ID   A0A3Q3ADD0_KRYMA        Unreviewed;       520 AA.
AC   A0A3Q3ADD0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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:ENSKMAP00000014080.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000014080.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000014080.1}
RP   IDENTIFICATION.
RG   Ensembl;
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}.
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DR   RefSeq; XP_017267151.1; XM_017411662.1.
DR   AlphaFoldDB; A0A3Q3ADD0; -.
DR   STRING; 37003.ENSKMAP00000014080; -.
DR   Ensembl; ENSKMAT00000014290.1; ENSKMAP00000014080.1; ENSKMAG00000010554.1.
DR   GeneID; 108233292; -.
DR   KEGG; kmr:108233292; -.
DR   CTD; 559295; -.
DR   GeneTree; ENSGT00950000183113; -.
DR   OMA; GHGYTIT; -.
DR   OrthoDB; 4403at2759; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   GO; GO:0060837; P:blood vessel endothelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0030223; P:neutrophil differentiation; IEA:Ensembl.
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:SF44; ADENOSINE DEAMINASE; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..113
FT                   /note="Adenosine/AMP deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08451"
FT   DOMAIN          214..501
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   520 AA;  58880 MW;  5BC079AF95E8448B CRC64;
     MFSFTAFSAR RLALRSEDMV VWLWLTLVTS APLLWLVRDT DGMPDPAHRD LLMRQEASRQ
     TGGLLTLTAA ERRLDASLRR LKEQEMSAAR FPPAVHFFKA KPLIERSSIF KLLQKMPKGA
     ALHIHSSSLV GAEWLVRNVT YRPRCYVCFT WDNSVRFLFS ARRPFPRWDC FHWQLLETLR
     ARIGDAAEFD NSLIQHLTLF TEDPDGEYPN QDVVWEKFEK AFIAAAGLVT HAPVLRDYYY
     QGLEELHKDN IMYLELRSGL SRTYELDGTI HDKTWTLNLF QEVTKEFIKD HPDFFGARII
     ISVHRALSVS EVRAAVKEAI QLKKDFPDVV AGFDMVGRED SGRSLWYFRE ALSLPAELGA
     ELPYFFHAGE TDDEGTDVDQ NVLDALLFNA SRLGHAFALA HHPLAKELSR KGNIAVELCP
     ISNQVLKLIS DLRNHPAAVL MSEGHPMVIS SDDPSLFGTS GLSYDFYEAF VGIGGLKANL
     GTLKELAANS IRYSSLPAHL KDIGLVMFQD QWDAFIADNS
//