ADA2_DICDI
ID ADA2_DICDI Reviewed; 543 AA.
AC Q553U5; Q86I77;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Adenosine deaminase 2 {ECO:0000250|UniProtKB:Q9NZK5};
DE EC=3.5.4.4 {ECO:0000250|UniProtKB:Q9NZK5};
DE Flags: Precursor;
GN Name=ADA2 {ECO:0000250|UniProtKB:Q9NZK5}; ORFNames=DDB_G0275179;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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: Adenosine deaminase that may contribute to the degradation of
CC extracellular adenosine, a signaling molecule that controls a variety
CC of cellular responses. May play a role in the regulation of cell
CC proliferation (By similarity). {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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69870.1; -; Genomic_DNA.
DR RefSeq; XP_643866.1; XM_638774.1.
DR AlphaFoldDB; Q553U5; -.
DR SMR; Q553U5; -.
DR STRING; 44689.DDB0230172; -.
DR PaxDb; Q553U5; -.
DR EnsemblProtists; EAL69870; EAL69870; DDB_G0275179.
DR GeneID; 8619917; -.
DR KEGG; ddi:DDB_G0275179; -.
DR dictyBase; DDB_G0275179; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_022829_3_0_1; -.
DR InParanoid; Q553U5; -.
DR OMA; IFPGMMF; -.
DR PhylomeDB; Q553U5; -.
DR Reactome; R-DDI-5683826; Surfactant metabolism.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q553U5; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR013659; A_deaminase_N.
DR InterPro; IPR006331; ADGF.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF08451; A_deaminase_N; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01431; adm_rel; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Metal-binding; Reference proteome; Secreted;
KW Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..543
FT /note="Adenosine deaminase 2"
FT /id="PRO_0000331430"
FT REGION 31..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 232..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 543 AA; 62616 MW; 06AB0D55BF927061 CRC64;
MFLKFKNIFF IVLTLSIVFN GLIVNSKNIH INNKNNNNNN NNKDLSSSES GSSSDINPYI
SQYNSERETL VNQENQIKLG SNTPFNSKEQ QANTIFLNIL QNEELSFSNN DPSGVNFFIE
KQIIENESTI FKIIQNMPKG SALHVHQDSS ATYDYLISVG SYLPNCYIYL TYDVNDANNG
TFHFYDSQPT DSNWKLLSTI REGVSNVESF DQQLLDSLTL IGQDYGDYVS LWRKFDGIFG
RVNGLVTYLP IATGYMEHLF QQMIQDGVQH IEVRKCFGDF YDLTGKIYDD YWFVQTMEEL
VLTTRQKYNM SEFALKIIGC NGRHNNQSVV YDAMVMSLDL RNKYPSTFVG YDLVGPEDEG
YPLIYFIEQF AEIKKLGYQY QYPLDYYFHA GETILYNNTN LYDAILLNTK RIGHGIQLPK
HPLLMDLVLK NDIGIEICPI SNQILQYVSD MRAHPGLDLL NRGLPVTISP DDPAIFNYGG
LSYDFFELTY SWGLNLQQLK QLAINSINHS NTFNQSEYNL LYNAWEVKWF NFIDYIINTY
SNI
