ID A0A0E3V6D9_9BACT Unreviewed; 553 AA.
AC A0A0E3V6D9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=SD10_05490 {ECO:0000313|EMBL:AKD54446.1};
OS Spirosoma radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD54446.1, ECO:0000313|Proteomes:UP000033054};
RN [1] {ECO:0000313|EMBL:AKD54446.1, ECO:0000313|Proteomes:UP000033054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG5A {ECO:0000313|EMBL:AKD54446.1,
RC ECO:0000313|Proteomes:UP000033054};
RX PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant bacterium
RT isolated from gamma ray-irradiated soil.";
RL Curr. Microbiol. 69:286-291(2014).
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; CP010429; AKD54446.1; -; Genomic_DNA.
DR RefSeq; WP_046376043.1; NZ_CP010429.1.
DR AlphaFoldDB; A0A0E3V6D9; -.
DR STRING; 1379870.SD10_05490; -.
DR KEGG; srd:SD10_05490; -.
DR PATRIC; fig|1379870.5.peg.1191; -.
DR HOGENOM; CLU_027935_0_0_10; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000033054; 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|HAMAP-Rule:MF_01518};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01518};
KW Reference proteome {ECO:0000313|Proteomes:UP000033054}.
FT DOMAIN 41..321
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 372..544
FT /note="Adenine deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13382"
SQ SEQUENCE 553 AA; 59790 MW; 198EAC9A8EA4385F CRC64;
MLSANILNLF DQTIFYGTIS VENGRIAQID RLGAERPGEP YVLPGFVDAH VHVESSLLTP
PQFARLAVVH GTVATVSDPH EIGNVLGVAG VKYMVDEARR VPFKFMFGAP SCVPATPFET
AGATISAQDV RALLAMKEIG YLAEVMNFPG VLHEDPDMMA KIALAKAFNK PVDGHAPGLT
GNDAQRYMDA GISTDHECFT YEEGLDKAQR GMNILIREGS AARNFEALIP LLAEFPTQIM
FCSDDKHPDT LAQGHINQLV VRALKKGHSL WQTLRAACLN PVLHYRLPVG LLREGDPADY
IVVTDLTELR VEQTVINGEI VAQNGQSAIP DWRSEHVNQF SCSPKTPTDF AVEVDLSAGK
PLIRVIEALD GQLITNELQE EARIENGEIV PDTDRDILKL VVVNRYQNAP PAVAFIKNVG
LKQGAIASSV GHDSHNITAV GCDDESICRA VNLVIEAKGG LSAVGASHNT QAPVSMLLPL
PVAGLMTDAD GYEVADQYAA LDQFAKHVLA STLTAPFMTL SFMALLVIPS LKLSDKGLFD
GQTFEFTPLQ IVK
//
