ID A0A1V8U5K4_9PEZI Unreviewed; 355 AA.
AC A0A1V8U5K4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
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=B0A51_17048 {ECO:0000313|EMBL:OQO19068.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO19068.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO19068.1}.
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DR EMBL; NAEU01000807; OQO19068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8U5K4; -.
DR STRING; 1974281.A0A1V8U5K4; -.
DR Proteomes; UP000192386; 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:UP000192386};
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 355 AA; 38534 MW; 67F426333CF8BEB9 CRC64;
MCKSALHGFL ADVPKCEHHI HLEGALAPSL LFRLAAKNKI DLPTNDPAFA SPEALTKRYT
NFASLDDFLG YYYIGMSALI TPEDFEALAT DYFEYAAKDA VMHADVFFDP QAHLSRGVSY
ETVLSGFTAA REKAEKNLNI TSTLICCFLR HLPVPESIET FHLSEVQASF ASGAVAGIGI
DSSEVPFPPH LFTPLYAEAA KLGLRLTAHA GEEAGPEYIA SALKDLQVTR IDHGVSLARD
PELMARVAAA GTLLTVCPMS NVFLKCVKSV AEVPIRKFLD AGVKFSLNSD DPAYFGGNYI
GANYCAVQEA FGLTVKEWEG IALAGVQGSW CSDVRREEMV QRVVRFVAQH ASSTS
//
