GenomeNet

Database: UniProt
Entry: A0A498I2S0_MALDO
LinkDB: A0A498I2S0_MALDO
Original site: A0A498I2S0_MALDO 
ID   A0A498I2S0_MALDO        Unreviewed;       534 AA.
AC   A0A498I2S0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN   ORFNames=DVH24_039440 {ECO:0000313|EMBL:RXH75741.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH75741.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH75741.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH75741.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXH75741.1}.
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; RDQH01000341; RXH75741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498I2S0; -.
DR   STRING; 3750.A0A498I2S0; -.
DR   UniPathway; UPA00053; UER00087.
DR   Proteomes; UP000290289; Chromosome 15.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro.
DR   CDD; cd00502; DHQase_I; 1.
DR   CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00214; AroD; 1.
DR   HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR011342; Shikimate_DH.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   NCBIfam; TIGR01093; aroD; 1.
DR   NCBIfam; TIGR00507; aroE; 1.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   DOMAIN          260..340
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          382..451
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          501..529
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   534 AA;  57741 MW;  952CB75C4EBAB65A CRC64;
     MDSPQNVLLA SDGLQVGVDG VRRSSTVICA PIMAESVDKM VIDMGKAKAL GADLVEIRLD
     HLKDFNCNED LKILIKESPL PTLVTYRPKW EGGQYDGDEK YRLDALRLAM EVGADFIDVE
     LQVAHEFIDS IYGKKPEKFK VIVSSHNYQE TPSVEALGNL VAKIQATGAD IVKIATSALD
     ITDVARIFHV TVHSQVPTIG LVMGERGLIS RILCAKFSGH LTFGTLDSGI VSAPGQPTIK
     DILHLYNFRQ IGPDTKVFGI VGKPVSHSKS PMLYNEAFKS VCFNGVYVHL LVDDIAKFLH
     TYSSKDFAGF SVTIPHKEAA LECCDEVDPV AKAIGAINCI IRRPTDGKLF GFNTDYVGAI
     SAIEDGLKGS HNSGSLTGSP LAGRLFVVIG AGGAGKALAY GAKQKGARIA IANRTYDRAR
     ELADTIGGDA LSLADLDNFH PEDGMILANT TSIGMQPKVD ETPISKHALR SYSLVFDAVY
     TPKMTRLLKE AKESGATVVS GLEMFIGQAY EQFERFTGLP APRELFRRVM DGSS
//
DBGET integrated database retrieval system