ID A0A0R2TM13_9RHOB Unreviewed; 569 AA.
AC A0A0R2TM13;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-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 ORFNames=ABR89_10000 {ECO:0000313|EMBL:KRO86434.1};
OS Rhodobacter sp. BACL10 MAG-120910-bin24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1655597 {ECO:0000313|EMBL:KRO86434.1, ECO:0000313|Proteomes:UP000051243};
RN [1] {ECO:0000313|EMBL:KRO86434.1, ECO:0000313|Proteomes:UP000051243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL7 MAG-120910-bin24 {ECO:0000313|EMBL:KRO86434.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO86434.1}.
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DR EMBL; LICH01000319; KRO86434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TM13; -.
DR Proteomes; UP000051243; 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 69..347
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 399..566
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 569 AA; 61131 MW; 9721829D480A5BDC CRC64;
MPNPSGRLKR RIRQGRGLEV ADIVLRGGRV FDLITGELVE SDVAICGDQI VGVFDRYEGK
TIVDCSGKIL VPGFIDTHLH IESSCVTPYE FDRLVTPRGV TTAICDPHEI ANVCGLEGIE
YFLTAAQDCV MDIKVQLSSC VPSTHMETTG ARLSASDLLP LADHPAVIGL AEFMNYPGLL
AEAPDAIEKL TAFQGRHIDG HAPLLSGRDL NGYISAGIRT EHEATSAAEA LEKLRKGLRV
LIREGSVSKD LHALAPLLTE RFSPYLCFCT DDRNPLDIAD QGHLDYVIRT AIALGADPLA
VYRSASLSAA EAFGLKDRGL IAPGKRADIV VIDALESCRA LRVMVAGIWA DATAFGARKI
APPVARNSVK LRAKLLAQSF RIGSNRVETP VIGVIEGKII TQHLTFDIAP TDGQKSVDLA
RDLVKIAIVE RHGKNGNVAA GFVQGFGLKR GAIGSTVCHD HHNIAVIGAD DTDMALAANR
LAEMEGGFVV VLDGQVLAEL ALPVAGLMSL EPFETVERAL RILRAAAQNL GVILHEPFLQ
LAFLALPVIP HLKITDHGMV DVDRFEVIP
//
