
Mass (Da):41,431
Last modified:July 21, 1986 - v1
Checksum:i60BC26366417443F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01597 Genomic DNA. Translation: AAA23538.1.
U00096 Genomic DNA. Translation: AAC73143.1.
AP009048 Genomic DNA. Translation: BAB96601.1.
X70017 Genomic DNA. Translation: CAA49615.1.
PIRiA01128. SYECCS.
B85484.
RefSeqiNP_414573.1. NC_000913.3.
YP_488338.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73143; AAC73143; b0032.
BAB96601; BAB96601; BAB96601.
GeneIDi12934451.
949025.
KEGGiecj:Y75_p0032.
eco:b0032.
PATRICi32115157. VBIEscCol129921_0030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01597 Genomic DNA. Translation: AAA23538.1 .
U00096 Genomic DNA. Translation: AAC73143.1 .
AP009048 Genomic DNA. Translation: BAB96601.1 .
X70017 Genomic DNA. Translation: CAA49615.1 .
PIRi A01128. SYECCS.
B85484.
RefSeqi NP_414573.1. NC_000913.3.
YP_488338.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A9X X-ray 1.80 B/D/F/H 2-380 [» ]
1BXR X-ray 2.10 B/D/F/H 1-382 [» ]
1C30 X-ray 2.00 B/D/F/H 1-382 [» ]
1C3O X-ray 2.10 B/D/F/H 1-382 [» ]
1CE8 X-ray 2.10 B/D/F/H 1-380 [» ]
1CS0 X-ray 2.00 B/D/F/H 1-382 [» ]
1JDB X-ray 2.10 C/F/I/L 1-382 [» ]
1KEE X-ray 2.10 B/D/F/H 1-382 [» ]
1M6V X-ray 2.10 B/D/F/H 1-382 [» ]
1T36 X-ray 2.10 B/D/F/H 1-382 [» ]
ProteinModelPortali P0A6F1.
SMRi P0A6F1. Positions 2-380.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35412N.
IntActi P0A6F1. 16 interactions.
STRINGi 511145.b0032.

Chemistry

BindingDBi P0A6F1.

Protein family/group databases

MEROPSi C26.954.

2D gel databases

SWISS-2DPAGE P0A6F1.

Proteomic databases

PaxDbi P0A6F1.
PRIDEi P0A6F1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73143 ; AAC73143 ; b0032 .
BAB96601 ; BAB96601 ; BAB96601 .
GeneIDi 12934451.
949025.
KEGGi ecj:Y75_p0032.
eco:b0032.
PATRICi 32115157. VBIEscCol129921_0030.

Organism-specific databases

EchoBASEi EB0132.
EcoGenei EG10134. carA.

Phylogenomic databases

eggNOGi COG0505.
HOGENOMi HOG000038087.
InParanoidi P0A6F1.
KOi K01956.
OMAi KTIKMKF.
OrthoDBi EOG61ZTH6.
PhylomeDBi P0A6F1.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00171 .
UPA00070 ; UER00115 .
BioCyci EcoCyc:CARBPSYN-SMALL.
ECOL316407:JW0030-MONOMER.
MetaCyc:CARBPSYN-SMALL.
SABIO-RK P0A6F1.

Miscellaneous databases

EvolutionaryTracei P0A6F1.
PROi P0A6F1.

Gene expression databases

Genevestigatori P0A6F1.

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPi MF_01209. CPSase_S_chain.
InterProi IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view ]
Pfami PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view ]
SMARTi SM01097. CPSase_sm_chain. 1 hit.
[Graphical view ]
SUPFAMi SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsi TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiCARA_ECOLI
AccessioniPrimary (citable) accession number: P0A6F1
Secondary accession number(s): P00907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3