ADA_PLAGA
ID ADA_PLAGA Reviewed; 362 AA.
AC A0A0K1SC59; A0A1J1H1V6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Adenosine deaminase {ECO:0000305};
DE EC=3.5.4.4 {ECO:0000269|PubMed:19728741};
GN Name=ADA {ECO:0000312|EMBL:AKV72186.1};
OS Plasmodium gallinaceum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=5849 {ECO:0000312|Proteomes:UP000220797};
RN [1] {ECO:0000312|EMBL:AKV72186.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=26243218; DOI=10.1186/s12936-015-0814-0;
RA Lauron E.J., Aw Yeang H.X., Taffner S.M., Sehgal R.N.;
RT "De novo assembly and transcriptome analysis of Plasmodium gallinaceum
RT identifies the Rh5 interacting protein (ripr), and reveals a lack of EBL
RT and RH gene family diversification.";
RL Malar. J. 14:296-296(2015).
RN [2] {ECO:0000312|Proteomes:UP000220797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8A {ECO:0000312|Proteomes:UP000220797};
RG Pathogen Informatics;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=19728741; DOI=10.1021/bi9012484;
RA Ho M.C., Cassera M.B., Madrid D.C., Ting L.M., Tyler P.C., Kim K.,
RA Almo S.C., Schramm V.L.;
RT "Structural and metabolic specificity of methylthiocoformycin for malarial
RT adenosine deaminases.";
RL Biochemistry 48:9618-9626(2009).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to produce
CC inosine (PubMed:19728741). Unlike other Plasmodium adenosine
CC deaminases, does not catalyze the deamination of 5'-methylthioadenosine
CC (MTA) (PubMed:19728741). Plays an essential role in the purine salvage
CC pathway which allows the parasite to use host cell purines for the
CC synthesis of nucleic acids (Probable). {ECO:0000269|PubMed:19728741,
CC ECO:0000305|PubMed:19728741}.
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:0000269|PubMed:19728741};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A5KE01};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:A5KE01};
CC -!- ACTIVITY REGULATION: Inhibited by coformycin but not by
CC methylthiocoformycin (MT-coformycin). {ECO:0000269|PubMed:19728741}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for adenosine (at pH 8) {ECO:0000269|PubMed:19728741};
CC Note=kcat is 1.9 sec(-1) with adenosine as substrate.
CC {ECO:0000269|PubMed:19728741};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000305|PubMed:19728741}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- CAUTION: Unlike other Plasmodium adenosine deaminases, lacks S-methyl-
CC 5'-thioadenosine deaminase activity due to the presence of a Glu
CC residue at position 171 instead of an Asp residue.
CC {ECO:0000269|PubMed:19728741}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CRG97310.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KP164513; AKV72186.1; -; mRNA.
DR EMBL; CVMV01000096; CRG97310.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0A0K1SC59; -.
DR SMR; A0A0K1SC59; -.
DR VEuPathDB; PlasmoDB:PGAL8A_00488900; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000220797; Unassembled WGS sequence.
DR GO; GO:0004000; F:adenosine deaminase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Purine salvage; Zinc.
FT CHAIN 1..362
FT /note="Adenosine deaminase"
FT /id="PRO_0000451866"
FT REGION 169..183
FT /note="Gating helix loop; regulates binding affinity for
FT substrates and thus substrate selectivity"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 43..45
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 200
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 228
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 252
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 309
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:A5KE01"
SQ SEQUENCE 362 AA; 42492 MW; 2EF8886153E72C03 CRC64;
MTILHEEINF LKKDELNINL KCLDKKERYK IWRRIPKCEL HCHLDLCFSL EFFLKCVRKY
NLQPDLTDDE VVDYYLFKDK GKSLNEFIER SRRVTDIFIN YDIIKDIAKN AVFNKYKEGV
ILIEFRYSPS YIAYKYNLCI DLIHKTIVEG INEAVEKLNH KIHVGLICIG ETGISEESLR
KAAEFCVKNK KDFVGFDHAG HERDLKPYKE IYDYVRENGI PLTIHAGEDL TLPNLNTIYS
AIEVLKAKRI GHGIRVIESE DLINLIKKND ILLEICPISN LLLNNVKSMD THPIKKLYDS
GIKVSVNTDD PGMFLTEIND EYEELYLNLN FNLEDFMKMN LWALEKSFVK SEIKDKLKKL
YF
