ID   A0A2H5N764_CITUN        Unreviewed;       531 AA.
AC   A0A2H5N764;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962};
DE            EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962};
GN   ORFNames=CUMW_020000 {ECO:0000313|EMBL:GAY36049.1};
OS   Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY36049.1};
RN   [1] {ECO:0000313|EMBL:GAY36049.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA   Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA   Fujiyama A., Kaminuma E., Nakamura Y.;
RT   "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT   unshiu Marc.) using a hybrid assembly approach.";
RL   Front. Genet. 8:180-180(2017).
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:GAY36049.1}.
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DR   EMBL; BDQV01000003; GAY36049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5N764; -.
DR   STRING; 55188.A0A2H5N764; -.
DR   UniPathway; UPA00053; UER00087.
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}.
FT   DOMAIN          258..338
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          378..448
FT                   /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT                   reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01488"
FT   DOMAIN          499..524
FT                   /note="SDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18317"
SQ   SEQUENCE   531 AA;  57384 MW;  686BAB1B973E7A53 CRC64;
     MESPNLLVAS GSKLVSGGMR KNPTLICVPI MGESVDKMVV DMGKANASGA DLVEIRLDGL
     KNFNPRENIK TLIKESPVPT LFTYRPIWEG GQYDGDENER VDVLRLAMEL GADYIDVELQ
     VAREFNDSIR GKKPEKCKVI VSSHNYQYTP SVEDLSNLVA RIQASGADIV KFATTALDIT
     DVAHVFQITV HSQVPIIGLV MGERGLISRI LCAKFGGFLT FGTLENGIVS APGQPTIKDL
     LDLYNFRQMG PDTKVFGIIG KPVGHSKSPI LYNEAFKSVG FNGVYVHLLV DDIAKFFQTY
     SSNDFAGFSC TIPHKEAAVK CCDEVDPVAK SIGAVNCIIR RQSDGKLFGY NTDCVGAISA
     IEDGLRGRLN VSGGVSSALA GKLFVVIGAG GAGKALAYGA KAKGARVVIA NRTYDRAREL
     AETVGGHALS LADLENFNPE DGMILANTTS IGMQPKVDET PIPKHALGHY ALVFDAVYTP
     KITRLLREAE ESGATIVSGL EMFIGQAYEQ YERFTGLPAP KELFQKIMAK Y
//