ADAL_DANRE
ID ADAL_DANRE Reviewed; 348 AA.
AC Q4V9P6; A7MCN2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Adenosine deaminase-like protein;
DE EC=3.5.4.-;
GN Name=adal; ORFNames=zgc:109912;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; BC096787; AAH96787.1; -; mRNA.
DR EMBL; BC152246; AAI52247.1; -; mRNA.
DR RefSeq; NP_001028916.1; NM_001033744.1.
DR AlphaFoldDB; Q4V9P6; -.
DR SMR; Q4V9P6; -.
DR STRING; 7955.ENSDARP00000067287; -.
DR PaxDb; Q4V9P6; -.
DR PRIDE; Q4V9P6; -.
DR DNASU; 619263; -.
DR GeneID; 619263; -.
DR KEGG; dre:619263; -.
DR CTD; 161823; -.
DR ZFIN; ZDB-GENE-050913-145; adal.
DR eggNOG; KOG1097; Eukaryota.
DR InParanoid; Q4V9P6; -.
DR OrthoDB; 981145at2759; -.
DR PhylomeDB; Q4V9P6; -.
DR Reactome; R-DRE-2161541; Abacavir metabolism.
DR Reactome; R-DRE-74217; Purine salvage.
DR PRO; PR:Q4V9P6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central.
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:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..348
FT /note="Adenosine deaminase-like protein"
FT /id="PRO_0000285092"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 20
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 22
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 142
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 175
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 205
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 287
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 288
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT SITE 226
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT CONFLICT 279
FT /note="G -> R (in Ref. 1; AAI52247)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="I -> R (in Ref. 1; AAI52247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39190 MW; 8C48166D231CB39C CRC64;
MDTEADLFYR QLPKVELHAH LNGSVSFETM EKLIKRKPHL NIEHSMTAIR RGQRRTLDEC
FQVFKVIHQL VDSEEDILMV AKSVIQEFAA DGVKYLELRS TPREVTETGL SKQRYIETVL
EAIRQCKQEG VDIDVRFLVA VDRRHGPEVA MQTVKLAEDF LLSSDGTVVG LDLSGDPTVG
HGKDLLAALQ KAKNCGLKLA LHLSEVPSQI DETELLLNLP PDRIGHGTFL HPDVGGSDSL
VDKVCKQNIP IEICLTSNVK GQTVPSYDKH HFKYWYNRGH PCVLCTDDKG VFCTDLSQEY
QLAASTFGLT KEAVWILSQQ AIGYTFAPEP IKQRLEKTWA ELKQQILQ
