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Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

ABAT

Organism
Sus scrofa (Pig)
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'-phosphate2 Publications, [2Fe-2S] cluster1 PublicationNote: Binds 1 [2Fe-2S] cluster per homodimer.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi163Iron-sulfur (2Fe-2S); shared with dimeric partner1 Publication1
Metal bindingi166Iron-sulfur (2Fe-2S); shared with dimeric partner1 Publication1
Binding sitei220Substrate1 Publication1 Publication1
Binding sitei381Pyridoxal phosphate; shared with dimeric partner2 Publications1

GO - Molecular functioni

GO - Biological processi

  • behavioral response to cocaine Source: UniProtKB
  • gamma-aminobutyric acid catabolic process Source: UniProtKB
  • neurotransmitter catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Neurotransmitter degradation

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.19. 6170.
SABIO-RKP80147.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • 4-aminobutyrate transaminase complex Source: UniProtKB
  • cytosol Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28Mitochondrion1 PublicationAdd BLAST28
ChainiPRO_000000125129 – 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 bondi321InterchainBy similarity
Modified residuei357N6-(pyridoxal phosphate)lysine1 Publication1
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

PaxDbiP80147.
PeptideAtlasiP80147.
PRIDEiP80147.

Expressioni

Gene expression databases

BgeeiENSSSCG00000007909.
GenevisibleiP80147. SS.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi1149627. 1 interactor.
STRINGi9823.ENSSSCP00000008445.

Chemistry databases

BindingDBiP80147.

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi53 – 65Combined sources13
Helixi77 – 79Combined sources3
Beta strandi84 – 87Combined sources4
Beta strandi92 – 97Combined sources6
Helixi98 – 101Combined sources4
Helixi110 – 117Combined sources8
Helixi119 – 121Combined sources3
Helixi122 – 126Combined sources5
Turni131 – 133Combined sources3
Helixi139 – 145Combined sources7
Helixi147 – 150Combined sources4
Beta strandi157 – 163Combined sources7
Helixi164 – 184Combined sources21
Helixi191 – 197Combined sources7
Turni198 – 200Combined sources3
Turni202 – 204Combined sources3
Beta strandi209 – 213Combined sources5
Helixi222 – 227Combined sources6
Helixi232 – 235Combined sources4
Helixi255 – 257Combined sources3
Helixi259 – 282Combined sources24
Beta strandi287 – 292Combined sources6
Beta strandi294 – 296Combined sources3
Turni298 – 300Combined sources3
Helixi306 – 318Combined sources13
Beta strandi322 – 326Combined sources5
Turni328 – 335Combined sources8
Beta strandi336 – 339Combined sources4
Helixi340 – 344Combined sources5
Beta strandi351 – 355Combined sources5
Helixi357 – 359Combined sources3
Beta strandi360 – 366Combined sources7
Helixi368 – 370Combined sources3
Beta strandi373 – 378Combined sources6
Beta strandi381 – 384Combined sources4
Helixi386 – 401Combined sources16
Helixi404 – 425Combined sources22
Turni427 – 429Combined sources3
Beta strandi431 – 436Combined sources6
Beta strandi439 – 443Combined sources5
Helixi447 – 459Combined sources13
Beta strandi465 – 467Combined sources3
Turni468 – 470Combined sources3
Beta strandi471 – 473Combined sources3
Helixi482 – 498Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OHVX-ray2.30A/B/C/D29-500[»]
1OHWX-ray2.30A/B/C/D29-500[»]
1OHYX-ray2.80A/B/C/D29-500[»]
4Y0DX-ray2.19A/B/C/D39-500[»]
4Y0HX-ray1.63A/B/C/D39-500[»]
4Y0IX-ray1.66A/B/C/D39-499[»]
4ZSWX-ray1.70A/B/C/D39-499[»]
4ZSYX-ray1.70A/B/C/D39-499[»]
ProteinModelPortaliP80147.
SMRiP80147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80147.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni164 – 165Pyridoxal phosphate binding1 Publication2

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1405. Eukaryota.
COG0160. LUCA.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP80147.
KOiK13524.
OrthoDBiEOG091G08T5.

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.

P80147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVLLTRRL ACSFRHNHRL LVPGWRHISQ AAAKVDVEFD YDGPLMKTEV
60 70 80 90 100
PGPRSRELMK QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI
110 120 130 140 150
SSIPIGYSHP ALVKLVQQPQ NVSTFINRPA LGILPPENFV EKLRESLLSV
160 170 180 190 200
APKGMSQLIT MACGSCSNEN AFKTIFMWYR SKERGQSAFS KEELETCMIN
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 KLRDISRKHG CAFLVDEVQT GGGSTGKFWA HEHWGLDDPA
360 370 380 390 400
DVMTFSKKMM TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK
410 420 430 440 450
REDLLSNAAH AGKVLLTGLL DLQARYPQFI SRVRGRGTFC SFDTPDESIR
460 470 480 490 500
NKLISIARNK GVMLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSDILADFK
Length:500
Mass (Da):56,620
Last modified:December 1, 1992 - v2
Checksum:iBFD0B80846CEF5B7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti454I → N in AAA96981 (PubMed:1559966).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84802 mRNA. Translation: AAA96981.1.
RefSeqiNP_999428.1. NM_214263.1.
UniGeneiSsc.16251.

Genome annotation databases

GeneIDi397500.
KEGGissc:397500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84802 mRNA. Translation: AAA96981.1.
RefSeqiNP_999428.1. NM_214263.1.
UniGeneiSsc.16251.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OHVX-ray2.30A/B/C/D29-500[»]
1OHWX-ray2.30A/B/C/D29-500[»]
1OHYX-ray2.80A/B/C/D29-500[»]
4Y0DX-ray2.19A/B/C/D39-500[»]
4Y0HX-ray1.63A/B/C/D39-500[»]
4Y0IX-ray1.66A/B/C/D39-499[»]
4ZSWX-ray1.70A/B/C/D39-499[»]
4ZSYX-ray1.70A/B/C/D39-499[»]
ProteinModelPortaliP80147.
SMRiP80147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149627. 1 interactor.
STRINGi9823.ENSSSCP00000008445.

Chemistry databases

BindingDBiP80147.
ChEMBLiCHEMBL2266.

Proteomic databases

PaxDbiP80147.
PeptideAtlasiP80147.
PRIDEiP80147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397500.
KEGGissc:397500.

Organism-specific databases

CTDi18.

Phylogenomic databases

eggNOGiKOG1405. Eukaryota.
COG0160. LUCA.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP80147.
KOiK13524.
OrthoDBiEOG091G08T5.

Enzyme and pathway databases

BRENDAi2.6.1.19. 6170.
SABIO-RKP80147.

Miscellaneous databases

EvolutionaryTraceiP80147.
PROiP80147.

Gene expression databases

BgeeiENSSSCG00000007909.
GenevisibleiP80147. SS.

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_PIG
AccessioniPrimary (citable) accession number: P80147
Secondary accession number(s): P27820
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.