ADEC_BORAP
ID ADEC_BORAP Reviewed; 548 AA.
AC Q0SLI9; G0ITY0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=BAPKO_3033, BafPKo_J0003;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OG Plasmid lp34, and Plasmid lp38.
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo; PLASMID=lp34;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo; PLASMID=lp38;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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; CP000398; ABH02289.1; -; Genomic_DNA.
DR EMBL; CP002949; AEL70584.1; -; Genomic_DNA.
DR RefSeq; WP_011703927.1; NC_017237.1.
DR AlphaFoldDB; Q0SLI9; -.
DR SMR; Q0SLI9; -.
DR EnsemblBacteria; AEL70584; AEL70584; BafPKo_J0003.
DR KEGG; baf:BAPKO_3033; -.
DR KEGG; bafz:BafPKo_J0003; -.
DR PATRIC; fig|390236.22.peg.1370; -.
DR HOGENOM; CLU_027935_0_0_12; -.
DR OMA; TDHECFT; -.
DR OrthoDB; 751534at2; -.
DR Proteomes; UP000005216; Plasmid lp38.
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; Plasmid.
FT CHAIN 1..548
FT /note="Adenine deaminase"
FT /id="PRO_0000296715"
SQ SEQUENCE 548 AA; 61030 MW; 42FD591045226392 CRC64;
MNLFKIKANY IDIFNKEIYP ASITIENGYI VSIEKIDATL DEYVLPGFID AHIHIESSFL
IPSNFAHLVV QHGTVATISD PHEIANVNGI DGINFMINNS KKTEFKIFFG APSCVPALSS
KFETSGHVLD DQDVDKLMES NDIYYLSEVM DFKGVINKDV EVINKINSAL KRNKVVDGHA
PGLSPHLTLK YMSSGISTDH ECSTIEDARY KLSLGVKIII REGSAAKNFE SLHPLISECS
NKYCDSLMFC FDDAHPNDIL HGHINSIVAR AIGYGHDFFD VLKIACINPV LHYKIPVGLL
RIGDPADFII TKDIKTFKID KTYINGKLVY SDGISHIPLI SEIPINNFNC SEKSILDFKF
STKNKMIPII NCINNQIITQ KTMIDSNLLA PDFQSNIAED ILKIAIINRY EDNSKISIGF
IKNFGIRKGA IGSTVAHDSH NIIVVGTNDE YLCKATNIII ENKGGLCALN NEKTIIIKLP
ISGLMSTLPA KEIAFQYMKL NDFCKNILGS QLDDPLMTLS FMSLTVVPHL KINDKGLFDV
DSFCFLDY