ID   ADEC2_JANSC             Reviewed;         623 AA.
AC   Q28MB2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Adenine deaminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            Short=Adenine aminase 2 {ECO:0000255|HAMAP-Rule:MF_01518};
DE            EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518};
GN   Name=ade2 {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=Jann_3233;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) 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; CP000264; ABD56150.1; -; Genomic_DNA.
DR   RefSeq; WP_011456352.1; NC_007802.1.
DR   AlphaFoldDB; Q28MB2; -.
DR   SMR; Q28MB2; -.
DR   STRING; 290400.Jann_3233; -.
DR   EnsemblBacteria; ABD56150; ABD56150; Jann_3233.
DR   KEGG; jan:Jann_3233; -.
DR   eggNOG; COG1001; Bacteria.
DR   HOGENOM; CLU_027935_0_0_5; -.
DR   OMA; CEASHEF; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000008326; 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..623
FT                   /note="Adenine deaminase 2"
FT                   /id="PRO_0000296726"
SQ   SEQUENCE   623 AA;  68761 MW;  77F1F6D106E1359A CRC64;
     MTDQPAPTDH LIRAADEVKI RQRLVRVALG HVAGDTRLRV GKLLDVHSRM WLSDQEIILS
     GRRIAYVGPA GSYPGGVAHE VHEPDLMAVP GFGEVHKHIE SSHVTPEWEA ALVLPHGNTW
     TCEASHEFSN VNGPHNLEFW LTARLAGSPQ KIFPLPGSAV PPTAYEWGGG HFGYDEQAGF
     LNESLMVAGL DEVMDWPAVW NPENPSYDRL WGMIEATFEK RGVIEGHAAG IRDMATINAF
     AAAGLASDHE AWTTEEVLDK LRRGLFMELR PHSLSEMVKG LLEAGLEDWG QFALTTDDRS
     CSDTLKMGAT DHNVRLAISA GLSPEVAIQM VTINPARHMR LTPWVGSLAP GRFADIVLLD
     DLPSVSIRQV WADGELVAED GTYLKPIPKI DWPDWATQTV KIDRAMMADD FAIPAKRGRD
     TMHAALLRPF HWDDDFITMD LPVKDGQVQR DPRRNVTKFA IVDRFSGEGK TSAMFWLGTG
     PRTSDTALAC SMGHDKHNVW AVGSSDAAMA MAVNALRDIQ GGWALVREGQ LVATVRYEVG
     GLMTCRPPAE LDAEMQALYA EGEKIDWMYE PTVSPRWFPG FPERLAFATL TCAPWRWVLV
     APSDRAPDGF VNVATGQTHP VVW