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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)DescriptionActionsGraphical viewLength
Binding sitei58Substrate; via amide nitrogen1
Binding sitei155Substrate1
Binding sitei208Substrate1
Binding sitei400Substrate1

GO - Molecular functioni

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: UniProtKB
  • aspartate catabolic process Source: GO_Central
  • aspartate metabolic process Source: UniProtKB
  • cellular amino acid metabolic process Source: Reactome
  • gluconeogenesis Source: Reactome
  • glutamate metabolic process Source: UniProtKB
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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 22Mitochondrion1 PublicationAdd BLAST22
ChainiPRO_000000121923 – 423Aspartate aminotransferase, mitochondrialAdd BLAST401

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei272N6-(pyridoxal phosphate)lysine1

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 interactor.
IntActiP00508. 1 interactor.
STRINGi9031.ENSGALP00000003646.

Structurei

Secondary structure

1423
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni25 – 28Combined sources4
Helixi36 – 46Combined sources11
Beta strandi56 – 58Combined sources3
Turni63 – 65Combined sources3
Helixi71 – 82Combined sources12
Helixi96 – 107Combined sources12
Helixi112 – 115Combined sources4
Beta strandi119 – 125Combined sources7
Helixi126 – 141Combined sources16
Beta strandi147 – 153Combined sources7
Helixi158 – 164Combined sources7
Beta strandi168 – 173Combined sources6
Turni177 – 180Combined sources4
Helixi184 – 191Combined sources8
Beta strandi199 – 206Combined sources8
Turni208 – 210Combined sources3
Helixi216 – 228Combined sources13
Beta strandi232 – 238Combined sources7
Turni240 – 244Combined sources5
Helixi247 – 250Combined sources4
Helixi252 – 259Combined sources8
Beta strandi265 – 269Combined sources5
Turni271 – 273Combined sources3
Helixi277 – 279Combined sources3
Beta strandi281 – 287Combined sources7
Helixi291 – 309Combined sources19
Helixi314 – 325Combined sources12
Helixi327 – 357Combined sources31
Helixi365 – 369Combined sources5
Beta strandi372 – 376Combined sources5
Helixi381 – 391Combined sources11
Turni397 – 399Combined sources3
Beta strandi400 – 402Combined sources3
Helixi403 – 405Combined sources3
Turni408 – 410Combined sources3
Helixi411 – 422Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti67S → P AA sequence (PubMed:6345546).Curated1
Sequence conflicti168Q → E AA sequence (PubMed:6345546).Curated1
Sequence conflicti216Q → E AA sequence (PubMed:6345546).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676777. 1 interactor.
IntActiP00508. 1 interactor.
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.
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...

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: November 2, 2016
This is version 133 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.