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AROG1_PETHY
ID   AROG1_PETHY             Reviewed;         533 AA.
AC   A0A067XH53;
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 1, chloroplastic {ECO:0000305};
DE            EC=2.5.1.54 {ECO:0000250|UniProtKB:O53512};
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1 {ECO:0000303|PubMed:23275577, ECO:0000303|PubMed:24815009};
DE            Short=DAHP synthase 1 {ECO:0000305};
DE            Short=PhDAHP1 {ECO:0000303|PubMed:24815009};
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase 1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=DAHP1 {ECO:0000303|PubMed:24815009};
GN   Synonyms=DAHPS {ECO:0000303|PubMed:23275577},
GN   DHS1 {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).
RN   [2]
RP   INDUCTION BY EOBI.
RC   STRAIN=cv. W115;
RX   PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA   Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA   Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT   "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT   regulates scent production by activating ODO1 and structural scent-related
RT   genes in petunia.";
RL   Plant Cell 24:5089-5105(2012).
CC   -!- FUNCTION: Involved in the production of volatile organic compounds
CC       (VOCs), including floral volatile benzenoids and phenylpropanoids
CC       (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv.
CC       V26), scent attracting pollinators (e.g. the night-active hawkmoth
CC       pollinator Manduca sexta) (PubMed:24815009). Catalyzes an aldol-like
CC       condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose
CC       4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-
CC       phosphate (DAH7P) and inorganic phosphate (By similarity).
CC       {ECO:0000250|UniProtKB:O53512, 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 flowers, especially in petal
CC       limbs and tubes, and, to a lower extent, in roots, stems, stigmas,
CC       anthers, leaves and sepals. {ECO:0000269|PubMed:24815009}.
CC   -!- DEVELOPMENTAL STAGE: During floral development, accumulates to highest
CC       levels during open flower stages. {ECO:0000269|PubMed:24815009}.
CC   -!- INDUCTION: Triggered by EOBI in flowers. {ECO:0000269|PubMed:23275577}.
CC   -!- DISRUPTION PHENOTYPE: Reduced 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; JQ955569; AFL02467.1; -; mRNA.
DR   AlphaFoldDB; A0A067XH53; -.
DR   SMR; A0A067XH53; -.
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   GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.20.20.70; -; 1.
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..533
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000451509"
FT   REGION          47..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         145
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         343..344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         429
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         471
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
FT   BINDING         501
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53512"
SQ   SEQUENCE   533 AA;  58894 MW;  16E7611033E00C01 CRC64;
     MALSTNSTTS SLLPKTPLVQ QPLLKNASLP TTTKAIRFIQ PISAIHSSDS SKNTPIVSAK
     PSSPPAATST AAATAVTKQE WSIDSWKTKK ALQLPEYPNQ EELKNVLKTI EDFPPIVFAG
     EARHLEEKLG EAAMGRAFLL QGGDCAESFK EFNANNIRDT FRILLQMGAV LMFGGQMPVI
     KVGRMAGQFA KPRSDNFEEK NGVKLPSYRG DNVNGDAFDL KSRTPDPQRL IRAYCQSAAT
     LNLLRAFATG GYAAMQRVTQ WNLDFTEHSE QGDRYRELAN RVDEALGFMN AAGLTTDHPI
     MTTTEFWTSH ECLLLPYEQS LTRLDSTSGL YYDCSAHFLW VGERTRQLDG AHVEFLRGIA
     NPLGIKVSDK MDPSALVKLI EILNPQNKAG RITIITRMGA ENMRVKLPHL IRAVRGAGQI
     VTWVSDPMHG NTIKAPCGLK TRPFDSIRAE VRAFFDVHEQ EGSHPGGVHL EMTGQNVTEC
     IGGSRTVTFD DLSSRYHTHC DPRLNASQSL ELAFIIAERL RKRRLGSQSV LGQ
 
 
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