ID A0A3B4VJJ3_SERDU Unreviewed; 506 AA.
AC A0A3B4VJJ3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN Name=ADA2 {ECO:0000313|Ensembl:ENSSDUP00000030717.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000030717.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000030717.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001466};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. ADGF subfamily.
CC {ECO:0000256|ARBA:ARBA00006083}.
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DR AlphaFoldDB; A0A3B4VJJ3; -.
DR STRING; 41447.ENSSDUP00000030717; -.
DR Ensembl; ENSSDUT00000031252.1; ENSSDUP00000030717.1; ENSSDUG00000022125.1.
DR GeneTree; ENSGT00950000183113; -.
DR OMA; SMKQCIE; -.
DR OrthoDB; 4403at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0046936; F:2'-deoxyadenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006154; P:adenosine catabolic process; IEA:InterPro.
DR CDD; cd01321; ADGF; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
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 NCBIfam; TIGR01431; adm_rel; 1.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF45; ADENOSINE DEAMINASE 2-A; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF08451; A_deaminase_N; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..506
FT /note="adenosine deaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017202139"
FT DOMAIN 31..97
FT /note="Adenosine/AMP deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08451"
FT DOMAIN 198..487
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 506 AA; 57735 MW; 6C78DA8F2E44DA93 CRC64;
MAVELQCPQA AVACLFLLQC LTGGLSIPDP RQREALIKLE ISMQTGGQLV LTDAEQRLDS
VLFKMKQKEI VGPDCPPAMH FFKARHLIKT SPIFSLLQKM PKGGALHVHD FSMVNVEWLV
KNVTYRPHCY MCFTDSQSIR FIFSSQWPKP LPHCSPWILL ENLRAKMINT TDLDNSIMGN
LTLFTDQDPE TVYPSQDVVW DRFEQSFLAV WGLVTYAPVF RDYYYQGLTE FYMDNIMYLE
LRALLPEIYE LDGSTHDTAW TLKTYQEVTR QFTTDHPDFY GARIIFTVHR GVNISTMTGA
VEKAMKLQRD FPDIMAGFDL VGREDTGRPL WYFRDALSLP VERGVTLPFF FHAGETDLEG
TEVDQNLLDA LLFNTSRIGH GFALLRHPVA KDLYRRRDVA AEVCPISNQV LMLVNDLRNH
PAAALMSENH PMVISSDDPA MFGTSGLSYD FYEVFVGFGG LRSNVGSLKE LATNSIRYSS
LTPKQQEEAL ALWQRRWDRF VSENAF
//