ID   A7ZI84_ECO24            Unreviewed;       427 AA.
AC   A7ZI84;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:ABV17899.1};
DE            EC=3.5.4.1 {ECO:0000313|EMBL:ABV17899.1};
GN   Name=codA {ECO:0000313|EMBL:ABV17899.1};
GN   OrderedLocusNames=EcE24377A_0361 {ECO:0000313|EMBL:ABV17899.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV17899.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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DR   EMBL; CP000800; ABV17899.1; -; Genomic_DNA.
DR   RefSeq; WP_001295686.1; NC_009801.1.
DR   AlphaFoldDB; A7ZI84; -.
DR   KEGG; ecw:EcE24377A_0361; -.
DR   HOGENOM; CLU_031758_0_1_6; -.
DR   Proteomes; UP000001122; 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:ABV17899.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122}.
FT   DOMAIN          48..405
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   427 AA;  47610 MW;  0878AC3F6CDB0BAD CRC64;
     MSNNALQTII NARLPGEEGL WQIHLQDGKI SAIDAQSGVM PITENSLDAE QGLVIPPFVE
     PHIHLDTTQT AGQPNWNQSG TLFEGIERWA ERKALLTHDD VKQRAWQTLK WQIANGIQHV
     RTHVDVSDAT LTALKAMLEV KQEVAPWIDL QIVAFPQEGI LSYPNGEALL EEALRLGADV
     VGAIPHFEFT REYGVESLHK TFALAQKYDR LIDVHCDEID DEQSRFVETV AALAHREGMG
     ARVTASHTTA MHSYNGAYTS RLFRLLKMSG INFVANPLVN IHLQGRFDTY PKRRGITRVK
     EMLESGINVC FGHDDVFDPW YPLGTANMLQ VLHMGLHVCQ LMGYGQINDG LNLITHHSAR
     TLNLQDYGIA AGNSANLIIL PAENGFDALR RQVPVRYSVR GGKVIASTQP AQTTVYLEQP
     EAIDYKR
//