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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

  1. cytosine deaminase activity Source: EcoCyc
  2. ferrous iron binding Source: EcoCyc
  3. identical protein binding Source: IntAct
  4. isoguanine deaminase activity Source: EcoCyc
  5. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. 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

  1. 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.

Expressioni

Gene expression databases

GenevestigatoriP25524.

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 22, 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.
YP_488631.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73440; AAC73440; b0337.
BAE76119; BAE76119; BAE76119.
GeneIDi12930819.
944996.
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.
YP_488631.1. NC_007779.1.

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.
GeneIDi12930819.
944996.
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.

Gene expression databases

GenevestigatoriP25524.

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(1991) [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(1992) [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 (DEC-1996) 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(2005) [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(1992) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Gene-directed enzyme prodrug therapy."
    Zhang J., Kale V., Chen M.
    AAPS J. 17:102-110(2014) [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(2001) [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(2003) [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(2008) [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(2010) [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 (FEB-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: April 30, 1992
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 128 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.