ID   A0A1E4IZH7_9BURK        Unreviewed;       426 AA.
AC   A0A1E4IZH7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:ODU15556.1};
GN   ORFNames=ABS94_18070 {ECO:0000313|EMBL:ODU15556.1};
OS   Variovorax sp. SCN 67-85.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU15556.1, ECO:0000313|Proteomes:UP000094461};
RN   [1] {ECO:0000313|EMBL:ODU15556.1, ECO:0000313|Proteomes:UP000094461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODU15556.1}.
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DR   EMBL; MEFM01000022; ODU15556.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4IZH7; -.
DR   Proteomes; UP000094461; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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          42..382
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   426 AA;  46014 MW;  21F1DE680EE1A3B9 CRC64;
     MLDLLITNAT LPDGRTGMSI AVQDGRIAEV AEGLDAPAHE KLDAQGMLLS PHFVDPHFHM
     DATLSYGLPR VNQSGTLLEG IALWGELKPL LTAEALIERA LAYCDWAVAK GLLAVRSHVD
     TSDPSLLAVD ALLEVKRKVA PYLDLQLVAF PQDGVLRSPG GVENLERALD KGVDVVGGIP
     HFERTMADGA ASVKLLCEMA AERGKLVDMH CDESDDPLSR HIETLAFEAQ RLGMHGRVTG
     SHCTSMHSMD NYYVSKLLPL IAQSGVAVIS NPLINITLQG RHDTYPKRRG MTRVPELMAA
     GVNVAFGHDC VMDPWYGMGS GDMLEVAHMG LHVAQMTSQA GIRQCFEAVT TNAARVMHLQ
     GYGIEAGCDA SFVLLQARDP VEAIRLRATR LKVFRKGRLL AQTPAATATL HLPGRAGETG
     WMIPKA
//