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Protein

Aspartate aminotransferase, cytoplasmic

Gene

GOT1

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

Functioni

Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H2S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain.

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate.

Cofactori

pyridoxal 5'-phosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381Aspartate; via amide nitrogen
Binding sitei140 – 1401Aspartate
Binding sitei194 – 1941Aspartate
Binding sitei386 – 3861Aspartate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis

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, cytoplasmic (EC:2.6.1.1, EC:2.6.1.3)
Short name:
cAspAT
Alternative name(s):
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
Short name:
cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
Gene namesi
Name:GOT1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 412411Aspartate aminotransferase, cytoplasmicPRO_0000123884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei258 – 2581N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00504.
PRIDEiP00504.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000012086.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 84Combined sources
Helixi16 – 2611Combined sources
Helixi51 – 6212Combined sources
Helixi77 – 8812Combined sources
Helixi93 – 964Combined sources
Beta strandi100 – 1067Combined sources
Helixi107 – 12216Combined sources
Beta strandi123 – 1275Combined sources
Beta strandi133 – 1386Combined sources
Helixi142 – 1498Combined sources
Beta strandi155 – 1584Combined sources
Turni163 – 1664Combined sources
Helixi170 – 1789Combined sources
Beta strandi185 – 1928Combined sources
Turni194 – 1963Combined sources
Helixi202 – 21514Combined sources
Beta strandi218 – 2247Combined sources
Turni226 – 2305Combined sources
Helixi233 – 2364Combined sources
Helixi238 – 2458Combined sources
Beta strandi250 – 2556Combined sources
Turni257 – 2593Combined sources
Helixi263 – 2653Combined sources
Beta strandi267 – 2737Combined sources
Helixi277 – 29216Combined sources
Turni293 – 2953Combined sources
Helixi301 – 31111Combined sources
Helixi313 – 34432Combined sources
Helixi352 – 3554Combined sources
Beta strandi358 – 3625Combined sources
Helixi367 – 3759Combined sources
Beta strandi386 – 3883Combined sources
Helixi389 – 3913Combined sources
Turni394 – 3963Combined sources
Helixi397 – 41014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AATX-ray2.80A/B2-412[»]
2CSTX-ray1.90A/B2-412[»]
ProteinModelPortaliP00504.
SMRiP00504. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00504.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00504.
KOiK14454.
PhylomeDBiP00504.

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.

P00504-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASIFAAVP RAPPVAVFKL TADFREDGDS RKVNLGVGAY RTDEGQPWVL
60 70 80 90 100
PVVRKVEQLI AGDGSLNHEY LPILGLPEFR ANASRIALGD DSPAIAQKRV
110 120 130 140 150
GSVQGLGGTG ALRIGAEFLR RWYNGNNNTA TPVYVSSPTW ENHNSVFMDA
160 170 180 190 200
GFKDIRTYRY WDAAKRGLDL QGLLDDMEKA PEFSIFILHA CAHNPTGTDP
210 220 230 240 250
TPDEWKQIAA VMKRRCLFPF FDSAYQGFAS GSLDKDAWAV RYFVSEGFEL
260 270 280 290 300
FCAQSFSKNF GLYNERVGNL SVVGKDEDNV QRVLSQMEKI VRTTWSNPPS
310 320 330 340 350
QGARIVATTL TSPQLFAEWK DNVKTMADRV LLMRSELRSR LESLGTPGTW
360 370 380 390 400
NHITDQIGMF SFTGLNPKQV EYMIKEKHIY LMASGRINMC GLTTKNLDYV
410
AKSIHEAVTK IQ
Length:412
Mass (Da):45,935
Last modified:January 23, 2007 - v3
Checksum:iC55BEE72669078E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631D → N AA sequence (PubMed:499525).Curated
Sequence conflicti63 – 631D → N AA sequence (Ref. 3) Curated
Sequence conflicti121 – 1211Missing AA sequence (PubMed:499525).Curated
Sequence conflicti121 – 1211Missing AA sequence (Ref. 3) Curated
Sequence conflicti140 – 1401W → S AA sequence (Ref. 3) Curated
Sequence conflicti175 – 1751D → S AA sequence (PubMed:499525).Curated
Sequence conflicti175 – 1751D → S AA sequence (Ref. 3) Curated
Sequence conflicti232 – 2343SLD → NLE AA sequence (PubMed:499525).Curated
Sequence conflicti232 – 2343SLD → NLE AA sequence (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15636 mRNA. Translation: CAA33646.1.
PIRiS05583. XNCHDC.
RefSeqiNP_990652.1. NM_205321.1.
UniGeneiGga.730.

Genome annotation databases

GeneIDi396261.
KEGGigga:396261.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15636 mRNA. Translation: CAA33646.1.
PIRiS05583. XNCHDC.
RefSeqiNP_990652.1. NM_205321.1.
UniGeneiGga.730.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AATX-ray2.80A/B2-412[»]
2CSTX-ray1.90A/B2-412[»]
ProteinModelPortaliP00504.
SMRiP00504. Positions 2-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000012086.

Proteomic databases

PaxDbiP00504.
PRIDEiP00504.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396261.
KEGGigga:396261.

Organism-specific databases

CTDi2805.

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00504.
KOiK14454.
PhylomeDBiP00504.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP00504.
NextBioi20816313.
PROiP00504.

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. "Structure of cDNA of cytosolic aspartate aminotransferase of chicken and its expression in E. coli."
    Mattes U., Jaussi R., Ziak M., Juretic N., Lindenmann J.-M., Christen P.
    Biochimie 71:411-416(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Primary structure of cytoplasmic aspartate aminotransferase from chicken heart and its homology with pig heart isoenzymes."
    Shlyapnikov S.V., Myasnikov A.N., Severin E.S., Myagkova M.A., Torchinsky Y.M., Braunstein A.E.
    FEBS Lett. 106:385-388(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-412, ACETYLATION AT ALA-2.
    Tissue: Heart.
  3. "Primary structure of cytoplasmic aspartate aminotransferase from chicken heart IV, Structure of cyanogen bromide peptides and the complete amino acid sequence of the protein."
    Shlyapnikov S.V., Myasnikov A.N., Severin E.S., Myagkova M.A., Demidkina T.V., Torchinsky Y.M., Braunstein A.E.
    Bioorg. Khim. 6:876-884(1980)
    Cited for: PROTEIN SEQUENCE OF 2-412.
    Tissue: Heart.
  4. "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.
  5. "Three-dimensional structure at 3.2-A resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate."
    Harutyunyan E.G., Malashkevich V.N., Tersyan S.S., Kochkina V.M., Torchinsky Y.M., Braunstein A.E.
    FEBS Lett. 138:113-116(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE.
  6. "Electron density map of chicken heart cytosol aspartate transaminase at 3.5-A resolution."
    Borisov V.V., Borisova S.N., Sosfenov N.I., Vainshtein B.K.
    Nature 284:189-190(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
  7. "Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9-A resolution."
    Malashkevich V.N., Strokopytov B.V., Borisov V.V., Dauter Z., Wilson K.S., Torchinsky Y.M.
    J. Mol. Biol. 247:111-124(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-258, SUBUNIT.

Entry informationi

Entry nameiAATC_CHICK
AccessioniPrimary (citable) accession number: P00504
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 130 of the entry and version 3 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.