ID   YLXG_ALIFS              Reviewed;         147 AA.
AC   P33968;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Uncharacterized deaminase in luxG 3'region;
DE            EC=3.5.-.-;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7744 / DSM 507 / NCIMB 1281 / 398;
RX   PubMed=8329441; DOI=10.1016/0005-2728(93)90206-u;
RA   Lee C.Y., Szittner R.B., Miyamoto C.M., Meighen E.A.;
RT   "The gene convergent to luxG in Vibrio fischeri codes for a protein related
RT   in sequence to RibG and deoxycytidylate deaminase.";
RL   Biochim. Biophys. Acta 1143:337-339(1993).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000305}.
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DR   EMBL; X70289; CAA49769.1; -; Genomic_DNA.
DR   AlphaFoldDB; P33968; -.
DR   SMR; P33968; -.
DR   GO; GO:0004132; F:dCMP deaminase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:InterPro.
DR   CDD; cd01286; deoxycytidylate_deaminase; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR016473; dCMP_deaminase.
DR   InterPro; IPR015517; dCMP_deaminase-rel.
DR   InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR   PANTHER; PTHR11086; PTHR11086; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   PIRSF; PIRSF006019; dCMP_deaminase; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..147
FT                   /note="Uncharacterized deaminase in luxG 3'region"
FT                   /id="PRO_0000171711"
FT   DOMAIN          4..120
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        69
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   147 AA;  16622 MW;  174FDA8DC1458D49 CRC64;
     MISKWAKRFF QMAELVGSWS KDPSTQVGAV ITKHNRIVSV GFNGYPHGVS DSADTDEREI
     KYLKTLHAEE NAILFAKRDL EGCDIWVTHF PCPNCAAKII QTGISKVYCP EQTEDFLSRW
     GEKIQVSQDM FSQAGVEVTW LPLDILK