ID A0A0U2P9X7_9BACL Unreviewed; 579 AA.
AC A0A0U2P9X7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=adenine deaminase {ECO:0000256|ARBA:ARBA00012782};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782};
GN ORFNames=AUC31_05405 {ECO:0000313|EMBL:ALS74695.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS74695.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS74695.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS74695.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenine + H(+) + H2O = hypoxanthine + NH4(+);
CC Xref=Rhea:RHEA:23688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17368, ChEBI:CHEBI:28938; EC=3.5.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000479};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773}.
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DR EMBL; CP013659; ALS74695.1; -; Genomic_DNA.
DR RefSeq; WP_058381402.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2P9X7; -.
DR STRING; 200991.AUC31_05405; -.
DR KEGG; prt:AUC31_05405; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000067683; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR026912; Adenine_deam_C.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF6; ADENINE DEAMINASE YERA-RELATED; 1.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000067683}.
FT DOMAIN 76..357
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 406..567
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 579 AA; 65316 MW; C9E42220C9384190 CRC64;
MVNPLWRNTE IRKQLKIVSK ELSPDLVLTN ATYLHGIFKK WMTGNIWING DRIIYAGQDM
PKIDDSTEVV DVSDKWIVPG YIEPHVHPYQ LYNPQQFADY AAQGGTTGFI SDNLPLFLSL
ENEKAFTLLD RMAELPFTFY WWTRFDSQTE LVGEDQKFTS KAVGEWLERP DVILGGELTG
WPKLLAGDDQ MLYWIQKAKI SLKKIEGHFP GASEKTLARM KLLGADGDHE AMTVDEVEMR
LLHGYGVTLR HSSIRPDLPQ LLSGIVEREL NVFDKLMMTT DGSTPVFHKD GVMDLCIQIA
LDAGVPAIDA YMMASYNVAR YYNLTSLHGL IATGRYANLN ILDSIDNPVP SGVISKGGWL
KRDGQKVRSL DDVDWSVLPE LNLDFELTDD DFQFSMPFGV DMVNDVITKP YSVSVDTNVE
RLSKEHGESF LMLIDRNGKW RVNTLIKGFA TEVDGFASSY TNTGDIVLIG KSRQDMWQAF
ERVKRLKGGI VLIEDGEIVC ELPLPIGGIM SDLPMEPLME QETALKSALK ERGYEHGDAV
YTLLFLMATH LPYVRITQKG IYDVMNKTIL FPAFMRGQG
//
