ID ADEC_METMJ Reviewed; 518 AA.
AC A3CVR8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=Memar_1539;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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:0000255|HAMAP-Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR EMBL; CP000562; ABN57468.1; -; Genomic_DNA.
DR AlphaFoldDB; A3CVR8; -.
DR SMR; A3CVR8; -.
DR STRING; 368407.Memar_1539; -.
DR KEGG; mem:Memar_1539; -.
DR eggNOG; arCOG00693; Archaea.
DR HOGENOM; CLU_027935_0_0_2; -.
DR Proteomes; UP000002146; 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; Manganese.
FT CHAIN 1..518
FT /note="Adenine deaminase"
FT /id="PRO_0000292403"
SQ SEQUENCE 518 AA; 55311 MW; 1B35F0DA990B03CB CRC64;
MDFGVKDGRI IGFGEYRGTR EYDLSGAYVV PGLIDAHVHI ESSLLAPAEY ARLVLAHGTT
TVIADPHEIA NVCGAPGIDY MLAQGARTPL DILVMLPSCV PATPFDAGGA VLTAADLARF
RGREGVVGLA EVMNVPGVLF GDEDLRAKMD LFEVVDGHAP FLSGKDLNAY IYAGVQSDHE
CTALPEAREK LLRGMYVMIR EGSTERNLHD LLPLVDACTA PRCCFATDDR HADMLAGEGH
IDDCVRKAVS GGLEVEQALR MATLSAAGRF GLHDRGALAP GRLADFCVAD DPDRFRVLRT
FKRGVEVVDA GYLPPACPKS PMHARVPEPG DIRITGRGEA RVIEIVPGQI TTRDLRYPVD
AAGIPDLDRD ILKAVVIDRY RATGSGVGLV HGFHLQEGAI AGSVSHDSHN IVAVGAGDAD
IVRAVAEVVR LGGGLAVVSG DDITALPLEC AGLMSALPYD EVVRRLAALE EHARRLGAIA
NPFMYLSFLA LTVIPEVRVT ERGVFDVGAF TDVPLFEE
//
