ID A0A1U7YYL0_NELNU Unreviewed; 358 AA.
AC A0A1U7YYL0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic-like {ECO:0000313|RefSeq:XP_010244660.1};
GN Name=LOC104588429 {ECO:0000313|RefSeq:XP_010244660.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010244660.1};
RN [1] {ECO:0000313|RefSeq:XP_010244660.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_010244660.1; XM_010246358.2.
DR AlphaFoldDB; A0A1U7YYL0; -.
DR STRING; 4432.A0A1U7YYL0; -.
DR GeneID; 104588429; -.
DR KEGG; nnu:104588429; -.
DR eggNOG; KOG0692; Eukaryota.
DR InParanoid; A0A1U7YYL0; -.
DR OrthoDB; 1308at2759; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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_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; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
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 Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT DOMAIN 84..164
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 201..276
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 325..353
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
SQ SEQUENCE 358 AA; 39004 MW; 474074BD5A8D63AC CRC64;
MPIYIIKVLF QYDTTLKFQV PIIGLVMGER GLMSRILCPK FGGYLTFGTL EAGKISAPGQ
PTIKDLLDLY NFRQLGPDTK IYGLLGKPVS HSKGPFLFNA AFKAASFNGV YMPLLVDDVA
KFFDVYSSPD FFGFSCTIPH KEDALKRCDE VHPVAKSIGA VNTIIRRSND GKLSGYNTDY
AGAISAIEDG LRGLHDMHNT IASPLAGKLF IVIGAGGAGK ALAYGAKEKG ARVVIANRTY
SRAKELADMV GGDALSLDEL GDFHPENGMI LANTTSIGMQ PKVDETPIPK KALSSYSLVF
DAVYTPKITR LLREAEESGV TIVTGLEMFI RQAYEQYEKF TGLPAPKQLF REIMATYA
//
