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Database: UniProt
Entry: A0A0R1VQZ7_9LACO
LinkDB: A0A0R1VQZ7_9LACO
Original site: A0A0R1VQZ7_9LACO 
ID   A0A0R1VQZ7_9LACO        Unreviewed;       412 AA.
AC   A0A0R1VQZ7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:KRM05219.1};
GN   ORFNames=FC89_GL001689 {ECO:0000313|EMBL:KRM05219.1};
OS   Liquorilactobacillus ghanensis DSM 18630.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM05219.1, ECO:0000313|Proteomes:UP000051451};
RN   [1] {ECO:0000313|EMBL:KRM05219.1, ECO:0000313|Proteomes:UP000051451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM05219.1,
RC   ECO:0000313|Proteomes:UP000051451};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(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:KRM05219.1}.
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DR   EMBL; AZGB01000022; KRM05219.1; -; Genomic_DNA.
DR   RefSeq; WP_057872278.1; NZ_AZGB01000022.1.
DR   AlphaFoldDB; A0A0R1VQZ7; -.
DR   STRING; 1423750.FC89_GL001689; -.
DR   PATRIC; fig|1423750.3.peg.1734; -.
DR   OrthoDB; 9815027at2; -.
DR   Proteomes; UP000051451; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051451}.
FT   DOMAIN          38..399
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   412 AA;  46230 MW;  94E3953A6AD9C5B2 CRC64;
     MLIKNVHVNN EKKITDVRIE NGKFTQILPN LSAKKGEEII DGQRKLLLPP FIDSHIHLDA
     TLTAGQPEWN ETGTLFDGIR IWSERKQSLT IADVKQRARQ TLLRQAGLGI QFVRSHVDTT
     DPQLIALQAL LELKAELKDV IELQLVAFPQ EGILSFPNGK ALLEQALKEG ADVVGGIPHY
     EFNQFYGADS LKYLMGLAEK YNVLVDVHCD EIDDPNSRNL EVLATLAYET GLKQRVTASH
     TTAMGSYNDA YTYKLFRLLK MANLNFVANP LVNIHLGGRF DTYPKRRGLT RVKELSAAGI
     NVSFGEDDVQ DPWNPLGNGN MLDPLQMGVY AAQLMGYQQL QQSFNYITYN AAKTLNIQDH
     YGIELGKPGN CILLNGTDFY QVLNQHAEVL YNIRNGKILA KTIPAKTEIH WK
//
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