ADEC_LACDA
ID ADEC_LACDA Reviewed; 565 AA.
AC Q1G825;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Ldb2182;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI98906.1; -; Genomic_DNA.
DR RefSeq; WP_003621704.1; NC_008054.1.
DR AlphaFoldDB; Q1G825; -.
DR SMR; Q1G825; -.
DR STRING; 390333.Ldb2182; -.
DR EnsemblBacteria; CAI98906; CAI98906; Ldb2182.
DR KEGG; ldb:Ldb2182; -.
DR eggNOG; COG1001; Bacteria.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; MVTACAY; -.
DR BioCyc; LDEL390333:LDB_RS09505-MON; -.
DR Proteomes; UP000001259; 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..565
FT /note="Adenine deaminase"
FT /id="PRO_0000292383"
SQ SEQUENCE 565 AA; 62389 MW; 7E773BB46EC4B865 CRC64;
MTKIDLLVKN AHVFNVYLRK FEDVNITIKD GKFYWINKEL PGIEAAKVID LQGKYVIPGF
VDAHMHIDSS MTTPKVMGQT IGKYGTTTII ADDHEITNVA GVKGLKDFID EKAPIDIFFG
IPSSVPSTNP NMETTGGLIG VKETEELLKD PRFVCLGEVM NFKDMTSDHD TLIKKIIAAC
RKARPTMPLE GHVPAYHSED LAKVIYAGIT TDHTQQTSSL VDEKIRSGMF VEIQLKSMHQ
EVIDTVIEHG YFEHVALVTD DSMPDTLLKG HLNLLVKKAI DMGMRPEDAI YISTYTPARH
MGLWDRGAIA PGRVADFIVL NNLEDLSIAQ VYKNGLPFAA KDEKDNNVYP EELLHSVKAP
KLSEADFDLK TDLVQNGKVV ANIIQINEVG TFTNHIQKCL EVKDGHVQWK KAGLALMLCQ
ERYGKNEGRY AFALIDRGIV GDGAIGATWA HDHHNLIILG TNIAGMVSVQ NLLVEEQGGY
IAAKGSQIVA NAPLPLGGVV SLEPMSVLGK QISKVRETMV DLGYKNTNEI MSFSTLSLLV
SPTLKISDKG IFEVKTQRHI PLFEC