ADEC_SHIDS
ID ADEC_SHIDS Reviewed; 584 AA.
AC Q329F0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=SDY_4146;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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 -!- SUBUNIT: Homodimer. {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; CP000034; ABB64055.1; -; Genomic_DNA.
DR RefSeq; WP_001065727.1; NC_007606.1.
DR RefSeq; YP_405546.1; NC_007606.1.
DR AlphaFoldDB; Q329F0; -.
DR SMR; Q329F0; -.
DR STRING; 300267.SDY_4146; -.
DR EnsemblBacteria; ABB64055; ABB64055; SDY_4146.
DR KEGG; sdy:SDY_4146; -.
DR PATRIC; fig|300267.13.peg.4873; -.
DR HOGENOM; CLU_027935_0_0_6; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000002716; 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; 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.
DR TIGRFAMs; TIGR01178; ade; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..584
FT /note="Adenine deaminase"
FT /id="PRO_0000296732"
SQ SEQUENCE 584 AA; 63398 MW; DDAF1B06670994AA CRC64;
MNNSINHKFH HISRAEYQEL LAVSRGDVVA DYIIDNVSIL DLINGGEISG PIVIKGRYIA
GVGAEYTDAP ALQRIDARGA TAVPGFIDAH LHIESSMMTP VTFETATLPR GLTTVICDPH
EIVNVMGEAG FAWFARCAKQ ARQNQYLQVS SCVPAMEGCD VNGASFTLEW RDHPQVTGLA
EMMDYPGVIS GQNALLDKLD AFRHLTLDGH CPGLGGKELN AYIAAGIENC HESYQLEEGR
RKLQLGMSLM IREGSAARNL NALAPLINEF NSPQCMLCTD DRNPWEIAHE GHIDALIRRL
IEQHNVPLYV AYRVASWSTA RHFGLNHLGL LAPGKQADIV LLSDARKVTV QQVLVKGEPI
DAQTLQAEES ARLAQSAPPY GNTIARQPVS ASDFALQFTP GKRYRVIDVI HNELITHSRS
SVYSENGFDR DDVCFIAVLE RYGQRLAPAC GLLGGFGLNE GALAATVSHD SHNIVVIGRS
AEEMALAVNQ VIQDGGGLCV VRNGQVQSYL PLPIAGLMST DTAQSLAEQI DALKAAAREC
GPLPDEPFIQ MAFLSLPVIP ALKLTSQGLF DGEKFAFTTL EVTE
