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Database: UniProt
Entry: A0A127K1Q7_9BURK
LinkDB: A0A127K1Q7_9BURK
Original site: A0A127K1Q7_9BURK 
ID   A0A127K1Q7_9BURK        Unreviewed;       416 AA.
AC   A0A127K1Q7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:AMO25142.1};
DE            EC=3.5.4.1 {ECO:0000313|EMBL:AMO25142.1};
GN   ORFNames=UC35_22815 {ECO:0000313|EMBL:AMO25142.1};
OS   Ramlibacter tataouinensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO25142.1, ECO:0000313|Proteomes:UP000070433};
RN   [1] {ECO:0000313|EMBL:AMO25142.1, ECO:0000313|Proteomes:UP000070433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-10 {ECO:0000313|EMBL:AMO25142.1,
RC   ECO:0000313|Proteomes:UP000070433};
RX   PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA   Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT   "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT   description of the genus Ramlibacter.";
RL   Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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DR   EMBL; CP010951; AMO25142.1; -; Genomic_DNA.
DR   RefSeq; WP_061503583.1; NZ_CP010951.1.
DR   AlphaFoldDB; A0A127K1Q7; -.
DR   PATRIC; fig|94132.3.peg.4648; -.
DR   OrthoDB; 9815027at2; -.
DR   Proteomes; UP000070433; 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:AMO25142.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070433}.
FT   DOMAIN          40..397
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   416 AA;  45041 MW;  2B766D31CAD8D010 CRC64;
     MLDLLITQAS LPDGRTDMSV AVQGGKIVEV REGLSAPARE TVEARGMLLS PPFCDAHFHM
     DSALTYGRPR VNESGTLLEG IALWGELKPT LAQDDIIGRA LTYCEWAVAQ GLLAIRSHVD
     TSDPRLLAVE ALLEVKRRVA GCIDLQLVAF PQDGVLRSPG GLANIERALD MGVDVVGGIP
     HFERTMGEGA ASVRLLCELA ARRGKPVDMH CDETDDPLSR HIETLAFETQ RLGLQGRVTG
     SHCTSMHSMD NAYASKLLAL VAESGVAVIA NPLINITLQG RHDSYPKRRG MTRVPELMQA
     GVTVAFGHDC VMDPWYAMGS GDMLDVAHMG LHVAQMTSQA GMRACFEAVT GNAAKIMQLP
     GYGLAPGCDA SFVLLQARDA VEAIRLRARR LKVWRQGSLL GEMPETAFHR QVEFRA
//
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