ID   ADEC_KLEP7              Reviewed;         603 AA.
AC   A6TBK1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 67.
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};
GN   OrderedLocusNames=KPN78578_25110; ORFNames=KPN_02554;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-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   -!- SUBUNIT: Homodimer. {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; CP000647; ABR77972.1; -; Genomic_DNA.
DR   RefSeq; WP_015958726.1; NC_009648.1.
DR   AlphaFoldDB; A6TBK1; -.
DR   SMR; A6TBK1; -.
DR   STRING; 272620.KPN_02554; -.
DR   EnsemblBacteria; ABR77972; ABR77972; KPN_02554.
DR   KEGG; kpn:KPN_02554; -.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; IEGHFPG; -.
DR   Proteomes; UP000000265; 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..603
FT                   /note="Adenine deaminase"
FT                   /id="PRO_0000318547"
SQ   SEQUENCE   603 AA;  64506 MW;  46E71B1B81330063 CRC64;
     MSSNAQVRRR AVQAARGESP FDLLLIDAQI VDMATGEIRP ADVGIVGEMI ASVHPRGSRE
     DAHEVRSLAG GYLSPGLMDT HVHLESSHLP PERYAEIVLT QGTTAVFWDP HELANVLGVA
     GVRYAVDASR HLPLQVMVAA PSSVPSTPGL EMSGADFAGA EMETMLGWPE VRGVAEVMDM
     HGVLHGSERM QEIVQAGLNS GKLIEGHARG LSGADLQAYL AAGVTSDHEL TSADDALEKL
     RAGLTIEIRG SHPYLLPDIV AALKTLPHLS SQITVCTDDV PPDILLEKGG IIALLNLLIE
     HGLPAVDALR FATLNAAIRL QRHDLGLIAA GRRADLVVFD SLEKLVAREV YIGGKLLARA
     GNLLTPIAPA AGVTPPRDTL QIAPLRADDF ILRVQGIRHG IARLRHIRGA RFTQWGEVEV
     QVRDGIVQLP AGFSLIWVKH RHGRHQATPQ IALLEGWGEL RGAIATSYSH DSHNLVVLGR
     DANDMALAAN QLIASGGGMA LAQQGEILAH VAMPIAGMLS DLPAAELARQ FRELRDLSSQ
     VADWEPPYRV FKAIEGTCLA CNAGPHLTDL GLTDGGSRQI VDPLIACREI PEPTDHNNNP
     QGA