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Protein

Cytosine deaminase

Gene

codA

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

Functioni

Catalyzes the hydrolytic deamination of cytosine to uracil. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis. Is also able to catalyze deamination of isoguanine, a mutagenic oxidation product of adenine in DNA, and of isocytosine. To a lesser extent, also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor.4 Publications

Catalytic activityi

Cytosine + H2O = uracil + NH3.4 Publications
Isoguanine + H2O = xanthine + NH3.1 Publication

Cofactori

Fe2+2 Publications, Mn2+1 Publication, Zn2+2 PublicationsNote: The purified enzyme contains a mixture of Fe(2+) and Zn(2+) bound in the active site, and a single equivalent of metal is required for full catalytic activity. After removal of the metal, the reconstitution of the enzyme with Fe(2+) gives the highest activity, followed by Mn(2+), and, to a much lesser extent, Co(2+) and Zn2+.2 Publications

Enzyme regulationi

Fe2+-CDase is rapidly inactivated by H2O2, whereas Mn2+-CDase, Co2+-CDase, and Zn2+-CDase are not inactivated by H2O2. CDase is also inhibited by excess divalent cations (PubMed:8226944). Phosphonocytosine, a mimic of the tetrahedral reaction intermediate, inhibits the deamination of cytosine with a Ki of 52 nM (PubMed:21545144).2 Publications

Kineticsi

kcat is 185 sec(-1) for the deamination of cytosine using Fe2+ as cofactor, kcat is 92 sec(-1) using Mn2+ as cofactor, kcat is 52 sec(-1) using Co2+ as cofactor, and kcat is 32 sec(-1) using Zn2+ as cofactor (PubMed:8226944). kcat is 165 sec(-1) for the deamination of cytosine and 75.6 sec(-1) for the deamination of 5-fluorocytosine (PubMed:15381761). kcat is 132 sec(-1) for the deamination of cytosine, 5.1 sec(-1) for the deamination of isocytosine, 5.6 sec(-1) for the deamination of creatinine and 2.3 sec(-1) for the hydrolysis of 3-oxauracil (PubMed:21545144). kcat is 45 sec(-1) for the deamination of cytosine and 49 sec(-1) for the deamination of isoguanine at pH 7.7 (PubMed:21604715).4 Publications

  1. KM=0.22 mM for cytosine1 Publication
  2. KM=0.2 mM for cytosine1 Publication
  3. KM=3.3 mM for 5-fluorocytosine1 Publication
  4. KM=0.97 mM for cytosine1 Publication
  5. KM=0.46 mM for isocytosine1 Publication
  6. KM=25 mM for creatinine1 Publication
  7. KM=4.1 mM for 3-oxauracil1 Publication
  8. KM=72 µM for isoguanine1 Publication
  9. KM=302 µM for cytosine1 Publication

    pH dependencei

    Activity is lost under pH 5 but not affected up to pH 10.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi62 – 621Iron or zinc; catalytic6 Publications
    Metal bindingi64 – 641Iron or zinc; catalytic6 Publications
    Binding sitei157 – 1571Substrate4 Publications
    Metal bindingi215 – 2151Iron or zinc; catalytic6 Publications
    Active sitei218 – 2181Proton donor3 Publications
    Sitei247 – 2471Activates the nucleophilic water2 Publications
    Metal bindingi314 – 3141Iron or zinc; catalytic6 Publications
    Binding sitei320 – 3201Substrate3 Publications

    GO - Molecular functioni

    • cytosine deaminase activity Source: EcoCyc
    • ferrous iron binding Source: EcoCyc
    • identical protein binding Source: IntAct
    • isoguanine deaminase activity Source: EcoCyc
    • zinc ion binding Source: EcoCyc

    GO - Biological processi

    • cytosine catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cytosine metabolism

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:CYTDEAM-MONOMER.
    ECOL316407:JW0328-MONOMER.
    MetaCyc:CYTDEAM-MONOMER.
    RETL1328306-WGS:GSTH-6950-MONOMER.
    BRENDAi3.5.4.1. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosine deaminase2 Publications (EC:3.5.4.14 Publications)
    Short name:
    CD1 Publication
    Short name:
    CDA1 Publication
    Short name:
    CDase1 Publication
    Alternative name(s):
    Cytosine aminohydrolase
    Isoguanine deaminase1 Publication (EC:3.5.4.-1 Publication)
    Gene namesi
    Name:codA
    Ordered Locus Names:b0337, JW0328
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11326. codA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Biotechnological usei

    Cytosine deaminase is being explored for use as a suicide gene for cancer gene therapy. The cytosine deaminase/5-fluorouracil combined therapy has been used successfully for a variety of animal tumor models and is currently under investigation for the treatment of human cancers.1 Publication1 Publication1 Publication

    Disruption phenotypei

    Cells lacking this gene have less than 1% of the isoguanine deaminase activity of the wild-type strain.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571Q → A or N: Less than 0.01% of wild-type enzymatic activity. 1 Publication
    Mutagenesisi218 – 2181E → A or Q: Less than 0.01% of wild-type enzymatic activity. 1 Publication
    Mutagenesisi247 – 2471H → A or N: Less than 0.01% of wild-type enzymatic activity. 1 Publication
    Mutagenesisi247 – 2471H → Q: 200-fold decrease in catalytic efficiency. 1 Publication
    Mutagenesisi314 – 3141D → A: 17-fold decrease in catalytic efficiency with cytosine as substrate and 2-fold increase in that with 5FC as substrate. Shows increased sensitivity to 5FC. 1 Publication
    Mutagenesisi314 – 3141D → A: Less than 0.01% of wild-type enzymatic activity. 1 Publication
    Mutagenesisi314 – 3141D → G or S: Still active towards cytosine. Shows increased sensitivity to 5FC. 1 Publication
    Mutagenesisi314 – 3141D → K, R or H: Loss of enzymatic activity. 1 Publication
    Mutagenesisi314 – 3141D → N: 35000-fold decrease in catalytic efficiency. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 427426Cytosine deaminasePRO_0000090002Add
    BLAST

    Proteomic databases

    PaxDbiP25524.
    PRIDEiP25524.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-559181,EBI-559181

    Protein-protein interaction databases

    DIPiDIP-9306N.
    IntActiP25524. 6 interactions.
    MINTiMINT-1307853.
    STRINGi511145.b0337.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 136Combined sources
    Beta strandi19 – 268Combined sources
    Beta strandi29 – 3810Combined sources
    Beta strandi46 – 483Combined sources
    Beta strandi53 – 564Combined sources
    Beta strandi58 – 636Combined sources
    Turni65 – 695Combined sources
    Beta strandi73 – 753Combined sources
    Helixi82 – 9312Combined sources
    Helixi98 – 11417Combined sources
    Beta strandi117 – 1259Combined sources
    Helixi132 – 14413Combined sources
    Turni145 – 1473Combined sources
    Beta strandi149 – 1557Combined sources
    Beta strandi160 – 1634Combined sources
    Helixi166 – 17510Combined sources
    Beta strandi179 – 1813Combined sources
    Helixi185 – 1873Combined sources
    Beta strandi188 – 1903Combined sources
    Helixi191 – 20818Combined sources
    Beta strandi211 – 2166Combined sources
    Helixi226 – 23712Combined sources
    Helixi240 – 2423Combined sources
    Beta strandi243 – 2475Combined sources
    Helixi249 – 2535Combined sources
    Helixi256 – 26914Combined sources
    Beta strandi272 – 2754Combined sources
    Helixi277 – 2837Combined sources
    Turni284 – 2874Combined sources
    Helixi299 – 3046Combined sources
    Beta strandi309 – 3113Combined sources
    Beta strandi316 – 3183Combined sources
    Helixi328 – 33811Combined sources
    Helixi344 – 3485Combined sources
    Helixi349 – 3546Combined sources
    Helixi356 – 3616Combined sources
    Beta strandi368 – 3703Combined sources
    Beta strandi373 – 3753Combined sources
    Beta strandi377 – 3848Combined sources
    Helixi385 – 3917Combined sources
    Beta strandi396 – 4005Combined sources
    Beta strandi403 – 4075Combined sources
    Beta strandi413 – 42311Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K6WX-ray1.75A2-427[»]
    1K70X-ray1.80A2-427[»]
    1R9XX-ray1.58A2-427[»]
    1R9YX-ray1.57A2-427[»]
    1R9ZX-ray1.32A2-427[»]
    1RA0X-ray1.12A2-427[»]
    1RA5X-ray1.40A2-427[»]
    1RAKX-ray1.32A2-427[»]
    3G77X-ray1.80A5-427[»]
    3O7UX-ray1.71A1-427[»]
    3R0DX-ray1.50A1-427[»]
    3RN6X-ray2.26A1-427[»]
    ProteinModelPortaliP25524.
    SMRiP25524. Positions 5-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25524.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytosine deaminase family.Curated

    Phylogenomic databases

    eggNOGiCOG0402.
    HOGENOMiHOG000184778.
    InParanoidiP25524.
    KOiK01485.
    OMAiNNINVCF.
    OrthoDBiEOG6QG8F9.
    PhylomeDBiP25524.

    Family and domain databases

    Gene3Di2.30.40.10. 1 hit.
    InterProiIPR013108. Amidohydro_3.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view]
    PfamiPF07969. Amidohydro_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P25524-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNNALQTII NARLPGEEGL WQIHLQDGKI SAIDAQSGVM PITENSLDAE
    60 70 80 90 100
    QGLVIPPFVE PHIHLDTTQT AGQPNWNQSG TLFEGIERWA ERKALLTHDD
    110 120 130 140 150
    VKQRAWQTLK WQIANGIQHV RTHVDVSDAT LTALKAMLEV KQEVAPWIDL
    160 170 180 190 200
    QIVAFPQEGI LSYPNGEALL EEALRLGADV VGAIPHFEFT REYGVESLHK
    210 220 230 240 250
    TFALAQKYDR LIDVHCDEID DEQSRFVETV AALAHHEGMG ARVTASHTTA
    260 270 280 290 300
    MHSYNGAYTS RLFRLLKMSG INFVANPLVN IHLQGRFDTY PKRRGITRVK
    310 320 330 340 350
    EMLESGINVC FGHDDVFDPW YPLGTANMLQ VLHMGLHVCQ LMGYGQINDG
    360 370 380 390 400
    LNLITHHSAR TLNLQDYGIA AGNSANLIIL PAENGFDALR RQVPVRYSVR
    410 420
    GGKVIASTQP AQTTVYLEQP EAIDYKR
    Length:427
    Mass (Da):47,591
    Last modified:January 23, 2007 - v3
    Checksum:i9F91A2C46B3B1E42
    GO

    Sequence cautioni

    The sequence AAB18061.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131R → W in strain: SO5076.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X63656 Genomic DNA. Translation: CAA45196.1.
    S56903 Genomic DNA. Translation: AAB25761.2.
    U73857 Genomic DNA. Translation: AAB18061.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73440.1.
    AP009048 Genomic DNA. Translation: BAE76119.1.
    PIRiS22662.
    RefSeqiNP_414871.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC73440; AAC73440; b0337.
    BAE76119; BAE76119; BAE76119.
    GeneIDi944996.
    KEGGiecj:Y75_p0326.
    eco:b0337.
    PATRICi32115805. VBIEscCol129921_0344.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X63656 Genomic DNA. Translation: CAA45196.1.
    S56903 Genomic DNA. Translation: AAB25761.2.
    U73857 Genomic DNA. Translation: AAB18061.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73440.1.
    AP009048 Genomic DNA. Translation: BAE76119.1.
    PIRiS22662.
    RefSeqiNP_414871.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K6WX-ray1.75A2-427[»]
    1K70X-ray1.80A2-427[»]
    1R9XX-ray1.58A2-427[»]
    1R9YX-ray1.57A2-427[»]
    1R9ZX-ray1.32A2-427[»]
    1RA0X-ray1.12A2-427[»]
    1RA5X-ray1.40A2-427[»]
    1RAKX-ray1.32A2-427[»]
    3G77X-ray1.80A5-427[»]
    3O7UX-ray1.71A1-427[»]
    3R0DX-ray1.50A1-427[»]
    3RN6X-ray2.26A1-427[»]
    ProteinModelPortaliP25524.
    SMRiP25524. Positions 5-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-9306N.
    IntActiP25524. 6 interactions.
    MINTiMINT-1307853.
    STRINGi511145.b0337.

    Proteomic databases

    PaxDbiP25524.
    PRIDEiP25524.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73440; AAC73440; b0337.
    BAE76119; BAE76119; BAE76119.
    GeneIDi944996.
    KEGGiecj:Y75_p0326.
    eco:b0337.
    PATRICi32115805. VBIEscCol129921_0344.

    Organism-specific databases

    EchoBASEiEB1302.
    EcoGeneiEG11326. codA.

    Phylogenomic databases

    eggNOGiCOG0402.
    HOGENOMiHOG000184778.
    InParanoidiP25524.
    KOiK01485.
    OMAiNNINVCF.
    OrthoDBiEOG6QG8F9.
    PhylomeDBiP25524.

    Enzyme and pathway databases

    BioCyciEcoCyc:CYTDEAM-MONOMER.
    ECOL316407:JW0328-MONOMER.
    MetaCyc:CYTDEAM-MONOMER.
    RETL1328306-WGS:GSTH-6950-MONOMER.
    BRENDAi3.5.4.1. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP25524.
    PROiP25524.

    Family and domain databases

    Gene3Di2.30.40.10. 1 hit.
    InterProiIPR013108. Amidohydro_3.
    IPR011059. Metal-dep_hydrolase_composite.
    [Graphical view]
    PfamiPF07969. Amidohydro_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of the Escherichia coli codBA operon encoding cytosine permease and cytosine deaminase."
      Danielsen S., Kilstrup M., Barilla K., Jochimsen B., Neuhard J.
      Mol. Microbiol. 6:1335-1344(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20.
      Strain: CSH01.
    2. "A first step in the development of gene therapy for colorectal carcinoma: cloning, sequencing, and expression of Escherichia coli cytosine deaminase."
      Austin E.A., Huber B.E.
      Mol. Pharmacol. 43:380-387(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "Cytosine deaminase. The roles of divalent metal ions in catalysis."
      Porter D.J., Austin E.A.
      J. Biol. Chem. 268:24005-24011(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    7. "Crystallization and preliminary X-ray analysis of bacterial cytosine deaminase."
      Ireton G.C., Black M.E., Stoddard B.L.
      Acta Crystallogr. D 57:1643-1645(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. "Gene-directed enzyme prodrug therapy."
      Zhang J., Kale V., Chen M.
      AAPS J. 17:102-110(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, BIOTECHNOLOGY.
    9. "The structure of Escherichia coli cytosine deaminase."
      Ireton G.C., McDermott G., Black M.E., Stoddard B.L.
      J. Mol. Biol. 315:687-697(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH A MECHANISM-BASED INHIBITOR AND IRON, REACTION MECHANISM, ACTIVE SITE.
    10. "Random mutagenesis and selection of Escherichia coli cytosine deaminase for cancer gene therapy."
      Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.
      Protein Eng. Des. Sel. 17:625-633(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF MUTANTS GLY-314; ALA-314 AND SER-315 UNCOMPLEXED AND IN COMPLEX WITH (4S)-5-FLUORO-4-HYDROXY-3,4-DIHYDROPYRIMIDIN-2(1H)-ONE AND IRON, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-314, BIOTECHNOLOGY.
    11. "Bacterial cytosine deaminase mutants created by molecular engineering show improved 5-fluorocytosine-mediated cell killing in vitro and in vivo."
      Fuchita M., Ardiani A., Zhao L., Serve K., Stoddard B.L., Black M.E.
      Cancer Res. 69:4791-4799(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 5-427 OF MUTANT ALA-153/CYS-317/GLY-318 IN COMPLEX WITH IRON, BIOTECHNOLOGY.
    12. "Three-dimensional structure and catalytic mechanism of cytosine deaminase."
      Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.
      Biochemistry 50:5077-5085(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND ASP-314, ACTIVE SITES, REACTION MECHANISM.
      Strain: K12.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH ISOGUANINE AND ZINC, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF ISOGUANINE AS SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
    14. "Crystal structure of cytosine deaminase from Escherichia coli complexed with two zinc atoms in the active site."
      Fedorov A.A., Fedorov E.V., Kamat S., Hitchcock D., Raushel F.M., Almo S.C.
      Submitted (MAR-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC.

    Entry informationi

    Entry nameiCODA_ECOLI
    AccessioniPrimary (citable) accession number: P25524
    Secondary accession number(s): Q2MC87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 130 of the entry and version 3 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.