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Database: UniProt
Entry: A0A2D0RH14_ICTPU
LinkDB: A0A2D0RH14_ICTPU
Original site: A0A2D0RH14_ICTPU 
ID   A0A2D0RH14_ICTPU        Unreviewed;       504 AA.
AC   A0A2D0RH14;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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=ada2a {ECO:0000313|RefSeq:XP_017329819.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017329819.1};
RN   [1] {ECO:0000313|RefSeq:XP_017329819.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017329819.1};
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}.
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DR   RefSeq; XP_017329819.1; XM_017474330.3.
DR   AlphaFoldDB; A0A2D0RH14; -.
DR   STRING; 7998.ENSIPUP00000016784; -.
DR   Ensembl; ENSIPUT00000017494; ENSIPUP00000016784; ENSIPUG00000011401.
DR   Ensembl; ENSIPUT00000017502; ENSIPUP00000016792; ENSIPUG00000011401.
DR   GeneID; 108268949; -.
DR   KEGG; ipu:108268949; -.
DR   CTD; 373884; -.
DR   OMA; SMKQCIE; -.
DR   OrthoDB; 4403at2759; -.
DR   Proteomes; UP000221080; Chromosome 8.
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..504
FT                   /note="adenosine deaminase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012135491"
FT   DOMAIN          31..97
FT                   /note="Adenosine/AMP deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08451"
FT   DOMAIN          196..490
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   504 AA;  57452 MW;  1EAD5A0908934611 CRC64;
     MCVPPWRIQL PLTWLLLLCF TPRCSSRPDP HQREVLIKME ASREIGGGVV LNKKEQLLDK
     KLYQMKQQEI AAPDFPPAMH FFKAKSLIDA SPVFSILQKM PKGAALHVHD FSMVGVEWLV
     KNVTYRENCY VCFTNNSFVR FVFSSVQPKA ASYCSTWTLL KTMREKYNTT ELDNSFIRNL
     TLFTEDPDSD YPNQDVVWER FEQAFLVAYG LVTHAPVFKD YLYEGFRQFQ MDNIMYVEIR
     ALLPLTYELD GRKNSRDWSM RACQEVLQRF TAQYPDFLGA RFIFTVHRGL NSTQAVQVVE
     EAMLLQRNFP DIMAGFDFVG REDSGNPLWY FKKALGLPEE RGVQLPYFFH AGETDSEGTA
     VDQNMMDALL FNTSRIGHGF AMPRHPVVKE LARKIGVAVE VCPISNQVLK LVSDMRNHPA
     AVLMAEGYPM VISSDDPALF GATGLSYDFY QAFVGFGGMK SNLATLKELV LNSLRYSSLS
     PTLKKKAIAA LLVKWDKFVS ETLL
//
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