ID A0A0D2C6N9_9EURO Unreviewed; 350 AA.
AC A0A0D2C6N9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Adenine deaminase {ECO:0000256|HAMAP-Rule:MF_03145};
DE Short=ADE {ECO:0000256|HAMAP-Rule:MF_03145};
DE EC=3.5.4.2 {ECO:0000256|HAMAP-Rule:MF_03145};
DE AltName: Full=Adenine aminohydrolase {ECO:0000256|HAMAP-Rule:MF_03145};
DE Short=AAH {ECO:0000256|HAMAP-Rule:MF_03145};
GN Name=AAH1 {ECO:0000256|HAMAP-Rule:MF_03145};
GN ORFNames=PV08_03543 {ECO:0000313|EMBL:KIW19249.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW19249.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW19249.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW19249.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenine to
CC hypoxanthine. Plays an important role in the purine salvage pathway and
CC in nitrogen catabolism. {ECO:0000256|HAMAP-Rule:MF_03145}.
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:0000256|HAMAP-Rule:MF_03145};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03145};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03145};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03145}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03145}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03145}.
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DR EMBL; KN847493; KIW19249.1; -; Genomic_DNA.
DR RefSeq; XP_016239465.1; XM_016377895.1.
DR AlphaFoldDB; A0A0D2C6N9; -.
DR STRING; 91928.A0A0D2C6N9; -.
DR GeneID; 27330626; -.
DR VEuPathDB; FungiDB:PV08_03543; -.
DR HOGENOM; CLU_039228_7_0_1; -.
DR OrthoDB; 316568at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0000034; F:adenine deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd01320; ADA; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01430; aden_deam; 1.
DR PANTHER; PTHR43114; ADENINE DEAMINASE; 1.
DR PANTHER; PTHR43114:SF2; ADENINE DEAMINASE; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03145};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03145};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03145};
KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03145};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03145};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03145}.
FT DOMAIN 14..344
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
FT SITE 233
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03145"
SQ SEQUENCE 350 AA; 38583 MW; E065AC32805112BA CRC64;
MCKESMHEFL KALPKCEHHM HIEGSLEPDL LFTLAKRNNI ALPAPEVDAS FASVDTLLAR
YRRFTSLDDF LHYYFIGMSV LVTAADFESL AYAYFGRAAA DGVAHAEVFF DPQAHTSRGV
SYATVVSGFR AAQARATADF NLTSELIVCI LRHLPPADGA AMYAAAVPDL ESGAVKGLGL
SSTELGNPPA LFTEPFLDAE ARGFHRTAHA GEEADVSYMA EALRELHIQR VDHGIKLTQS
PEVLAEFVAR DVLVTMCPLS NVELRCVKRV ADLPIRTYLD RGVKFSINSD DPAYFGGYIL
DNYCAVQDAF DLSKPEWETI VRNSINGSWC GDDRKKEMIS ALEQVMAKFS
//
