ID   ADEC_SULNB              Reviewed;         533 AA.
AC   A6Q8K5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=SUN_0856;
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX   NCBI_TaxID=387093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF71814.1; -; Genomic_DNA.
DR   RefSeq; WP_011980547.1; NC_009663.1.
DR   AlphaFoldDB; A6Q8K5; -.
DR   SMR; A6Q8K5; -.
DR   STRING; 387093.SUN_0856; -.
DR   PRIDE; A6Q8K5; -.
DR   EnsemblBacteria; BAF71814; BAF71814; SUN_0856.
DR   KEGG; sun:SUN_0856; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_7; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000006378; 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..533
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000068613"
SQ   SEQUENCE   533 AA;  58791 MW;  957CF4898C9CA46F CRC64;
     MEMKSNYVDI FKREIFPAKV RVEKGKIASI ERIDTPCDTY ILPGFVDAHI HIESSMLPPS
     EFARLAVCHG TVATVSDPHE IANVLGIPGV GYMLDNSEMT PFKFYFGASP CVPATTFETS
     GATLGPDEIE SLLKMPQIKY LSEVMNFPGV INGDPDMLAK IAKAKALHKR IDGHAPGLRG
     DELTKYIEAG IETDHEAFTY EEGLEKLQKG MKILIREGSA AKNFEALAPL IPAYPNKLMF
     CSDDRHPNDL AREHIDGHVR RAIAKGYDLF DVLRIASVNP VEHYGLEVGL LRVGDPADFI
     VVEDLKDFKV LQTVIDGEIV ARGKKPLIDS VTVETPNHFH TGIKKEEDFI LERCVHTEII
     HALDHSLITE EEIMDLSSGK AKDVLKITVV NRYEDVKPAV AYVHGFGLKK GAIASSVAHD
     SHNIIAVGCS DALIAKAVNT IIGNRGGICA VTEEEIEVLS LPIAGLMSDK DGFEVANRYA
     DLDRMVREYF TSLLSAPFMT LSFMALLVIP ELKLSDKGLF DGRSFHFIDS CRR