ADA_XENLA
ID ADA_XENLA Reviewed; 358 AA.
AC Q6GP70;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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; BC073271; AAH73271.1; -; mRNA.
DR RefSeq; NP_001085740.1; NM_001092271.1.
DR AlphaFoldDB; Q6GP70; -.
DR SMR; Q6GP70; -.
DR DNASU; 444167; -.
DR GeneID; 444167; -.
DR KEGG; xla:444167; -.
DR CTD; 444167; -.
DR Xenbase; XB-GENE-950506; ada.S.
DR OrthoDB; 1045809at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 444167; Expressed in muscle tissue and 16 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:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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:0046103; P:inosine biosynthetic process; ISS:UniProtKB.
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 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_0000194357"
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; 40676 MW; C6119F12592CB059 CRC64;
MESKAFNKPK VELHVHLDGS IKPETIIHFA KKRQIKLPAD TVEGLLEHVS YKEPLSLTEF
LQKFNHYMPA IAGDREAIKR IAYEFVEMKA KEGVIYVEVR YSPHFLANSK VDPIPWGQKE
GDITPDEVVD LVNQGLRKGE KTFNIKARSI LCCMRHMPNW SSEVIELCKK YQNDTVVAID
LAGDESLNCE SYPGHRKAYE EAVKCGIHRT VHAGEVGPPS VVKEAVEVLK AERIGHGYHT
TEDPNLYKEL LENNMHFEVC PWSSYLTSAC HPDFTKHPAT QFRKDKANFS LNTDDPLIFG
STLDVDYSIA VQHMGFTEDE FKRVNINAAK SSFLPDNEKK ELLYKLYEAY GMILSTGL
