ID Q64AN1_9ARCH Unreviewed; 568 AA.
AC Q64AN1;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AAU83546.1};
GN Synonyms=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=GZ30H9_33 {ECO:0000313|EMBL:AAU83546.1};
OS uncultured archaeon GZfos30H9.
OC Archaea; environmental samples.
OX NCBI_TaxID=285372 {ECO:0000313|EMBL:AAU83546.1};
RN [1] {ECO:0000313|EMBL:AAU83546.1}
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:AAU83546.1}
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; AY714852; AAU83546.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64AN1; -.
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 65..351
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 413..561
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 568 AA; 62160 MW; 182260FF0D5B4F01 CRC64;
MTKMNDLVDI ALGNKKADLV LKNVNLVNVC SGEIYETDIA IAHDVIAGLG RYEGRLEIDA
QDNYAVPGLI DGHTHIEMSM LSVREFAKAV VPRGTTAVVA DPHEIANVLG IAGIRALLDD
ARTTALKVFC MAPSCVPSTD PSLGLETSGA MIDHTEIRKL LRMDGIIGLA EVMNYVGVIA
KEEEVWEKIE IAKALKMPID GHAPLLSGKE LNAYVVSGAG SDHENTTYEE SEEKLRLGMR
VMVREGSVAK NLKNIAPLLR TVDTRNCMLV TDGDRTPLDL KDEGYLDYVL RRAIEEGIDP
VKAVQMCTIN PAQWFKLDAE IGCIAPGKIA DIVLLKKLDT FEVEKVIVNG KPDFAQRSEY
SFNYPHYRES VRIMRVKPDE FVIEQEGAIK ARIIGLIEGE LQTEELVEEI SGIEIARDIL
EICVLERHHY SGNMGLGFVK GFGLKTGAIA STIAHDSHNI VVIGTNEEDM AVACNRLKDI
GGGIVLCNGE EVTSELKLPI AGLMSDNGLD YVMRKQKEMD DNISEMGCKL PAPFIAISFL
ALPVIPKLKI TDKGLVDVAK REIVGVFL
//
