AROG2_PETHY
ID AROG2_PETHY Reviewed; 512 AA.
AC A0A067XGX8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic {ECO:0000305};
DE EC=2.5.1.54 {ECO:0000250|UniProtKB:O53512};
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 2 {ECO:0000303|PubMed:24815009};
DE Short=DAHP synthase 2 {ECO:0000305};
DE Short=PhDAHP2 {ECO:0000303|PubMed:24815009};
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=DAHP2 {ECO:0000303|PubMed:24815009};
GN Synonyms=DHS2 {ECO:0000303|PubMed:24815009};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Mitchell; TISSUE=Corolla, and Leaf;
RX PubMed=24815009; DOI=10.1016/j.phytochem.2014.04.004;
RA Langer K.M., Jones C.R., Jaworski E.A., Rushing G.V., Kim J.Y., Clark D.G.,
RA Colquhoun T.A.;
RT "PhDAHP1 is required for floral volatile benzenoid/phenylpropanoid
RT biosynthesis in Petunia x hybrida cv 'Mitchell Diploid'.";
RL Phytochemistry 103:22-31(2014).
CC -!- FUNCTION: Involved in the production of volatile organic compounds
CC (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction
CC between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to
CC generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and
CC inorganic phosphate (By similarity). {ECO:0000250|UniProtKB:O53512,
CC ECO:0000269|PubMed:24815009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000250|UniProtKB:O53512};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O53512};
CC Note=Binds 1 divalent metal cation per subunit that could be manganese.
CC {ECO:0000250|UniProtKB:O53512};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000250|UniProtKB:O53512}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O53512}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24815009}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and stems, and, to a
CC lower extent, in roots, stigmas, anthers, petal tubes, petal limbs and
CC sepals. {ECO:0000269|PubMed:24815009}.
CC -!- DEVELOPMENTAL STAGE: During floral development, expressed
CC constitutively. {ECO:0000269|PubMed:24815009}.
CC -!- DISRUPTION PHENOTYPE: Normal floral volatile benzenoids and
CC phenylpropanoids (FVBP) emission. {ECO:0000269|PubMed:24815009}.
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000305}.
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DR EMBL; JQ955570; AFL02468.1; -; mRNA.
DR AlphaFoldDB; A0A067XGX8; -.
DR SMR; A0A067XGX8; -.
DR UniPathway; UPA00053; UER00084.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR PANTHER; PTHR21337; PTHR21337; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR TIGRFAMs; TIGR01358; DAHP_synth_II; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Manganese; Metal-binding; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..512
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase 2,
FT chloroplastic"
FT /id="PRO_0000451510"
FT REGION 37..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 324..325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 410
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 452
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
FT BINDING 482
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O53512"
SQ SEQUENCE 512 AA; 57062 MW; 36E3C0D6A3B6A0A6 CRC64;
MALTATATTR GGSALPNSCL QTPKFQSLQK PTFISSFPTN KKTKPRTKHI SAVQSPPSTT
KWNLESWKTK PAFQLPDYPD KVELESVLKT LSTYPPIVFA GEARNLEEKL GEAALGNAFL
LQGGDCAESF KEFSANNIRD TFRVMLQMGV VLMFGGQMPV IKVGRMAGQF AKPRSDPFEE
KDGVKLPSYR GDNVNGDAFD EKSRIPDPHR MVRAYTQSVA TLNLLRAFAS GGYAAMQRVN
QWNLDFTDQS EQGDRYRELA HRVDEAMGFM TAAGLTVDHT IMTTTDFWTS HECLLLPYEQ
ALTREDSTSG LYYDCSAHMI WVGERTRQLD GAHVEFLRGI ANPLGIKVSH KMDPDELVKL
IDILNPQNKP GRITVITRMG ADNMRVKLPH LIRAVRGAGQ IVTWVSDPMH GNTTKAPCGL
KTRSFDSIRA ELRAFFDVHE QEGSYPGGVH LEMTGQNVTE CVGGSRTITY NDLSSRYHTH
CDPRLNASQA LELAFAIAER LRRRRLGPKF SL
