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Database: UniProt
Entry: B5F7J4_SALA4
LinkDB: B5F7J4_SALA4
Original site: B5F7J4_SALA4 
ID   B5F7J4_SALA4            Unreviewed;       426 AA.
AC   B5F7J4;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:ACH48692.1};
DE            EC=3.5.4.1 {ECO:0000313|EMBL:ACH48692.1};
GN   OrderedLocusNames=SeAg_B3525 {ECO:0000313|EMBL:ACH48692.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH48692.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH48692.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH48692.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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DR   EMBL; CP001138; ACH48692.1; -; Genomic_DNA.
DR   RefSeq; WP_001180680.1; NC_011149.1.
DR   AlphaFoldDB; B5F7J4; -.
DR   KEGG; sea:SeAg_B3525; -.
DR   HOGENOM; CLU_031758_0_1_6; -.
DR   OMA; YGLPRVN; -.
DR   Proteomes; UP000008819; Chromosome.
DR   GO; GO:0102480; F:5-fluorocytosine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004131; F:cytosine deaminase activity; IEA:UniProtKB-EC.
DR   CDD; cd01293; Bact_CD; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR32027; CYTOSINE DEAMINASE; 1.
DR   PANTHER; PTHR32027:SF0; CYTOSINE DEAMINASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ACH48692.1}.
FT   DOMAIN          44..404
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   426 AA;  47598 MW;  CD368AE3CDB2D84F CRC64;
     MQNNNITIRQ TRLQGHEGLW QITIENGRFS RIEPQEAASL PQGEVLDAEG GLAIPPFVEP
     HIHLDTTQTA GEPSWNQSGT LFEGIERWAE RKAMLTHEDV KARAMQTLKW QMANGIQYVR
     THVDVSDPTL TALKAMLEVK QEVAPWVDLQ IVAFPQEGIL SYPNGEALLE EAVRLGADVI
     GAIPHFEFTR EYGVESLHKI FALAQKYDRL IDVHCDEIDD EQSRFVETVA ALAHRDGMGA
     RVTASHTTAM HSYNGAYASR LFRLLKMSGI NFVANPLVNI HLQGRFDTYP KRRGVTRVKE
     MLEAGINVCF GHDDVFDPWY PLGTANMLQV LHMGLHVCQL MGYGQINDGL NLITTHSAKT
     LHLQDYGLSV GNAANLVILP AENGFDAVRR QTPARYSIRH GRVIAETVPS QTTLHLTQPE
     AVTFKR
//
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