ADEC_METKA
ID ADEC_METKA Reviewed; 599 AA.
AC Q8TX47;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 93.
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}; Synonyms=adeC;
GN OrderedLocusNames=MK0829;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02042.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TX47; -.
DR SMR; Q8TX47; -.
DR STRING; 190192.MK0829; -.
DR PRIDE; Q8TX47; -.
DR EnsemblBacteria; AAM02042; AAM02042; MK0829.
DR KEGG; mka:MK0829; -.
DR HOGENOM; CLU_027935_0_0_2; -.
DR OMA; TDHECFT; -.
DR Proteomes; UP000001826; Chromosome.
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.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Reference proteome.
FT CHAIN 1..599
FT /note="Adenine deaminase"
FT /id="PRO_0000142441"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 65401 MW; 2978B26973FFB877 CRC64;
MARSNRRGGR GDPEDDPAWA PPGHRCAGER AVGGPTVIPR AYLPAVPAGG NESRAFQGRF
VDPWFSGIRT GYVIWDGGRL LGVTRNEPEH ADVIDVDGII CPGFVDAHVH VESSGLRPAR
YAEIVVREGT TAVVWDPHEV VNVSGELGLE WAVKTAEEAL PFKFYIALPS CVPALGPPYE
TVEGEITVDV ARKFASHPMV VSVGELMDVA GVMEGEKDEF IELKSLYGLT VDGHAPGLTG
FEAMRYFAAG PETDHECSTA EEFTSRRELG VWTFVRQGSS SKDMEVALET LEDLRGVCFV
TDDLHVKDMD EISLRKIVGR AIEAGFDPLE SLSAVTLNPS LCYGLQSGRL VPGFHADIVV
VEDLDENMEL TDVWIGGKRS ERVRFRDAEA ELPDVELSVD PREVSFQDGK YEVRCVGLVR
GSIRTEEIVR EITVKDGAVK DDDVAFLVVT DRYGQGSWSI GFVEGFEELD CAVVSTVAHD
SHNVVVAGRR LDDVRRALQL VSEVGGCVGA VAGDRAEFVR LDVAGLMSSS DPEEVKKSYE
DVLELIRSSS GVDWDPFQAL SFVTLPVVPE LRLTDRGLVK VEPDEIRFVD IITDGDPVE