GenomeNet

Database: UniProt
Entry: A0A251R3M8_PRUPE
LinkDB: A0A251R3M8_PRUPE
Original site: A0A251R3M8_PRUPE 
ID   A0A251R3M8_PRUPE        Unreviewed;       901 AA.
AC   A0A251R3M8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE            EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN   ORFNames=PRUPE_1G265900 {ECO:0000313|EMBL:ONI30671.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI30671.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI30671.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP
CC       from AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004955}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM007651; ONI30671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251R3M8; -.
DR   STRING; 3760.A0A251R3M8; -.
DR   EnsemblPlants; ONI30671; ONI30671; PRUPE_1G265900.
DR   Gramene; ONI30671; ONI30671; PRUPE_1G265900.
DR   eggNOG; KOG1096; Eukaryota.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000006882; Chromosome g1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003876; F:AMP deaminase activity; IBA:GO_Central.
DR   GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR   GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01319; AMPD; 1.
DR   Gene3D; 4.10.800.20; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01429; AMP_deaminase; 1.
DR   PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR   PANTHER; PTHR11359:SF14; AMP DEAMINASE; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          58..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  102980 MW;  4EF21403C0B0BCDC CRC64;
     MDSSSSSSSA PSTSSLHLAM AAFVGASLMA VSAFYIHKRS VDQVLQRLIE IRRKPSRISD
     NRSATEDGRE ESYIEDGEER GFESDGEVTD VAIDRNMRPR SVDDKALQSY RISSSLPNVA
     SRSTDWMEEE AKFDPPPNFR PPRFSSSLDK LNFIPSGLPL LRTDQRTGEG QSGNHSGSNT
     RMTPIGRLMT PRSQAGNAFE SIADSDEEGT EFANEDDDTF NYGNVDSLDN TVTSVYQNEV
     LRKSDVKNFI QDRMYQVTST EAKSGVDLQG DGKVDTASGN SVKNDHNFTS IVLPLSASMH
     ESISKEEEEV HKMIRECLDL RKRYLYREEV APWTVARTDS IASEKKSDPF HFEPVEASTH
     CFRMEDGVIH VYASENDTVD IFPVASSTAF FTDMHYLLKV LSIGNVRSAC HHRLRFLEEK
     FRVHLLLNAD REFLAQKSAP HRDFYNVRKV DTHVHHSACM NQKHLLSFIK SKLKKEPDEV
     VIFRDGKYLT LKEVFESLDL TGHDLNVDLL DVHADKSTFH RFDKFNLKYN PCGQSRLREI
     FLKQDNLIQG RFLAEVTKEV LSDLEASRYQ MAEYRISVYG RKQSEWDQLA SWFVNNSIYS
     ENAVWLIQLP RLYNIYKKMG IVTSFQNILD NVFIPLFEAT VNPNSHPQLH LFLMQVVGFD
     VVDDESKPER RPTKHMPTPA EWTNEFNPAY SYYAYYCYAN LYTLNKLRES KGLPTIKFRP
     HCGEAGDIDH LAAGFLLCHN ISHGINLRKT PVLQYLYYLA QVGLLMSPLS NNSLFLDYHR
     NPFPMFFQRG LNVSLSSDDP LQIHLTKEPL VEEYSVAAQV WKLSACDLCE VARNSVYQSG
     FSHVAKSHWL GSKYFLRGPE GNDMQKTNVP HLRIAFRHET WKEEIQYIYA GKAKFPVETD
     P
//
DBGET integrated database retrieval system