ADEC_BORBU
ID ADEC_BORBU Reviewed; 548 AA.
AC O50821;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=BB_K17;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OG Plasmid lp36.
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AE000788; AAC66139.1; -; Genomic_DNA.
DR PIR; C70253; C70253.
DR RefSeq; NP_045591.1; NC_001855.1.
DR RefSeq; WP_010890337.1; NC_001855.1.
DR AlphaFoldDB; O50821; -.
DR SMR; O50821; -.
DR PRIDE; O50821; -.
DR EnsemblBacteria; AAC66139; AAC66139; BB_K17.
DR KEGG; bbu:BB_K17; -.
DR PATRIC; fig|224326.49.peg.1437; -.
DR HOGENOM; CLU_027935_0_0_12; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000001807; Plasmid lp36.
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; Reference proteome.
FT CHAIN 1..548
FT /note="Adenine deaminase"
FT /id="PRO_0000142406"
SQ SEQUENCE 548 AA; 60864 MW; 012AE5222AD8301E CRC64;
MDLFKIEANY IDIFNKEIYP ASIAIANGHI ASIEKINATL DEYVLPGFID AHIHIESSFL
VPSNFAHLVV AHGTVATISD PHEIANVNGI DGINFMINNS KKTEFKFFFG APSCVPALSQ
EFETSGYVLN DKDIDELMKL DDIYYLAEVM DFKGVINKDI EIINKINSAL KRNKVVDGHA
PGLSPNLTLK YASSGISTDH ECLTIEDARY KLSLGMKILI REGSAAKNFE SLHPLISECS
KKYCDSLMFC FDDAHPNDIL NGHINLIVAR AIKHGHDFFD VLKIACINPV LHYKIPVGLL
RIGDPADFII TKDIKTFKIN KTYINGKLVF NDGISLIPLI NEIPINNFNC SKKSISDFKF
STKNKMIPVI KCISNQIITH KTMIDSNLLA PDFQSNIAED ILKIAIINRY KDNSKISIGF
IKNFGIRNGA IGSTVAHDSH NIILVGSNDE YLCKAANTII QNKGGLCALN NEKTIIMELP
ISGLMSTLSA ERVASQYIKL NDFCKNVLGS RLDDPLMTLS FMSLTVVPHL KINDKGLFDV
DSFCFVDY