Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B1LKP0

- CDD_ECOSM

UniProt

B1LKP0 - CDD_ECOSM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cytidine deaminase

Gene

cdd

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.UniRule annotation

Catalytic activityi

Cytidine + H2O = uridine + NH3.UniRule annotation
2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Zinc; catalyticUniRule annotation
Active sitei104 – 1041Proton donorUniRule annotation
Metal bindingi129 – 1291Zinc; catalyticUniRule annotation
Metal bindingi132 – 1321Zinc; catalyticUniRule annotation

GO - Molecular functioni

  1. cytidine deaminase activity Source: UniProtKB-HAMAP
  2. zinc ion binding Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciECOL439855:GHHB-2288-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidine deaminaseUniRule annotation (EC:3.5.4.5UniRule annotation)
Alternative name(s):
Cytidine aminohydrolaseUniRule annotation
Short name:
CDAUniRule annotation
Gene namesi
Name:cddUniRule annotation
Ordered Locus Names:EcSMS35_2290
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Cytidine deaminasePRO_1000147102Add
BLAST

Proteomic databases

PRIDEiB1LKP0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi439855.EcSMS35_2290.

Structurei

3D structure databases

ProteinModelPortaliB1LKP0.
SMRiB1LKP0. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13984CMP/dCMP deaminase zinc-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni89 – 913Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the cytidine and deoxycytidylate deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0295.
HOGENOMiHOG000218617.
KOiK01489.
OMAiNRSHAPY.
OrthoDBiEOG6XDH25.

Family and domain databases

HAMAPiMF_01558. Cyt_deam.
InterProiIPR016192. 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]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006334. Cdd_plus_pseudo. 1 hit.
SUPFAMiSSF53927. SSF53927. 2 hits.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1LKP0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED
60 70 80 90 100
ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT
110 120 130 140 150
VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP
160 170 180 190 200
GREAHALRDY LPDAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN
210 220 230 240 250
RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK
260 270 280 290
GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHSIDR VLLA
Length:294
Mass (Da):31,540
Last modified:April 29, 2008 - v1
Checksum:iF0B5CD68AB145D7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB16248.1.
RefSeqiYP_001744337.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB16248; ACB16248; EcSMS35_2290.
GeneIDi6143970.
KEGGiecm:EcSMS35_2290.
PATRICi18433480. VBIEscCol6161_2457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB16248.1 .
RefSeqi YP_001744337.1. NC_010498.1.

3D structure databases

ProteinModelPortali B1LKP0.
SMRi B1LKP0. Positions 1-294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439855.EcSMS35_2290.

Proteomic databases

PRIDEi B1LKP0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB16248 ; ACB16248 ; EcSMS35_2290 .
GeneIDi 6143970.
KEGGi ecm:EcSMS35_2290.
PATRICi 18433480. VBIEscCol6161_2457.

Phylogenomic databases

eggNOGi COG0295.
HOGENOMi HOG000218617.
KOi K01489.
OMAi NRSHAPY.
OrthoDBi EOG6XDH25.

Enzyme and pathway databases

BioCyci ECOL439855:GHHB-2288-MONOMER.

Family and domain databases

HAMAPi MF_01558. Cyt_deam.
InterProi IPR016192. 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 ]
Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006334. Cdd_plus_pseudo. 1 hit.
SUPFAMi SSF53927. SSF53927. 2 hits.
TIGRFAMsi TIGR01355. cyt_deam_dimer. 1 hit.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiCDD_ECOSM
AccessioniPrimary (citable) accession number: B1LKP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: November 26, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3