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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)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
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.
ReactomeiR-RNO-916853. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi620948. Abat.

Subcellular locationi

GO - Cellular componenti

  • 4-aminobutyrate transaminase complex Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • mitochondrial matrix Source: RGD
  • mitochondrion Source: UniProtKB
  • neuron projection Source: RGD
Complete GO annotation...

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-2DPAGE0004:P50554.

PTM databases

iPTMnetiP50554.
PhosphoSitePlusiP50554.

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.
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.
OMAiLIQQPQN.
OrthoDBiEOG091G08T5.
PhylomeDBiP50554.
TreeFamiTF105021.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
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. 2 hits.
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)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.

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_006245760.3.
UniGeneiRn.10090.

3D structure databases

ProteinModelPortaliP50554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003633.

Chemistry databases

BindingDBiP50554.
ChEMBLiCHEMBL3148.

PTM databases

iPTMnetiP50554.
PhosphoSitePlusiP50554.

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

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

Enzyme and pathway databases

BRENDAi2.6.1.19. 5301.
ReactomeiR-RNO-916853. Degradation of GABA.
SABIO-RKP50554.

Miscellaneous databases

PROiP50554.

Gene expression databases

BgeeiENSRNOG00000002636.
GenevisibleiP50554. RN.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
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. 2 hits.
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...

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: November 2, 2016
This is version 140 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

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 one 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.