ADA_XENTR
ID ADA_XENTR Reviewed; 358 AA.
AC Q63ZU0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Adenosine deaminase;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P00813};
DE AltName: Full=Adenosine aminohydrolase;
GN Name=ada;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-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}.
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DR EMBL; BC082820; AAH82820.1; -; mRNA.
DR RefSeq; NP_001011025.1; NM_001011025.1.
DR AlphaFoldDB; Q63ZU0; -.
DR SMR; Q63ZU0; -.
DR STRING; 8364.ENSXETP00000009691; -.
DR PaxDb; Q63ZU0; -.
DR DNASU; 496434; -.
DR GeneID; 496434; -.
DR KEGG; xtr:496434; -.
DR CTD; 100; -.
DR Xenbase; XB-GENE-950501; ada.
DR eggNOG; KOG1097; Eukaryota.
DR InParanoid; Q63ZU0; -.
DR OrthoDB; 1045809at2759; -.
DR Reactome; R-XTR-74217; Purine salvage.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003459; Expressed in skeletal muscle tissue and 14 other tissues.
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; ISS:UniProtKB.
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..358
FT /note="Adenosine deaminase"
FT /id="PRO_0000194358"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 294
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="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT SITE 236
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
SQ SEQUENCE 358 AA; 40555 MW; FBE993ECF3A080D2 CRC64;
MESKAFNKPK VELHVHLDGS IKPETIIHFA KKRQIKLPAD TVEGLLEHVS YKEPLSLTEF
LSKFNHYMPA IAGDREAIKR IAYEFVEMKA KEGVIYVEVR YSPHFLANSK VEPIPWGQKE
GDITPDEVVD LVNQGLRKGE KAFNIKARSI LCCMRHMPSW STEVVELCKK YQNDTVVAID
LAGDESLNCE SYPGHRKAYE EAVKCGIHRT VHAGEVGPSS VVKEAVEVLK AERIGHGYHT
TEDPNLYKEL LEKNMHFEVC PWSSYLTGAC HPDFTKHPAT QFRKDKANYS LNTDDPLIFG
STLDVDYSIA AKHMGFTEEE FKRVNINAAK SSFLPESEKK ELLYKLYEAY GMILSTGL
