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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_HORSE              Reviewed;         401 AA.
P08907;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
25-APR-2018, entry version 120.
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;
Name=GOT2;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
PROTEIN SEQUENCE.
PubMed=3104605; DOI=10.1007/BF02100642;
Doonan S., Martini F., Angelaccio S., Pascarella S., Barra D.,
Bossa F.;
"The complete amino acid sequences of cytosolic and mitochondrial
aspartate aminotransferases from horse heart, and inferences on
evolution of the isoenzymes.";
J. Mol. Evol. 23:328-335(1986).
[2]
PARTIAL PROTEIN SEQUENCE.
PubMed=6641173;
Martini F., Angelaccio S., Barra D., Doonan S., Bossa F.;
"Primary structure of aspartate aminotransferase from horse heart and
comparison with that of other homotopic and heterotopic isoenzymes.";
Comp. Biochem. Physiol. 76B:483-487(1983).
-!- FUNCTION: Catalyzes the irreversible transamination of the L-
tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
Plays a key role in amino acid metabolism. Important for
metabolite exchange between mitochondria and cytosol. Facilitates
cellular uptake of long-chain free fatty acids (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
L-glutamate.
-!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2-
aminophenyl)-2,4-dioxobutanoate + L-glutamate.
-!- 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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PIR; B26341; B26341.
ProteinModelPortal; P08907; -.
SMR; P08907; -.
STRING; 9796.ENSECAP00000014550; -.
PaxDb; P08907; -.
PeptideAtlas; P08907; -.
PRIDE; P08907; -.
eggNOG; KOG1411; Eukaryota.
eggNOG; COG1448; LUCA.
HOGENOM; HOG000185898; -.
HOVERGEN; HBG000951; -.
InParanoid; P08907; -.
Proteomes; UP000002281; Unplaced.
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; -; 2.
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; Complete proteome;
Direct protein sequencing; Lipid transport; Membrane; Methylation;
Mitochondrion; Nitration; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Transferase; Transport.
CHAIN 1 401 Aspartate aminotransferase,
mitochondrial.
/FTId=PRO_0000123885.
BINDING 36 36 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 133 133 Substrate. {ECO:0000250}.
BINDING 186 186 Substrate. {ECO:0000250}.
BINDING 378 378 Substrate. {ECO:0000250}.
MOD_RES 19 19 Phosphothreonine.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 30 30 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 44 44 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 44 44 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 61 61 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 61 61 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 67 67 Nitrated tyrosine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 67 67 Phosphotyrosine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 78 78 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 78 78 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 93 93 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 93 93 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 130 130 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 130 130 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 156 156 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 156 156 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 198 198 N6-succinyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 205 205 N6-acetyllysine.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 250 250 N6-(pyridoxal phosphate)lysine;
alternate.
MOD_RES 250 250 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 267 267 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 267 267 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 273 273 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 280 280 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 280 280 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P12344}.
MOD_RES 284 284 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 309 309 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 309 309 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 316 316 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 334 334 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 334 334 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 335 335 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 358 358 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 367 367 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 367 367 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
MOD_RES 375 375 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P00505}.
MOD_RES 375 375 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P05202}.
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


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