ID A0A0U2ZG82_9BACL Unreviewed; 584 AA.
AC A0A0U2ZG82;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Adenine deaminase {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000256|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000256|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000256|ARBA:ARBA00012782, ECO:0000256|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=AUC31_06595 {ECO:0000313|EMBL:ALS74913.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS74913.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS74913.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS74913.1,
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, ECO:0000256|HAMAP-
CC Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000256|ARBA:ARBA00006773,
CC ECO:0000256|HAMAP-Rule:MF_01518}.
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DR EMBL; CP013659; ALS74913.1; -; Genomic_DNA.
DR RefSeq; WP_058381620.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2ZG82; -.
DR STRING; 200991.AUC31_06595; -.
DR KEGG; prt:AUC31_06595; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000067683; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR CDD; cd01295; AdeC; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR HAMAP; MF_01518; Adenine_deamin; 1.
DR InterPro; IPR006679; Adenine_deam.
DR InterPro; IPR026912; Adenine_deam_C.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01178; ade; 1.
DR PANTHER; PTHR11113:SF2; ADENINE DEAMINASE; 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, ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000067683}.
FT DOMAIN 66..344
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 398..565
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 584 AA; 62530 MW; 9BDB10639B1941CF CRC64;
MKKAQLKNRI TAANKEQKAD LVIRHASIVN VFTKTLTTGD VAISDGVIVG IGDYEGSEEI
DATGKFIAPG LIDAHVHIES SMVTPQQFSQ VVLPHGVTTV ITDPHEIANV SGTAGLEFML
KDAQQAMLDI KMMLPSCVPA TPFENAGARL SAEDLMPFVG RDSVLGLAEV MDFPAVLQGD
DAMLDKLLLS RQIDGHAAGL TDNDINVYGT AGILTDHECV TKEEMTARIE RGLYVMLREG
SVAKDLHAVL EGVTEQNAQR CLFCTDDKHL DDLIEEGSVD HNVRTAIRYG INPITAISMA
TLNAAQCFGL HQKGAIAPGY DADFVLLDNL ENFTIAEVYK GGQLAAKDGR YAGSVQEESE
TSTVRETVRI AELSADKLQI PMGTNTSAHV IGINPNKLIT QHLIEEVPVA DGMFVSNPAS
GHLKIAVIER HRATGNIGLG IVKGLGLQNG AIATTVAHDS HNIIEVGTND EDMLAAIRAL
QELQGGLAVV QNGQVLASLS LPIAGLMSDE PFATVYEQLK TIDKSLLQIG APTHFNAFLT
LSFLSLPVIP HLKLTDRGLF DVASFRHISV SVPVHDTIQP SGND
//
