AATM_XENTR
ID AATM_XENTR Reviewed; 427 AA.
AC Q28F67;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=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=Transaminase A;
DE Flags: Precursor;
GN Name=got2; ORFNames=TGas123d19.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) 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.
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}.
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; CR762138; CAJ83961.1; -; mRNA.
DR RefSeq; NP_001016933.1; NM_001016933.2.
DR AlphaFoldDB; Q28F67; -.
DR SMR; Q28F67; -.
DR PaxDb; Q28F67; -.
DR Ensembl; ENSXETT00000100393; ENSXETP00000087856; ENSXETG00000015896.
DR GeneID; 549687; -.
DR KEGG; xtr:549687; -.
DR CTD; 2806; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_0_1; -.
DR InParanoid; Q28F67; -.
DR OrthoDB; 1104596at2759; -.
DR Reactome; R-XTR-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-XTR-70263; Gluconeogenesis.
DR Reactome; R-XTR-8963693; Aspartate and asparagine metabolism.
DR Reactome; R-XTR-8964539; Glutamate and glutamine metabolism.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000015896; Expressed in skeletal muscle tissue and 21 other tissues.
DR ExpressionAtlas; Q28F67; baseline.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
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 Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 27..427
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000327598"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 276
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47575 MW; 240F95773AC1A12C CRC64;
MALLKSRLLV GVARCQPCLA AVQGRASSWW SHVEMGPPDP ILGVTEAFKR DTNSKKMNLG
VGAYRDDNGK PYVLSSVRKA EAQLASKNLD KEYLPIGGLA EFARASAQLA LGENCDAIQS
GRFITVQTIS GTGSLRVGAN FLQRFYKYSR DVYLPKPSWG NHTPIFRDAG LEVKGYRYYD
PKTCGFDFTG ALDDISKIPE QSIILFHACA HNPTGVDPKQ EQWKELAALI KSRRLFPFFD
MAYQGFASGD TNRDAWAVRH FIQEGINVVL SQSYAKNMGL YGERVGAFTV VCSDAEEAKR
VESQLKILIR PMYSNPPLNG ARIAAAILTQ PDLRKEWLQE VKGMANRIIS MREQLVSNLK
KEGSIHNWQH ISDQIGMFCF TGLRPEQVER LIKEFSIYMT KDGRISVAGV TSANNGYLAH
AIHQVTK
