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C6V2M9 (C6V2M9_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 19. 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 HAMAP MF_01558 PIRNR PIRNR006334
EC=3.5.4.5 HAMAP MF_01558 PIRNR PIRNR006334
Alternative name(s):
Cytidine aminohydrolase HAMAP MF_01558
Gene names
Name:cdd HAMAP MF_01558 EMBL ACT72803.1
Ordered Locus Names:ECSP_3021
OrganismEscherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier544404 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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. HAMAP MF_01558 SAAS SAAS002125

Catalytic activity

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

Cofactor

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

Subunit structure

Homodimer By similarity. HAMAP MF_01558 SAAS SAAS002125

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region89 – 913Substrate binding By similarity HAMAP MF_01558 PIRSR PIRSR006334-2

Sites

Active site1041Proton donor By similarity HAMAP MF_01558 PIRSR PIRSR006334-1
Metal binding1021Zinc; catalytic By similarity HAMAP MF_01558 PIRSR PIRSR006334-3
Metal binding1291Zinc; catalytic By similarity HAMAP MF_01558 PIRSR PIRSR006334-3
Metal binding1321Zinc; catalytic By similarity HAMAP MF_01558 PIRSR PIRSR006334-3

Sequences

Sequence LengthMass (Da)Tools
C6V2M9 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 69B5D87DA4B147DC

FASTA29431,541
        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 LADAFGPKDL EIKTLLMDEQ 

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

       250        260        270        280        290 
QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHNIDR VLLA

« Hide

References

[1]"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. expand/collapse author list , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed: 19564389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001368 Genomic DNA. Translation: ACT72803.1.
RefSeqYP_003078879.1. NC_013008.1.

3D structure databases

ProteinModelPortalC6V2M9.
SMRC6V2M9. Positions 1-294.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6V2M9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000168185; EBESCP00000155549; EBESCG00000169287.
GeneID8217587.
GenomeReviewsGene locus ECSP_3021 in contig CP001368_GR.
KEGGetw:ECSP_3021.
PATRIC18390080. VBIEscCol9396_3068.

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 nameC6V2M9_ECO5T
AccessionPrimary (citable) accession number: C6V2M9
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: December 14, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info