Cytosine deaminase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P25524 (CODA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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)

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.
Sequence caution	The sequence AAB18061.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cytosine metabolism
Ligand	Iron Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 metal 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

Removed Ref.1

Chain

2 – 427

426

Cytosine deaminase

PRO_0000090002

Sites

Metal binding

Iron

Metal binding

Iron

Natural variations

Natural variant

R → W in strain: SO5076.

Secondary structure

427

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P25524 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9F91A2C46B3B1E42
Show »

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

« Hide

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

EMBL
GenBank
DDBJ

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

NP_414871.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3G77	X-ray	1.80	A	5-427	[»]
3O7U	X-ray	1.71	A	1-427	[»]
3RN6	X-ray	2.26	A	1-427	[»]

ProteinModelPortal

P25524.

SMR

P25524. Positions 5-427.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9306N.

IntAct

P25524. 8 interactions.

MINT

MINT-1307853.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003145; EBESCP00000003145; EBESCG00000002581.
EBESCT00000016326; EBESCP00000015617; EBESCG00000015386.

GeneID

944996.

GenomeReviews

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

KEGG

ecj:JW0328.
eco:b0337.

PATRIC

32115805. VBIEscCol129921_0344.

Organism-specific databases

EchoBASE

EB1302.

EcoGene

EG11326. codA.

Phylogenomic databases

eggNOG

COG0402.

GeneTree

EBGT00050000010834.

HOGENOM

HBG699324.

OMA

AKQTLKW.

PhylomeDB

P25524.

ProtClustDB

PRK09230.

Enzyme and pathway databases

BioCyc

EcoCyc:CYTDEAM-MONOMER.
MetaCyc:CYTDEAM-MONOMER.

Gene expression databases

Genevestigator

P25524.

Family and domain databases

InterPro

IPR013108. Amidohydro_3.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]

K01485.

Pfam

PF07969. Amidohydro_3. 1 hit.
[Graphical view]

SUPFAM

SSF51338. Metalo_hydrolase. 1 hit.

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:	January 25, 2012
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents