ID I0IBS2_PHYMF Unreviewed; 528 AA.
AC I0IBS2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222};
DE Short=SDH {ECO:0000256|HAMAP-Rule:MF_00222};
DE EC=1.1.1.25 {ECO:0000256|ARBA:ARBA00012962, ECO:0000256|HAMAP-Rule:MF_00222};
GN Name=aroD {ECO:0000313|EMBL:BAM02710.1};
GN Synonyms=aroE {ECO:0000256|HAMAP-Rule:MF_00222,
GN ECO:0000313|EMBL:BAM02710.1};
GN OrderedLocusNames=PSMK_05510 {ECO:0000313|EMBL:BAM02710.1};
OS Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC Phycisphaeraceae; Phycisphaera.
OX NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM02710.1, ECO:0000313|Proteomes:UP000007881};
RN [1] {ECO:0000313|EMBL:BAM02710.1, ECO:0000313|Proteomes:UP000007881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC {ECO:0000313|Proteomes:UP000007881};
RA Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC (SA). {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001648, ECO:0000256|HAMAP-
CC Rule:MF_00222};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000256|ARBA:ARBA00004871, ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00222}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00222}.
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DR EMBL; AP012338; BAM02710.1; -; Genomic_DNA.
DR RefSeq; WP_014435930.1; NC_017080.1.
DR AlphaFoldDB; I0IBS2; -.
DR STRING; 1142394.PSMK_05510; -.
DR GeneID; 80847114; -.
DR KEGG; phm:PSMK_05510; -.
DR eggNOG; COG0169; Bacteria.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_019120_0_0_0; -.
DR OrthoDB; 9792692at2; -.
DR UniPathway; UPA00053; UER00087.
DR Proteomes; UP000007881; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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_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 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00222};
KW Lyase {ECO:0000313|EMBL:BAM02710.1};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00222};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00222,
KW ECO:0000313|EMBL:BAM02710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007881};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT DOMAIN 238..329
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 360..428
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 483..507
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT ACT_SITE 302
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 246..248
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 298
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 327
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 343
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 369..373
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 460
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 462
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 483
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
FT BINDING 490
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00222"
SQ SEQUENCE 528 AA; 54254 MW; 2976B4E53A102A37 CRC64;
MTLLCCPITV NDADDALAAC GRAAEAGADL VEFRCDRFTD DRDALARLVA DASLPCIVTL
RHASEGGGFS GLESLRVGLL LFLSQQPRPP AYLDFEHARL AALSAGERAD LEDAATRCGL
ILSTHDFAGR PADLDRRVLA MADTPGVRVL KAAWAARSLR DNLQAFELIE RRLAPTAALC
MGDAGLPSRV LARKFGGFVT FAAADRASGT APGQPTIAEL RDLYRWDAIG PATRVYGVIG
DPVGHSKSPA LHNAGFDASG FDGVYLPMPI PAGYEHLKAT LSAWLDHGSL RFRGASVTIP
HKADLLRFAE ERGATIDPLA ARIGAANTLI VGEDGALAVR NTDCDAALGV VRRALGGVGL
RGAAVAVLGA GGVSRAVVAG FADAGCRVTV FNRSVERARS LAAAFGVEAA PLAEAAAGAA
DVWINATSIG METAEDPAPD ASPLPDPPGS WGPGTVVFDT VYTPPETRLL RDAAAAGCVT
AGGTAMFLAQ AAAQFEAWTG VEAPEAVFGS GGAGHPAGAI EGFAGDAG
//
