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Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

Abat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

pyridoxal 5'-phosphateBy similarity, [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per homodimer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi163 – 1631Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity
Metal bindingi166 – 1661Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity
Binding sitei220 – 2201SubstrateBy similarity
Binding sitei381 – 3811Pyridoxal phosphate; shared with dimeric partnerBy similarity

GO - Molecular functioni

GO - Biological processi

  • behavioral response to cocaine Source: UniProtKB
  • copulation Source: RGD
  • gamma-aminobutyric acid biosynthetic process Source: RGD
  • gamma-aminobutyric acid catabolic process Source: UniProtKB
  • locomotory behavior Source: RGD
  • negative regulation of blood pressure Source: RGD
  • neurotransmitter catabolic process Source: UniProtKB
  • positive regulation of heat generation Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • response to cocaine Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to hypoxia Source: RGD
  • response to iron ion Source: RGD
  • response to nicotine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Neurotransmitter degradation

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.19. 5301.
ReactomeiREACT_335886. Degradation of GABA.
SABIO-RKP50554.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following 2 chains:
Gene namesi
Name:Abat
Synonyms:Gabat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi620948. Abat.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionAdd
BLAST
Chaini28 – 5004734-aminobutyrate aminotransferase, brain isoformPRO_0000001252Add
BLAST
Chaini35 – 5004664-aminobutyrate aminotransferase, liver isoformPRO_0000001253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311N6-succinyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysine; alternateBy similarity
Modified residuei252 – 2521N6-succinyllysine; alternateBy similarity
Modified residuei279 – 2791N6-acetyllysineBy similarity
Modified residuei318 – 3181N6-acetyllysineBy similarity
Disulfide bondi321 – 321InterchainBy similarity
Modified residuei357 – 3571N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei413 – 4131N6-acetyllysine; alternateBy similarity
Modified residuei413 – 4131N6-succinyllysine; alternateBy similarity
Modified residuei452 – 4521N6-acetyllysineBy similarity
Modified residuei470 – 4701N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP50554.
PRIDEiP50554.

2D gel databases

World-2DPAGE0004:P50554.

PTM databases

PhosphoSiteiP50554.

Expressioni

Gene expression databases

GenevestigatoriP50554.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003633.

Structurei

3D structure databases

ProteinModelPortaliP50554.
SMRiP50554. Positions 39-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 1652Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00550000074885.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP50554.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG7ZPNJW.
PhylomeDBiP50554.
TreeFamiTF105021.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50554-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLLTTRRL VCSSQKNLHL FTPGSRYISQ AAAKVDFEFD YDGPLMKTEV
60 70 80 90 100
PGPRSQELMK QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI
110 120 130 140 150
SSVPIGYNHP ALAKLVQQPQ NASTFINRPA LGILPPENFV DKLRESLMSV
160 170 180 190 200
APKGMCQLIT MACGSCSNEN AFKTIFMWYR SKERGQRGFS KEELETCMVN
210 220 230 240 250
QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR
260 270 280 290 300
LKYPLEEFVT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG
310 320 330 340 350
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA
360 370 380 390 400
DVMSFSKKMM TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK
410 420 430 440 450
REDLLNNVAH AGKTLLTGLL DLQAQYPQFV SRVRGRGTFC SFDTPDEAIR
460 470 480 490 500
NKLILIARNK GVVLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSGILADFK
Length:500
Mass (Da):56,456
Last modified:January 9, 2007 - v3
Checksum:i1EA7180B72797B72
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31F → L in AAA70415 (PubMed:8133261).Curated
Sequence conflicti25 – 251S → T in AAA70415 (PubMed:8133261).Curated
Sequence conflicti36 – 361D → T in AAA70415 (PubMed:8133261).Curated
Sequence conflicti135 – 17036PPENF…CSNEN → LQRTLWTSSGSPCSRWLPKA CVSSSRWPAGPAPMRM in AAA70415 (PubMed:8133261).CuratedAdd
BLAST
Sequence conflicti277 – 2771I → N in AAA70415 (PubMed:8133261).Curated
Sequence conflicti425 – 4251Q → R in AAA70415 (PubMed:8133261).Curated
Sequence conflicti447 – 4471E → K (PubMed:10447691).Curated
Sequence conflicti447 – 4471E → K in BAA25570 (PubMed:10989446).Curated
Sequence conflicti486 – 4861H → Q in AAA70415 (PubMed:8133261).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29701 mRNA. Translation: AAA70415.1.
D87839 mRNA. Translation: BAA25570.1.
BC081787 mRNA. Translation: AAH81787.1.
PIRiI56502.
RefSeqiNP_112265.1. NM_031003.2.
XP_006245822.1. XM_006245760.2.
UniGeneiRn.10090.

Genome annotation databases

EnsembliENSRNOT00000003633; ENSRNOP00000003633; ENSRNOG00000002636.
GeneIDi81632.
KEGGirno:81632.
UCSCiRGD:620948. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29701 mRNA. Translation: AAA70415.1.
D87839 mRNA. Translation: BAA25570.1.
BC081787 mRNA. Translation: AAH81787.1.
PIRiI56502.
RefSeqiNP_112265.1. NM_031003.2.
XP_006245822.1. XM_006245760.2.
UniGeneiRn.10090.

3D structure databases

ProteinModelPortaliP50554.
SMRiP50554. Positions 39-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003633.

Chemistry

BindingDBiP50554.
ChEMBLiCHEMBL3148.

PTM databases

PhosphoSiteiP50554.

2D gel databases

World-2DPAGE0004:P50554.

Proteomic databases

PaxDbiP50554.
PRIDEiP50554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003633; ENSRNOP00000003633; ENSRNOG00000002636.
GeneIDi81632.
KEGGirno:81632.
UCSCiRGD:620948. rat.

Organism-specific databases

CTDi18.
RGDi620948. Abat.

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00550000074885.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP50554.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG7ZPNJW.
PhylomeDBiP50554.
TreeFamiTF105021.

Enzyme and pathway databases

BRENDAi2.6.1.19. 5301.
ReactomeiREACT_335886. Degradation of GABA.
SABIO-RKP50554.

Miscellaneous databases

NextBioi615107.
PROiP50554.

Gene expression databases

GenevestigatoriP50554.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGABT_RAT
AccessioniPrimary (citable) accession number: P50554
Secondary accession number(s): O70539, Q66HM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 9, 2007
Last modified: May 27, 2015
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.