ID A0A0Q1A5S1_9EURY Unreviewed; 558 AA.
AC A0A0Q1A5S1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=ade {ECO:0000256|HAMAP-Rule:MF_01518};
GN ORFNames=APR53_05270 {ECO:0000313|EMBL:KQC03506.1};
OS Methanoculleus sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1735326 {ECO:0000313|EMBL:KQC03506.1, ECO:0000313|Proteomes:UP000051748};
RN [1] {ECO:0000313|EMBL:KQC03506.1, ECO:0000313|Proteomes:UP000051748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC03506.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) 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:KQC03506.1}.
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DR EMBL; LKUD01000086; KQC03506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q1A5S1; -.
DR STRING; 1735326.APR53_05270; -.
DR Proteomes; UP000051748; 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 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 65..339
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 399..545
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 558 AA; 59256 MW; 356C0DEB85DFD825 CRC64;
MTADALISVA LGERPADLVC HDVSLFNPFS CEWEETSFAV AGGRVAGIGA YEGIREIRFG
GAQCVPGLID AHVHIESSLL TPVEYGRLVL GHGTTTVVAD PHEIANVAGT DGLDYMLAER
KKTPLDILLM LPSCVPATPM DRGGATLTAE DLSAYTDREG ILGLGEMMNV PGVLSGDPGV
AAKMSLCRII DGHAPLLSGH ALNAYIGAGA QSDHECTNLT EAREKLRRGM YIMIREGSTE
RNLRDLIPLI TPATLSRLCF ATDDRHADML VAEGHIDDCI RKAVGYGCEP EHALRMATLS
AAERFGLADR GAVAPGRIAD FCILEDGKEF RVARTFRAGV EFRDPGYTRP ASISRPFSCT
LPVPADLTIT KGGNARVIRL LEHQILTGAE EIGIAPGSIP DTERDILPAV VCDRYRASGF
GIGLVQGLHL KSGAIASSVS HDSHNIVAAG ADTADILKAV GEVIDHKGGM AAVNGDSIAV
LPLPCAGLMS DLPYEEVARR IGALEQAVAG MGGIAHPFMY LSFLALTVIP HRRLTERGVF
DADRFEDISL FSGEDPPP
//