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Database: UniProt
Entry: A0A0D3BQZ1_BRAOL
LinkDB: A0A0D3BQZ1_BRAOL
Original site: A0A0D3BQZ1_BRAOL 
ID   A0A0D3BQZ1_BRAOL        Unreviewed;       838 AA.
AC   A0A0D3BQZ1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=AMP deaminase {ECO:0000256|ARBA:ARBA00012775};
DE            EC=3.5.4.6 {ECO:0000256|ARBA:ARBA00012775};
GN   Name=106342671 {ECO:0000313|EnsemblPlants:Bo4g029670.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo4g029670.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo4g029670.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo4g029670.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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}.
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DR   RefSeq; XP_013637128.1; XM_013781674.1.
DR   AlphaFoldDB; A0A0D3BQZ1; -.
DR   STRING; 109376.A0A0D3BQZ1; -.
DR   EnsemblPlants; Bo4g029670.1; Bo4g029670.1; Bo4g029670.
DR   GeneID; 106342671; -.
DR   Gramene; Bo4g029670.1; Bo4g029670.1; Bo4g029670.
DR   KEGG; boe:106342671; -.
DR   eggNOG; KOG1096; Eukaryota.
DR   HOGENOM; CLU_003782_3_0_1; -.
DR   OMA; RKERGMC; -.
DR   OrthoDB; 20951at2759; -.
DR   UniPathway; UPA00591; UER00663.
DR   Proteomes; UP000032141; Chromosome C4.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:UniProtKB-EC.
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:SF0; 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   Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT   REGION          41..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  94905 MW;  8DEC856B26716948 CRC64;
     MEPNIYQLAL AALFGASFVA VSGFFMHFKA LNLVLERGRE KKDTNNNTEG GDSPQHQSQS
     LSRRRSQVRR KGLSPASLPD ATPFTAATDG GGGDAGRTNG HVCVDEIPPG LPRLHTPSEG
     RSSVHGTNSI RKTGSFVRPI SPKSPVASAS AFESMGESDD DDNLTDTAGL DASYLQTNGD
     LPADATEEQI SMAASSMIRS HSVSGDLHGV QPDPIAADIL RKEPEQETFV RLNVPLEVPT
     SDEVEAYKCL QECLELRKRY VFQETVAPWE KEVISDPSTP KPNLEPFAHY PQGKSDHHFE
     MLDGVVHVFP NKDVKEELFP VADATAFFTD LHHVLKVIAA GNMRTLCHRR LVLLEQKFNL
     HLMLNADKEF LAQKSAPHRD FYNVRKVDTH VHHSACMNQK HLLRFIKSKL RKEPDEVVIF
     RDGTYLTLKE VFESLDLTGY DLNVDLLDVH ADKSTFHRFD KFNLKYNPCG QSRLREIFLK
     QDNLIQGRFL GEITKQVFSD LEASKYQMAE YRISIYGRKM SEWDQLASWI VNNDLYSENV
     VWLIQLPRLY NIYKDMGIVT SFQNILDNIF IPLFEATVDP DSHPQLHVFL KQVVGFDLVD
     DESKPERRPT KHMPTPAQWT NAFNPAFSYY VYYCYANLYV LNKLRESKGM TTITLRPHSG
     EAGDIDHLAA TFLTCHSIAH GINLRKSPVL QYLYYLAQIG LAMSPLSNNS LFLDYHRNPF
     PVFFLRGLNV SLSTDDPLQI HLTKEPLVEE YSIAASVWKL SSCDLCEIAR NSVYQSGFSH
     ALKSHWIGKD YYKRGPDGND IHKTNVPHIR VEFRDTIWKE EMQQVYLGKA VISDEVVP
//
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