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
//