ID A0A1F8MSU0_9CHLR Unreviewed; 569 AA.
AC A0A1F8MSU0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A2Y72_06880 {ECO:0000313|EMBL:OGO01673.1};
OS Chloroflexi bacterium RBG_13_53_26.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797629 {ECO:0000313|EMBL:OGO01673.1, ECO:0000313|Proteomes:UP000180304};
RN [1] {ECO:0000313|EMBL:OGO01673.1, ECO:0000313|Proteomes:UP000180304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO01673.1}.
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DR EMBL; MGMW01000096; OGO01673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MSU0; -.
DR Proteomes; UP000180304; 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|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 67..348
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 398..564
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 569 AA; 60942 MW; 9209201AD8673F06 CRC64;
MNQRNLKELI SVARGQSPAD LLLANARIIN VFSGEIEQGN VAVYGGSIAG IGDYHQGRDI
LDLKGKYLAP GFIDGHTHVE SSLLYITQYA RAVVPHGTTA VVTDLHEVAN VCGLEGARQI
LMACDDLPLD VFFMVPSCVP ATHLETAGAE ITADSVQAAL NWKHALGLGE MMNFPGVINC
DPEVLLKLAF ACGLVIDGHA PGLSGRDLNA YAAAGIRSDH ESTSLEEARE KLNRGMWVMI
REGSSEKNLT ALLPLVTDKT WHRCFFVVDD RSCVDLLADG DIDAVVRKAI QLGLDPIRAI
QMATINPAQY FSLEGLGAIA PGYQADLVVF SDLASLGIEM VFHRGRLVTQ DGHALFNEDS
TPGNALRHTV KMKPFGSEAL RIPADKRHQP VIEIVPGQII TKKNKDEVKV RDSFVVSDVE
RDMLKLAVVE RHKASGNIGL GLVKGFGLKK GALASSVAHD SHNVIAVGAD DGDMFEAIRE
IERLQGGLVV AGEGHILASL PLPIAGLLSD EPLEAVVAKL AYLESVAADL GCTLNSPFST
LSFLALPVIP EIRLTDLGLV DVESYGLLT
//
