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Database: UniProt
Entry: D7M1U8_ARALL
LinkDB: D7M1U8_ARALL
Original site: D7M1U8_ARALL 
ID   D7M1U8_ARALL            Unreviewed;       355 AA.
AC   D7M1U8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Adenosine/AMP deaminase family protein {ECO:0000313|EMBL:EFH51076.1};
GN   ORFNames=ARALYDRAFT_911747 {ECO:0000313|EMBL:EFH51076.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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:0000256|ARBA:ARBA00036622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC         Evidence={ECO:0000256|ARBA:ARBA00036622};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR   EMBL; GL348718; EFH51076.1; -; Genomic_DNA.
DR   RefSeq; XP_002874817.1; XM_002874771.1.
DR   AlphaFoldDB; D7M1U8; -.
DR   STRING; 81972.D7M1U8; -.
DR   EnsemblPlants; scaffold_603804.1; scaffold_603804.1; scaffold_603804.1.
DR   GeneID; 9310884; -.
DR   Gramene; scaffold_603804.1; scaffold_603804.1; scaffold_603804.1.
DR   KEGG; aly:9310884; -.
DR   eggNOG; KOG1097; Eukaryota.
DR   HOGENOM; CLU_039228_3_0_1; -.
DR   OrthoDB; 20281at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR   CDD; cd00443; ADA_AMPD; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR001365; A_deaminase_dom.
DR   InterPro; IPR006330; Ado/ade_deaminase.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR   PANTHER; PTHR11409:SF42; ADENOSINE DEAMINASE-LIKE PROTEIN; 1.
DR   Pfam; PF00962; A_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   DOMAIN          8..343
FT                   /note="Adenosine deaminase"
FT                   /evidence="ECO:0000259|Pfam:PF00962"
SQ   SEQUENCE   355 AA;  40102 MW;  B780E22D226888DA CRC64;
     MEWIKSMPKI ELHAHLNGSI RDSTLLELAR VLGEKGVIVF ADVEHVIRKN DRSLVEVFKL
     FDLIHKLTTD HKTVTRITRE VVEDFALENV VYLELRTTPK RNDSIGMSKR SYMDAVIEGL
     RSVSEVDIDF VTASDSQKLL NACDGIGRKK IYVRLLLSID RRETTESAME TVKLALEMRD
     VGVVGIDLSG NPLVGEWSTF LPALQFAKDS NLHITLHCGE VPNPKEIQAM LDFKPHRIGH
     ACFFKDEDWT KLKSFRTPVE ICLTSNIITK SISSIDIHHF ADLYNANHPL ILCTDDFGVF
     STSLSNEYAL AVRSFGLSKR ETFALARTAI DATFAEDEVK QQLWLIFDSA SPEYA
//
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