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Protein

Aspartate aminotransferase, cytoplasmic

Gene

GOT1

Organism
Sus scrofa (Pig)
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 (By similarity).By similarity

Catalytic activityi

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.1 Publication
L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Aspartate; via amide nitrogen
Binding sitei141 – 1411Aspartate
Binding sitei195 – 1951Aspartate
Binding sitei387 – 3871Aspartate

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

BioCyciMetaCyc:MONOMER-13031.
ReactomeiR-SSC-70263. Gluconeogenesis.
R-SSC-70614. Amino acid synthesis and interconversion (transamination).

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 413412Aspartate aminotransferase, cytoplasmicPRO_0000123881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP00503.
PeptideAtlasiP00503.
PRIDEiP00503.

Expressioni

Gene expression databases

GenevisibleiP00503. SS.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011226.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 94Combined sources
Helixi17 – 2610Combined sources
Helixi52 – 6211Combined sources
Helixi78 – 8912Combined sources
Helixi94 – 974Combined sources
Beta strandi101 – 1077Combined sources
Helixi108 – 12316Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi134 – 1396Combined sources
Helixi143 – 1508Combined sources
Beta strandi156 – 1605Combined sources
Turni164 – 1674Combined sources
Helixi171 – 18010Combined sources
Beta strandi186 – 1938Combined sources
Turni195 – 1973Combined sources
Helixi203 – 21614Combined sources
Beta strandi219 – 2257Combined sources
Turni227 – 2315Combined sources
Helixi234 – 2374Combined sources
Helixi239 – 2468Combined sources
Beta strandi251 – 2566Combined sources
Turni258 – 2603Combined sources
Helixi264 – 2663Combined sources
Beta strandi268 – 2747Combined sources
Helixi278 – 29316Combined sources
Turni294 – 2963Combined sources
Helixi302 – 31211Combined sources
Helixi314 – 34431Combined sources
Helixi352 – 3565Combined sources
Beta strandi359 – 3635Combined sources
Helixi368 – 3769Combined sources
Beta strandi386 – 3894Combined sources
Helixi390 – 3923Combined sources
Turni395 – 3973Combined sources
Helixi398 – 41114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJRX-ray1.74A/B2-413[»]
1AJSX-ray1.60A/B2-413[»]
ProteinModelPortaliP00503.
SMRiP00503. Positions 2-413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00503.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00503.
KOiK14454.
OMAiYYSNPTW.
OrthoDBiEOG74J980.
TreeFamiTF314089.

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.

P00503-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPSVFAEV PQAQPVLVFK LIADFREDPD PRKVNLGVGA YRTDDCQPWV
60 70 80 90 100
LPVVRKVEQR IANDSSLNHE YLPILGLAEF RTCASRLALG DDSPALQEKR
110 120 130 140 150
VGGVQSLGGT GALRIGAEFL ARWYNGTNNK DTPVYVSSPT WENHNGVFTT
160 170 180 190 200
AGFKDIRSYR YWDTEKRGLD LQGFLSDLEN APEFSIFVLH ACAHNPTGTD
210 220 230 240 250
PTPEQWKQIA SVMKRRFLFP FFDSAYQGFA SGNLEKDAWA IRYFVSEGFE
260 270 280 290 300
LFCAQSFSKN FGLYNERVGN LTVVAKEPDS ILRVLSQMEK IVRVTWSNPP
310 320 330 340 350
AQGARIVART LSDPELFHEW TGNVKTMADR ILSMRSELRA RLEALKTPGT
360 370 380 390 400
WNHITDQIGM FSFTGLNPKQ VEYLINEKHI YLLPSGRINM CGLTTKNLDY
410
VATSIHEAVT KIQ
Length:413
Mass (Da):46,475
Last modified:January 23, 2007 - v3
Checksum:iE466EDAD9446EF25
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451N → D AA sequence (PubMed:11946901).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24088 mRNA. Translation: AAA53531.1.
PIRiA30138. XNPGDC.
RefSeqiNP_999092.1. NM_213927.1.
UniGeneiSsc.3528.

Genome annotation databases

EnsembliENSSSCT00000011527; ENSSSCP00000011226; ENSSSCG00000010537.
GeneIDi396967.
KEGGissc:396967.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24088 mRNA. Translation: AAA53531.1.
PIRiA30138. XNPGDC.
RefSeqiNP_999092.1. NM_213927.1.
UniGeneiSsc.3528.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJRX-ray1.74A/B2-413[»]
1AJSX-ray1.60A/B2-413[»]
ProteinModelPortaliP00503.
SMRiP00503. Positions 2-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011226.

Proteomic databases

PaxDbiP00503.
PeptideAtlasiP00503.
PRIDEiP00503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000011527; ENSSSCP00000011226; ENSSSCG00000010537.
GeneIDi396967.
KEGGissc:396967.

Organism-specific databases

CTDi2805.

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
GeneTreeiENSGT00390000014081.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00503.
KOiK14454.
OMAiYYSNPTW.
OrthoDBiEOG74J980.
TreeFamiTF314089.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13031.
ReactomeiR-SSC-70263. Gluconeogenesis.
R-SSC-70614. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

EvolutionaryTraceiP00503.

Gene expression databases

GenevisibleiP00503. SS.

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. "cDNA cloning and expression of pig cytosolic aspartate aminotransferase in Escherichia coli: amino-terminal heterogeneity of expressed products and lack of its correlation with enzyme function."
    Nagashima F., Tanase S., Fukumoto Y., Joh T., Nomiyama H., Tsuzuki T., Shimada K., Kuramitsu S., Kagamiyama H., Morino Y.
    Biochemistry 28:1153-1160(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: PROTEIN SEQUENCE OF 2-413.
    Tissue: Heart muscle.
  3. "The complete primary structure of cytoplasmic aspartate amino-transferase from pig heart muscle."
    Ovchinnikov Y.A., Egorov T.A., Aldanova N.A., Feigina M.Y., Lipkin V.M., Abdulaev N.G., Grishin E.V., Kiselev A.P., Modyanov N.N., Braunstein A.E., Polyanovsky O.L., Nosikov V.V.
    Izv. Akad. Nauk SSSR, Ser. Khim. 1974:1189-1196(1974)
    Cited for: PROTEIN SEQUENCE OF 2-413.
  4. "The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues."
    Doonan S., Doonan H.J., Hanford R., Vernon C.A., Walker J.M., Airoldi L.P., Da S., Bossa F., Barra D., Carloni M., Fasella P., Riva F.
    Biochem. J. 149:497-506(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-413.
  5. "The position of an essential tyrosine residue in the polypeptide chain of aspartate transaminase."
    Polyanovsky O.L., Demidkina T.V., Egorov C.A.
    FEBS Lett. 23:262-264(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  6. "Primary structure of pyridoxal phosphate binding site in the mitochondrial and extramitochondrial aspartate aminotransferases from pig heart muscle. Chymotryptic peptides."
    Morino Y., Watanabe T.
    Biochemistry 8:3412-3417(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  7. "Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate."
    Rhee S., Silva M.M., Hyde C.C., Rogers P.H., Metzler C.M., Metzler D.E., Arnone A.
    J. Biol. Chem. 272:17293-17302(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND 2-METHYLASPARTATE, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-259, SUBUNIT.

Entry informationi

Entry nameiAATC_PIG
AccessioniPrimary (citable) accession number: P00503
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 142 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.