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Database: UniProt
Entry: C3TN17_ECOLX
LinkDB: C3TN17_ECOLX
Original site: C3TN17_ECOLX 
ID   C3TN17_ECOLX            Unreviewed;       427 AA.
AC   C3TN17;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:ACI70669.1};
GN   ORFNames=ECs0390 {ECO:0000313|EMBL:ACI70669.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ACI70669.1};
RN   [1] {ECO:0000313|EMBL:ACI70669.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=493/89 {ECO:0000313|EMBL:ACI70669.1}, and TB182A
RC   {ECO:0000313|EMBL:ACI70672.1};
RX   PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA   Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA   Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA   Sawyer S.A., Whittam T.S., Tarr P.I.;
RT   "A precise reconstruction of the emergence and constrained radiations of
RT   Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
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DR   EMBL; EU905555; ACI70669.1; -; Genomic_DNA.
DR   EMBL; EU905558; ACI70672.1; -; Genomic_DNA.
DR   RefSeq; WP_001358763.1; NZ_UGDO01000002.1.
DR   AlphaFoldDB; C3TN17; -.
DR   PATRIC; fig|562.7216.peg.1152; -.
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;
FT   DOMAIN          48..405
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   427 AA;  47639 MW;  759FBB780C65D814 CRC64;
     MSNNALQTII NARLPGKEGL 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
     TLNLQDYSIA AGNSANLIIL PAENGFDALR RQVPVRYSVR GGKVIASTQP AQTTVYLEQP
     EAIDYKR
//
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