Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A6F1

- CARA_ECOLI

UniProt

P0A6F1 - CARA_ECOLI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    3. protein binding Source: IntAct

    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

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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.
    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

    MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR    50
    QIVTLTYPHI GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS 100
    YLKRHNIVAI ADIDTRKLTR LLREKGAQNG CIIAGDNPDA ALALEKARAF 150
    PGLNGMDLAK EVTTAEAYSW TQGSWTLTGG LPEAKKEDEL PFHVVAYDFG 200
    AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN GPGDPAPCDY 250
    AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV 300
    EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF 350
    QGHPEASPGP HDAAPLFDHF IELIEQYRKT AK 382
    Length:382
    Mass (Da):41,431
    Last modified:July 21, 1986 - v1
    Checksum:i60BC26366417443F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

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

    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.
    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

    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: October 1, 2014
    This is version 99 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