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