ADEC_LISMF
ID ADEC_LISMF Reviewed; 579 AA.
AC Q71YS6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=LMOf2365_1767;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT04538.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71YS6; -.
DR SMR; Q71YS6; -.
DR KEGG; lmf:LMOf2365_1767; -.
DR HOGENOM; CLU_027935_0_0_9; -.
DR OMA; TDHECFT; -.
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.
FT CHAIN 1..579
FT /note="Adenine deaminase"
FT /id="PRO_0000142428"
SQ SEQUENCE 579 AA; 62057 MW; 0A37715F6BE00005 CRC64;
MENLEQLQER VAVSDGRAKA DLVIKNGRII NVFSGEIMDG DIAIKNGYIA GIGNFPDAEK
IIDAAGAFIA PGFIDAHVHV ESAMVTPAEF ARVLLPNGVT TIVTDPHEIA NVAGEKGIEF
MLEDAKGVPI DMFVMLPSSV PATEGEHNGE TLHAEKLHPL YRHEKVIGLA EVMDFPSVAK
GSSDILTKII DAKKEGGRID GHGAGLTSAD LNNYLAVGIR TDHESTTAKE ATDRLRAGMF
VMLREGTVGR DLLQTIPAVS EKNSHRFCFC TDDKLINDLI TEGSINYNIR LAIKNGIDPI
TAIQMATINA ANCHNLPYLG AVAAGYQADI VFLTDIETVE ISKVLKNGEV VVDNGVRHEA
AFKQQAAVPF VSPPINHHVS LQDLALPLTK ETCYVIGMQP NSLFTEKRIE QVAIQDGKFV
PTVENDLLKM AVVERHHDTG CVGLGIVKGF GLTEGAIATT VAHDSHNIVA VGISDEAMKA
AIDHITQTGG GIAVVNGAGQ VLHDLALPIA GLLSDKSYEE VENDLAGLLN AFKQISTADG
FDPFLTLSFL TLPVIPELKL TDQGLFDFAT FQIISNEVN