ID   AAT2_PSEMZ              Reviewed;          34 AA.
AC   P85951;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Aspartate aminotransferase 2 {ECO:0000250|UniProtKB:P28011};
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A {ECO:0000250|UniProtKB:P28011};
DE   Flags: Fragments;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- FUNCTION: Important for the metabolism of amino acids and Krebs-cycle
CC       related organic acids. In plants, it is involved in nitrogen metabolism
CC       and in aspects of carbon and energy metabolism (By similarity).
CC       {ECO:0000250}.
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:0000305};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28011}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
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DR   AlphaFoldDB; P85951; -.
DR   SMR; P85951; -.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           <1..>34
FT                   /note="Aspartate aminotransferase 2"
FT                   /id="PRO_0000347319"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         34
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   34 AA;  3587 MW;  F857A8A5C3C806B2 CRC64;
     VATVQGLSGT GSLRNLGLYA ERQIGMFSFT GLNK