ID C4GHU5_9NEIS Unreviewed; 265 AA.
AC C4GHU5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative cytidine deaminase {ECO:0000313|EMBL:EEP68533.1};
GN ORFNames=GCWU000324_00433 {ECO:0000313|EMBL:EEP68533.1};
OS Kingella oralis ATCC 51147.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=629741 {ECO:0000313|EMBL:EEP68533.1, ECO:0000313|Proteomes:UP000003009};
RN [1] {ECO:0000313|EMBL:EEP68533.1, ECO:0000313|Proteomes:UP000003009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51147 {ECO:0000313|EMBL:EEP68533.1,
RC ECO:0000313|Proteomes:UP000003009};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006334-3};
CC Note=Binds 1 zinc ion. {ECO:0000256|PIRSR:PIRSR006334-3};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000256|ARBA:ARBA00006576}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEP68533.1}.
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DR EMBL; ACJW02000002; EEP68533.1; -; Genomic_DNA.
DR RefSeq; WP_003793807.1; NZ_GG665871.1.
DR AlphaFoldDB; C4GHU5; -.
DR STRING; 629741.GCWU000324_00433; -.
DR GeneID; 84907164; -.
DR HOGENOM; CLU_052424_0_0_4; -.
DR OrthoDB; 9795347at2; -.
DR Proteomes; UP000003009; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004126; F:cytidine deaminase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01283; cytidine_deaminase; 2.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 2.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR013171; Cyd/dCyd_deaminase_Zn-bd.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR PANTHER; PTHR11644; CYTIDINE DEAMINASE; 1.
DR PANTHER; PTHR11644:SF2; CYTIDINE DEAMINASE; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF08211; dCMP_cyt_deam_2; 1.
DR PIRSF; PIRSF006334; Cdd_plus_pseudo; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006334-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000003009};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006334-3}.
FT DOMAIN 20..140
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT DOMAIN 160..265
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 76
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-1"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-2"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006334-3"
SQ SEQUENCE 265 AA; 28732 MW; A39F84DE68D21EBC CRC64;
MLSFIPKHEV QTRAAAFNGD KIALALSLLP EAAKLAVVPV SQFHVGAIAI DGEGNFYFGA
NQECATASMG QTVHAEQSAV SHAWQRGATR ITDIVVNYTP CGHCRQFLNE LPDAGSLKIH
LPHSHDNTLN SYLPDSFSPK DLNIPERLLT PVQHAIRQPE NLDAAQQAAF AAAQTCHAPY
SRAYAGIALV AGNEIYTGRY AENAAYNPTL PPLQVAINLL RMSGHDTSEV TRAVLCCTRH
GGHEAMTRAL WNEIGACKLE IVWLD
//
