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

4-aminobutyrate aminotransferase, mitochondrial

Gene

Abat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi163Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity1
Metal bindingi166Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity1
Binding sitei220SubstrateBy similarity1
Binding sitei381Pyridoxal phosphate; shared with dimeric partnerBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • behavioral response to cocaine Source: UniProtKB
  • cerebellum development Source: RGD
  • copulation Source: RGD
  • exploration behavior 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
  • negative regulation of dopamine secretion Source: RGD
  • negative regulation of gamma-aminobutyric acid secretion Source: RGD
  • negative regulation of platelet aggregation Source: RGD
  • neurotransmitter catabolic process Source: UniProtKB
  • positive regulation of aspartate secretion Source: RGD
  • positive regulation of dopamine metabolic process Source: RGD
  • positive regulation of heat generation Source: RGD
  • positive regulation of inhibitory postsynaptic potential Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • positive regulation of prolactin secretion Source: RGD
  • positive regulation of uterine smooth muscle contraction 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

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processNeurotransmitter degradation
LigandIron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.19 5301
ReactomeiR-RNO-916853 Degradation of GABA
SABIO-RKiP50554

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi620948 Abat

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3148

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27MitochondrionAdd BLAST27
ChainiPRO_000000125228 – 5004-aminobutyrate aminotransferase, brain isoformAdd BLAST473
ChainiPRO_000000125335 – 5004-aminobutyrate aminotransferase, liver isoformAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei231N6-succinyllysineBy similarity1
Modified residuei252N6-acetyllysine; alternateBy similarity1
Modified residuei252N6-succinyllysine; alternateBy similarity1
Modified residuei279N6-acetyllysineBy similarity1
Modified residuei318N6-acetyllysineBy similarity1
Disulfide bondi321InterchainBy similarity
Modified residuei357N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei413N6-acetyllysine; alternateBy similarity1
Modified residuei413N6-succinyllysine; alternateBy similarity1
Modified residuei452N6-acetyllysineBy similarity1
Modified residuei470N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP50554
PRIDEiP50554

2D gel databases

World-2DPAGEi0004:P50554

PTM databases

iPTMnetiP50554
PhosphoSitePlusiP50554
SwissPalmiP50554

Expressioni

Gene expression databases

BgeeiENSRNOG00000002636
GenevisibleiP50554 RN

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003633

Chemistry databases

BindingDBiP50554

Structurei

3D structure databases

ProteinModelPortaliP50554
SMRiP50554
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni164 – 165Pyridoxal phosphate bindingBy similarity2

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1405 Eukaryota
COG0160 LUCA
GeneTreeiENSGT00550000074885
HOGENOMiHOG000020208
HOVERGENiHBG000634
InParanoidiP50554
KOiK13524
OMAiIQTGGCG
OrthoDBiEOG091G08T5
PhylomeDBiP50554
TreeFamiTF105021

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
InterProiView protein in InterPro
IPR004631 4NH2But_aminotransferase_euk
IPR005814 Aminotrans_3
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00202 Aminotran_3, 1 hit
PIRSFiPIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR00699 GABAtrns_euk, 1 hit
PROSITEiView protein in PROSITE
PS00600 AA_TRANSFER_CLASS_3, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti3F → L in AAA70415 (PubMed:8133261).Curated1
Sequence conflicti25S → T in AAA70415 (PubMed:8133261).Curated1
Sequence conflicti36D → T in AAA70415 (PubMed:8133261).Curated1
Sequence conflicti135 – 170PPENF…CSNEN → LQRTLWTSSGSPCSRWLPKA CVSSSRWPAGPAPMRM in AAA70415 (PubMed:8133261).CuratedAdd BLAST36
Sequence conflicti277I → N in AAA70415 (PubMed:8133261).Curated1
Sequence conflicti425Q → R in AAA70415 (PubMed:8133261).Curated1
Sequence conflicti447E → K (PubMed:10447691).Curated1
Sequence conflicti447E → K in BAA25570 (PubMed:10989446).Curated1
Sequence conflicti486H → Q in AAA70415 (PubMed:8133261).Curated1

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_006245760.3
UniGeneiRn.10090

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiGABT_RAT
AccessioniPrimary (citable) accession number: P50554
Secondary accession number(s): O70539, Q66HM1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 9, 2007
Last modified: May 23, 2018
This is version 150 of the entry and version 3 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health