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ECOLI:CODA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) codA
Protein Name(s) Cytosine deaminase

Cytosine aminohydrolase

External Links
UniProt P25524
EMBL X63656
S56903
U73857
U00096
AP009048
PIR S22662
RefSeq NP_414871.1
YP_488631.1
PDB 1K6W
1K70
1R9X
1R9Y
1R9Z
1RA0
1RA5
1RAK
3G77
3O7U
3R0D
3RN6
PDBsum 1K6W
1K70
1R9X
1R9Y
1R9Z
1RA0
1RA5
1RAK
3G77
3O7U
3R0D
3RN6
ProteinModelPortal P25524
SMR P25524
DIP DIP-9306N
IntAct P25524
MINT MINT-1307853
STRING 511145.b0337
PaxDb P25524
PRIDE P25524
EnsemblBacteria AAC73440
BAE76119
GeneID 12930819
944996
KEGG ecj:Y75_p0326
eco:b0337
PATRIC 32115805
EchoBASE EB1302
EcoGene EG11326
eggNOG COG0402
HOGENOM HOG000184778
InParanoid P25524
KO K01485
OMA NNINVCF
OrthoDB EOG6QG8F9
PhylomeDB P25524
BioCyc EcoCyc:CYTDEAM-MONOMER
ECOL316407:JW0328-MONOMER
MetaCyc:CYTDEAM-MONOMER
RETL1328306-WGS:GSTH-6950-MONOMER
EvolutionaryTrace P25524
PRO PR:P25524
Proteomes UP000000318
UP000000625
Genevestigator P25524
GO GO:0005829
GO:0004131
GO:0008198
GO:0042802
GO:0035888
GO:0008270
GO:0006209
Gene3D 2.30.40.10
InterPro IPR013108
IPR011059
Pfam PF07969
SUPFAM SSF51338

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0040029

regulation of gene expression, epigenetic

PMID:12700271[1]

ECO:0000270

P

Figure 2 confirms that the NAC activation of codBA is direct and requires no other factors on codBA expression.

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0035888

isoguanine deaminase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11326
PANTHER:PTN000783467

F

Seeded From UniProt

complete

involved_in

GO:0006209

cytosine catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11326
PANTHER:PTN000783467

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11326
PANTHER:PTN000783459

C

Seeded From UniProt

complete

enables

GO:0004131

cytosine deaminase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11326
PANTHER:PTN000783467

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25524

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25524

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:11812140[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0035888

isoguanine deaminase activity

PMID:21604715[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:21545144[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:8226944[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006209

cytosine catabolic process

PMID:4561896[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004131

cytosine deaminase activity

PMID:8226944[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016810

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011059

F

Seeded From UniProt

complete

enables

GO:0004131

cytosine deaminase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.5.4.1

F

Seeded From UniProt

complete

enables

GO:0102480

5-fluorocytosine deaminase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.5.4.1

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0019858

cytosine metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0205

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Muse, WB et al. (2003) Nitrogen regulation of the codBA (cytosine deaminase) operon from Escherichia coli by the nitrogen assimilation control protein, NAC. J. Bacteriol. 185 2920-6 PubMed GONUTS page
  2. 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  5. Ireton, GC et al. (2002) The structure of Escherichia coli cytosine deaminase. J. Mol. Biol. 315 687-97 PubMed GONUTS page
  6. Hitchcock, DS et al. (2011) Rescue of the orphan enzyme isoguanine deaminase. Biochemistry 50 5555-7 PubMed GONUTS page
  7. Hall, RS et al. (2011) Three-dimensional structure and catalytic mechanism of cytosine deaminase. Biochemistry 50 5077-85 PubMed GONUTS page
  8. 8.0 8.1 Porter, DJ & Austin, EA (1993) Cytosine deaminase. The roles of divalent metal ions in catalysis. J. Biol. Chem. 268 24005-11 PubMed GONUTS page
  9. de Haan, PG et al. (1972) Mapping of the gene for cytosine deaminase on the Escherichia coli chromosome. Antonie Van Leeuwenhoek 38 257-63 PubMed GONUTS page