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C6EAG9 (C6EAG9_ECOBD) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytidine deaminase PIRNR PIRNR006334 HAMAP MF_01558

EC=3.5.4.5 PIRNR PIRNR006334 HAMAP MF_01558
Alternative name(s):
Cytidine aminohydrolase HAMAP MF_01558
Gene names
Name:cdd HAMAP MF_01558 EMBL ACT43896.1
Ordered Locus Names:B21_02031, ECBD_1515, ECD_02072
OrganismEscherichia coli (strain B / BL21-DE3) [Complete proteome] [HAMAP]
Taxonomic identifier469008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis By similarity. SAAS SAAS002125 HAMAP MF_01558

Catalytic activity

Cytidine + H2O = uridine + NH3. SAAS SAAS002125 PIRNR PIRNR006334 HAMAP MF_01558

Cofactor

Binds 1 zinc ion By similarity. SAAS SAAS002125 PIRNR PIRNR006334 PIRSR PIRSR006334-3 HAMAP MF_01558

Subunit structure

Homodimer By similarity. SAAS SAAS002125 HAMAP MF_01558

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family. PIRNR PIRNR006334 HAMAP MF_01558

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region89 – 913Substrate binding By similarity PIRSR PIRSR006334-2

Sites

Active site1041Proton donor By similarity PIRSR PIRSR006334-1
Metal binding1021Zinc; catalytic By similarity PIRSR PIRSR006334-3
Metal binding1291Zinc; catalytic By similarity PIRSR PIRSR006334-3
Metal binding1321Zinc; catalytic By similarity PIRSR PIRSR006334-3

Sequences

Sequence LengthMass (Da)Tools
C6EAG9 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: F0B5CD68AB145D7D

FASTA29431,540
        10         20         30         40         50         60 
MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA 

        70         80         90        100        110        120 
AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA 

       130        140        150        160        170        180 
AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LPDAFGPKDL EIKTLLMDEQ 

       190        200        210        220        230        240 
DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL 

       250        260        270        280        290 
QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHSIDR VLLA 

« Hide

References

[1]"Genome sequences of Escherichia coli B strains REL606 and BL21(DE3)."
Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.
J. Mol. Biol. 394:644-652(2009) [PubMed: 19786035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Korea].
[2]"Sequencing and gene expression analysis of Escherichia coli BL21."
Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [Austria].
[3]"Complete sequence of Escherichia coli BL21(DE3)."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B / BL21-DE3 [JGI].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001665 Genomic DNA. Translation: ACT28576.1.
CP001509 Genomic DNA. Translation: ACT43896.1.
AM946981 Genomic DNA. Translation: CAQ32548.1.

3D structure databases

ProteinModelPortalC6EAG9.
SMRC6EAG9. Positions 1-294.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6EAG9.

Proteomic databases

PRIDEC6EAG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000156839; EBESCP00000146993; EBESCG00000155295.
EBESCT00000189578; EBESCP00000178941; EBESCG00000189030.
EBESCT00000195833; EBESCP00000182992; EBESCG00000192539.
GenomeReviewsGene locus B21_02031 in contig AM946981_GR.
Gene locus ECD_02072 in contig CP001509_GR.
Gene locus ECBD_1515 in contig CP001665_GR.
KEGGebd:ECBD_1515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010652.
OMANRSHAPY.
ProtClustDBPRK09027.

Family and domain databases

HAMAPMF_01558. Cyt_deam.
[Tree]
InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR013171. Cyd/dCyd_deaminase_Zn-bd.
IPR006263. Cyt_deam_dimer.
IPR016193. Cytidine_deaminase-like.
IPR020797. Cytidine_deaminase_bacteria.
[Graphical view]
KOK01489.
PANTHERPTHR11644:SF12. PTHR11644:SF12. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view]
PIRSFPIRSF006334. Cdd_plus_pseudo. 1 hit.
SUPFAMSSF53927. Cytidine_deaminase-like. 2 hits.
TIGRFAMsTIGR01355. Cyt_deam_dimer. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC6EAG9_ECOBD
AccessionPrimary (citable) accession number: C6EAG9
Secondary accession number(s): C5W6N9
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: December 14, 2011
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)