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
//