ID A0A0Q8BCG3_9BURK Unreviewed; 396 AA.
AC A0A0Q8BCG3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Cytosine deaminase {ECO:0000313|EMBL:KQZ99154.1};
GN ORFNames=ASD71_19910 {ECO:0000313|EMBL:KQZ99154.1};
OS Achromobacter sp. Root565.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1736564 {ECO:0000313|EMBL:KQZ99154.1, ECO:0000313|Proteomes:UP000052040};
RN [1] {ECO:0000313|EMBL:KQZ99154.1, ECO:0000313|Proteomes:UP000052040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root565 {ECO:0000313|EMBL:KQZ99154.1,
RC ECO:0000313|Proteomes:UP000052040};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ99154.1, ECO:0000313|Proteomes:UP000052040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root565 {ECO:0000313|EMBL:KQZ99154.1,
RC ECO:0000313|Proteomes:UP000052040};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQZ99154.1}.
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DR EMBL; LMGO01000005; KQZ99154.1; -; Genomic_DNA.
DR RefSeq; WP_056568603.1; NZ_LMGO01000005.1.
DR AlphaFoldDB; A0A0Q8BCG3; -.
DR Proteomes; UP000052040; 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:SF9; BLL3847 PROTEIN; 1.
DR PANTHER; PTHR32027; 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 41..387
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 396 AA; 41774 MW; 0E8550AB89F79263 CRC64;
MADLLLKNVR TAKGEGVDVL VRGGRILRIG PGLDADPGIA VEDGGGALLL PALIEGHTHL
DKTTWGSAWY VNQVGPSLTD RIDNERNWRA ATGHDAASHA HALALAFLRA GTTRIRTHVD
VDTDAGLKHL EGVHATRQAL AGRVEIQTVA FPQSGLLARA GTAELLDQAL AGGADVLGGL
DPSAIDRDPV TSLDVLFGLA DKHGKPLDIH LHEPGELGAF TLELILDRVQ ALDMKGKVVI
SHAFCLGALD AARLNGLLRR LALLDVALLT TAPASRPVPA VRACREAAVT LFGGNDGIRD
TWTPYGSPDM LERAALIGLR NDLRRDDEIE WAFECVTRAA ARACGFADYG LVPGARADLV
LADASCVAQA VVQRTPRRLV VSSGVVVARN GEDAIA
//