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Reviewed, UniProtKB/Swiss-Prot P50554 (GABT_RAT)

Last modified February 9, 2010. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    4-aminobutyrate aminotransferase, mitochondrial
    EC=2.6.1.19
Alternative name(s):
    Gamma-amino-N-butyrate transaminase
      Short name=GABA transaminase
      Short name=GABA-T
    GABA aminotransferase
      Short name=GABA-AT
    L-AIBAT
    (S)-3-amino-2-methylpropionate transaminase
    EC=2.6.1.22
Cleaved into the following 2 chains:
    1- Recommended name:
            4-aminobutyrate aminotransferase, brain isoform
    2- Recommended name:
            4-aminobutyrate aminotransferase, liver isoform
Gene names
Name: Abat
Synonyms: Gabat
OrganismRattus norvegicus (Rat)
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.

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
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processbehavioral response to cocaine

Inferred from sequence or structural similarity. Source: UniProtKB

copulation

Inferred from mutant phenotype. Source: RGD

gamma-aminobutyric acid catabolic process Ref.2

Inferred by curator. Source: UniProtKB

locomotory behavior

Inferred from mutant phenotype. Source: RGD

negative regulation of blood pressure

Inferred from mutant phenotype. Source: RGD

neurotransmitter catabolic process Ref.2

Inferred by curator. Source: UniProtKB

response to drug

Inferred from direct assay. Source: RGD

response to ethanol

Inferred from direct assay. Source: RGD

response to hypoxia

Inferred from mutant phenotype. Source: RGD

response to iron ion

Inferred from direct assay. Source: RGD

response to nicotine

Inferred from mutant phenotype. Source: RGD

   Cellular component4-aminobutyrate transaminase complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptosome

Inferred from direct assay. Source: RGD

   Molecular function(S)-3-amino-2-methylpropionate transaminase activity

Inferred from electronic annotation. Source: EC

4-aminobutyrate transaminase activity Ref.2

Inferred from direct assay. 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 residue3181N6-acetyllysine By similarity
Modified residue3571N6-(pyridoxal phosphate)lysine

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
P50554-1 [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: 8133261] [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: 10447691] [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: 10989446] [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: 15489334] [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, 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.
IPIIPI00199426.
PIRI56502.
RefSeqNP_112265.1.
UniGeneRn.10090

3D structure databases

SMRP50554. Positions 39-499.
ModBaseSearch...

Protein-protein interaction databases

STRINGP50554.

PTM databases

PhosphoSiteP50554.

Proteomic databases

PRIDEP50554.

Genome annotation databases

EnsemblENSRNOT00000003633; ENSRNOP00000003633; ENSRNOG00000002636; Rattus norvegicus. [Genome view]
GeneID81632.
KEGGrno:81632.
NMPDRfig|10116.3.peg.4435.
UCSCNM_031003. rat.

Organism-specific databases

CTD81632.
RGD620948. Abat.

Phylogenomic databases

eggNOGroNOG08236.
HOVERGENP50554.
InParanoidP50554.
OMAINIIKRE.
OrthoDBEOG9KM1NJ.
PhylomeDBP50554.

Enzyme and pathway databases

BRENDA2.6.1.19. 248.
2.6.1.22. 248.

Gene expression databases

ArrayExpressP50554.
GenevestigatorP50554.
GermOnlineENSRNOG00000002636. Rattus norvegicus.

Family and domain databases

InterProIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF6. GABAtrns_euk. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615107.

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: February 9, 2010
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents