ID A0A0K1F2E1_9ACTN Unreviewed; 608 AA.
AC A0A0K1F2E1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ADJ70_06720 {ECO:0000313|EMBL:AKT48705.1};
OS Olsenella sp. oral taxon 807.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=712411 {ECO:0000313|EMBL:AKT48705.1, ECO:0000313|Proteomes:UP000059853};
RN [1] {ECO:0000313|Proteomes:UP000059853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0089 {ECO:0000313|Proteomes:UP000059853};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (AUG-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}.
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DR EMBL; CP012069; AKT48705.1; -; Genomic_DNA.
DR RefSeq; WP_050342243.1; NZ_CP012069.2.
DR AlphaFoldDB; A0A0K1F2E1; -.
DR STRING; 712411.ADJ70_06720; -.
DR KEGG; olo:ADJ70_06720; -.
DR PATRIC; fig|712411.3.peg.3059; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000059853; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
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 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 85..372
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 431..597
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 608 AA; 65180 MW; B012AA8D0409E5C0 CRC64;
MINRFCKMPL WECNDTLVRV AQGQQPAELV IKDAHLVSVD TRELLEHADI AIACGRIAYL
GIGGHSAAHC IGKTTEVVDA NGLFAAPGLL DSHIHIESSM VGPSEYARAV VPHGTVGIYA
DPHEVANVCG LDGVRAMWED AARTPLKTML TTPSCVPAVT DVEDTGASID AAQIAESMTW
PETCALGEMM NFPGILACEK NALDEVRETL KTDRVVTGHY VTPDIDRGLA AYIASGASCC
HESGSVADVL AKLRMGMYAQ LRQGSAWLNL PGYLPQLIES GVDMHHCLLC TDDSHPHTIV
SDGHMDRVVR DAVALGLDAV VALQLATINV AEYFGVGRDM GSIAPGKCAD IVLFEDLRDF
RAVRVWIDGS QVAERGQALF DVRPFAWPTF MTSTMNLGGQ LCPQSFEFRE GEGRPDGSCQ
VRAMAVSGGD TITQDSVVEV PVRGGKLMAD PDHDILKVCV FDRHHADAGT FSHGFATGFG
IHGALAQTVS HDAHNLLVMG DNDADMLLAA RTLEACGGGE VAVQDGKVLA LVELPVCGLM
SDGRVEVVSE KVSRIEEAWR TMGCRLPSPF MTMGVMSLAC IPVLRQTNRG YVNCVSFQTE
PLIVEETA
//
