ID   M3Y0H1_MUSPF            Unreviewed;       430 AA.
AC   M3Y0H1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   Name=GOT2 {ECO:0000313|RefSeq:XP_012907626.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000004822.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000004822.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_012907626.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_012907626.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037556}.
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:0000256|ARBA:ARBA00000984,
CC         ECO:0000256|RuleBase:RU000480};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU000480}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; AEYP01015566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01015567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01015568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01015569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004744353.1; XM_004744296.2.
DR   RefSeq; XP_012907626.1; XM_013052172.2.
DR   STRING; 9669.ENSMPUP00000004822; -.
DR   Ensembl; ENSMPUT00000004906.1; ENSMPUP00000004822.1; ENSMPUG00000004862.1.
DR   GeneID; 101676462; -.
DR   KEGG; mpuf:101676462; -.
DR   CTD; 2806; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   GeneTree; ENSGT00950000183082; -.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   OMA; VGACTIV; -.
DR   OrthoDB; 1123851at2759; -.
DR   Proteomes; UP000000715; Unplaced.
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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000480,
KW   ECO:0000313|RefSeq:XP_012907626.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          58..425
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   430 AA;  47492 MW;  D7DAE0FC95AC59F7 CRC64;
     MALLHSGRVL AGVAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
     NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIA GLAEFCKASA ELALGENNEV
     LKSSRYVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLHGYR
     YYDPKTCGFD FTGALEDISK MPQQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKNNLFA
     FFDMAYQGFA SGDGNKDAWA VRYFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDADE
     AKRVESQLKI LIRPMYSNPP INGARIASTI LTSPDLRKQW LQEVKGMADR IISMRTQLVS
     NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY
     LAHAIHQVTK
//