ID A0A0S7XF20_9BACT Unreviewed; 569 AA.
AC A0A0S7XF20;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AMJ46_04960 {ECO:0000313|EMBL:KPJ60815.1};
OS Latescibacteria bacterium DG_63.
OC Bacteria; Candidatus Latescibacteria.
OX NCBI_TaxID=1703781 {ECO:0000313|EMBL:KPJ60815.1, ECO:0000313|Proteomes:UP000051457};
RN [1] {ECO:0000313|EMBL:KPJ60815.1, ECO:0000313|Proteomes:UP000051457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_63 {ECO:0000313|EMBL:KPJ60815.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPJ60815.1}.
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DR EMBL; LJNC01000007; KPJ60815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XF20; -.
DR PATRIC; fig|1703781.3.peg.3052; -.
DR Proteomes; UP000051457; 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 63..344
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 394..560
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 569 AA; 60980 MW; A507D03C6EBF215A CRC64;
MSVEELIAVA AGEQEADLVL KGGEVVNVFS GESYEADVAI HGNRIAGVGS YSGKVHLDMK
GKYVCPGLID GHVHLESSMV SVPEFARVVV PLGTTTVVVD PHEIANVMGA EGILFTLKAS
KYNPLNVFVM LPSCVPSTDF ETAGAELKAV DLFPFLSDKW VLGLGEMMNY HGVISRSEDV
MDMIKIADGK RIDGHAPGVT GCRLNAYVAG GIESDHESVT VEEAREKLRV GLHIMLREGS
ASRNLLDLLP LVTEKNTDRF IFVTDDKHPG DLLSEGHVNY MLKLAVANGI APALAVKMAS
LNAAEYYGLD KIGAIAPGYY ADIAVLEDFE SCKAALVMKS GEIVARNGVP DYEMPRSHKL
PLRSSVNIKA LTTDDLAIHA SDAEANIIGL VPGQITTEWF RERVKSRDGL VVPDTAADVV
KVAVVERHHA SGNIGLGLVR GFGLKRGAFA SSVAHDSHNI IVVGMDETDM LCCIMRIAEM
QGGLCVCADG NVVESLPLPI AGLMSLEPMT HVRDELEKLN GALRDLGIGV DQPFIAASFL
ALPVIPKLKV TDQGLIDVER LKRISLFSS
//
