ID Q64CB5_9ARCH Unreviewed; 565 AA.
AC Q64CB5;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:AAU82962.1};
GN Synonyms=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=GZ24D9_5 {ECO:0000313|EMBL:AAU82962.1};
OS uncultured archaeon GZfos24D9.
OC Archaea; environmental samples.
OX NCBI_TaxID=285390 {ECO:0000313|EMBL:AAU82962.1};
RN [1] {ECO:0000313|EMBL:AAU82962.1}
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:AAU82962.1}
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; AY714837; AAU82962.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64CB5; -.
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 62..348
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 410..558
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 565 AA; 61607 MW; AE28BB019440261D CRC64;
MNDLVDFASG DKKADLVLKN ANLVNVCSGE IYKTDIAIAH GLIVGLGRYE GRVEIDAQDN
YAVPGLIDGH THIEMSMLSV REFAKAVVPR GTTAVVADPH EIANVLGIAG IRALLDDART
TALKVFCMAP SCVPSTDPSL GLETSGATID HTEIRKLLQM DGIIGLAEVM NYVGVIAKEK
EVWEKIEIAK ALKMPIDGHA PLLSGKELNA YVVSGAGSDH ENTTYEESQE KLRLGMRVMV
REGSVAKNLK KIAPLLRTVD TRNCMLVTDG DRTPLDLKDE GYLDYVLRRA IEEGIDPVKA
VQMCTINPAQ WFKLDAEIGC IAPGKIADIV LLKDLDTFEV EKVIVNGKPD FAQRSEYSFN
YPQYRESVRI MRVKPDEFVI EQEGAIKARI IGLIEGELLT EELVEEISGI EIARDILEIG
VLERHHYSGN MGLGFVKGFG LKTGAIASTI AHDSHNIVVI GTNEEDMALA CNRLKDIGGG
IVLCNGKEVT SELKLPIAGL MSDNGLDYVM RKQKEMDDNI SVMGCKLPAP FVAMSFLALP
VIPKLKITDK GLVDVAKREI VGVFL
//
