ADEC_CLOAB
ID ADEC_CLOAB Reviewed; 570 AA.
AC Q97KN0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=CA_C0887;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78863.1; -; Genomic_DNA.
DR PIR; D97009; D97009.
DR RefSeq; NP_347523.1; NC_003030.1.
DR RefSeq; WP_010964205.1; NC_003030.1.
DR AlphaFoldDB; Q97KN0; -.
DR SMR; Q97KN0; -.
DR STRING; 272562.CA_C0887; -.
DR PRIDE; Q97KN0; -.
DR EnsemblBacteria; AAK78863; AAK78863; CA_C0887.
DR GeneID; 44997398; -.
DR KEGG; cac:CA_C0887; -.
DR PATRIC; fig|272562.8.peg.1097; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; EHECSTV; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000000814; 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..570
FT /note="Adenine deaminase"
FT /id="PRO_0000142412"
SQ SEQUENCE 570 AA; 62622 MW; B0E95F3EC03ECCD7 CRC64;
MYCIEEKIEK ALGIKEASLV LKNCNIVNVF SSEIIRGDLA IDGDTIIGIG KYKGKTEIDL
SNKYVAPGFI DSHVHIESSM VSPKEFARAV ISRGTTTIIV DPHEIANVCG MDGIKYMMEE
TKNMPLDVFF MLSSCVPATS FETSGAVLKA EDLKELIDSD RVLGLGEMMN YPGVLSREEE
VLNKLKLAGS YNKIVDGHAP SVRGNELNAY NLAGIKTDHE CSSIEEMNEK IRNGMYIAIR
EGSAAKNLDI LIKGVNAKNE RRIMFCADDR HPDDILKSGH MDNCVRRAIY NGIENTAAIR
MASINAAECY KLERVGAIAP SYKADLVVLE DLKDVKVNMV IKSGEVVFKD NKHLKDMGSK
SDITKVSNTV NIKKVSEENL ELKLDTDVCS IISVALNSIS TKNVKRKVNL SNGIFKCELN
YGINKVAVIE RHKKSGSIGI GLVENFGLKR GAIASTVAHD SHNIIVLGNN DEDMVKAVNE
IERVGGGITI SLDGKIIETL ELEIAGLMSN KSMEFVAERV SKMINICHNT LGVNKDIQPF
MTLAFLALPV IPEIRITDKG VFDVVNFKFL