ID Q64D09_9ARCH Unreviewed; 571 AA.
AC Q64D09;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:AAU82718.1};
GN Synonyms=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=GZ19C7_14 {ECO:0000313|EMBL:AAU82718.1};
OS uncultured archaeon GZfos19C7.
OC Archaea; environmental samples.
OX NCBI_TaxID=285365 {ECO:0000313|EMBL:AAU82718.1};
RN [1] {ECO:0000313|EMBL:AAU82718.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15353801; DOI=10.1126/science.1100025;
RA Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA Richardson P.M., DeLong E.F.;
RT "Reverse methanogenesis: testing the hypothesis with environmental
RT genomics.";
RL Science 305:1457-1462(2004).
RN [2] {ECO:0000313|EMBL:AAU82718.1}
RP NUCLEOTIDE SEQUENCE.
RA Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL Submitted (AUG-2004) 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; AY714830; AAU82718.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64D09; -.
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|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 64..351
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 412..565
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 571 AA; 61935 MW; 3AE753243814C4D8 CRC64;
MNTIDLLDVA LGTEKAELVI KNANLVSVCS GEIYETDIAI ADGIVAGLGR YEGRSEIEAK
DKYAVPGLID GHTHIEMCML SVAEFARAVV PRGTTTVVAD PHEIANVLGI EGIRAILEEA
KATPLNVFCM APSCVPSTDP ELGLETSGAR IGAEEIKQLL QLEEVIGLAE VMNYGGVIAK
EEEVWTKIEV AKALKMPIDG HAPLVSGKEL NAYVLSSVGS DHESVSYEEA HEKLRLGMRV
MVREGSVAKN LKNIAPKLKS ADTRNCMLVT DGDRTPLDLQ KEGYLDHVFR RAIEEGIDPL
NAVQMCTINP ARWFKLDNFL GCVAPGKIAD IVLLNNLERF DVEKVVVNGT ILTDFGPRSG
HNYRYPEYGT TVRIKPVKSE DFELKLNSEE GTRKARIIGL IEGELLTEEL VEGISGIDIA
RDILKIAVVE RHHYTGNIGL GFVKGFGLKT GAVASSIAHD SHNIVVIGTN EADMACACNR
LKEIGGGIVL CSGREVMSEL KLPIAGLMTD KGLAYVVRNQ KELEAGITAM GCKLQAPFIS
MSFLALPVIP KLKITDKGLV DVEKRRIVDI F
//
