ID A0A1E5SYI7_9BACT Unreviewed; 542 AA.
AC A0A1E5SYI7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BFP71_11970 {ECO:0000313|EMBL:OEK04194.1};
OS Roseivirga misakiensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1563681 {ECO:0000313|EMBL:OEK04194.1, ECO:0000313|Proteomes:UP000095552};
RN [1] {ECO:0000313|EMBL:OEK04194.1, ECO:0000313|Proteomes:UP000095552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-8 {ECO:0000313|EMBL:OEK04194.1,
RC ECO:0000313|Proteomes:UP000095552};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Fabibacter sp. strain SK-8.";
RL Submitted (AUG-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}.
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:OEK04194.1}.
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DR EMBL; MDGQ01000005; OEK04194.1; -; Genomic_DNA.
DR RefSeq; WP_069835699.1; NZ_MDGQ01000005.1.
DR AlphaFoldDB; A0A1E5SYI7; -.
DR STRING; 1563681.BFP71_11970; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000095552; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000095552}.
FT DOMAIN 41..318
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 368..535
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 542 AA; 59182 MW; 37AD22B37B42E7D5 CRC64;
MKIVSGKIVD VRNRRIYTGE IHIENDRIKK IIETAEVQDQ YILPGFVDAH IHIESSMLVP
SEFARLAVVH GTVATVSDPH EIGNVLGVQG VEYMIKDGKK VNFKFAFGAP SCVPATTFET
AGAEITPKEV EYLLAKPEVK YLAEMMNWPG VLFNDKTVYE KLNIAKALGK PIDGHAPGLR
GEQAEAYVKA GISTDHECFT ADEARDKLKH GMKIAIREGS AAKNFEALVD LFAEAPEQLM
FCSDDKHPDN LVEGHINDLV KRALNKGYDL FDVLQAACIT PVDHYNLDVG TLKEGDYADF
IVTKDTSNLD VLATYINGIQ VADKGKSLIE SSRSEIVNQF HCDPIKEDAI SVKATSENIK
VIEALDGQLI TNCLHYSAKV DPAGFVQSDV SRDLLKMVVV NRYQNAQPAV AFIKNFNLKD
GAIASSVGHD SHNIIAVGVD DASICKAINL IINEKGGVSA VSSKEEAILP LPVAGIMSNG
DGYEIAKNYT QIDRMAKSMG STLNSPFMTL SFMGLLVIPN LKLSDLGLFD GQSFKFTPLF
SR
//
