ID   ADEC_SHEHH              Reviewed;         587 AA.
AC   B0TMM7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Shal_2836;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenine deaminase family. {ECO:0000255|HAMAP-Rule:MF_01518}.
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DR   EMBL; CP000931; ABZ77387.1; -; Genomic_DNA.
DR   RefSeq; WP_012277914.1; NC_010334.1.
DR   AlphaFoldDB; B0TMM7; -.
DR   SMR; B0TMM7; -.
DR   STRING; 458817.Shal_2836; -.
DR   EnsemblBacteria; ABZ77387; ABZ77387; Shal_2836.
DR   KEGG; shl:Shal_2836; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001317; 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.
DR   TIGRFAMs; TIGR01178; ade; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese.
FT   CHAIN           1..587
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000215363"
SQ   SEQUENCE   587 AA;  64176 MW;  527132439B491B77 CRC64;
     MSNLMDKHTQ KIDPQSLQHM LSVLRLEQLG DLKLTNVSLL DLINGEVIPG PILIDKGHII
     AVGQEVDLLA AVRVVDCHGQ IAVPGFIDAH MHVESSTMTP FEFERTTLPL GTTSIVCDPH
     ELVNVMGRQG IDWFLRCSET MHQNMFVQIS SCVPAVAGLD INGSDFSLDE MAAYREHKHV
     LGLAEVMDYP AVINGEQAMQ DKLTTFNNLN LDGHSPLLSG LSLSAYVACG IQNCHETTNV
     EEGKEKLAKG MAVIMREGSV AKNLDALAPL ITDFSSPYCL LCTDDRNPHE IANEGHINFM
     VKRLIQQHDI PAYLAYRVAS WSAAKHFGLR RLGLIAPGYR ADINLVSTLD AVDIQRVLIA
     GEFVDELTLE SELEAKLEAS SPPLHNTVKH RPITEAELTI PLKEGEYRVI GVVKDELLTN
     HLVCHFDGQH FAEPGVNKLA VIERYGHQLP PALSLVKGFD IEQGAIATSV GHDSHNIVVI
     GADEKSMAHA VNHLLEIGGG FCVVQQGEVT ADLMLPLGGI MSLERSEKIA EQISDLKTAV
     KAIGVSLSEP FVQMSFLSLP VIPSLKMTVK GLFDVDQFKF VSLRVDS