ID   PAT_PINPS               Reviewed;         492 AA.
AC   Q5F4K8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=PpAAT;
DE            EC=2.6.1.1;
DE   Flags: Precursor;
GN   Name=AAT;
OS   Pinus pinaster (Maritime pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=71647;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Xylem;
RX   PubMed=16623902; DOI=10.1111/j.1365-313x.2006.02713.x;
RA   de la Torre F., De Santis L., Suarez M.F., Crespillo R., Canovas F.M.;
RT   "Identification and functional analysis of a prokaryotic-type aspartate
RT   aminotransferase: implications for plant amino acid metabolism.";
RL   Plant J. 46:414-425(2006).
CC   -!- FUNCTION: Prokaryotic-type aspartate aminotransferase. Specific for
CC       aspartate and no activity with glutamine, asparagine, alanine,
CC       histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine,
CC       phenylalanine or kynureine. {ECO:0000269|PubMed:16623902}.
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:16623902};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:16623902};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.5 mM for aspartate {ECO:0000269|PubMed:16623902};
CC         KM=1.0 mM for glutamate {ECO:0000269|PubMed:16623902};
CC         KM=150 uM for oxaloacetate {ECO:0000269|PubMed:16623902};
CC         KM=80 uM for 2-oxoglutarate {ECO:0000269|PubMed:16623902};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:16623902}.
CC   -!- DEVELOPMENTAL STAGE: Not detected in the embryo, but accumulates upon
CC       germination of the seed and during seedling development.
CC       {ECO:0000269|PubMed:16623902}.
CC   -!- MISCELLANEOUS: The orthologous protein in Arabidopsis has an additional
CC       glutamate/aspartate-prephenate aminotransferase activity.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ628016; CAF31327.1; -; mRNA.
DR   AlphaFoldDB; Q5F4K8; -.
DR   SMR; Q5F4K8; -.
DR   BRENDA; 2.6.1.1; 4852.
DR   SABIO-RK; Q5F4K8; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   Aminotransferase; Chloroplast; Plastid; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..66
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           67..492
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000401476"
FT   BINDING         119
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  52804 MW;  31ACA73126EA36CB CRC64;
     MMSASFKCPV SLSGVENICN GDKAIPGINS RTLFTGSSFL QRHHSANKIF FRTCGKKGSC
     CLFNIRAMAE TDSGNGVPQL DISLSPRVAA LKPSKTMAIT DLATALKQAG VPVIGLAAGE
     PDFNTPDAVA EAGIKAIQDG YTRYTPNAGT MEIRTAICHK LKEENGLSYT PDQILVSNGA
     KQCIMAAAVL AVCSPGDEVI IPAPFWVSYT EMARLADATP VIIPTLLSDD FLLNPEVFSS
     KLNENSRLLI LCSPSNPTGS VYPRELLEEI AKIVAKHPKL LVLSDEIYEH IMYPPAKHTS
     FASLPGMWER TLTVNGFSKA FAMTGWRLGY LAGPKHFVTA CGRIQSQSTS GASSISQKAG
     VAALALGYAG SEAVSTMVKA YRERRDFLVQ RLQAMEGVKL PVPQGAFYLF PDFSSYYGTE
     VEDFGVINGS EALCRFFLEK AQVALVPGDA FGNDDCIRIS YAASLDTLRT AINNIEKSLL
     LLRPAAAASK AS