位置:首页 > 蛋白库 > CDD_SHIDS
CDD_SHIDS
ID   CDD_SHIDS               Reviewed;         294 AA.
AC   Q32EM3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cytidine deaminase {ECO:0000255|HAMAP-Rule:MF_01558};
DE            EC=3.5.4.5 {ECO:0000255|HAMAP-Rule:MF_01558};
DE   AltName: Full=Cytidine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01558};
DE            Short=CDA {ECO:0000255|HAMAP-Rule:MF_01558};
GN   Name=cdd {ECO:0000255|HAMAP-Rule:MF_01558}; OrderedLocusNames=SDY_2144;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC       2'-deoxycytidine for UMP synthesis. {ECO:0000255|HAMAP-Rule:MF_01558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC         Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01558};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC         Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01558};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01558};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_01558};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01558}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01558}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000034; ABB62232.1; -; Genomic_DNA.
DR   RefSeq; WP_000553543.1; NC_007606.1.
DR   RefSeq; YP_403723.1; NC_007606.1.
DR   AlphaFoldDB; Q32EM3; -.
DR   SMR; Q32EM3; -.
DR   STRING; 300267.SDY_2144; -.
DR   EnsemblBacteria; ABB62232; ABB62232; SDY_2144.
DR   KEGG; sdy:SDY_2144; -.
DR   PATRIC; fig|300267.13.peg.2591; -.
DR   HOGENOM; CLU_052424_0_0_6; -.
DR   OMA; NYSPCGH; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01558; Cyt_deam; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd.
DR   InterPro; IPR006263; Cyt_deam_dimer.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR020797; Cytidine_deaminase_bacteria.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   Pfam; PF08211; dCMP_cyt_deam_2; 1.
DR   SUPFAM; SSF53927; SSF53927; 2.
DR   TIGRFAMs; TIGR01355; cyt_deam_dimer; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..294
FT                   /note="Cytidine deaminase"
FT                   /id="PRO_0000171666"
FT   DOMAIN          48..168
FT                   /note="CMP/dCMP-type deaminase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   DOMAIN          186..294
FT                   /note="CMP/dCMP-type deaminase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01558"
FT   BINDING         89..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01558"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01558"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01558"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01558"
SQ   SEQUENCE   294 AA;  31497 MW;  6E019C2DBF41C224 CRC64;
     MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA
     AACALTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA
     AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LPDAFGPKDL EIKTLLMDEQ
     DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL
     QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHSIDR VLLA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024