ADA_DICDI
ID ADA_DICDI Reviewed; 772 AA.
AC Q54KF3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable adenosine deaminase;
DE EC=3.5.4.4;
DE AltName: Full=Adenosine aminohydrolase;
GN Name=ada; Synonyms=add; ORFNames=DDB_G0287371;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine. Plays an
CC important role in purine metabolism and in adenosine homeostasis, and
CC may thereby contribute to cellular signaling events (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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000100; EAL63753.1; -; Genomic_DNA.
DR RefSeq; XP_637270.1; XM_632178.1.
DR AlphaFoldDB; Q54KF3; -.
DR SMR; Q54KF3; -.
DR STRING; 44689.DDB0230171; -.
DR PaxDb; Q54KF3; -.
DR EnsemblProtists; EAL63753; EAL63753; DDB_G0287371.
DR GeneID; 8626101; -.
DR KEGG; ddi:DDB_G0287371; -.
DR dictyBase; DDB_G0287371; ada.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_362256_0_0_1; -.
DR InParanoid; Q54KF3; -.
DR OMA; YEMCEDA; -.
DR PhylomeDB; Q54KF3; -.
DR Reactome; R-DDI-74217; Purine salvage.
DR PRO; PR:Q54KF3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000034; F:adenine deaminase activity; ISS:dictyBase.
DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006146; P:adenine catabolic process; ISS:dictyBase.
DR GO; GO:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 2.
DR Pfam; PF00962; A_deaminase; 2.
DR SUPFAM; SSF51556; SSF51556; 2.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..772
FT /note="Probable adenosine deaminase"
FT /id="PRO_0000350574"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT SITE 231
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 772 AA; 87516 MW; 00443985D821FEA3 CRC64;
MIENNKEITL DIIKLLPKAE LHRHLDGSIR ISTLLELAKE QNVELPTYDQ NELAKLIHKD
ENCSGLVNFL EAFQYTCSVL QHAYAITRVF YEMCEDAVAD GVSYLEIRFS PVLHTSFGLS
LSEVMEAVCD GMAIAELNLP IKARIIVCGL RHLDPSISKD LAEITWRYRH KGAIAFDLAG
PEDGFSSKHH KEAFSIIRNK GINCTLHSGE DSNWTSVADS IHHCGAHRIG HGIAIQQNEE
LLNHVVNRRI PIECCITSNY QIKAISNASE HPIRKYFDSG AIVSICCDNC TMSNITLSGE
YKLAIDTFNF KVEEVIRLID YSFASSFIDP PLKINIRRES FKKALKIFQT NGYDISGVIE
NKFYYFEEIG LDVELEIQNN LANNFSLGKN VIRNYPQITL ELLENLPKSD LHCRFDGGVS
IEQIWNEVQL LGIDKCEKSK QEFLKKLSSK HLACYANFKD FKEFKSLIQS SSHTPQTIRL
SKEIINLLLQ TPEQINRAFD DIIKVALKDK VQYLELMIRP NSHSRNGLTK EQVLALIIEN
KDKWEKSSSI KIGLVVFSSS TSDDPIETLD SARLAIANRN SGVIGFGIFG ADPISPTESR
HFSQTFSLLK ENNFNLVQFA GKSDVESLIS TIHCSGSTRL SGAFQSHKIP RLMSYLGNYS
IPVEISLTEK LKSFTSDDLS FTTPIRHLLD GKCPVVICSF RSSLYPYSRS KMYYKIVKNA
KLDFKQVVRL LKNPFAYNFQ SHQQRIELVQ QFNKLSKEYL NSVNINYSNI II
