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Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membrane-associated fatty acid-binding protein) (FABPpm) (Transaminase A)

 AATM_PIG                Reviewed;         430 AA.
P00506; Q29230;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
17-JUN-2020, entry version 149.
RecName: Full=Aspartate aminotransferase, mitochondrial;
Short=mAspAT;
EC=2.6.1.1;
EC=2.6.1.7;
AltName: Full=Fatty acid-binding protein;
Short=FABP-1;
AltName: Full=Glutamate oxaloacetate transaminase 2;
AltName: Full=Kynurenine aminotransferase 4;
AltName: Full=Kynurenine aminotransferase IV;
AltName: Full=Kynurenine--oxoglutarate transaminase 4;
AltName: Full=Kynurenine--oxoglutarate transaminase IV;
AltName: Full=Plasma membrane-associated fatty acid-binding protein;
Short=FABPpm;
AltName: Full=Transaminase A;
Flags: Precursor;
Name=GOT2;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3862118; DOI=10.1073/pnas.82.18.6065;
Joh T., Nomiyama H., Maeda S., Shimada K., Morino Y.;
"Cloning and sequence analysis of a cDNA encoding porcine mitochondrial
aspartate aminotransferase precursor.";
Proc. Natl. Acad. Sci. U.S.A. 82:6065-6069(1985).
[2]
PROTEIN SEQUENCE OF 30-430.
PubMed=7408859; DOI=10.1111/j.1432-1033.1980.tb04736.x;
Barra D., Bossa F., Doonan S., Fahmy H.M.A., Hughes G.J., Martini F.,
Petruzzelli R., Wittmann-Liebold B.;
"The cytosolic and mitochondrial aspartate aminotransferases from pig
heart. A comparison of their primary structures, predicted secondary
structures and some physical properties.";
Eur. J. Biochem. 108:405-414(1980).
[3]
PROTEIN SEQUENCE OF 30-430.
TISSUE=Heart muscle;
PubMed=7391012;
Kagamiyama H., Sakakibara R., Tanase S., Morino Y., Wada H.;
"Complete amino acid sequence of mitochondrial aspartate aminotransferase
from pig heart muscle. Peptide ordering procedures and the complete
sequence.";
J. Biol. Chem. 255:6153-6159(1980).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-399.
TISSUE=Small intestine;
PubMed=8672129; DOI=10.1007/s003359900153;
Winteroe A.K., Fredholm M., Davies W.;
"Evaluation and characterization of a porcine small intestine cDNA library:
analysis of 839 clones.";
Mamm. Genome 7:509-517(1996).
[5]
PARTIAL PROTEIN SEQUENCE.
PubMed=121997;
Barra D., Savi M.R., Petruzzelli R., Bossa F., Doonan S.;
"The primary structure of mitochondrial aspartate aminotransferase from pig
heart: peptides obtained by cleavage with pepsin and with Staphylococcus
aureus protease.";
Ital. J. Biochem. 28:478-490(1979).
-!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
redox balance. Is important for metabolite exchange between
mitochondria and cytosol, and for amino acid metabolism. Facilitates
cellular uptake of long-chain free fatty acids.
{ECO:0000250|UniProtKB:P00505}.
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
-!- CATALYTIC ACTIVITY:
Reaction=2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-
dioxobutanoate + L-glutamate; Xref=Rhea:RHEA:20964,
ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
ChEBI:CHEBI:58147; EC=2.6.1.7;
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane
{ECO:0000250}.
-!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
chloroplastic isozymes.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; M11732; AAA30999.1; -; mRNA.
EMBL; F14822; CAA23279.1; -; mRNA.
PIR; A25165; XNPGDM.
RefSeq; NP_999093.1; NM_213928.1.
SMR; P00506; -.
STRING; 9823.ENSSSCP00000003017; -.
iPTMnet; P00506; -.
PaxDb; P00506; -.
PeptideAtlas; P00506; -.
PRIDE; P00506; -.
Ensembl; ENSSSCT00000062696; ENSSSCP00000037314; ENSSSCG00000032985.
Ensembl; ENSSSCT00005037831; ENSSSCP00005023175; ENSSSCG00005023696.
Ensembl; ENSSSCT00035110663; ENSSSCP00035048324; ENSSSCG00035080663.
Ensembl; ENSSSCT00040044357; ENSSSCP00040018648; ENSSSCG00040032679.
Ensembl; ENSSSCT00040044476; ENSSSCP00040018700; ENSSSCG00040032679.
Ensembl; ENSSSCT00045007235; ENSSSCP00045004972; ENSSSCG00045004323.
Ensembl; ENSSSCT00050040765; ENSSSCP00050016831; ENSSSCG00050030308.
Ensembl; ENSSSCT00065092962; ENSSSCP00065040677; ENSSSCG00065067696.
GeneID; 396968; -.
KEGG; ssc:396968; -.
CTD; 2806; -.
VGNC; VGNC:88562; GOT2.
eggNOG; KOG1411; Eukaryota.
eggNOG; COG1448; LUCA.
GeneTree; ENSGT00950000183082; -.
InParanoid; P00506; -.
KO; K14455; -.
OrthoDB; 1104596at2759; -.
Proteomes; UP000008227; Chromosome 6.
ExpressionAtlas; P00506; baseline and differential.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
GO; GO:0006533; P:aspartate catabolic process; IBA:GO_Central.
GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR000796; Asp_trans.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR11879; PTHR11879; 1.
Pfam; PF00155; Aminotran_1_2; 1.
PRINTS; PR00799; TRANSAMINASE.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
Acetylation; Aminotransferase; Cell membrane; Direct protein sequencing;
Lipid transport; Membrane; Methylation; Mitochondrion; Nitration;
Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase;
Transit peptide; Transport.
TRANSIT 1..29
/note="Mitochondrion"
/evidence="ECO:0000269|PubMed:7391012,
ECO:0000269|PubMed:7408859"
CHAIN 30..430
/note="Aspartate aminotransferase, mitochondrial"
/id="PRO_0000001217"
BINDING 65
/note="Substrate; via amide nitrogen"
/evidence="ECO:0000250"
BINDING 162
/note="Substrate"
/evidence="ECO:0000250"
BINDING 215
/note="Substrate"
/evidence="ECO:0000250"
BINDING 407
/note="Substrate"
/evidence="ECO:0000250"
MOD_RES 48
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 59
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 73
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 73
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 82
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 90
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 90
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 96
/note="Nitrated tyrosine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 96
/note="Phosphotyrosine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 107
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 107
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 122
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 122
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 159
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 159
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 185
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 185
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 227
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 234
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 279
/note="N6-(pyridoxal phosphate)lysine; alternate"
MOD_RES 279
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 296
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 296
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 302
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 309
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 309
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P12344"
MOD_RES 313
/note="Asymmetric dimethylarginine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 345
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 363
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 363
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 364
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 387
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 396
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 396
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
MOD_RES 404
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P00505"
MOD_RES 404
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P05202"
CONFLICT 71
/note="N -> D (in Ref. 3; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 256
/note="K -> R (in Ref. 4; CAA23279)"
/evidence="ECO:0000305"
CONFLICT 273
/note="L -> F (in Ref. 4; CAA23279)"
/evidence="ECO:0000305"
CONFLICT 305
/note="E -> Q (in Ref. 2; AA sequence)"
/evidence="ECO:0000305"
SEQUENCE 430 AA; 47436 MW; 23280D11821A8BC4 CRC64;
MALLHSGRVL SGVASAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA FKRDTNSKKM
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV
LKSGRYVTVQ TISGTGALRI GANFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLHSYR
YYDPKTCGFD FTGALEDISK IPAQSVILLH ACAHNPTGVD PRPEQWKEMA TLVKKNNLFA
FFDMAYQGFA SGDGNKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
AKRVESQLKI LIRPMYSNPP VNGARIASTI LTSPDLRQQW LQEVKGMADR IISMRTQLVS
NLKKEGSSHN WQHIVDQIGM FCFTGIKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY
LAHAIHQVTK


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