AATM_CHICK
ID AATM_CHICK Reviewed; 423 AA.
AC P00508;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 154.
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=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=Transaminase A;
DE Flags: Precursor;
GN Name=GOT2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3840803; DOI=10.1016/s0021-9258(17)36199-9;
RA Jaussi R., Cotton B., Juretic N., Christen P., Schumperli D.;
RT "The primary structure of the precursor of chicken mitochondrial aspartate
RT aminotransferase. Cloning and sequence analysis of cDNA.";
RL J. Biol. Chem. 260:16060-16063(1985).
RN [2]
RP PROTEIN SEQUENCE OF 23-423.
RX PubMed=6345546; DOI=10.1016/s0021-9258(18)32129-x;
RA Graf-Hausner U., Wilson K.J., Christen P.;
RT "The covalent structure of mitochondrial aspartate aminotransferase from
RT chicken. Identification of segments of the polypeptide chain invariant
RT specifically in the mitochondrial isoenzyme.";
RL J. Biol. Chem. 258:8813-8826(1983).
RN [3]
RP GENE STRUCTURE.
RC STRAIN=White leghorn;
RX PubMed=2401287; DOI=10.1111/j.1432-1033.1990.tb19204.x;
RA Juretic N., Mattes U., Ziak M., Christen P., Jaussi R.;
RT "Structure of the genes of two homologous intracellularly heterotopic
RT isoenzymes. Cytosolic and mitochondrial aspartate aminotransferase of
RT chicken.";
RL Eur. J. Biochem. 192:119-126(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL
RP PHOSPHATE, PYRIDOXAL PHOSPHATE AT LYS-272, COFACTOR, AND SUBUNIT.
RX PubMed=1593633; DOI=10.1016/0022-2836(92)90935-d;
RA McPhalen C.A., Vincent M.G., Jansonius J.N.;
RT "X-ray structure refinement and comparison of three forms of mitochondrial
RT aspartate aminotransferase.";
RL J. Mol. Biol. 225:495-517(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-423 IN COMPLEXES WITH PYRIDOXAL
RP PHOSPHATE; L-ASPARTATE AND L-GLUTAMATE, COFACTOR, AND SUBUNIT.
RX PubMed=7903048; DOI=10.1021/bi00212a010;
RA Malashkevich V.N., Toney M.D., Jansonius J.N.;
RT "Crystal structures of true enzymatic reaction intermediates: aspartate and
RT glutamate ketimines in aspartate aminotransferase.";
RL Biochemistry 32:13451-13462(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-423 IN COMPLEX WITH
RP ERYTHRO-BETA-HYDROXYASPARTATE, AND COFACTOR.
RX PubMed=8952476; DOI=10.1021/bi960994z;
RA von Stosch A.G.;
RT "Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate:
RT crystallographic and spectroscopic identification of the carbinolamine
RT intermediate.";
RL Biochemistry 35:15260-15268(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-423 IN COMPLEXES WITH PYRIDOXAL
RP PHOSPHATE AND SUBSTRATE ANALOGS, COFACTOR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=8665890; DOI=10.1111/j.1432-1033.1996.01025.x;
RA Markovic-Housley Z., Schirmer T., Hohenester E., Khomutov A.R.,
RA Khomutov R.M., Karpeisky M.Y., Sandmeier E., Christen P., Jansonius J.N.;
RT "Crystal structures and solution studies of oxime adducts of mitochondrial
RT aspartate aminotransferase.";
RL Eur. J. Biochem. 236:1025-1032(1996).
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.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:1593633, ECO:0000269|PubMed:7903048,
CC ECO:0000269|PubMed:8665890, ECO:0000269|PubMed:8952476};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1593633,
CC ECO:0000269|PubMed:7903048, ECO:0000269|PubMed:8665890,
CC ECO:0000269|PubMed:8952476}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:8665890}.
CC -!- TISSUE SPECIFICITY: Detected in heart (at protein level).
CC {ECO:0000269|PubMed:8665890}.
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; M12105; AAA48603.1; -; mRNA.
DR PIR; A24554; XNCHDM.
DR RefSeq; NP_990854.1; NM_205523.1.
DR PDB; 1AKA; X-ray; 2.10 A; A/B=23-423.
DR PDB; 1AKB; X-ray; 2.30 A; A=23-423.
DR PDB; 1AKC; X-ray; 2.30 A; A=23-423.
DR PDB; 1AMA; X-ray; 2.30 A; A=23-423.
DR PDB; 1IVR; X-ray; 2.40 A; A=23-423.
DR PDB; 1MAP; X-ray; 2.40 A; A=23-423.
DR PDB; 1MAQ; X-ray; 2.30 A; A=23-423.
DR PDB; 1OXO; X-ray; 2.30 A; A/B=23-423.
DR PDB; 1OXP; X-ray; 2.50 A; A=23-423.
DR PDB; 1TAR; X-ray; 2.20 A; A/B=23-423.
DR PDB; 1TAS; X-ray; 2.80 A; A/B=23-423.
DR PDB; 1TAT; X-ray; 3.00 A; A/B=23-423.
DR PDB; 7AAT; X-ray; 1.90 A; A/B=23-423.
DR PDB; 8AAT; X-ray; 2.30 A; A/B=23-423.
DR PDB; 9AAT; X-ray; 2.20 A; A/B=23-423.
DR PDBsum; 1AKA; -.
DR PDBsum; 1AKB; -.
DR PDBsum; 1AKC; -.
DR PDBsum; 1AMA; -.
DR PDBsum; 1IVR; -.
DR PDBsum; 1MAP; -.
DR PDBsum; 1MAQ; -.
DR PDBsum; 1OXO; -.
DR PDBsum; 1OXP; -.
DR PDBsum; 1TAR; -.
DR PDBsum; 1TAS; -.
DR PDBsum; 1TAT; -.
DR PDBsum; 7AAT; -.
DR PDBsum; 8AAT; -.
DR PDBsum; 9AAT; -.
DR AlphaFoldDB; P00508; -.
DR SMR; P00508; -.
DR BioGRID; 676777; 1.
DR IntAct; P00508; 1.
DR STRING; 9031.ENSGALP00000003646; -.
DR PaxDb; P00508; -.
DR GeneID; 396533; -.
DR KEGG; gga:396533; -.
DR CTD; 2806; -.
DR VEuPathDB; HostDB:geneid_396533; -.
DR eggNOG; KOG1411; Eukaryota.
DR InParanoid; P00508; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P00508; -.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-372568; Amino acid metabolism.
DR EvolutionaryTrace; P00508; -.
DR PRO; PR:P00508; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR GO; GO:0006533; P:aspartate catabolic process; IBA:GO_Central.
DR GO; GO:0006531; P:aspartate metabolic process; IDA:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
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 3D-structure; Aminotransferase; Direct protein sequencing; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6345546"
FT CHAIN 23..423
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000001219"
FT BINDING 58
FT /ligand="substrate"
FT BINDING 155
FT /ligand="substrate"
FT BINDING 208
FT /ligand="substrate"
FT BINDING 400
FT /ligand="substrate"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 67
FT /note="S -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1AKA"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1OXP"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1TAT"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:7AAT"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:7AAT"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:7AAT"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:7AAT"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 291..309
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 327..357
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 365..369
FT /evidence="ECO:0007829|PDB:7AAT"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:7AAT"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:1AKA"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:7AAT"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:7AAT"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:7AAT"
SQ SEQUENCE 423 AA; 47241 MW; 59D65D4ED4DDF8BA CRC64;
MALLQSRLLL SAPRRAAATA RASSWWSHVE MGPPDPILGV TEAFKRDTNS KKMNLGVGAY
RDDNGKSYVL NCVRKAEAMI AAKKMDKEYL PIAGLADFTR ASAELALGEN SEAFKSGRYV
TVQGISGTGS LRVGANFLQR FFKFSRDVYL PKPSWGNHTP IFRDAGLQLQ AYRYYDPKTC
SLDFTGAMED ISKIPEKSII LLHACAHNPT GVDPRQEQWK ELASVVKKRN LLAYFDMAYQ
GFASGDINRD AWALRHFIEQ GIDVVLSQSY AKNMGLYGER AGAFTVICRD AEEAKRVESQ
LKILIRPMYS NPPMNGARIA SLILNTPELR KEWLVEVKGM ADRIISMRTQ LVSNLKKEGS
SHNWQHITDQ IGMFCFTGLK PEQVERLTKE FSIYMTKDGR ISVAGVASSN VGYLAHAIHQ
VTK
