AATM_PONAB
ID AATM_PONAB Reviewed; 430 AA.
AC Q5REB0; Q5R7M0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Aspartate aminotransferase, mitochondrial;
DE Short=mAspAT;
DE EC=2.6.1.1 {ECO:0000250|UniProtKB:P00507};
DE EC=2.6.1.7 {ECO:0000250|UniProtKB:P00507};
DE AltName: Full=Fatty acid-binding protein;
DE Short=FABP-1;
DE AltName: Full=Glutamate oxaloacetate transaminase 2;
DE AltName: Full=Kynurenine aminotransferase 4;
DE AltName: Full=Kynurenine aminotransferase IV;
DE AltName: Full=Kynurenine--oxoglutarate transaminase 4;
DE AltName: Full=Kynurenine--oxoglutarate transaminase IV;
DE AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE Short=FABPpm;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN Name=GOT2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
CC malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
CC redox balance. Is important for metabolite exchange between
CC mitochondria and cytosol, and for amino acid metabolism. Facilitates
CC cellular uptake of long-chain free fatty acids.
CC {ECO:0000250|UniProtKB:P00505}.
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:0000250|UniProtKB:P00507};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:P00507};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Cell membrane
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CR857622; CAH89897.1; -; mRNA.
DR EMBL; CR860094; CAH92240.1; -; mRNA.
DR RefSeq; NP_001124888.1; NM_001131416.1.
DR AlphaFoldDB; Q5REB0; -.
DR SMR; Q5REB0; -.
DR STRING; 9601.ENSPPYP00000008377; -.
DR Ensembl; ENSPPYT00000008719; ENSPPYP00000008378; ENSPPYG00000007413.
DR GeneID; 100171753; -.
DR KEGG; pon:100171753; -.
DR CTD; 2806; -.
DR eggNOG; KOG1411; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; Q5REB0; -.
DR OMA; VGACTIV; -.
DR OrthoDB; 1104596at2759; -.
DR TreeFam; TF300641; -.
DR Proteomes; UP000001595; Chromosome 16.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006532; P:aspartate biosynthetic process; IEA:Ensembl.
DR GO; GO:0006533; P:aspartate catabolic process; IEA:Ensembl.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IEA:Ensembl.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
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 PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminotransferase; Cell membrane; Lipid transport; Membrane;
KW Methylation; Mitochondrion; Nitration; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..430
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000278665"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 73
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 73
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 90
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 90
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 96
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 96
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 107
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 107
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 122
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 159
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 159
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 185
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 185
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 227
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 279
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 296
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 296
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 302
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 309
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 309
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12344"
FT MOD_RES 313
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 338
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 338
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 363
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 363
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 396
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 396
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 404
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 404
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT CONFLICT 339
FT /note="Q -> T (in Ref. 1; CAH92240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47433 MW; 4A3B7B89A5FEB9C5 CRC64;
MALLHSGRAL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV
LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE
AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKGMADR IIGMRTQLVS
NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY
LAHAIHQVTK
