CDD_KLEP7
ID CDD_KLEP7 Reviewed; 294 AA.
AC A6TBN1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=KPN78578_25410; ORFNames=KPN_02584;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000647; ABR78002.1; -; Genomic_DNA.
DR RefSeq; WP_002912869.1; NC_009648.1.
DR PDB; 6K63; X-ray; 2.07 A; A/B/C/D=1-294.
DR PDBsum; 6K63; -.
DR AlphaFoldDB; A6TBN1; -.
DR SMR; A6TBN1; -.
DR STRING; 272620.KPN_02584; -.
DR jPOST; A6TBN1; -.
DR EnsemblBacteria; ABR78002; ABR78002; KPN_02584.
DR KEGG; kpn:KPN_02584; -.
DR HOGENOM; CLU_052424_0_0_6; -.
DR OMA; NYSPCGH; -.
DR BRENDA; 3.5.4.5; 2817.
DR Proteomes; UP000000265; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..294
FT /note="Cytidine deaminase"
FT /id="PRO_1000068957"
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"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:6K63"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:6K63"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:6K63"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:6K63"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:6K63"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:6K63"
SQ SEQUENCE 294 AA; 31477 MW; F19BB2A84665249A CRC64;
MHSRFQAALT TLAADLQAAI APMLADPHFP ALLEADQVAT LQHATGLDED ALAFALLPLA
AACARPDLSH FNVGAIARGV SGRWYFGGNM EFLGATMQQT VHAEQSAISH AWLRGETSLR
AITVNYTPCG HCRQFMNELN SGLALRIHLP GREAHALEHY LPDAFGPKDL EIKTLLMDEQ
DHGFPVSGDA LTQAAIQAAN RCHAPYSHSP SGVALELKDG TIFSGSYAEN AAFNPTLPPL
QGALNLLSLN GYDYPAIQRA ILAEKADAAL IQWDATVATL KALGCHNIER VLLG
