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Database: UniProt
Entry: B7MD14_ECO45
LinkDB: B7MD14_ECO45
Original site: B7MD14_ECO45 
ID   B7MD14_ECO45            Unreviewed;       427 AA.
AC   B7MD14;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:CAR01699.1};
DE            EC=3.5.4.1 {ECO:0000313|EMBL:CAR01699.1};
GN   Name=codA {ECO:0000313|EMBL:CAR01699.1};
GN   OrderedLocusNames=ECS88_0348 {ECO:0000313|EMBL:CAR01699.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR01699.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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DR   EMBL; CU928161; CAR01699.1; -; Genomic_DNA.
DR   RefSeq; WP_000069181.1; NC_011742.1.
DR   AlphaFoldDB; B7MD14; -.
DR   KEGG; ecz:ECS88_0348; -.
DR   HOGENOM; CLU_031758_0_1_6; -.
DR   Proteomes; UP000000747; 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:CAR01699.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT   DOMAIN          48..405
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   427 AA;  47576 MW;  86FF130A933A99D7 CRC64;
     MSNNALQTII NAQLPGKEGL WQIHLHDGKI SAIDAQSGVM PVTENSLDAE QGLVLPPFVE
     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
//
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