ID   ADEC_STAMF              Reviewed;         605 AA.
AC   A3DLI4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=Smar_0382;
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000575; ABN69494.1; -; Genomic_DNA.
DR   RefSeq; WP_011838685.1; NC_009033.1.
DR   AlphaFoldDB; A3DLI4; -.
DR   SMR; A3DLI4; -.
DR   EnsemblBacteria; ABN69494; ABN69494; Smar_0382.
DR   GeneID; 4907710; -.
DR   KEGG; smr:Smar_0382; -.
DR   eggNOG; arCOG00693; Archaea.
DR   HOGENOM; CLU_027935_0_0_2; -.
DR   OMA; TDHECFT; -.
DR   OrthoDB; 12286at2157; -.
DR   Proteomes; UP000000254; 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..605
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000296737"
SQ   SEQUENCE   605 AA;  66575 MW;  1600C78750C46F03 CRC64;
     MVLPKIFSYD IDERINLIQT ITGKKPADIV ISNVNLVLTP TGEILDNASI IISGKRIAGA
     GKYSELHRFI GKNTLVIDGE NNYAMPGFID PHIHIESSLL TPHGFAKLAL RHGTTTVVAD
     PHEIGNVLGS RGVEIFMDAA RNLPLKILID IPSCVPATDP KFGLETTANI IGADEVEKLA
     ALEGTIGLGE VMDFVSVLNS NKSVLEKIRV AHRYRLIVNG HAPLLRGAEL DAYIDAGIWS
     DHESTIYEEA LEKARKGMYV FIREGSAWKD LKALLPLIKN HTIDHRFLSF ASDDINVVDL
     MEKGHMDRII NIAIEYGVDP VKAIQLATIG PAMRIHLEDH VGVVGPARLA DIVLSKNIEY
     IKPHTVIANG EIIYYKGELK KTFNNYKYPE ETLNTVKLAK IPEPQEFIPK INTREGIVEA
     NIIEVTPGSA LTKHVIEELA VKNYNVLADP NRDIIYAAVI DRHKATGSMG KGFIKGLGFR
     AGAIAQTIAH DTHNLIVAGN NPEDMSRAVK RIVEIQGGIV VVDEGKIIGE LPLRLAGLMS
     IEEPETVYEK YKKITNELNN GYGLEFESFF MTLALVALPV IPEIRLTDKG LVDVRKAKLI
     PLINK