ID   A0A3B4ZKG7_9TELE        Unreviewed;       503 AA.
AC   A0A3B4ZKG7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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:ENSSPAP00000009418.1};
GN   Synonyms=LOC103365027 {ECO:0000313|RefSeq:XP_008290577.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000009418.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000009418.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008290577.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
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   RefSeq; XP_008290577.1; XM_008292355.1.
DR   AlphaFoldDB; A0A3B4ZKG7; -.
DR   STRING; 144197.ENSSPAP00000009418; -.
DR   Ensembl; ENSSPAT00000009583.1; ENSSPAP00000009418.1; ENSSPAG00000007168.1.
DR   GeneID; 103365027; -.
DR   CTD; 373884; -.
DR   GeneTree; ENSGT00950000183113; -.
DR   OrthoDB; 4403at2759; -.
DR   Proteomes; UP000261400; Unplaced.
DR   Proteomes; UP000694891; 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   Reference proteome {ECO:0000313|Proteomes:UP000694891};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..503
FT                   /note="adenosine deaminase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041086994"
FT   DOMAIN          28..94
FT                   /note="Adenosine/AMP deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08451"
FT   DOMAIN          197..485
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   503 AA;  57177 MW;  0BA699BBA44A1ADB CRC64;
     MAVPLQRPHV VCVLLCCLTT GLSIPDPRQR EALIKQEASM QTGGQVVLTD AEQRLDDLLV
     KMKQEEMAKA DFPPSMHFFK ARDLIRSSPI FSLLQKMPKG GALHLHDLAI VDVEWLVKNV
     TYRPHCYMCL TDDRSIRFVF SSQQPKPLLH CSTWMLLEDL RAKMANVTDL DNSIRGNLTL
     FTDQDPEVAY PSQDVVWKIF EQKFQALWGL VTYVPVFKDY FYQGLSEFYV DNVMYLELRV
     LLPELYELDG CSYDKAYTLK TYQDVTKQFR ANHPDFFGMK VIFTVHRQVN ASVMTGVVEE
     AMKLQKDFPD FMAGFDLVGR EDSGKPLWYF RDALSLPADR GVPMPFFFHA GETNLQGTEV
     DENLLDALLL NTSRIGHGFA LPRHPLAKDM SRRRGVALEV CPISNQVMNM VKDLRNHPAA
     ALMSEDHPMV ISSDDPGIFG ASGLSYDFYI AFVGFGGIRS HVGSLKQLAI NSIRYSALSQ
     KQQEEALALW QTKWNKFVSE NAF
//