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P80147 (GABT_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-aminobutyrate aminotransferase, mitochondrial

EC=2.6.1.19
Alternative name(s):
(S)-3-amino-2-methylpropionate transaminase
EC=2.6.1.22
GABA aminotransferase
Short name=GABA-AT
Gamma-amino-N-butyrate transaminase
Short name=GABA transaminase
Short name=GABA-T
L-AIBAT
Gene names
Name:ABAT
Synonyms:GABAT
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.

Catalytic activity

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to cocaine

Inferred from sequence or structural similarity. Source: UniProtKB

gamma-aminobutyric acid catabolic process

Inferred by curator PubMed 11561735. Source: UniProtKB

neurotransmitter catabolic process

Inferred by curator PubMed 11561735. Source: UniProtKB

   Cellular_component4-aminobutyrate transaminase complex

Inferred from direct assay PubMed 6470007. Source: UniProtKB

cytosol

Traceable author statement PubMed 8565962. Source: UniProtKB

mitochondrial matrix

Traceable author statement PubMed 6470007. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function(S)-3-amino-2-methylpropionate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

4-aminobutyrate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein homodimerization activity

Inferred from physical interaction PubMed 648527. Source: UniProtKB

pyridoxal phosphate binding

Inferred from direct assay PubMed 6470007. Source: UniProtKB

succinate-semialdehyde dehydrogenase binding

Inferred from direct assay PubMed 6470007. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Ref.2
Chain29 – 5004724-aminobutyrate aminotransferase, mitochondrial
PRO_0000001251

Amino acid modifications

Modified residue2311N6-succinyllysine By similarity
Modified residue2521N6-acetyllysine; alternate By similarity
Modified residue2521N6-succinyllysine; alternate By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine By similarity
Modified residue3571N6-(pyridoxal phosphate)lysine
Modified residue4131N6-acetyllysine; alternate By similarity
Modified residue4131N6-succinyllysine; alternate By similarity
Modified residue4521N6-acetyllysine By similarity
Modified residue4701N6-acetyllysine By similarity
Disulfide bond163 ↔ 166
Disulfide bond321Interchain By similarity

Experimental info

Sequence conflict4541I → N in AAA96981. Ref.1

Secondary structure

............................................................................... 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80147 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: BFD0B80846CEF5B7

FASTA50056,620
        10         20         30         40         50         60 
MASVLLTRRL ACSFRHNHRL LVPGWRHISQ AAAKVDVEFD YDGPLMKTEV PGPRSRELMK 

        70         80         90        100        110        120 
QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSIPIGYSHP ALVKLVQQPQ 

       130        140        150        160        170        180 
NVSTFINRPA LGILPPENFV EKLRESLLSV APKGMSQLIT MACGSCSNEN AFKTIFMWYR 

       190        200        210        220        230        240 
SKERGQSAFS KEELETCMIN QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS 

       250        260        270        280        290        300 
FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG 

       310        320        330        340        350        360 
DNHASDDFFR KLRDISRKHG CAFLVDEVQT GGGSTGKFWA HEHWGLDDPA DVMTFSKKMM 

       370        380        390        400        410        420 
TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLSNAAH AGKVLLTGLL 

       430        440        450        460        470        480 
DLQARYPQFI SRVRGRGTFC SFDTPDESIR NKLISIARNK GVMLGGCGDK SIRFRPTLVF 

       490        500 
RDHHAHLFLN IFSDILADFK 

« Hide

References

[1]"Brain 4-aminobutyrate aminotransferase. Isolation and sequence of a cDNA encoding the enzyme."
Kwon O.S., Park J., Churchich J.E.
J. Biol. Chem. 267:7215-7216(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Protein structure of pig liver 4-aminobutyrate aminotransferase and comparison with a cDNA-deduced sequence."
de Biase D., Maras B., Bossa F., Barra D., John R.A.
Eur. J. Biochem. 208:351-357(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-500.
Tissue: Liver.
[3]"Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy."
Storici P., Capitani G., De Biase D., Moser M., John R.A., Jansonius J.N., Schirmer T.
Biochemistry 38:8628-8634(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84802 mRNA. Translation: AAA96981.1.
RefSeqNP_999428.1. NM_214263.1.
UniGeneSsc.16251.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OHVX-ray2.30A/B/C/D29-500[»]
1OHWX-ray2.30A/B/C/D29-500[»]
1OHYX-ray2.80A/B/C/D29-500[»]
ProteinModelPortalP80147.
SMRP80147. Positions 39-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1149627. 1 interaction.
STRING9823.ENSSSCP00000008445.

Chemistry

BindingDBP80147.
ChEMBLCHEMBL2266.

Proteomic databases

PaxDbP80147.
PRIDEP80147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397500.
KEGGssc:397500.

Organism-specific databases

CTD18.

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020208.
HOVERGENHBG000634.
KOK13524.

Enzyme and pathway databases

SABIO-RKP80147.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80147.

Entry information

Entry nameGABT_PIG
AccessionPrimary (citable) accession number: P80147
Secondary accession number(s): P27820
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references