ADA_CHICK
ID ADA_CHICK Reviewed; 357 AA.
AC Q5ZKP6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Adenosine deaminase;
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:P00813};
DE AltName: Full=Adenosine aminohydrolase;
GN Name=ADA; ORFNames=RCJMB04_9m8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720038; CAG31697.1; -; mRNA.
DR RefSeq; NP_001006290.1; NM_001006290.2.
DR AlphaFoldDB; Q5ZKP6; -.
DR SMR; Q5ZKP6; -.
DR STRING; 9031.ENSGALP00000006620; -.
DR PaxDb; Q5ZKP6; -.
DR GeneID; 419194; -.
DR KEGG; gga:419194; -.
DR CTD; 100; -.
DR VEuPathDB; HostDB:geneid_419194; -.
DR eggNOG; KOG1097; Eukaryota.
DR InParanoid; Q5ZKP6; -.
DR OrthoDB; 1045809at2759; -.
DR PhylomeDB; Q5ZKP6; -.
DR BRENDA; 3.5.4.4; 1306.
DR PRO; PR:Q5ZKP6; -.
DR Proteomes; UP000000539; 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; 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..357
FT /note="Adenosine deaminase"
FT /id="PRO_0000194355"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
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 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56658"
FT BINDING 185
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 357 AA; 40679 MW; 207806303E3FD54E CRC64;
MERGVRVFGE PKVELHIHLD GAIRPETILH FGKKRGVPLP GSTVDELMKH VSYQTPLSLK
LFLEKFNHYM PAIAGDREAV RRIAYELVET KAKEGVVYVE VRYSPHLLAN CRVEPIPWGQ
AEGDLTPEEV VNLVNQGLQD GERNFRIKAR SILCCMRHMP SWSPEVVELC KKYQNNSVVA
IDLAGDELLM ASSDHKAAYE EAERCGIHRT VHAGEAGPAT MIKEAVYLLK AERIGHGYHV
LEDPELYREL LRTRMHFEVC PWSSYLTGAC LPDFRKHPVV QFKKDQANYS INTDDPLIFN
SNIDKDYGIV KEYMDFTEED FKRVNINAAQ SSFLPEKEKQ ELLNTLYEAY GMVPATS
