ID A0A1I8PLX3_STOCA Unreviewed; 505 AA.
AC A0A1I8PLX3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=adenosine deaminase {ECO:0000256|ARBA:ARBA00012784};
DE EC=3.5.4.4 {ECO:0000256|ARBA:ARBA00012784};
GN Name=106095808 {ECO:0000313|EnsemblMetazoa:SCAU009293-PC};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU009293-PC, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU009293-PC}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU009293-PC};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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_013118640.1; XM_013263186.1.
DR AlphaFoldDB; A0A1I8PLX3; -.
DR EnsemblMetazoa; SCAU009293-RC; SCAU009293-PC; SCAU009293.
DR GeneID; 106095808; -.
DR VEuPathDB; VectorBase:SCAU009293; -.
DR Proteomes; UP000095300; Unassembled WGS sequence.
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:SF47; 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 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..505
FT /note="adenosine deaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009326865"
FT DOMAIN 14..103
FT /note="Adenosine/AMP deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08451"
FT DOMAIN 195..486
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
SQ SEQUENCE 505 AA; 58624 MW; CB5CEC3345FAA02D CRC64;
MAQLAECMKM MLILSVLMLM NSVYAMELSY DALRAKIMEA ERASSLGGNV WLSSAEEKAN
SILMNAKKEE INEGLKDPTK YPPSMHFFQG KQFLRQSEVF RIIQKMPKGA LLHAHNKGMV
SSKWVIGNLT NLYNLYTCRD VSGLLIFTYD QAQCHSEITN VCLERVNAED KRVYEKRLEK
HISMYTMHPE SMITDTRKIW KRFENIFVSM DQMFKYQPAF CNYHKRLLEE LCEDNIIYAE
IRASLSPLYG DNNRTFNSLE VATELEKIVE SFKVKHPDFL GLKIIYAKRN KGTVDEMAQR
IMTFKQLHNA KPNFIIGFDL IGNEDTGDPL QKFANELTDL PPTANFFFHA GETNWYGKSD
WNMMDALLLN TKRIGHGFAL PKHPQLWSTI KKRNIAIEVN PLSNQVLGYI WDLRNHPASF
LIAENFPIII SSDDPGLWNA KGLSYDFYYA FMAFAPAEAD LRFLKQLALN SIKYSILTSE
ERRKINRIFQ KKWEEFIYNV INMKF
//