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P00968

- CARB_ECOLI

UniProt

P00968 - CARB_ECOLI

Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 4 manganese ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi285 – 2851Manganese 1
    Metal bindingi299 – 2991Manganese 1
    Metal bindingi299 – 2991Manganese 2
    Metal bindingi301 – 3011Manganese 2
    Metal bindingi829 – 8291Manganese 3
    Metal bindingi841 – 8411Manganese 3
    Metal bindingi841 – 8411Manganese 4By similarity
    Metal bindingi843 – 8431Manganese 4By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi159 – 21658ATPBy similarityAdd
    BLAST
    Nucleotide bindingi705 – 76258ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. amino acid binding Source: EcoliWiki
    2. ATP binding Source: EcoCyc
    3. carbamoyl-phosphate synthase (ammonia) activity Source: EcoliWiki
    4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
    5. metal ion binding Source: EcoliWiki
    6. nucleotide binding Source: EcoliWiki
    7. protein binding Source: IntAct

    GO - Biological processi

    1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    2. arginine biosynthetic process Source: UniProtKB-UniPathway
    3. biofilm formation Source: CACAO
    4. cellular amino acid biosynthetic process Source: EcoliWiki
    5. pyrimidine nucleobase biosynthetic process Source: EcoliWiki

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:CARBPSYN-LARGE.
    ECOL316407:JW0031-MONOMER.
    MetaCyc:CARBPSYN-LARGE.
    SABIO-RKP00968.
    UniPathwayiUPA00068; UER00171.
    UPA00070; UER00115.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbamoyl-phosphate synthase large chain (EC:6.3.5.5)
    Alternative name(s):
    Carbamoyl-phosphate synthetase ammonia chain
    Gene namesi
    Name:carB
    Synonyms:pyrA
    Ordered Locus Names:b0033, JW0031
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10135. carB.

    Subcellular locationi

    GO - Cellular componenti

    1. carbamoyl-phosphate synthase complex Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 10731072Carbamoyl-phosphate synthase large chainPRO_0000145004Add
    BLAST

    Proteomic databases

    PaxDbiP00968.
    PRIDEiP00968.

    Expressioni

    Gene expression databases

    GenevestigatoriP00968.

    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
    carAP0A6F111EBI-546118,EBI-546107

    Protein-protein interaction databases

    DIPiDIP-1025N.
    IntActiP00968. 13 interactions.
    MINTiMINT-1255866.
    STRINGi511145.b0033.

    Structurei

    Secondary structure

    1
    1073
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Helixi25 – 4016
    Beta strandi43 – 475
    Helixi54 – 563
    Helixi58 – 603
    Beta strandi61 – 655
    Helixi71 – 8111
    Beta strandi84 – 874
    Beta strandi89 – 913
    Helixi92 – 10413
    Helixi107 – 1115
    Helixi120 – 1278
    Helixi129 – 13810
    Beta strandi145 – 1517
    Helixi152 – 16211
    Beta strandi164 – 1707
    Turni175 – 1784
    Beta strandi180 – 1845
    Helixi185 – 19814
    Beta strandi204 – 2085
    Beta strandi213 – 22210
    Beta strandi228 – 23811
    Helixi244 – 2463
    Beta strandi249 – 2524
    Helixi258 – 27518
    Beta strandi279 – 28810
    Turni290 – 2923
    Beta strandi295 – 3039
    Helixi306 – 31510
    Helixi319 – 3279
    Helixi332 – 3343
    Turni338 – 3425
    Beta strandi344 – 3463
    Beta strandi353 – 3619
    Helixi364 – 3663
    Beta strandi382 – 3909
    Helixi391 – 40111
    Beta strandi402 – 4054
    Beta strandi407 – 4093
    Helixi420 – 42910
    Helixi435 – 44410
    Helixi449 – 4568
    Helixi460 – 47920
    Helixi481 – 4833
    Helixi486 – 4949
    Helixi499 – 5057
    Helixi510 – 51910
    Beta strandi525 – 5284
    Beta strandi541 – 5477
    Beta strandi557 – 5593
    Beta strandi561 – 5655
    Helixi576 – 59116
    Beta strandi595 – 5995
    Helixi606 – 6083
    Beta strandi612 – 6176
    Helixi623 – 63311
    Beta strandi636 – 6394
    Beta strandi641 – 6433
    Helixi645 – 6484
    Helixi651 – 6566
    Beta strandi661 – 6644
    Helixi666 – 6738
    Helixi675 – 68511
    Beta strandi692 – 6943
    Helixi698 – 70811
    Beta strandi710 – 7156
    Turni721 – 7244
    Beta strandi725 – 7284
    Helixi731 – 74010
    Beta strandi751 – 7544
    Beta strandi760 – 7689
    Beta strandi773 – 78311
    Helixi789 – 7913
    Beta strandi794 – 7974
    Beta strandi799 – 8013
    Helixi803 – 81917
    Beta strandi824 – 8329
    Beta strandi837 – 8437
    Helixi850 – 8578
    Helixi861 – 8699
    Helixi874 – 8774
    Beta strandi886 – 8949
    Helixi896 – 8994
    Beta strandi915 – 9239
    Helixi924 – 93411
    Beta strandi941 – 9488
    Helixi951 – 9544
    Helixi957 – 96610
    Beta strandi970 – 9734
    Helixi975 – 9828
    Turni983 – 9853
    Beta strandi989 – 9924
    Turni994 – 9963
    Beta strandi998 – 10003
    Helixi1001 – 10077
    Beta strandi1011 – 10155
    Helixi1020 – 10256
    Helixi1027 – 10359
    Beta strandi1039 – 10435
    Helixi1044 – 105411
    Turni1058 – 10603
    Helixi1065 – 10706

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00968.
    SMRiP00968. Positions 1-1073.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00968.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini133 – 328196ATP-grasp 1Add
    BLAST
    Domaini679 – 870192ATP-grasp 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 403402Carboxyphosphate synthetic domainAdd
    BLAST
    Regioni404 – 553150Oligomerization domainAdd
    BLAST
    Regioni554 – 936383Carbamoyl phosphate synthetic domainAdd
    BLAST
    Regioni937 – 1073137Allosteric domainAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CarB family.Curated
    Contains 2 ATP-grasp domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0458.
    HOGENOMiHOG000234582.
    KOiK01955.
    OMAiGSDRIWY.
    OrthoDBiEOG6J1DC6.
    PhylomeDBiP00968.

    Family and domain databases

    Gene3Di1.10.1030.10. 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.
    HAMAPiMF_01210_A. CPSase_L_chain_A.
    MF_01210_B. CPSase_L_chain_B.
    InterProiIPR011761. 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]
    PfamiPF00289. CPSase_L_chain. 2 hits.
    PF02786. CPSase_L_D2. 2 hits.
    PF02787. CPSase_L_D3. 1 hit.
    PF02142. MGS. 1 hit.
    [Graphical view]
    PRINTSiPR00098. CPSASE.
    SMARTiSM01096. CPSase_L_D3. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48108. SSF48108. 1 hit.
    SSF52335. SSF52335. 1 hit.
    SSF52440. SSF52440. 2 hits.
    TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 2 hits.
    PS00866. CPSASE_1. 2 hits.
    PS00867. CPSASE_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00968-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN     50
    PATIMTDPEM ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL 100
    ELERQGVLEE FGVTMIGATA DAIDKAEDRR RFDVAMKKIG LETARSGIAH 150
    TMEEALAVAA DVGFPCIIRP SFTMGGSGGG IAYNREEFEE ICARGLDLSP 200
    TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM GIHTGDSITV 250
    APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM 300
    NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP 350
    SIDYVVTKIP RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR 400
    GLEVGATGFD PKVSLDDPEA LTKIRRELKD AGADRIWYIA DAFRAGLSVD 450
    GVFNLTNIDR WFLVQIEELV RLEEKVAEVG ITGLNADFLR QLKRKGFADA 500
    RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT AYMYSTYEEE 550
    CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 600
    CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL 650
    ARALEAAGVP VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM 700
    AVEKAKEIGY PLVVRPSYVL GGRAMEIVYD EADLRRYFQT AVSVSNDAPV 750
    LLDHFLDDAV EVDVDAICDG EMVLIGGIME HIEQAGVHSG DSACSLPAYT 800
    LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI EVNPRAARTV 850
    PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF 900
    PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR 950
    EGDKERVVDL AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH 1000
    IQDRIKNGEY TYIINTTSGR RAIEDSRVIR RSALQYKVHY DTTLNGGFAT 1050
    AMALNADATE KVISVQEMHA QIK 1073
    Length:1,073
    Mass (Da):117,842
    Last modified:January 23, 2007 - v2
    Checksum:iA09D019CBDFF8D2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01597 Genomic DNA. Translation: AAA23539.1.
    V01500 Genomic DNA. Translation: CAA24744.1.
    U00096 Genomic DNA. Translation: AAC73144.1.
    AP009048 Genomic DNA. Translation: BAB96602.1.
    PIRiA01198. SYECCP.
    RefSeqiNP_414574.1. NC_000913.3.
    YP_488339.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73144; AAC73144; b0033.
    BAB96602; BAB96602; BAB96602.
    GeneIDi12930732.
    944775.
    KEGGiecj:Y75_p0033.
    eco:b0033.
    PATRICi32115159. VBIEscCol129921_0031.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01597 Genomic DNA. Translation: AAA23539.1 .
    V01500 Genomic DNA. Translation: CAA24744.1 .
    U00096 Genomic DNA. Translation: AAC73144.1 .
    AP009048 Genomic DNA. Translation: BAB96602.1 .
    PIRi A01198. SYECCP.
    RefSeqi NP_414574.1. NC_000913.3.
    YP_488339.1. 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 A/C/E/G 1-1073 [» ]
    1BXR X-ray 2.10 A/C/E/G 1-1073 [» ]
    1C30 X-ray 2.00 A/C/E/G 1-1073 [» ]
    1C3O X-ray 2.10 A/C/E/G 1-1073 [» ]
    1CE8 X-ray 2.10 A/C/E/G 1-1073 [» ]
    1CS0 X-ray 2.00 A/C/E/G 1-1073 [» ]
    1JDB X-ray 2.10 B/E/H/K 1-1073 [» ]
    1KEE X-ray 2.10 A/C/E/G 1-1073 [» ]
    1M6V X-ray 2.10 A/C/E/G 1-1073 [» ]
    1T36 X-ray 2.10 A/C/E/G 1-1073 [» ]
    ProteinModelPortali P00968.
    SMRi P00968. Positions 1-1073.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-1025N.
    IntActi P00968. 13 interactions.
    MINTi MINT-1255866.
    STRINGi 511145.b0033.

    Proteomic databases

    PaxDbi P00968.
    PRIDEi P00968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73144 ; AAC73144 ; b0033 .
    BAB96602 ; BAB96602 ; BAB96602 .
    GeneIDi 12930732.
    944775.
    KEGGi ecj:Y75_p0033.
    eco:b0033.
    PATRICi 32115159. VBIEscCol129921_0031.

    Organism-specific databases

    EchoBASEi EB0133.
    EcoGenei EG10135. carB.

    Phylogenomic databases

    eggNOGi COG0458.
    HOGENOMi HOG000234582.
    KOi K01955.
    OMAi GSDRIWY.
    OrthoDBi EOG6J1DC6.
    PhylomeDBi P00968.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00171 .
    UPA00070 ; UER00115 .
    BioCyci EcoCyc:CARBPSYN-LARGE.
    ECOL316407:JW0031-MONOMER.
    MetaCyc:CARBPSYN-LARGE.
    SABIO-RK P00968.

    Miscellaneous databases

    EvolutionaryTracei P00968.
    PROi P00968.

    Gene expression databases

    Genevestigatori P00968.

    Family and domain databases

    Gene3Di 1.10.1030.10. 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.
    HAMAPi MF_01210_A. CPSase_L_chain_A.
    MF_01210_B. CPSase_L_chain_B.
    InterProi IPR011761. 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 ]
    Pfami PF00289. CPSase_L_chain. 2 hits.
    PF02786. CPSase_L_D2. 2 hits.
    PF02787. CPSase_L_D3. 1 hit.
    PF02142. MGS. 1 hit.
    [Graphical view ]
    PRINTSi PR00098. CPSASE.
    SMARTi SM01096. CPSase_L_D3. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48108. SSF48108. 1 hit.
    SSF52335. SSF52335. 1 hit.
    SSF52440. SSF52440. 2 hits.
    TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 2 hits.
    PS00866. CPSASE_1. 2 hits.
    PS00867. CPSASE_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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).

    Entry informationi

    Entry nameiCARB_ECOLI
    AccessioniPrimary (citable) accession number: P00968
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 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