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Protein

Aspartate aminotransferase, mitochondrial

Gene

GOT2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May facilitate cellular uptake of long-chain free fatty acids (By similarity).By similarity

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

Cofactori

pyridoxal 5'-phosphate4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581Substrate; via amide nitrogen
Binding sitei155 – 1551Substrate
Binding sitei208 – 2081Substrate
Binding sitei400 – 4001Substrate

GO - Molecular functioni

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: UniProtKB
  • aspartate catabolic process Source: GO_Central
  • aspartate metabolic process Source: UniProtKB
  • carbohydrate metabolic process Source: Reactome
  • cellular amino acid metabolic process Source: Reactome
  • gluconeogenesis Source: Reactome
  • glutamate metabolic process Source: UniProtKB
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-GGA-352875. Gluconeogenesis.
R-GGA-372568. Amino acid metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate aminotransferase, mitochondrial (EC:2.6.1.1, EC:2.6.1.7)
Short name:
mAspAT
Alternative name(s):
Glutamate oxaloacetate transaminase 2
Kynurenine aminotransferase 4
Kynurenine aminotransferase IV
Kynurenine--oxoglutarate transaminase 4
Kynurenine--oxoglutarate transaminase IV
Transaminase A
Gene namesi
Name:GOT2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222Mitochondrion1 PublicationAdd
BLAST
Chaini23 – 423401Aspartate aminotransferase, mitochondrialPRO_0000001219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP00508.
PRIDEiP00508.

Expressioni

Tissue specificityi

Detected in heart (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.4 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi676777. 1 interaction.
IntActiP00508. 1 interaction.
STRINGi9031.ENSGALP00000003646.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 284Combined sources
Helixi36 – 4611Combined sources
Beta strandi56 – 583Combined sources
Turni63 – 653Combined sources
Helixi71 – 8212Combined sources
Helixi96 – 10712Combined sources
Helixi112 – 1154Combined sources
Beta strandi119 – 1257Combined sources
Helixi126 – 14116Combined sources
Beta strandi147 – 1537Combined sources
Helixi158 – 1647Combined sources
Beta strandi168 – 1736Combined sources
Turni177 – 1804Combined sources
Helixi184 – 1918Combined sources
Beta strandi199 – 2068Combined sources
Turni208 – 2103Combined sources
Helixi216 – 22813Combined sources
Beta strandi232 – 2387Combined sources
Turni240 – 2445Combined sources
Helixi247 – 2504Combined sources
Helixi252 – 2598Combined sources
Beta strandi265 – 2695Combined sources
Turni271 – 2733Combined sources
Helixi277 – 2793Combined sources
Beta strandi281 – 2877Combined sources
Helixi291 – 30919Combined sources
Helixi314 – 32512Combined sources
Helixi327 – 35731Combined sources
Helixi365 – 3695Combined sources
Beta strandi372 – 3765Combined sources
Helixi381 – 39111Combined sources
Turni397 – 3993Combined sources
Beta strandi400 – 4023Combined sources
Helixi403 – 4053Combined sources
Turni408 – 4103Combined sources
Helixi411 – 42212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKAX-ray2.10A/B23-423[»]
1AKBX-ray2.30A23-423[»]
1AKCX-ray2.30A23-423[»]
1AMAX-ray2.30A23-423[»]
1IVRX-ray2.40A23-423[»]
1MAPX-ray2.40A23-423[»]
1MAQX-ray2.30A23-423[»]
1OXOX-ray2.30A/B23-423[»]
1OXPX-ray2.50A23-423[»]
1TARX-ray2.20A/B23-423[»]
1TASX-ray2.80A/B23-423[»]
1TATX-ray3.00A/B23-423[»]
7AATX-ray1.90A/B23-423[»]
8AATX-ray2.30A/B23-423[»]
9AATX-ray2.20A/B23-423[»]
ProteinModelPortaliP00508.
SMRiP00508. Positions 23-423.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00508.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00508.
KOiK14455.
PhylomeDBiP00508.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLQSRLLL SAPRRAAATA RASSWWSHVE MGPPDPILGV TEAFKRDTNS
60 70 80 90 100
KKMNLGVGAY RDDNGKSYVL NCVRKAEAMI AAKKMDKEYL PIAGLADFTR
110 120 130 140 150
ASAELALGEN SEAFKSGRYV TVQGISGTGS LRVGANFLQR FFKFSRDVYL
160 170 180 190 200
PKPSWGNHTP IFRDAGLQLQ AYRYYDPKTC SLDFTGAMED ISKIPEKSII
210 220 230 240 250
LLHACAHNPT GVDPRQEQWK ELASVVKKRN LLAYFDMAYQ GFASGDINRD
260 270 280 290 300
AWALRHFIEQ GIDVVLSQSY AKNMGLYGER AGAFTVICRD AEEAKRVESQ
310 320 330 340 350
LKILIRPMYS NPPMNGARIA SLILNTPELR KEWLVEVKGM ADRIISMRTQ
360 370 380 390 400
LVSNLKKEGS SHNWQHITDQ IGMFCFTGLK PEQVERLTKE FSIYMTKDGR
410 420
ISVAGVASSN VGYLAHAIHQ VTK
Length:423
Mass (Da):47,241
Last modified:October 1, 1989 - v2
Checksum:i59D65D4ED4DDF8BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671S → P AA sequence (PubMed:6345546).Curated
Sequence conflicti168 – 1681Q → E AA sequence (PubMed:6345546).Curated
Sequence conflicti216 – 2161Q → E AA sequence (PubMed:6345546).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12105 mRNA. Translation: AAA48603.1.
PIRiA24554. XNCHDM.
RefSeqiNP_990854.1. NM_205523.1.
UniGeneiGga.4425.

Genome annotation databases

GeneIDi396533.
KEGGigga:396533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12105 mRNA. Translation: AAA48603.1.
PIRiA24554. XNCHDM.
RefSeqiNP_990854.1. NM_205523.1.
UniGeneiGga.4425.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKAX-ray2.10A/B23-423[»]
1AKBX-ray2.30A23-423[»]
1AKCX-ray2.30A23-423[»]
1AMAX-ray2.30A23-423[»]
1IVRX-ray2.40A23-423[»]
1MAPX-ray2.40A23-423[»]
1MAQX-ray2.30A23-423[»]
1OXOX-ray2.30A/B23-423[»]
1OXPX-ray2.50A23-423[»]
1TARX-ray2.20A/B23-423[»]
1TASX-ray2.80A/B23-423[»]
1TATX-ray3.00A/B23-423[»]
7AATX-ray1.90A/B23-423[»]
8AATX-ray2.30A/B23-423[»]
9AATX-ray2.20A/B23-423[»]
ProteinModelPortaliP00508.
SMRiP00508. Positions 23-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676777. 1 interaction.
IntActiP00508. 1 interaction.
STRINGi9031.ENSGALP00000003646.

Proteomic databases

PaxDbiP00508.
PRIDEiP00508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396533.
KEGGigga:396533.

Organism-specific databases

CTDi2806.

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00508.
KOiK14455.
PhylomeDBiP00508.

Enzyme and pathway databases

ReactomeiR-GGA-352875. Gluconeogenesis.
R-GGA-372568. Amino acid metabolism.

Miscellaneous databases

EvolutionaryTraceiP00508.
NextBioi20816569.
PROiP00508.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11879. PTHR11879. 1 hit.
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSiPR00799. TRANSAMINASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The primary structure of the precursor of chicken mitochondrial aspartate aminotransferase. Cloning and sequence analysis of cDNA."
    Jaussi R., Cotton B., Juretic N., Christen P., Schumperli D.
    J. Biol. Chem. 260:16060-16063(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The covalent structure of mitochondrial aspartate aminotransferase from chicken. Identification of segments of the polypeptide chain invariant specifically in the mitochondrial isoenzyme."
    Graf-Hausner U., Wilson K.J., Christen P.
    J. Biol. Chem. 258:8813-8826(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-423.
  3. "Structure of the genes of two homologous intracellularly heterotopic isoenzymes. Cytosolic and mitochondrial aspartate aminotransferase of chicken."
    Juretic N., Mattes U., Ziak M., Christen P., Jaussi R.
    Eur. J. Biochem. 192:119-126(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE STRUCTURE.
    Strain: White leghorn.
  4. "X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase."
    McPhalen C.A., Vincent M.G., Jansonius J.N.
    J. Mol. Biol. 225:495-517(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE, PYRIDOXAL PHOSPHATE AT LYS-272, COFACTOR, SUBUNIT.
  5. "Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase."
    Malashkevich V.N., Toney M.D., Jansonius J.N.
    Biochemistry 32:13451-13462(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-423 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE; L-ASPARTATE AND L-GLUTAMATE, COFACTOR, SUBUNIT.
  6. "Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate."
    von Stosch A.G.
    Biochemistry 35:15260-15268(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-423 IN COMPLEX WITH ERYTHRO-BETA-HYDROXYASPARTATE, COFACTOR.
  7. "Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase."
    Markovic-Housley Z., Schirmer T., Hohenester E., Khomutov A.R., Khomutov R.M., Karpeisky M.Y., Sandmeier E., Christen P., Jansonius J.N.
    Eur. J. Biochem. 236:1025-1032(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-423 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND SUBSTRATE ANALOGS, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.

Entry informationi

Entry nameiAATM_CHICK
AccessioniPrimary (citable) accession number: P00508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: February 17, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.