ID   ADE_SINMW               Reviewed;         324 AA.
AC   A6UET5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01962};
DE            Short=ADE {ECO:0000255|HAMAP-Rule:MF_01962};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01962};
DE   AltName: Full=Adenine aminohydrolase {ECO:0000255|HAMAP-Rule:MF_01962};
DE            Short=AAH {ECO:0000255|HAMAP-Rule:MF_01962};
GN   OrderedLocusNames=Smed_3344;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC       hypoxanthine. Plays an important role in the purine salvage pathway and
CC       in nitrogen catabolism. {ECO:0000255|HAMAP-Rule:MF_01962}.
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_01962};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01962};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01962};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. Adenine deaminase type 2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01962}.
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DR   EMBL; CP000738; ABR62165.1; -; Genomic_DNA.
DR   RefSeq; WP_012067546.1; NC_009636.1.
DR   RefSeq; YP_001329000.1; NC_009636.1.
DR   AlphaFoldDB; A6UET5; -.
DR   SMR; A6UET5; -.
DR   STRING; 366394.Smed_3344; -.
DR   EnsemblBacteria; ABR62165; ABR62165; Smed_3344.
DR   GeneID; 61610895; -.
DR   KEGG; smd:Smed_3344; -.
DR   PATRIC; fig|366394.8.peg.6590; -.
DR   eggNOG; COG1816; Bacteria.
DR   HOGENOM; CLU_039228_7_1_5; -.
DR   OMA; NHFTIHA; -.
DR   OrthoDB; 554648at2; -.
DR   Proteomes; UP000001108; Chromosome.
DR   GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01320; ADA; 1.
DR   HAMAP; MF_01962; Adenine_deaminase; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR028892; ADE.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43114; PTHR43114; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01430; aden_deam; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nucleotide metabolism; Zinc.
FT   CHAIN           1..324
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000017708"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
FT   SITE            213
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01962"
SQ   SEQUENCE   324 AA;  35291 MW;  D6D3242CE51656E4 CRC64;
     MTAHLKKAEL HCHIEGATPP ELAVRQARKY GVDTGTIIRD GAYVWEDFTS FVKCYDAVAS
     LFRTEGDYAL LAEAYLTELA EAGTIYSEII VSPDHGNTVG LGADAYLEGL AAGMEAAKAR
     KGIESRMLIT GIRHLGPEAV VRTAEYAASH RHPLVTGFNL AGEERMHSVA EFSRAFDIVR
     DAGLGLTIHA GELSGAFSVR DALDHVRPAR ISHGVRAIED TDLVRRLADE GVVLEVCPGS
     NIALKVFPDF PSHPLRRLYD AGVRVTLNSD DPPFFHTSLA QEYEIAAHAM GFSDGEIDRM
     TRTALEAAFV DEPTRERLLA ALHI