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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.
28-MAR-2018, entry version 144.
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 ENZYME 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, ENZYME
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: Cytosine + H(2)O = uracil + NH(3).
{ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144,
ECO:0000269|PubMed:21604715, ECO:0000269|PubMed:8226944}.
-!- CATALYTIC ACTIVITY: Isoguanine + H(2)O = xanthine + NH(3).
{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};
-!- ENZYME 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; -.
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; -.
OMA; ERTMADG; -.
PhylomeDB; P25524; -.
BioCyc; EcoCyc:CYTDEAM-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; -; 2.
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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