AATM_PIG
ID AATM_PIG Reviewed; 430 AA.
AC P00506; Q29230;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 156.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3862118; DOI=10.1073/pnas.82.18.6065;
RA Joh T., Nomiyama H., Maeda S., Shimada K., Morino Y.;
RT "Cloning and sequence analysis of a cDNA encoding porcine mitochondrial
RT aspartate aminotransferase precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6065-6069(1985).
RN [2]
RP PROTEIN SEQUENCE OF 30-430.
RX PubMed=7408859; DOI=10.1111/j.1432-1033.1980.tb04736.x;
RA Barra D., Bossa F., Doonan S., Fahmy H.M.A., Hughes G.J., Martini F.,
RA Petruzzelli R., Wittmann-Liebold B.;
RT "The cytosolic and mitochondrial aspartate aminotransferases from pig
RT heart. A comparison of their primary structures, predicted secondary
RT structures and some physical properties.";
RL Eur. J. Biochem. 108:405-414(1980).
RN [3]
RP PROTEIN SEQUENCE OF 30-430.
RC TISSUE=Heart muscle;
RX PubMed=7391012; DOI=10.1016/s0021-9258(18)43714-3;
RA Kagamiyama H., Sakakibara R., Tanase S., Morino Y., Wada H.;
RT "Complete amino acid sequence of mitochondrial aspartate aminotransferase
RT from pig heart muscle. Peptide ordering procedures and the complete
RT sequence.";
RL J. Biol. Chem. 255:6153-6159(1980).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-399.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=121997;
RA Barra D., Savi M.R., Petruzzelli R., Bossa F., Doonan S.;
RT "The primary structure of mitochondrial aspartate aminotransferase from pig
RT heart: peptides obtained by cleavage with pepsin and with Staphylococcus
RT aureus protease.";
RL Ital. J. Biochem. 28:478-490(1979).
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. 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; M11732; AAA30999.1; -; mRNA.
DR EMBL; F14822; CAA23279.1; -; mRNA.
DR PIR; A25165; XNPGDM.
DR RefSeq; NP_999093.1; NM_213928.1.
DR AlphaFoldDB; P00506; -.
DR SMR; P00506; -.
DR STRING; 9823.ENSSSCP00000003017; -.
DR iPTMnet; P00506; -.
DR PaxDb; P00506; -.
DR PeptideAtlas; P00506; -.
DR PRIDE; P00506; -.
DR Ensembl; ENSSSCT00000062696; ENSSSCP00000037314; ENSSSCG00000032985.
DR Ensembl; ENSSSCT00005037831; ENSSSCP00005023175; ENSSSCG00005023696.
DR Ensembl; ENSSSCT00035110663; ENSSSCP00035048324; ENSSSCG00035080663.
DR Ensembl; ENSSSCT00040044357; ENSSSCP00040018648; ENSSSCG00040032679.
DR Ensembl; ENSSSCT00040044476; ENSSSCP00040018700; ENSSSCG00040032679.
DR Ensembl; ENSSSCT00045007235; ENSSSCP00045004972; ENSSSCG00045004323.
DR Ensembl; ENSSSCT00050040765; ENSSSCP00050016831; ENSSSCG00050030308.
DR Ensembl; ENSSSCT00065092962; ENSSSCP00065040677; ENSSSCG00065067696.
DR GeneID; 396968; -.
DR KEGG; ssc:396968; -.
DR CTD; 2806; -.
DR VGNC; VGNC:88562; GOT2.
DR eggNOG; KOG1411; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR InParanoid; P00506; -.
DR OrthoDB; 1104596at2759; -.
DR SABIO-RK; P00506; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000032985; Expressed in psoas major muscle and 44 other tissues.
DR ExpressionAtlas; P00506; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
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:0006533; P:aspartate catabolic process; IBA:GO_Central.
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 GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Cell membrane; Direct protein sequencing;
KW Lipid transport; Membrane; Methylation; Mitochondrion; Nitration;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7391012,
FT ECO:0000269|PubMed:7408859"
FT CHAIN 30..430
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000001217"
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 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 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 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 71
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="K -> R (in Ref. 4; CAA23279)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="L -> F (in Ref. 4; CAA23279)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
