Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartate aminotransferase, mitochondrial

Gene

GOT2

Organism
Sus scrofa (Pig)
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. Facilitates 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651Substrate; via amide nitrogenBy similarity
Binding sitei162 – 1621SubstrateBy similarity
Binding sitei215 – 2151SubstrateBy similarity
Binding sitei407 – 4071SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Pyridoxal phosphate

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):
Fatty acid-binding protein
Short name:
FABP-1
Glutamate oxaloacetate transaminase 2
Kynurenine aminotransferase 4
Kynurenine aminotransferase IV
Kynurenine--oxoglutarate transaminase 4
Kynurenine--oxoglutarate transaminase IV
Plasma membrane-associated fatty acid-binding protein
Short name:
FABPpm
Transaminase A
Gene namesi
Name:GOT2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929Mitochondrion2 PublicationsAdd
BLAST
Chaini30 – 430401Aspartate aminotransferase, mitochondrialPRO_0000001217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphothreonineBy similarity
Modified residuei59 – 591N6-acetyllysineBy similarity
Modified residuei73 – 731N6-acetyllysine; alternateBy similarity
Modified residuei73 – 731N6-succinyllysine; alternateBy similarity
Modified residuei82 – 821N6-acetyllysineBy similarity
Modified residuei90 – 901N6-acetyllysine; alternateBy similarity
Modified residuei90 – 901N6-succinyllysine; alternateBy similarity
Modified residuei96 – 961Nitrated tyrosine; alternateBy similarity
Modified residuei96 – 961Phosphotyrosine; alternateBy similarity
Modified residuei107 – 1071N6-acetyllysine; alternateBy similarity
Modified residuei107 – 1071N6-succinyllysine; alternateBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
Modified residuei159 – 1591N6-acetyllysine; alternateBy similarity
Modified residuei159 – 1591N6-succinyllysine; alternateBy similarity
Modified residuei185 – 1851N6-acetyllysine; alternateBy similarity
Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
Modified residuei227 – 2271N6-succinyllysineBy similarity
Modified residuei234 – 2341N6-acetyllysineBy similarity
Modified residuei279 – 2791N6-(pyridoxal phosphate)lysine; alternate
Modified residuei279 – 2791N6-acetyllysine; alternateBy similarity
Modified residuei296 – 2961N6-acetyllysine; alternateBy similarity
Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
Modified residuei302 – 3021N6-acetyllysineBy similarity
Modified residuei309 – 3091N6-acetyllysine; alternateBy similarity
Modified residuei309 – 3091N6-succinyllysine; alternateBy similarity
Modified residuei345 – 3451N6-acetyllysineBy similarity
Modified residuei363 – 3631N6-acetyllysine; alternateBy similarity
Modified residuei363 – 3631N6-succinyllysine; alternateBy similarity
Modified residuei364 – 3641N6-acetyllysineBy similarity
Modified residuei387 – 3871N6-acetyllysineBy similarity
Modified residuei396 – 3961N6-acetyllysine; alternateBy similarity
Modified residuei396 – 3961N6-succinyllysine; alternateBy similarity
Modified residuei404 – 4041N6-acetyllysine; alternateBy similarity
Modified residuei404 – 4041N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP00506.
PRIDEiP00506.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003017.

Structurei

3D structure databases

ProteinModelPortaliP00506.
SMRiP00506. Positions 30-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00506.
KOiK14455.

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.

P00506-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLHSGRVL SGVASAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA
60 70 80 90 100
FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG
110 120 130 140 150
GLAEFCKASA ELALGENNEV LKSGRYVTVQ TISGTGALRI GANFLQRFFK
160 170 180 190 200
FSRDVFLPKP SWGNHTPIFR DAGMQLHSYR YYDPKTCGFD FTGALEDISK
210 220 230 240 250
IPAQSVILLH ACAHNPTGVD PRPEQWKEMA TLVKKNNLFA FFDMAYQGFA
260 270 280 290 300
SGDGNKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
310 320 330 340 350
AKRVESQLKI LIRPMYSNPP VNGARIASTI LTSPDLRQQW LQEVKGMADR
360 370 380 390 400
IISMRTQLVS NLKKEGSSHN WQHIVDQIGM FCFTGIKPEQ VERLTKEFSI
410 420 430
YMTKDGRISV AGVTSGNVGY LAHAIHQVTK
Length:430
Mass (Da):47,436
Last modified:October 1, 1989 - v2
Checksum:i23280D11821A8BC4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711N → D AA sequence (PubMed:7391012).Curated
Sequence conflicti256 – 2561K → R in CAA23279 (PubMed:8672129).Curated
Sequence conflicti273 – 2731L → F in CAA23279 (PubMed:8672129).Curated
Sequence conflicti305 – 3051E → Q AA sequence (PubMed:7408859).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11732 mRNA. Translation: AAA30999.1.
F14822 mRNA. Translation: CAA23279.1.
PIRiA25165. XNPGDM.
RefSeqiNP_999093.1. NM_213928.1.
UniGeneiSsc.3588.

Genome annotation databases

GeneIDi396968.
KEGGissc:396968.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11732 mRNA. Translation: AAA30999.1.
F14822 mRNA. Translation: CAA23279.1.
PIRiA25165. XNPGDM.
RefSeqiNP_999093.1. NM_213928.1.
UniGeneiSsc.3588.

3D structure databases

ProteinModelPortaliP00506.
SMRiP00506. Positions 30-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000003017.

Proteomic databases

PaxDbiP00506.
PRIDEiP00506.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396968.
KEGGissc:396968.

Organism-specific databases

CTDi2806.

Phylogenomic databases

eggNOGiKOG1411. Eukaryota.
COG1448. LUCA.
HOGENOMiHOG000185898.
HOVERGENiHBG000951.
InParanoidiP00506.
KOiK14455.

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

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a cDNA encoding porcine mitochondrial aspartate aminotransferase precursor."
    Joh T., Nomiyama H., Maeda S., Shimada K., Morino Y.
    Proc. Natl. Acad. Sci. U.S.A. 82:6065-6069(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The cytosolic and mitochondrial aspartate aminotransferases from pig heart. A comparison of their primary structures, predicted secondary structures and some physical properties."
    Barra D., Bossa F., Doonan S., Fahmy H.M.A., Hughes G.J., Martini F., Petruzzelli R., Wittmann-Liebold B.
    Eur. J. Biochem. 108:405-414(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-430.
  3. "Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Peptide ordering procedures and the complete sequence."
    Kagamiyama H., Sakakibara R., Tanase S., Morino Y., Wada H.
    J. Biol. Chem. 255:6153-6159(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-430.
    Tissue: Heart muscle.
  4. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
    Winteroe A.K., Fredholm M., Davies W.
    Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-399.
    Tissue: Small intestine.
  5. "The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage with pepsin and with Staphylococcus aureus protease."
    Barra D., Savi M.R., Petruzzelli R., Bossa F., Doonan S.
    Ital. J. Biochem. 28:478-490(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiAATM_PIG
AccessioniPrimary (citable) accession number: P00506
Secondary accession number(s): Q29230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: February 17, 2016
This is version 125 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.