PAT_PETHY
ID PAT_PETHY Reviewed; 479 AA.
AC E9L7A5;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase {ECO:0000303|PubMed:21102469};
DE Short=PhPPA-AT {ECO:0000303|PubMed:21102469};
DE EC=2.6.1.1 {ECO:0000269|PubMed:21102469};
DE EC=2.6.1.78 {ECO:0000269|PubMed:21102469};
DE EC=2.6.1.79 {ECO:0000269|PubMed:21102469};
DE Flags: Precursor;
GN Name=PPA-AT {ECO:0000303|PubMed:21102469};
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, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=21102469; DOI=10.1038/nchembio.485;
RA Maeda H., Yoo H., Dudareva N.;
RT "Prephenate aminotransferase directs plant phenylalanine biosynthesis via
RT arogenate.";
RL Nat. Chem. Biol. 7:19-21(2011).
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: Prokaryotic-type aspartate aminotransferase. Has also a
CC prenate transaminase activity (PubMed:21102469). Involved in the
CC aromatic amino acids biosynthesis pathway via the arogenate route
CC (PubMed:21102469). Required for the transamination of prephenate into
CC arogenate (PubMed:21102469). Can use 2-oxoglutarate, oxaloacetate and
CC prephenate as substrates, but not phenylpyruvate or 4-
CC hydroxyphenylpyruvate (PubMed:21102469). {ECO:0000269|PubMed:21102469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:21102469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate;
CC Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78;
CC Evidence={ECO:0000269|PubMed:21102469};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20447;
CC Evidence={ECO:0000269|PubMed:21102469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate;
CC Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79;
CC Evidence={ECO:0000269|PubMed:21102469};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22882;
CC Evidence={ECO:0000269|PubMed:21102469};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:21102469};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=317 uM for prephenate (with 20 mM aspartate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC KM=478 uM for prephenate (with 20 mM glutamate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC KM=1045 uM for 2-oxoglutarate (with 20 mM aspartate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC KM=3328 uM for glutamate (with 3 mM prephenate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC KM=3238 uM for aspartate (with 3 mM prephenate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC KM=2060 uM for arogenate (with 20 mM 2-oxoglutarate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC KM=11629 uM for oxaloacetate (with 20 mM glutamate as cosubstrate)
CC {ECO:0000269|PubMed:21102469};
CC Vmax=115 nmol/sec/mg enzyme toward prephenate with 20 mM aspartate as
CC cosubstrate {ECO:0000269|PubMed:21102469};
CC Vmax=253 nmol/sec/mg enzyme toward prephenate with 20 mM glutamate as
CC cosubstrate {ECO:0000269|PubMed:21102469};
CC Vmax=654 nmol/sec/mg enzyme toward 2-oxoglutarate with 20 mM
CC aspartate as cosubstrate {ECO:0000269|PubMed:21102469};
CC Vmax=85 nmol/sec/mg enzyme toward glutamate with 3 mM prephenate as
CC cosubstrate {ECO:0000269|PubMed:21102469};
CC Vmax=81 nmol/sec/mg enzyme toward aspartate with 3 mM prephenate as
CC cosubstrate {ECO:0000269|PubMed:21102469};
CC Vmax=120 nmol/sec/mg enzyme toward arogenate with 20 mM 2-
CC oxoglutarate as cosubstrate {ECO:0000269|PubMed:21102469};
CC Vmax=1057 nmol/sec/mg enzyme toward oxaloacetate with 20 mM glutamate
CC as cosubstrate {ECO:0000269|PubMed:21102469};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC arogenate from prephenate (L-Asp route): step 1/1.
CC {ECO:0000269|PubMed:21102469}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC arogenate from prephenate (L-Glu route): step 1/1.
CC {ECO:0000269|PubMed:21102469}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21102469}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, pistils, stamens, ovaries and
CC at lower levels in leaves and sepals. {ECO:0000269|PubMed:21102469}.
CC -!- INDUCTION: Triggered by EOBI in flowers. {ECO:0000269|PubMed:23275577}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; HM635905; ADM67557.1; -; mRNA.
DR AlphaFoldDB; E9L7A5; -.
DR SMR; E9L7A5; -.
DR SABIO-RK; E9L7A5; -.
DR UniPathway; UPA00121; UER00342.
DR UniPathway; UPA00121; UER00343.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0033853; F:aspartate-prephenate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0033854; F:glutamate-prephenate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0009095; P:aromatic amino acid family biosynthetic process, prephenate pathway; IDA:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Chloroplast; Plastid;
KW Pyridoxal phosphate; Transferase; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..479
FT /note="Bifunctional aspartate aminotransferase and
FT glutamate/aspartate-prephenate aminotransferase"
FT /id="PRO_0000418331"
FT BINDING 111
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 172..173
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 197
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 247
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 247
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 279
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 307..309
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O84395"
FT BINDING 318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT BINDING 449
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT SITE 84
FT /note="Important for prephenate aminotransferase activity"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 310
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O84395"
SQ SEQUENCE 479 AA; 51743 MW; 478016CA551B815F CRC64;
MAATTTTSSS SRIAYSRHNI PGLHSDSLNP KSISFSSNLH TFSLKSSGSR RQLYSRRTGA
VVIMQSMDKV EVDISLSPRV NSVKPSKTVA ITDQATALVQ AGVPVIRLAA GEPDFDTPAP
IVEAGINAIR EGHTRYTPNA GTMELRSAIS HKLKEENGLS YTPDQILVSN GAKQSIIQAV
LAVCSPGDEV LIPAPYWVSY PEMARLADAT PVILPTSISE DFLLDPKLLE SKLTEKSRLL
ILCSPSNPTG SVYPRKLLEQ IAEIVARHPR LLVISDEIYE HIIYAPATHT SFASLPGMWD
RTLTVNGFSK AFAMTGWRLG YIAGPKHFIA ACNKIQSQFT SGASSISQKA AVAALGLGYA
GGELVATMVK SFRERRDYLV KSFGEIEGVK ISEPRGAFYL FIDLSSYYGV EVDGFGSINN
SESLCRYLLD KAQVALVPGD AFGDDTCIRI SYAASLSTLQ AAVERIKKAL VTIKPPVPV
