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Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

ABAT

Organism
Homo sapiens (Human)
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

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

BioCyciMetaCyc:HS02477-MONOMER.
ZFISH:HS02477-MONOMER.
ReactomeiR-HSA-916853. Degradation of GABA.
SABIO-RKP80404.

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
Gene namesi
Name:ABAT
Synonyms:GABAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:23. ABAT.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

GABA transaminase deficiency (GABATD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn enzymatic deficiency resulting in psychomotor retardation, hypotonia, hyperreflexia, lethargy, refractory seizures, and EEG abnormalities.
See also OMIM:613163
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008883220R → K in GABATD; 25% reduction in activity. 1 PublicationCorresponds to variant rs121434578dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi321C → M, S, A, G or K: Loss of activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi18.
MalaCardsiABAT.
MIMi613163. phenotype.
OpenTargetsiENSG00000183044.
Orphaneti2066. Gamma-aminobutyric acid transaminase deficiency.
PharmGKBiPA24372.

Chemistry databases

ChEMBLiCHEMBL2044.
DrugBankiDB00160. L-Alanine.
DB00780. Phenelzine.
DB00119. Pyruvic acid.
DB00313. Valproic Acid.
DB01080. Vigabatrin.
GuidetoPHARMACOLOGYi2464.

Polymorphism and mutation databases

BioMutaiABAT.
DMDMi48429239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28MitochondrionAdd BLAST28
ChainiPRO_000000124929 – 5004-aminobutyrate aminotransferase, mitochondrialAdd BLAST472

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 bondi321Interchain
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

EPDiP80404.
PaxDbiP80404.
PeptideAtlasiP80404.
PRIDEiP80404.

PTM databases

iPTMnetiP80404.
PhosphoSitePlusiP80404.
SwissPalmiP80404.

Expressioni

Tissue specificityi

Liver > pancreas > brain > kidney > heart > placenta.

Gene expression databases

BgeeiENSG00000183044.
CleanExiHS_ABAT.
ExpressionAtlasiP80404. baseline and differential.
GenevisibleiP80404. HS.

Organism-specific databases

HPAiHPA041528.
HPA041690.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • succinate-semialdehyde dehydrogenase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106536. 32 interactors.
IntActiP80404. 2 interactors.
STRINGi9606.ENSP00000268251.

Chemistry databases

BindingDBiP80404.

Structurei

3D structure databases

ProteinModelPortaliP80404.
SMRiP80404.
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.
HOVERGENiHBG000634.
InParanoidiP80404.
KOiK13524.
PhylomeDBiP80404.
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.

P80404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASMLLAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGPLMKTEV
60 70 80 90 100
PGPRSQELMK QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI
110 120 130 140 150
SSVPIGYSHP ALLKLIQQPQ NASMFVNRPA LGILPPENFV EKLRQSLLSV
160 170 180 190 200
APKGMSQLIT MACGSCSNEN ALKTIFMWYR SKERGQRGFS QEELETCMIN
210 220 230 240 250
QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR
260 270 280 290 300
LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG
310 320 330 340 350
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA
360 370 380 390 400
DVMTFSKKMM TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK
410 420 430 440 450
REDLLNNAAH AGKALLTGLL DLQARYPQFI SRVRGRGTFC SFDTPDDSIR
460 470 480 490 500
NKLILIARNK GVVLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSDILADFK
Length:500
Mass (Da):56,439
Last modified:June 7, 2004 - v3
Checksum:iF990B0B6B77BD3F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17S → T in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti109H → D in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti113L → V in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti132G → E in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti155 – 171MSQLI…SNENA → CPSSSPWPACPAPMKTT in AAB38510 (Ref. 2) CuratedAdd BLAST17
Sequence conflicti191Q → K in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti204G → W in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti216A → S in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti247P → T in AAB38510 (Ref. 2) Curated1
Sequence conflicti268R → G in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti320G → C in AAA74449 (PubMed:7721088).Curated1
Sequence conflicti366H → L in AAA74449 (PubMed:7721088).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01897956Q → R.1 PublicationCorresponds to variant rs1731017dbSNPEnsembl.1
Natural variantiVAR_008883220R → K in GABATD; 25% reduction in activity. 1 PublicationCorresponds to variant rs121434578dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32961 mRNA. Translation: AAA74449.1.
U80226 mRNA. Translation: AAB38510.1.
AK290501 mRNA. Translation: BAF83190.1.
BC015628 mRNA. Translation: AAH15628.1.
BC031413 mRNA. Translation: AAH31413.1.
S75578 mRNA. Translation: AAD14176.1.
CCDSiCCDS10534.1.
PIRiJC4022.
S67470.
RefSeqiNP_000654.2. NM_000663.4.
NP_001120920.1. NM_001127448.1.
NP_065737.2. NM_020686.5.
XP_011520702.1. XM_011522400.2.
XP_011520703.1. XM_011522401.2.
UniGeneiHs.336768.

Genome annotation databases

EnsembliENST00000268251; ENSP00000268251; ENSG00000183044.
ENST00000396600; ENSP00000379845; ENSG00000183044.
ENST00000425191; ENSP00000411916; ENSG00000183044.
GeneIDi18.
KEGGihsa:18.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L32961 mRNA. Translation: AAA74449.1.
U80226 mRNA. Translation: AAB38510.1.
AK290501 mRNA. Translation: BAF83190.1.
BC015628 mRNA. Translation: AAH15628.1.
BC031413 mRNA. Translation: AAH31413.1.
S75578 mRNA. Translation: AAD14176.1.
CCDSiCCDS10534.1.
PIRiJC4022.
S67470.
RefSeqiNP_000654.2. NM_000663.4.
NP_001120920.1. NM_001127448.1.
NP_065737.2. NM_020686.5.
XP_011520702.1. XM_011522400.2.
XP_011520703.1. XM_011522401.2.
UniGeneiHs.336768.

3D structure databases

ProteinModelPortaliP80404.
SMRiP80404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106536. 32 interactors.
IntActiP80404. 2 interactors.
STRINGi9606.ENSP00000268251.

Chemistry databases

BindingDBiP80404.
ChEMBLiCHEMBL2044.
DrugBankiDB00160. L-Alanine.
DB00780. Phenelzine.
DB00119. Pyruvic acid.
DB00313. Valproic Acid.
DB01080. Vigabatrin.
GuidetoPHARMACOLOGYi2464.

PTM databases

iPTMnetiP80404.
PhosphoSitePlusiP80404.
SwissPalmiP80404.

Polymorphism and mutation databases

BioMutaiABAT.
DMDMi48429239.

Proteomic databases

EPDiP80404.
PaxDbiP80404.
PeptideAtlasiP80404.
PRIDEiP80404.

Protocols and materials databases

DNASUi18.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268251; ENSP00000268251; ENSG00000183044.
ENST00000396600; ENSP00000379845; ENSG00000183044.
ENST00000425191; ENSP00000411916; ENSG00000183044.
GeneIDi18.
KEGGihsa:18.

Organism-specific databases

CTDi18.
DisGeNETi18.
GeneCardsiABAT.
HGNCiHGNC:23. ABAT.
HPAiHPA041528.
HPA041690.
MalaCardsiABAT.
MIMi137150. gene.
613163. phenotype.
neXtProtiNX_P80404.
OpenTargetsiENSG00000183044.
Orphaneti2066. Gamma-aminobutyric acid transaminase deficiency.
PharmGKBiPA24372.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1405. Eukaryota.
COG0160. LUCA.
GeneTreeiENSGT00550000074885.
HOVERGENiHBG000634.
InParanoidiP80404.
KOiK13524.
PhylomeDBiP80404.
TreeFamiTF105021.

Enzyme and pathway databases

BioCyciMetaCyc:HS02477-MONOMER.
ZFISH:HS02477-MONOMER.
ReactomeiR-HSA-916853. Degradation of GABA.
SABIO-RKP80404.

Miscellaneous databases

ChiTaRSiABAT. human.
GenomeRNAii18.
PROiP80404.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000183044.
CleanExiHS_ABAT.
ExpressionAtlasiP80404. baseline and differential.
GenevisibleiP80404. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P80404
Secondary accession number(s): A8K386
, Q16260, Q8N5W2, Q96BG2, Q99800
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 7, 2004
Last modified: November 2, 2016
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.