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Database: UniProt
Entry: A0A162FCQ2_9EURY
LinkDB: A0A162FCQ2_9EURY
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ID   A0A162FCQ2_9EURY        Unreviewed;       602 AA.
AC   A0A162FCQ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=adeC {ECO:0000313|EMBL:KZX11085.1};
GN   Synonyms=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN   ORFNames=MBCUR_15650 {ECO:0000313|EMBL:KZX11085.1};
OS   Methanobrevibacter curvatus.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=49547 {ECO:0000313|EMBL:KZX11085.1, ECO:0000313|Proteomes:UP000077245};
RN   [1] {ECO:0000313|EMBL:KZX11085.1, ECO:0000313|Proteomes:UP000077245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11111 {ECO:0000313|EMBL:KZX11085.1,
RC   ECO:0000313|Proteomes:UP000077245};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanobrevibacter curvatus DSM 11111.";
RL   Submitted (APR-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}.
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:KZX11085.1}.
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DR   EMBL; LWMV01000195; KZX11085.1; -; Genomic_DNA.
DR   RefSeq; WP_067092292.1; NZ_LWMV01000195.1.
DR   AlphaFoldDB; A0A162FCQ2; -.
DR   STRING; 49547.MBCUR_15650; -.
DR   PATRIC; fig|49547.3.peg.1672; -.
DR   OrthoDB; 24954at2157; -.
DR   Proteomes; UP000077245; Unassembled WGS sequence.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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|HAMAP-Rule:MF_01518, ECO:0000313|EMBL:KZX11085.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077245}.
FT   DOMAIN          47..372
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          425..596
FT                   /note="Adenine deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13382"
SQ   SEQUENCE   602 AA;  67154 MW;  9AB6B24B9C7D3281 CRC64;
     MKLKNFKARI LDFNLNEVVP VEVKIENGFF SEIKRISEDE LLDFNGIILP GFIDSHIHIE
     SSLLTPSLFC EAVLPFGTTS VVCDPHEIAS VLGMDGINFM VENGKNAPFD FYFTAPSSVP
     ATNFDKSGAT IDSNDIDELL KREEFVALAE MMNFNGVINK NWEVMAKLKS AKKHFKPIDG
     HCPELSGEDL KKYIYFDGFD EKHLEDDSDL SKPNLKSSYI STEHESSSFK EAIEKKALNM
     KIMVRDGSSA KNMQAILNFN ERLEFLKTQD FFGHISSEDF QKILKNPIFD FIVSDDKEPT
     DLIKGHLNLS LKKAIDLGID TIEAIKMVSL NPSNHYNLNS GEIALGKIAN FIEVDSLENL
     NVLKTYVHGE LVAKNGKSLY NGKRPQIINN FNVSRRLSKD FDIYIGDKNL KTVNVNVIGL
     NEGKLITDKL NCNLNLENNI IQPNLNEDVL KISVINRYLD NEKNNLSSIG NGFVKGFNLK
     NGAIATSVSH DSHNLIVVGV NSNLMAKAAN LVIENKGAIV AVSENEEIIL PLPIAGLMSD
     KKIDEVADKL NSLNLFVKSC GSKFEYPFMN LSFLALLVIP HLKINSSGLF DADNFQFIDL
     IN
//
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