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ADEC_KLEP3
ID   ADEC_KLEP3              Reviewed;         603 AA.
AC   B5XP95;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=KPK_1614;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI11456.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XP95; -.
DR   SMR; B5XP95; -.
DR   EnsemblBacteria; ACI11456; ACI11456; KPK_1614.
DR   KEGG; kpe:KPK_1614; -.
DR   HOGENOM; CLU_027935_0_0_6; -.
DR   OMA; IEGHFPG; -.
DR   OrthoDB; 751534at2; -.
DR   Proteomes; UP000001734; 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.
FT   CHAIN           1..603
FT                   /note="Adenine deaminase"
FT                   /id="PRO_1000146241"
SQ   SEQUENCE   603 AA;  64605 MW;  C849F6A31134B568 CRC64;
     MSSNAQVRRR AVQAARGESP FDLLLVEAQI VDMATGEIRP ADVGIVGEMI ASVHPRGSRT
     DAHEVRSLAG GYLSPGLMDT HVHLESSHLP PERYAEIVLT QGTTAVFWDP HELANVLGVE
     GVRYAVDASR HLPLQVMVAA PSSVPSTPGL EMSGADFAGA EMETMLGWPE VRGVAEVMDM
     HGVLHGSERM QEIVQAGLNS GKLIEGHARG LSGADLQAYL AAGVTSDHEL TSADDALEKL
     RAGLTIEIRG SHPYLLPDIV AALKTLPHLS SQITVCTDDV PPDMLLEKGG IIALLNLLIE
     HGLPAVDALR FATLNAAIRL QRHDLGLIAA GRRADLVVFD SLEKLVAREV YVGGERLAHA
     GRLLKPIAPA PGVTPPRDTL PIAPLRADDF VLRVQGIRHG VARLRHIRGA RFTQWGEVEV
     QVRDGKVQLP AGFSLIWVKH RHGRHQATPQ IALLEGWGEL RGAIATSYSH DSHNLVVLGR
     DADDMALAAN QLIASGGGMA LAQQGEILAH VAMPIAGMLS DLPAAELARQ FRELRDLSSQ
     VADWEPPYRV FKAIEGTCLA CNAGPHLTDL GLTDGGSRQI VDPLIACRET PEPTDHNNNP
     QGA
 
 
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