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Q9KSM5

- CDD_VIBCH

UniProt

Q9KSM5 - CDD_VIBCH

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Protein

Cytidine deaminase

Gene

cdd

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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

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: TIGR
  2. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyrimidine-containing compound salvage Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciVCHO:VC1231-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:VC_1231
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Cytidine deaminasePRO_0000171669Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VC1231.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1110
Turni14 – 163
Helixi17 – 248
Beta strandi31 – 333
Helixi35 – 4511
Helixi49 – 6113
Turni67 – 693
Beta strandi74 – 796
Beta strandi84 – 885
Helixi97 – 993
Helixi103 – 11311
Beta strandi119 – 1268
Helixi130 – 1367
Turni140 – 1445
Beta strandi146 – 1483
Beta strandi150 – 1523
Helixi157 – 1604
Helixi167 – 1704
Helixi191 – 20010
Turni206 – 2083
Beta strandi212 – 2187
Beta strandi223 – 2275
Helixi240 – 25011
Helixi255 – 2573
Beta strandi258 – 2658
Helixi274 – 28411
Beta strandi290 – 2945

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EG2X-ray2.20A/B/C/D/E/F/G/H1-295[»]
ProteinModelPortaliQ9KSM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 14081CMP/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.
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.

Q9KSM5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRNRIEQALQ QMPASFAPYL RELVLAKDFD ATFSAEQYQQ LLTLSGLEDA
60 70 80 90 100
DLRVALLPIA AAYSYAPISE FYVGAIVRGI SGRLYLGANM EFTGAQLGQT
110 120 130 140 150
VHAEQCAISH AWMKGEKGVA DITINFSPCG HCRQFMNELT TASSLKIQLP
160 170 180 190 200
KRAAKTLQEY LPESFGPADL GIDSGLMSPV NHGKTSDDDE ELIQQALRAM
210 220 230 240 250
NISHSPYTQN FSGVALKMRS GAIYLGAYAE NAAFNPSLPP LQVALAQAMM
260 270 280 290
MGESFEDIEA AALVESATGK ISHLADTQAT LEVINPDIPL SYLSL
Length:295
Mass (Da):31,955
Last modified:October 1, 2000 - v1
Checksum:i7AA766021089D736
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF94390.1.
PIRiG82226.
RefSeqiNP_230876.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF94390; AAF94390; VC_1231.
GeneIDi2614668.
KEGGivch:VC1231.
PATRICi20081548. VBIVibCho83274_1173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF94390.1 .
PIRi G82226.
RefSeqi NP_230876.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EG2 X-ray 2.20 A/B/C/D/E/F/G/H 1-295 [» ]
ProteinModelPortali Q9KSM5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC1231.

Protocols and materials databases

DNASUi 2614668.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF94390 ; AAF94390 ; VC_1231 .
GeneIDi 2614668.
KEGGi vch:VC1231.
PATRICi 20081548. VBIVibCho83274_1173.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci VCHO:VC1231-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiCDD_VIBCH
AccessioniPrimary (citable) accession number: Q9KSM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2000
Last modified: October 1, 2014
This is version 80 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3