ID A0A160F261_9BACI Unreviewed; 570 AA.
AC A0A160F261;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ECO:0000313|EMBL:ANB59752.1};
GN ORFNames=GFC30_719 {ECO:0000313|EMBL:ANB59752.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB59752.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB59752.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB59752.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
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; CP015438; ANB59752.1; -; Genomic_DNA.
DR RefSeq; WP_066322933.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A160F261; -.
DR KEGG; aamy:GFC30_719; -.
DR PATRIC; fig|294699.3.peg.715; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000076865; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076865}.
FT DOMAIN 60..343
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 397..564
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 570 AA; 62035 MW; DC6909B7F902EC18 CRC64;
MKQLAVASKR QLADVVVKNG KIVNVFTHEI MQADIAIADG KIVGIGAYDG HTVIDAKGKY
VCPGLIDGHV HIESSMVTPS EFARVVVPHG VTTVITDPHE IANVAGTRGI EFMLNDSEHT
PLDVYVMLPS CVPATAFEHA GATLHAEQLA PFFSHPRVLG LAEVMDYPSL LEGKQHMLAK
LIAAMEANKL IDGHLAGLDE TAVNVYRSAN VHTDHECVTV DEALARVQRG MYVLIREGSV
AKDLHKLLPA VHTYNARRFL FCTDDKHIDE LVTEGSVDHH IRLAIQAGIE PITAIQMATL
NAAECYRLYT KGAIAPGYDA DFLLVEDLHS FSITHVFKKG ALVAENGRVT CSVTKATSID
KTIIQSVHTK KITKENVQIP FTRGNQANVI QIIPNHLHTK RLITEVHVEN GVFQPSIEQD
LLKLVVVERH RGLGVGVGIV NGFQLKKGAI ASSIAHDSHN IIATGTNDND IIVAIEHVRK
MNGGLVVVKN GDVLADLSLE IGGLMTVKNY EDVLQRLQSI HHALSTLGAS DEFNPFITLA
FLALPVIPEL KLTDQGLFDV SSFQFIDVEV
//
