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Cytosine deaminase (CD) (CDA) (CDase) (EC 3.5.4.1) (Cytosine aminohydrolase) (Isoguanine deaminase) (EC 3.5.4.-)

 CODA_ECOLI              Reviewed;         427 AA.
P25524; Q2MC87;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
13-FEB-2019, entry version 149.
RecName: Full=Cytosine deaminase {ECO:0000303|PubMed:1640834, ECO:0000303|PubMed:8226944};
Short=CD {ECO:0000303|PubMed:15381761};
Short=CDA {ECO:0000303|PubMed:21545144};
Short=CDase {ECO:0000303|PubMed:8226944};
EC=3.5.4.1 {ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|PubMed:8226944};
AltName: Full=Cytosine aminohydrolase;
AltName: Full=Isoguanine deaminase {ECO:0000303|PubMed:21604715};
EC=3.5.4.- {ECO:0000269|PubMed:21604715};
Name=codA; OrderedLocusNames=b0337, JW0328;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-20.
STRAIN=CSH01;
PubMed=1640834; DOI=10.1111/j.1365-2958.1992.tb00854.x;
Danielsen S., Kilstrup M., Barilla K., Jochimsen B., Neuhard J.;
"Characterization of the Escherichia coli codBA operon encoding
cytosine permease and cytosine deaminase.";
Mol. Microbiol. 6:1335-1344(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8450832;
Austin E.A., Huber B.E.;
"A first step in the development of gene therapy for colorectal
carcinoma: cloning, sequencing, and expression of Escherichia coli
cytosine deaminase.";
Mol. Pharmacol. 43:380-387(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
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.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
AND ACTIVITY REGULATION.
PubMed=8226944;
Porter D.J., Austin E.A.;
"Cytosine deaminase. The roles of divalent metal ions in catalysis.";
J. Biol. Chem. 268:24005-24011(1993).
[7]
SUBUNIT.
PubMed=11679731; DOI=10.1107/S0907444901011064;
Ireton G.C., Black M.E., Stoddard B.L.;
"Crystallization and preliminary X-ray analysis of bacterial cytosine
deaminase.";
Acta Crystallogr. D 57:1643-1645(2001).
[8]
REVIEW, AND BIOTECHNOLOGY.
PubMed=25338741; DOI=10.1208/s12248-014-9675-7;
Zhang J., Kale V., Chen M.;
"Gene-directed enzyme prodrug therapy.";
AAPS J. 17:102-110(2015).
[9]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH A MECHANISM-BASED INHIBITOR AND IRON, REACTION MECHANISM, AND
ACTIVE SITE.
PubMed=11812140; DOI=10.1006/jmbi.2001.5277;
Ireton G.C., McDermott G., Black M.E., Stoddard B.L.;
"The structure of Escherichia coli cytosine deaminase.";
J. Mol. Biol. 315:687-697(2002).
[10]
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, AND BIOTECHNOLOGY.
PubMed=15381761; DOI=10.1093/protein/gzh074;
Mahan S.D., Ireton G.C., Knoeber C., Stoddard B.L., Black M.E.;
"Random mutagenesis and selection of Escherichia coli cytosine
deaminase for cancer gene therapy.";
Protein Eng. Des. Sel. 17:625-633(2004).
[11]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 5-427 OF MUTANT
ALA-153/CYS-317/GLY-318 IN COMPLEX WITH IRON, AND BIOTECHNOLOGY.
PubMed=19487291; DOI=10.1158/0008-5472.CAN-09-0615;
Fuchita M., Ardiani A., Zhao L., Serve K., Stoddard B.L., Black M.E.;
"Bacterial cytosine deaminase mutants created by molecular engineering
show improved 5-fluorocytosine-mediated cell killing in vitro and in
vivo.";
Cancer Res. 69:4791-4799(2009).
[12]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH
PHOSPHONOCYTOSINE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
ACTIVITY REGULATION, MUTAGENESIS OF GLN-157; GLU-218; HIS-247 AND
ASP-314, ACTIVE SITES, AND REACTION MECHANISM.
STRAIN=K12;
PubMed=21545144; DOI=10.1021/bi200483k;
Hall R.S., Fedorov A.A., Xu C., Fedorov E.V., Almo S.C., Raushel F.M.;
"Three-dimensional structure and catalytic mechanism of cytosine
deaminase.";
Biochemistry 50:5077-5085(2011).
[13]
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, AND DISRUPTION PHENOTYPE.
PubMed=21604715; DOI=10.1021/bi200680y;
Hitchcock D.S., Fedorov A.A., Fedorov E.V., Dangott L.J., Almo S.C.,
Raushel F.M.;
"Rescue of the orphan enzyme isoguanine deaminase.";
Biochemistry 50:5555-5557(2011).
[14]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC.
Fedorov A.A., Fedorov E.V., Kamat S., Hitchcock D., Raushel F.M.,
Almo S.C.;
"Crystal structure of cytosine deaminase from Escherichia coli
complexed with two zinc atoms in the active site.";
Submitted (MAR-2011) to the PDB data bank.
-!- FUNCTION: 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. {ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715,
ECO:0000269|PubMed:8226944}.
-!- CATALYTIC ACTIVITY:
Reaction=cytosine + H(+) + H2O = NH4(+) + uracil;
Xref=Rhea:RHEA:20605, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16040, ChEBI:CHEBI:17568, ChEBI:CHEBI:28938;
EC=3.5.4.1; Evidence={ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715,
ECO:0000269|PubMed:8226944};
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + H2O + isoguanine = NH4(+) + xanthine;
Xref=Rhea:RHEA:47720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17712, ChEBI:CHEBI:28938, ChEBI:CHEBI:62462;
Evidence={ECO:0000269|PubMed:21604715};
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:8226944};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:8226944};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:8226944};
Note=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 Zn(2+). {ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:8226944};
-!- ACTIVITY REGULATION: Fe(2+)-CDase is rapidly inactivated by
H(2)O(2), whereas Mn(2+)-CDase, Co(2+)-CDase, and Zn(2+)-CDase are
not inactivated by H(2)O(2). 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).
{ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:8226944}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.22 mM for cytosine {ECO:0000269|PubMed:8226944};
KM=0.2 mM for cytosine {ECO:0000269|PubMed:15381761};
KM=3.3 mM for 5-fluorocytosine {ECO:0000269|PubMed:15381761};
KM=0.97 mM for cytosine {ECO:0000269|PubMed:21545144};
KM=0.46 mM for isocytosine {ECO:0000269|PubMed:21545144};
KM=25 mM for creatinine {ECO:0000269|PubMed:21545144};
KM=4.1 mM for 3-oxauracil {ECO:0000269|PubMed:21545144};
KM=72 uM for isoguanine {ECO:0000269|PubMed:21604715};
KM=302 uM for cytosine {ECO:0000269|PubMed:21604715};
Note=kcat is 185 sec(-1) for the deamination of cytosine using
Fe(2+) as cofactor, kcat is 92 sec(-1) using Mn(2+) as cofactor,
kcat is 52 sec(-1) using Co(2+) as cofactor, and kcat is 32
sec(-1) using Zn(2+) 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). {ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715,
ECO:0000269|PubMed:8226944};
pH dependence:
Activity is lost under pH 5 but not affected up to pH 10.
{ECO:0000269|PubMed:21545144};
-!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11679731}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-559181, EBI-559181;
-!- DISRUPTION PHENOTYPE: Cells lacking this gene have less than 1% of
the isoguanine deaminase activity of the wild-type strain.
{ECO:0000269|PubMed:21604715}.
-!- BIOTECHNOLOGY: 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.
{ECO:0000269|PubMed:19487291, ECO:0000303|PubMed:25338741,
ECO:0000305|PubMed:15381761}.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. Cytosine deaminase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB18061.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X63656; CAA45196.1; -; Genomic_DNA.
EMBL; S56903; AAB25761.2; -; Genomic_DNA.
EMBL; U73857; AAB18061.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73440.1; -; Genomic_DNA.
EMBL; AP009048; BAE76119.1; -; Genomic_DNA.
PIR; S22662; S22662.
RefSeq; NP_414871.1; NC_000913.3.
RefSeq; WP_001301240.1; NZ_LN832404.1.
PDB; 1K6W; X-ray; 1.75 A; A=2-427.
PDB; 1K70; X-ray; 1.80 A; A=2-427.
PDB; 1R9X; X-ray; 1.58 A; A=2-427.
PDB; 1R9Y; X-ray; 1.57 A; A=2-427.
PDB; 1R9Z; X-ray; 1.32 A; A=2-427.
PDB; 1RA0; X-ray; 1.12 A; A=2-427.
PDB; 1RA5; X-ray; 1.40 A; A=2-427.
PDB; 1RAK; X-ray; 1.32 A; A=2-427.
PDB; 3G77; X-ray; 1.80 A; A=5-427.
PDB; 3O7U; X-ray; 1.71 A; A=1-427.
PDB; 3R0D; X-ray; 1.50 A; A=1-427.
PDB; 3RN6; X-ray; 2.26 A; A=1-427.
PDBsum; 1K6W; -.
PDBsum; 1K70; -.
PDBsum; 1R9X; -.
PDBsum; 1R9Y; -.
PDBsum; 1R9Z; -.
PDBsum; 1RA0; -.
PDBsum; 1RA5; -.
PDBsum; 1RAK; -.
PDBsum; 3G77; -.
PDBsum; 3O7U; -.
PDBsum; 3R0D; -.
PDBsum; 3RN6; -.
ProteinModelPortal; P25524; -.
SMR; P25524; -.
BioGrid; 4259813; 4.
DIP; DIP-9306N; -.
IntAct; P25524; 6.
STRING; 316407.85674479; -.
jPOST; P25524; -.
PaxDb; P25524; -.
PRIDE; P25524; -.
EnsemblBacteria; AAC73440; AAC73440; b0337.
EnsemblBacteria; BAE76119; BAE76119; BAE76119.
GeneID; 944996; -.
KEGG; ecj:JW0328; -.
KEGG; eco:b0337; -.
PATRIC; fig|1411691.4.peg.1940; -.
EchoBASE; EB1302; -.
EcoGene; EG11326; codA.
eggNOG; ENOG4105DZC; Bacteria.
eggNOG; COG0402; LUCA.
HOGENOM; HOG000184778; -.
InParanoid; P25524; -.
KO; K01485; -.
PhylomeDB; P25524; -.
BioCyc; EcoCyc:CYTDEAM-MONOMER; -.
BioCyc; ECOL316407:JW0328-MONOMER; -.
BioCyc; MetaCyc:CYTDEAM-MONOMER; -.
BRENDA; 3.5.4.1; 2026.
EvolutionaryTrace; P25524; -.
PRO; PR:P25524; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0102480; F:5-fluorocytosine deaminase activity; IEA:UniProtKB-EC.
GO; GO:0004131; F:cytosine deaminase activity; IDA:EcoCyc.
GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0035888; F:isoguanine deaminase activity; IDA:EcoCyc.
GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
GO; GO:0006209; P:cytosine catabolic process; IMP:EcoCyc.
Gene3D; 2.30.40.10; -; 1.
InterPro; IPR013108; Amidohydro_3.
InterPro; IPR011059; Metal-dep_hydrolase_composite.
InterPro; IPR032466; Metal_Hydrolase.
Pfam; PF07969; Amidohydro_3; 1.
SUPFAM; SSF51338; SSF51338; 1.
SUPFAM; SSF51556; SSF51556; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytosine metabolism;
Direct protein sequencing; Hydrolase; Iron; Metal-binding;
Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1640834}.
CHAIN 2 427 Cytosine deaminase.
/FTId=PRO_0000090002.
ACT_SITE 218 218 Proton donor.
{ECO:0000305|PubMed:11812140,
ECO:0000305|PubMed:21545144,
ECO:0000305|PubMed:21604715}.
METAL 62 62 Iron or zinc; catalytic.
{ECO:0000269|PubMed:11812140,
ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:19487291,
ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:21604715,
ECO:0000269|Ref.14}.
METAL 64 64 Iron or zinc; catalytic.
{ECO:0000269|PubMed:11812140,
ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:19487291,
ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:21604715,
ECO:0000269|Ref.14}.
METAL 215 215 Iron or zinc; catalytic.
{ECO:0000269|PubMed:11812140,
ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:19487291,
ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:21604715,
ECO:0000269|Ref.14}.
METAL 314 314 Iron or zinc; catalytic.
{ECO:0000269|PubMed:11812140,
ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:19487291,
ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:21604715,
ECO:0000269|Ref.14}.
BINDING 157 157 Substrate. {ECO:0000269|PubMed:11812140,
ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:21604715}.
BINDING 320 320 Substrate. {ECO:0000269|PubMed:11812140,
ECO:0000269|PubMed:15381761,
ECO:0000269|PubMed:21545144}.
SITE 247 247 Activates the nucleophilic water.
{ECO:0000305|PubMed:21545144,
ECO:0000305|PubMed:21604715}.
VARIANT 13 13 R -> W (in strain: SO5076).
MUTAGEN 157 157 Q->A,N: Less than 0.01% of wild-type
enzymatic activity.
{ECO:0000269|PubMed:21545144}.
MUTAGEN 218 218 E->A,Q: Less than 0.01% of wild-type
enzymatic activity.
{ECO:0000269|PubMed:21545144}.
MUTAGEN 247 247 H->A,N: Less than 0.01% of wild-type
enzymatic activity.
{ECO:0000269|PubMed:21545144}.
MUTAGEN 247 247 H->Q: 200-fold decrease in catalytic
efficiency.
{ECO:0000269|PubMed:21545144}.
MUTAGEN 314 314 D->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. {ECO:0000269|PubMed:15381761}.
MUTAGEN 314 314 D->A: Less than 0.01% of wild-type
enzymatic activity.
{ECO:0000269|PubMed:21545144}.
MUTAGEN 314 314 D->G,S: Still active towards cytosine.
Shows increased sensitivity to 5FC.
{ECO:0000269|PubMed:15381761}.
MUTAGEN 314 314 D->K,R,H: Loss of enzymatic activity.
{ECO:0000269|PubMed:15381761}.
MUTAGEN 314 314 D->N: 35000-fold decrease in catalytic
efficiency.
{ECO:0000269|PubMed:21545144}.
STRAND 8 13 {ECO:0000244|PDB:1RA0}.
STRAND 19 26 {ECO:0000244|PDB:1RA0}.
STRAND 29 38 {ECO:0000244|PDB:1RA0}.
STRAND 46 48 {ECO:0000244|PDB:1RA0}.
STRAND 53 56 {ECO:0000244|PDB:1RA0}.
STRAND 58 63 {ECO:0000244|PDB:1RA0}.
TURN 65 69 {ECO:0000244|PDB:1RA0}.
STRAND 73 75 {ECO:0000244|PDB:1RA0}.
HELIX 82 93 {ECO:0000244|PDB:1RA0}.
HELIX 98 114 {ECO:0000244|PDB:1RA0}.
STRAND 117 125 {ECO:0000244|PDB:1RA0}.
HELIX 132 144 {ECO:0000244|PDB:1RA0}.
TURN 145 147 {ECO:0000244|PDB:1RA0}.
STRAND 149 155 {ECO:0000244|PDB:1RA0}.
STRAND 160 163 {ECO:0000244|PDB:1RA0}.
HELIX 166 175 {ECO:0000244|PDB:1RA0}.
STRAND 179 181 {ECO:0000244|PDB:1RA0}.
HELIX 185 187 {ECO:0000244|PDB:1RA0}.
STRAND 188 190 {ECO:0000244|PDB:1RA0}.
HELIX 191 208 {ECO:0000244|PDB:1RA0}.
STRAND 211 216 {ECO:0000244|PDB:1RA0}.
HELIX 226 237 {ECO:0000244|PDB:1RA0}.
HELIX 240 242 {ECO:0000244|PDB:1RA0}.
STRAND 243 247 {ECO:0000244|PDB:1RA0}.
HELIX 249 253 {ECO:0000244|PDB:1RA0}.
HELIX 256 269 {ECO:0000244|PDB:1RA0}.
STRAND 272 275 {ECO:0000244|PDB:1RA0}.
HELIX 277 283 {ECO:0000244|PDB:1RA0}.
TURN 284 287 {ECO:0000244|PDB:1RA0}.
HELIX 299 304 {ECO:0000244|PDB:1RA0}.
STRAND 309 311 {ECO:0000244|PDB:1RA0}.
STRAND 316 318 {ECO:0000244|PDB:1RA0}.
HELIX 328 338 {ECO:0000244|PDB:1RA0}.
HELIX 344 348 {ECO:0000244|PDB:1RA0}.
HELIX 349 354 {ECO:0000244|PDB:1RA0}.
HELIX 356 361 {ECO:0000244|PDB:1RA0}.
STRAND 368 370 {ECO:0000244|PDB:3R0D}.
STRAND 373 375 {ECO:0000244|PDB:3RN6}.
STRAND 377 384 {ECO:0000244|PDB:1RA0}.
HELIX 385 391 {ECO:0000244|PDB:1RA0}.
STRAND 396 400 {ECO:0000244|PDB:1RA0}.
STRAND 403 407 {ECO:0000244|PDB:1RA0}.
STRAND 413 423 {ECO:0000244|PDB:1RA0}.
SEQUENCE 427 AA; 47591 MW; 9F91A2C46B3B1E42 CRC64;
MSNNALQTII NARLPGEEGL WQIHLQDGKI SAIDAQSGVM PITENSLDAE QGLVIPPFVE
PHIHLDTTQT AGQPNWNQSG TLFEGIERWA ERKALLTHDD VKQRAWQTLK WQIANGIQHV
RTHVDVSDAT LTALKAMLEV KQEVAPWIDL QIVAFPQEGI LSYPNGEALL EEALRLGADV
VGAIPHFEFT REYGVESLHK TFALAQKYDR LIDVHCDEID DEQSRFVETV AALAHHEGMG
ARVTASHTTA MHSYNGAYTS RLFRLLKMSG INFVANPLVN IHLQGRFDTY PKRRGITRVK
EMLESGINVC FGHDDVFDPW YPLGTANMLQ VLHMGLHVCQ LMGYGQINDG LNLITHHSAR
TLNLQDYGIA AGNSANLIIL PAENGFDALR RQVPVRYSVR GGKVIASTQP AQTTVYLEQP
EAIDYKR


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1623: Atrazine degradation

Related Genes :
[codA b0337 JW0328] Cytosine deaminase (CD) (CDA) (CDase) (EC 3.5.4.1) (Cytosine aminohydrolase) (Isoguanine deaminase) (EC 3.5.4.-)
[FCY1 YPR062W YP9499.17] Cytosine deaminase (EC 3.5.4.1) (Cytosine aminohydrolase)
[AICDA AID] Single-stranded DNA cytosine deaminase (EC 3.5.4.38) (Activation-induced cytidine deaminase) (AID) (Cytidine aminohydrolase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[APOBEC3G MDS019] DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.-) (APOBEC-related cytidine deaminase) (APOBEC-related protein) (ARCD) (APOBEC-related protein 9) (ARP-9) (CEM-15) (CEM15) (Deoxycytidine deaminase) (A3G)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3K24_08940 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3I61_16000 DD762_13665 DIV22_29760 DIV25_29790 DL545_05995 DL800_20505 DNQ41_18960 DNR41_08670 DQE83_04685 DS732_20695 DS966_06010 DTL43_09355 DTL84_00105 DTL90_02675 DTM10_03745 DTM25_22630 DTM27_13675 DTM45_13530 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9010_01168 NCTC9036_01135 NCTC9037_01243 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753106_03183 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753391_02580 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[SPCC965.14c] Probable cytosine deaminase (EC 3.5.4.1) (Cytosine aminohydrolase)
[ADA ADA1] Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[amdA DDB_G0292266] AMP deaminase (EC 3.5.4.6)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BHF46_18455 BMT91_24760 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 EC3234A_36c00010 NCTC8500_02249 NCTC9010_02117 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Pre C,C C core E PC pre-C pre-C/C PreC preC PreC/C preC/C precore-core HBVgp4] Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[PYRR PHS1 At3g47390 T21L8.140] Riboflavin biosynthesis protein PYRR, chloroplastic [Includes: Inactive diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (Riboflavin-specific deaminase); 5-amino-6-(5-phosphoribosylamino)uracil reductase (EC 1.1.1.193) (HTP reductase); Riboflavin biosynthesis intermediates N-glycosidase (EC 3.2.2.-)]
[APOBEC1] C->U-editing enzyme APOBEC-1 (EC 3.5.4.36) (Apolipoprotein B mRNA-editing enzyme 1) (mRNA(cytosine(6666)) deaminase 1)

Bibliography :
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