AATM_HORSE
ID AATM_HORSE Reviewed; 401 AA.
AC P08907;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 137.
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;
GN Name=GOT2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3104605; DOI=10.1007/bf02100642;
RA Doonan S., Martini F., Angelaccio S., Pascarella S., Barra D., Bossa F.;
RT "The complete amino acid sequences of cytosolic and mitochondrial aspartate
RT aminotransferases from horse heart, and inferences on evolution of the
RT isoenzymes.";
RL J. Mol. Evol. 23:328-335(1986).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=6641173; DOI=10.1016/0305-0491(83)90280-8;
RA Martini F., Angelaccio S., Barra D., Doonan S., Bossa F.;
RT "Primary structure of aspartate aminotransferase from horse heart and
RT comparison with that of other homotopic and heterotopic isoenzymes.";
RL Comp. Biochem. Physiol. 76B:483-487(1983).
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 PIR; B26341; B26341.
DR AlphaFoldDB; P08907; -.
DR SMR; P08907; -.
DR STRING; 9796.ENSECAP00000014550; -.
DR PaxDb; P08907; -.
DR PeptideAtlas; P08907; -.
DR InParanoid; P08907; -.
DR Proteomes; UP000002281; Unplaced.
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 Transport.
FT CHAIN 1..401
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000123885"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 44
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 44
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 61
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 61
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 67
FT /note="3'-nitrotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 67
FT /note="Phosphotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 130
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 130
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 156
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 156
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 198
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 205
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 250
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT MOD_RES 250
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 267
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 267
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 273
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 280
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 280
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P12344"
FT MOD_RES 284
FT /note="Asymmetric dimethylarginine"
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:P05202"
FT MOD_RES 316
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 334
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 334
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 367
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 367
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
FT MOD_RES 375
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00505"
FT MOD_RES 375
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05202"
SQ SEQUENCE 401 AA; 44567 MW; 8562D82170A40487 CRC64;
SSWWAHVEMG PPDPILGVTE AYKRDTNSKK MNLGVGAYRD DNGKPYVLPS VRKAEAQIAA
KNLDKEYLPI GGLAEFCKAS AELALGENSE ALKSGRYVTV QSISGTGALR IGANFLQRFF
KFSRDVFLPK PSWGNHTPIF RDAGLQLHAY RYYDPKTCGF DVTGALEDIS KIPQQSIILL
HACAHNPTGV DPRPEQWKEI ATLVKKNNLF AFFDMAYQGF ASGDGNKDAW AVRYFIEQGI
NVCLCQSYAK NMGLYGERVG AFTMVCKDAD EAKRVESQLK ILIRPLYSNP PLNGARIAST
ILTSPDLRKQ WLQEVKGMAD RIISMRTQLV SNLKKEGSSH SWQHIADQIG MFCFTGLKPE
QVERLTKEFS IYMTKDGRIS VAGVTSGNVG YLAHAIHQVT K
