ADAL_CAEEL
ID ADAL_CAEEL Reviewed; 388 AA.
AC Q8IG39;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Adenosine deaminase-like protein;
DE EC=3.5.4.- {ECO:0000250|UniProtKB:Q6DHV7};
GN Name=adal-1 {ECO:0000312|WormBase:C44B7.12};
GN ORFNames=C44B7.12 {ECO:0000312|WormBase:C44B7.12};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; BX284602; CCD61565.1; -; Genomic_DNA.
DR RefSeq; NP_871955.2; NM_182155.4.
DR AlphaFoldDB; Q8IG39; -.
DR SMR; Q8IG39; -.
DR STRING; 6239.C44B7.12; -.
DR EPD; Q8IG39; -.
DR PaxDb; Q8IG39; -.
DR PeptideAtlas; Q8IG39; -.
DR DNASU; 259441; -.
DR EnsemblMetazoa; C44B7.12.1; C44B7.12.1; WBGene00016632.
DR GeneID; 259441; -.
DR KEGG; cel:CELE_C44B7.12; -.
DR UCSC; C44B7.12; c. elegans.
DR CTD; 259441; -.
DR WormBase; C44B7.12; CE39336; WBGene00016632; adal-1.
DR eggNOG; KOG1097; Eukaryota.
DR GeneTree; ENSGT00950000183113; -.
DR HOGENOM; CLU_039228_3_0_1; -.
DR InParanoid; Q8IG39; -.
DR OMA; RPQFKPY; -.
DR OrthoDB; 981145at2759; -.
DR PhylomeDB; Q8IG39; -.
DR Reactome; R-CEL-2161541; Abacavir metabolism.
DR Reactome; R-CEL-74217; Purine salvage.
DR PRO; PR:Q8IG39; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016632; Expressed in adult organism and 3 other tissues.
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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Nucleotide metabolism; Reference proteome; Zinc.
FT CHAIN 1..388
FT /note="Adenosine deaminase-like protein"
FT /id="PRO_0000285096"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 67
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 114
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 146..149
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 186
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 218
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 248
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 326
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 327
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT SITE 269
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
SQ SEQUENCE 388 AA; 44922 MW; 845DFD0ADA36B923 CRC64;
MPNNSKHKKK QQRRQQEAQK KSRAKQIETD KKNDEFLDTE LDEVSPLVID DDMTEFKNMP
KVELHAHLSG SLSPETIKLI MESDETRAEE IMKKYKLEKP ENMTGVFDCF PVIHAILRKP
EAIRIAIRQT IKEFEEDNCV YLELRTSPKE TDFMTYEDYL QVCIESFEAA KHEFPRIKTF
LIVSLDRRMP FETAAHILGL IGEAQQRTNV IVGVELSGDP HLDGRRLLKL FVAARRFHGL
GITIHLAEVL QNMADVEDYL NLRPDRIGHG TFLHTDPYTE YLTNKYKIPL EICLSSNVYS
KTTTNYRNSH FNYWRKRGVP VFICTDDKGV IPGATLTEEY YKAAITFDLS TEELIGINQD
ALLNSFAYKY NVTDLTETFR KINNNVLD
