ADEC_CLOP1
ID ADEC_CLOP1 Reviewed; 568 AA.
AC Q0TR21;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=CPF_1476;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000246; ABG82839.1; -; Genomic_DNA.
DR RefSeq; WP_011590725.1; NC_008261.1.
DR AlphaFoldDB; Q0TR21; -.
DR SMR; Q0TR21; -.
DR STRING; 195103.CPF_1476; -.
DR EnsemblBacteria; ABG82839; ABG82839; CPF_1476.
DR GeneID; 29571413; -.
DR KEGG; cpf:CPF_1476; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; MVTACAY; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000001823; 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.
PE 3: Inferred from homology;
KW Hydrolase; Manganese.
FT CHAIN 1..568
FT /note="Adenine deaminase"
FT /id="PRO_0000296720"
SQ SEQUENCE 568 AA; 64186 MW; EA2B76E0921E9E38 CRC64;
MQVELIIKNL NVYNSYFKKF IKGDILINKG KFLHIGKGYE DRLWSENVID GEGKYIIPGL
IDIHMHIESS MTIPREFSKA AIKHGVTTVV ADPHEIANVF GIRGIEEFIK FKGNLDIFYG
IPSSVPSTSS SLETTGEKIT HNEVKRLLEY DNIICLGEVM NFKDLIEDDD SNINKIINIS
KEKNIPLEGH CPKIQGVDLS LYIYRGVNGD HTQQSVGSLQ EKIQNGMFIE MQHKSMTLEN
IKFLIENNLY EHFALVTDDV MADKLVKGHL DEILKEAVKL GMSIENAIYA STYTPARRMN
LLDRGTIAPG KLADFILLDS IEDFNIYEVY KNGEMVFNRD KGLKEEFFED KSKLDYRFYN
SIELNNITKE SLEVKVPNKY KNKVNCRTMK VLKNTTFTEE GEVTLNVYNN ILQWEKSSCA
LIAVFERYGK NNNISFGLVE GEIIKEGAIA TTWAHDHHNL MVMGRNISDM TIAANEVINS
RGGYVVSKNN EVIAKLELPI GGIISDEPIE IIGEKLGEVR SAMRDLGYNH MNEIMSFSTL
SLPVSPALKI TDKGLIDVKK GSIVSLFK