Reviewed, UniProtKB/Swiss-Prot P25524 (CODA_ECOLI)

Names and origin

Protein names

Recommended name:
    Cytosine deaminase
    EC=3.5.4.1
Alternative name(s):
    Cytosine aminohydrolase

Gene names

Name:	codA
Ordered Locus Names:	b0337, JW0328

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Cytosine + H2O = uracil + NH3.
Cofactor	Iron or another divalent metal ion.
Subunit structure	Homotetramer.

Ontologies

Keywords
Biological process	Cytosine metabolism
Ligand	Iron Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cytosine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	cytosine deaminase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 427

426

Cytosine deaminase

PRO_0000090002

Sites

Metal binding

62

1

Iron

Metal binding

64

1

Iron

Natural variations

Natural variant

13

1

R → W in strain: SO5076.

Secondary structure

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427

Helix Strand Turn

Details...

Beta strand

8 – 13

6

Beta strand

19 – 26

8

Beta strand

29 – 38

10

Beta strand

46 – 48

3

Beta strand

53 – 56

4

Beta strand

58 – 63

6

Turn

65 – 69

5

Beta strand

73 – 75

3

Helix

82 – 90

9

Helix

91 – 95

5

Helix

98 – 114

17

Beta strand

117 – 125

9

Helix

132 – 144

13

Turn

145 – 147

3

Beta strand

149 – 155

7

Beta strand

160 – 163

4

Helix

166 – 175

10

Beta strand

179 – 183

5

Helix

185 – 187

3

Beta strand

188 – 190

3

Helix

191 – 208

18

Beta strand

211 – 216

6

Helix

226 – 237

12

Helix

240 – 242

3

Beta strand

243 – 247

5

Helix

249 – 253

5

Helix

256 – 269

14

Beta strand

272 – 275

4

Helix

277 – 283

7

Turn

284 – 287

4

Helix

299 – 304

6

Beta strand

309 – 311

3

Helix

328 – 338

11

Helix

344 – 348

5

Helix

349 – 354

6

Helix

356 – 361

6

Beta strand

377 – 384

8

Helix

385 – 391

7

Beta strand

396 – 400

5

Beta strand

403 – 409

7

Beta strand

412 – 423

12

Sequences

	Sequence		Length	Mass (Da)
	P25524-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9F91A2C46B3B1E42	FASTA	427	47,591
	10 20 30 40 50 60 MSNNALQTII NARLPGEEGL WQIHLQDGKI SAIDAQSGVM PITENSLDAE QGLVIPPFVE 70 80 90 100 110 120 PHIHLDTTQT AGQPNWNQSG TLFEGIERWA ERKALLTHDD VKQRAWQTLK WQIANGIQHV 130 140 150 160 170 180 RTHVDVSDAT LTALKAMLEV KQEVAPWIDL QIVAFPQEGI LSYPNGEALL EEALRLGADV 190 200 210 220 230 240 VGAIPHFEFT REYGVESLHK TFALAQKYDR LIDVHCDEID DEQSRFVETV AALAHHEGMG 250 260 270 280 290 300 ARVTASHTTA MHSYNGAYTS RLFRLLKMSG INFVANPLVN IHLQGRFDTY PKRRGITRVK 310 320 330 340 350 360 EMLESGINVC FGHDDVFDPW YPLGTANMLQ VLHMGLHVCQ LMGYGQINDG LNLITHHSAR 370 380 390 400 410 420 TLNLQDYGIA AGNSANLIIL PAENGFDALR RQVPVRYSVR GGKVIASTQP AQTTVYLEQP EAIDYKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1640834] [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: 8450832] [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]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"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: 11812140] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

S22662.

RefSeq

AP_000989.1.
NP_414871.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K6W	X-ray	1.75	A	2-427	[»]
1K70	X-ray	1.80	A	2-427	[»]
1R9X	X-ray	1.58	A	3-426	[»]
1R9Y	X-ray	1.57	A	3-426	[»]
1R9Z	X-ray	1.32	A	3-426	[»]
1RA0	X-ray	1.12	A	3-426	[»]
1RA5	X-ray	1.40	A	3-426	[»]
1RAK	X-ray	1.32	A	3-426	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9306N.

Genome annotation databases

GeneID

944996.

GenomeReviews

Gene locus JW0328 in contig AP009048_GR.
Gene locus b0337 in contig U00096_GR.

KEGG

ecj:JW0328.
eco:b0337.

Organism-specific databases

EchoBASE

EB1302.

EcoGene

EG11326. codA.

CMR

Search...

Phylogenomic databases

HOGENOM

P25524.

OMA

P25524. AKQTLKW.

Enzyme and pathway databases

BioCyc

EcoCyc:CYTDEAM-MON.
MetaCyc:CYTDEAM-MON.

Family and domain databases

InterPro

IPR013108. Amidohydro_3.
[Graphical view]

Pfam

PF07969. Amidohydro_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CODA_ECOLI

Accession

Primary (citable) accession number: P25524
Secondary accession number(s): Q2MC87

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)