ADA_DANRE
ID ADA_DANRE Reviewed; 359 AA.
AC Q6DG22;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Adenosine deaminase;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P00813};
DE AltName: Full=Adenosine aminohydrolase;
GN Name=ada;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-
CC deoxyadenosine. Plays an important role in purine metabolism and in
CC adenosine homeostasis. Modulates signaling by extracellular adenosine,
CC and so contributes indirectly to cellular signaling events. May act as
CC a positive regulator of T-cell coactivation (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+);
CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4;
CC Evidence={ECO:0000250|UniProtKB:P00813};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P03958};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P03958};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction
CC {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Lysosome
CC {ECO:0000250|UniProtKB:P00813}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH76532.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC076532; AAH76532.1; ALT_INIT; mRNA.
DR RefSeq; NP_001002646.1; NM_001002646.1.
DR AlphaFoldDB; Q6DG22; -.
DR SMR; Q6DG22; -.
DR STRING; 7955.ENSDARP00000005284; -.
DR PaxDb; Q6DG22; -.
DR PeptideAtlas; Q6DG22; -.
DR PRIDE; Q6DG22; -.
DR GeneID; 436919; -.
DR KEGG; dre:436919; -.
DR CTD; 100; -.
DR ZFIN; ZDB-GENE-040718-393; ada.
DR eggNOG; KOG1097; Eukaryota.
DR InParanoid; Q6DG22; -.
DR OrthoDB; 1045809at2759; -.
DR PhylomeDB; Q6DG22; -.
DR Reactome; R-DRE-74217; Purine salvage.
DR PRO; PR:Q6DG22; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004000; F:adenosine deaminase activity; IDA:CACAO.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006154; P:adenosine catabolic process; ISS:UniProtKB.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0060169; P:negative regulation of adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_00540; A_deaminase; 1.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR028893; A_deaminase.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Hydrolase;
KW Lysosome; Membrane; Metal-binding; Nucleotide metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="Adenosine deaminase"
FT /id="PRO_0000194356"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT SITE 237
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
SQ SEQUENCE 359 AA; 40844 MW; B389F4EC527586A7 CRC64;
MNGKPAFDKP KVELHVHLDG AIRLKTVLDV AKRRGISLPV SMEEELKELC TVNEPATLTE
FLGKFSHFMH VIAGDREAIK RIAYEFVETK AKEGVIYVEA RYSPHFLANK GVEPLPWDQK
PGDITPDDVV DLVNQGFKEG EQAFKTKARS ILCCMRHMPN WSMEVVELCK KFHKDGVVAI
DLAGDESMNC ESYPGHKKAF EEAVRSNVHR TVHAGEVGPA SVVREAVEVL KAERIGHGYH
TLEDQNLYKQ LLHQNMHFEM CPVSSRLTGA CEPDFTKHPL ITFKKDKANY SLNTDDPTIF
NSTLNSDYEV VQKYMDFTEE EFKRLNINAA KSCFLPEKEK EKLLNQLYEA YGMRKSTSF
