ID   ADEC_EDWI9              Reviewed;         591 AA.
AC   C5BF52;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-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=NT01EI_3924;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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   -!- 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; CP001600; ACR71035.1; -; Genomic_DNA.
DR   RefSeq; WP_015873062.1; NC_012779.2.
DR   AlphaFoldDB; C5BF52; -.
DR   SMR; C5BF52; -.
DR   STRING; 67780.B6E78_11140; -.
DR   EnsemblBacteria; ACR71035; ACR71035; NT01EI_3924.
DR   GeneID; 7961490; -.
DR   KEGG; eic:NT01EI_3924; -.
DR   PATRIC; fig|634503.3.peg.3495; -.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001485; 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..591
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000215361"
SQ   SEQUENCE   591 AA;  63675 MW;  E114366A4EB333FB CRC64;
     MEDIHHKHTQ SVSRSDMLRL LAVSRGDQPA DLIIDNVFLL DLINGGTLPG PILISGDSIA
     GVGPAYAGTA ALERIDAGGA IAVPGFIDAH LHIESSMMTP IAFESVTLPL GVTTIVCDPH
     EIVNVMGEKG LTWFLRCAEG AQQNQFIQIS SCVPALAGTD INGAEFPLTA MLPYREHPHV
     LGLAEMMNFP GVIAGDEPTL DKLDAFRHLT LDGHSPMLSG KALNAYLAAG VENCHETLAL
     EEGREKLALG MALMIREGSA ARNLDTLAPL ISEFNSPQCM LCTDDRNPWE IAHEGHIDAL
     IRRLIQRHHI APHVAYRVAS WSAARHFGLK RLGLIAPGKK ADIVLLDNLE QVAIRQVFAG
     GKAIDAQQLL RSAAMRQLAS CPPQHNTLRR APLSAEDLTL PLTQDADYRA IQLIPNELIT
     PARTVRWLGD GFDTPDVCRI AVMERYGQQR VPALGLLHNS GLSKGALAAT VSHDSHNIVV
     IGHHPAEMAL AVNQLIDDGG GLCVVADGQV VVHLPLPIAG LMSSRSAAEI ADIIDALKQA
     CRNCGMTLNE PFIQMAFLSL PVIPSLKLTS LGLYDVDHFR FTEVRIPEES A