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P50554 (GABT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to cocaine

Inferred from sequence or structural similarity. Source: UniProtKB

copulation

Inferred from mutant phenotype PubMed 8117236. Source: RGD

gamma-aminobutyric acid catabolic process

Inferred by curator Ref.2. Source: UniProtKB

locomotory behavior

Inferred from mutant phenotype PubMed 7945972. Source: RGD

negative regulation of blood pressure

Inferred from mutant phenotype PubMed 8336820. Source: RGD

neurotransmitter catabolic process

Inferred by curator Ref.2. Source: UniProtKB

response to cocaine

Inferred from mutant phenotype PubMed 12373739. Source: RGD

response to drug

Inferred from direct assay PubMed 7931216. Source: RGD

response to ethanol

Inferred from direct assay PubMed 7710740. Source: RGD

response to hypoxia

Inferred from mutant phenotype PubMed 10727784. Source: RGD

response to iron ion

Inferred from direct assay PubMed 9719948. Source: RGD

response to nicotine

Inferred from mutant phenotype PubMed 10025686. Source: RGD

   Cellular_component4-aminobutyrate transaminase complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from direct assay PubMed 8247350. Source: RGD

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

Inferred from electronic annotation. Source: UniProtKB-EC

4-aminobutyrate transaminase activity

Inferred from direct assay Ref.2. Source: RGD

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

pyridoxal phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

succinate-semialdehyde dehydrogenase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion
Chain28 – 5004734-aminobutyrate aminotransferase, brain isoform
PRO_0000001252
Chain35 – 5004664-aminobutyrate aminotransferase, liver isoform
PRO_0000001253

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 By similarity
Disulfide bond321Interchain By similarity

Experimental info

Sequence conflict31F → L in AAA70415. Ref.1
Sequence conflict251S → T in AAA70415. Ref.1
Sequence conflict361D → T in AAA70415. Ref.1
Sequence conflict135 – 17036PPENF…CSNEN → LQRTLWTSSGSPCSRWLPKA CVSSSRWPAGPAPMRM in AAA70415. Ref.1
Sequence conflict2771I → N in AAA70415. Ref.1
Sequence conflict4251Q → R in AAA70415. Ref.1
Sequence conflict4471E → K Ref.2
Sequence conflict4471E → K in BAA25570. Ref.3
Sequence conflict4861H → Q in AAA70415. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50554 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: 1EA7180B72797B72

FASTA50056,456
        10         20         30         40         50         60 
MAFLLTTRRL VCSSQKNLHL FTPGSRYISQ AAAKVDFEFD YDGPLMKTEV PGPRSQELMK 

        70         80         90        100        110        120 
QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYNHP ALAKLVQQPQ 

       130        140        150        160        170        180 
NASTFINRPA LGILPPENFV DKLRESLMSV APKGMCQLIT MACGSCSNEN AFKTIFMWYR 

       190        200        210        220        230        240 
SKERGQRGFS KEELETCMVN QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS 

       250        260        270        280        290        300 
FDWPIAPFPR LKYPLEEFVT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG 

       310        320        330        340        350        360 
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMSFSKKMM 

       370        380        390        400        410        420 
TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNVAH AGKTLLTGLL 

       430        440        450        460        470        480 
DLQAQYPQFV SRVRGRGTFC SFDTPDEAIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF 

       490        500 
RDHHAHLFLN IFSGILADFK 

« Hide

References

« Hide 'large scale' references
[1]"A rat brain cDNA encodes enzymatically active GABA transaminase and provides a molecular probe for GABA-catabolizing cells."
Medina-Kauwe L.K., Tillakaratne N.J., Wu J.Y., Tobin A.J.
J. Neurochem. 62:1267-1275(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The mature size of rat 4-aminobutyrate aminotransferase is different in liver and brain."
Kontani Y., Sakata S.F., Matsuda K., Ohyama T., Sano K., Tamaki N.
Eur. J. Biochem. 264:218-222(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-54, PROTEOLYTIC PROCESSING.
Strain: Sprague-Dawley.
Tissue: Brain and Liver.
[3]"Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver."
Tamaki N., Sakata S.F., Matsuda K.
Methods Enzymol. 324:376-389(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: Sprague-Dawley.
Tissue: Liver.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 253-268 AND 389-400, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U29701 mRNA. Translation: AAA70415.1.
D87839 mRNA. Translation: BAA25570.1.
BC081787 mRNA. Translation: AAH81787.1.
PIRI56502.
RefSeqNP_112265.1. NM_031003.2.
XP_006245822.1. XM_006245760.1.
UniGeneRn.10090.

3D structure databases

ProteinModelPortalP50554.
SMRP50554. Positions 39-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000003633.

Chemistry

BindingDBP50554.
ChEMBLCHEMBL3148.

PTM databases

PhosphoSiteP50554.

2D gel databases

World-2DPAGE0004:P50554.

Proteomic databases

PaxDbP50554.
PRIDEP50554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003633; ENSRNOP00000003633; ENSRNOG00000002636.
GeneID81632.
KEGGrno:81632.
UCSCRGD:620948. rat.

Organism-specific databases

CTD18.
RGD620948. Abat.

Phylogenomic databases

eggNOGCOG0160.
GeneTreeENSGT00550000074885.
HOGENOMHOG000020208.
HOVERGENHBG000634.
InParanoidP50554.
KOK13524.
OMAKLIQQPQ.
OrthoDBEOG7ZPNJW.
PhylomeDBP50554.
TreeFamTF105021.

Enzyme and pathway databases

SABIO-RKP50554.

Gene expression databases

GenevestigatorP50554.

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

NextBio615107.
PROP50554.

Entry information

Entry nameGABT_RAT
AccessionPrimary (citable) accession number: P50554
Secondary accession number(s): O70539, Q66HM1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 120 of the entry and version 3 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