ADEC_DEIGD
ID ADEC_DEIGD Reviewed; 564 AA.
AC Q1J1B1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518};
DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518};
DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=Dgeo_0420;
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) 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:0000255|HAMAP-Rule:MF_01518};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR EMBL; CP000359; ABF44723.1; -; Genomic_DNA.
DR RefSeq; WP_011529567.1; NC_008025.1.
DR AlphaFoldDB; Q1J1B1; -.
DR SMR; Q1J1B1; -.
DR STRING; 319795.Dgeo_0420; -.
DR EnsemblBacteria; ABF44723; ABF44723; Dgeo_0420.
DR KEGG; dge:Dgeo_0420; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_0; -.
DR OMA; TDHECFT; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000002431; Chromosome.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:InterPro.
DR Gene3D; 2.30.40.10; -; 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 PANTHER; PTHR11113:SF2; PTHR11113:SF2; 1.
DR Pfam; PF13382; Adenine_deam_C; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..564
FT /note="Adenine deaminase"
FT /id="PRO_0000292380"
SQ SEQUENCE 564 AA; 58273 MW; 6BD31BF5143E30CA CRC64;
MTTASAASER AVRQRLVRVA RGLEAGDLLV RGAQVVQPAT GEVFGADVLV AEGRVAALVG
PGLGVRAART VEARGAYLAP GFLDAHIHIE SSLLTPARFA AAVLPRGTTA VVAEPHETVN
VMGLSGLRWM LEAGKGSGLR VFGSVPSSVP ASPFECGGAV LDAAEVAEAL RLPGVLGLAE
MMNYPGVLNL ERGAWEVLDA GYGGRIDGHA AGVAGRDLQA YAAAGPHSDH EATTPEEARE
RLRAGLWLMV REGSAARNLE ALLPVLRERP RRAMLVSDDV SVDELLSLGH LDRLLRACVA
GGLHPADAVA LVTCNPAEYW GLHDLGLVAP GYHADFVLLR DLERFEVLDT FVGGVEAQAG
SETPPLPGGG VNLGPSWATA TFEVPASWPV MQVRPDQITT GVGAPGSGDA RLVVADRYGR
GEHAACWTSG TGLTGGALAI SLLHDAHHVA VLGGSNADVR AAGRALEAMG GGVVVVAGGE
VRSNLPLPYA GLMSDLPPQE AAARLSEVTA AARVLGCTLP YPVTTLSFLG LSVIPALKLT
PRGLLDVGAW QLLPRETVRV GAEG