ADAL_DROPS
ID ADAL_DROPS Reviewed; 340 AA.
AC Q295P6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Adenosine deaminase-like protein;
DE EC=3.5.4.-;
GN ORFNames=GA11319;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of the free cytosolic methylated
CC adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol
CC monophosphate (IMP) and methylamine. Is required for the catabolism of
CC cytosolic N6-mAMP, which is derived from the degradation of mRNA
CC containing N6-methylated adenine (m6A). {ECO:0000250|UniProtKB:Q6DHV7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine;
CC Xref=Rhea:RHEA:16001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:59338, ChEBI:CHEBI:144842;
CC Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q6DHV7};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6DHV7}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; CM000070; EAL28662.2; -; Genomic_DNA.
DR RefSeq; XP_001359516.2; XM_001359479.3.
DR AlphaFoldDB; Q295P6; -.
DR SMR; Q295P6; -.
DR STRING; 7237.FBpp0284548; -.
DR EnsemblMetazoa; FBtr0286110; FBpp0284548; FBgn0071373.
DR GeneID; 4802632; -.
DR KEGG; dpo:Dpse_GA11319; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_3_0_1; -.
DR InParanoid; Q295P6; -.
DR OMA; RPQFKPY; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0071373; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0062154; F:N6-mAMP deaminase activity; IEA:RHEA.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..340
FT /note="Adenosine deaminase-like protein"
FT /id="PRO_0000285095"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 16
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 18
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 68
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 100..103
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 173
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 203
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 278
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 279
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT SITE 223
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
SQ SEQUENCE 340 AA; 38455 MW; 36085C55097A763B CRC64;
MWKFLKEMPK VELHAHLNGS LNTNSLQDLA EKVYGNTSEE FSHLCARFVN FEKDSNLDKC
FEKFAFVHEL TSTAAGLQYA TELVIRDFAN DNIQYLELRT TPKANKNYLR RDYLRIVLDT
IKRSRKKYPN ILVKLLPSIN RSEPVAVAEE TVALALEFAK TDPDLVVGID LSGIPTKGKF
TDFCGALDLA RREGLKLVIH CAEIDNPPEI KEMLSFGMSR CGHGTYLTEE DFAQMKAANI
PIECCLTSNI KSGSVSSFEE HHLKRLMESD APRVVCTDDS GVFDTSLTNE FLLVVETFNV
TRDQCIDLTL EAVKHSFASE QERQQMALKV EHYVNSLQTD
