ID A0A1I6C7N7_9BACI Unreviewed; 578 AA.
AC A0A1I6C7N7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN04488577_3430 {ECO:0000313|EMBL:SFQ89095.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ89095.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ89095.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ89095.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOYF01000005; SFQ89095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6C7N7; -.
DR STRING; 1761761.SAMN04488577_3430; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000199578; 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|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:UP000199578}.
FT DOMAIN 68..349
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 404..571
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 578 AA; 62866 MW; 8CF3527E9C743208 CRC64;
MNLNRISLKR QILTAAKNEV ADVVIKNGKI IDVFNLTIFE ADIAITDGVI VGLGNYDGKK
VIDVSGKYVC PGFIDGHVHI ESAMVTPAEF AKVVLPHGVT TIIADPHEIG NVAGAEGIQF
MIDHSKNLPL SIYYMLPSCV PATPFENAGA VLRAEDLAPF YEYELVLGLG EVMDYPSVAQ
CQPEMMNKLS DALERKVCID GHAAGIDADG INVYMTSGIR TDHECVNAEE VIERLQRGMY
VMLREGSAAR DLKQLIKAVN EKNARRCLFV TDDKHLDDLL AEGSIDYNVK LAIAEGLDPI
LVIQMATLNA AECFGLRNKG AIAPSYDADL LILDSLDHLS IESVFQSGNL VAEKGACLPF
EEYTGDIPNR LTNSVQIENI VESDLLLRAE EEEANIIEVV PNSLVTKRLR EGITVENGFF
QTSITNDQLK MAVVERHHQT GNIGMGIVKG FGIKSGALAS TVAHDSHNIV VAGTNDQDMF
AAIIAIEEMN GGLVVINDGK VIASLPLNIA GLISNKDYQS INNELNDINA ALEQIGFSGN
FNPFLTLSFL ALPVIPQLKL TDMGLFDVER FRHIGLHE
//
