ID A0A0G1DES7_9BACT Unreviewed; 541 AA.
AC A0A0G1DES7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=UV73_C0012G0120 {ECO:0000313|EMBL:KKS96092.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS96092.1, ECO:0000313|Proteomes:UP000034894};
RN [1] {ECO:0000313|EMBL:KKS96092.1, ECO:0000313|Proteomes:UP000034894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS96092.1}.
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DR EMBL; LCFP01000012; KKS96092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1DES7; -.
DR STRING; 1618443.UV73_C0012G0120; -.
DR PATRIC; fig|1618443.3.peg.1445; -.
DR Proteomes; UP000034894; 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 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, ECO:0000313|EMBL:KKS96092.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518}.
FT DOMAIN 41..321
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 369..534
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 541 AA; 58721 MW; 12F2B3341E75CFC0 CRC64;
MEKISGNIVD LIGFRIYPGT LVISGGRIKD IIPGKRKYRE FILPGFVDAH IHIESSMLPP
AEFARLAVAH GTVATVSDPH EIGNVLGVAG VEYMIREGKR VPFKFYFGAP SCVPATSFET
SGSEIIPGDV DRLMKRAEIK YLSEVMNYPG VIARDKDFMA KIKSSLDKGK PVDGHAPGLR
GGLLKKYASA GISTDHESFE YKEGLEKIKL GMKLIIREGS AAKNFEALIP LLDLYPDSCM
FGSDDKHPDD LARGHINLLV ERALKKGINV FKVLRAASLN PVKHYKLAVG LLQKNDPADF
IITANLDDLN ILATVIDGQQ VAAKGKSLIP AKKAALVNKF AALQITLKDL AVRQKTGKMR
VMAALDKQLV TGKLTVKPAA GLNGFVAADP LRDILKIAVV NRYKKALPSV GFIKNFGLKK
GAIASSVAHD SHNVVAVGAN DEDLLLSINS ILGIKGGLSV VYKNKVTLLE LPIGGLMSGR
DGYEVARKYE ELDRLAKKLG SRLTSPFMTL SFMALPVIPS LKITDKGLFD VDKFRPVDLF
I
//
