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P80147

- GABT_PIG

UniProt

P80147 - GABT_PIG

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Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

ABAT

Organism
Sus scrofa (Pig)
Status
Reviewed - 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 phosphate.

GO - Molecular functioni

  1. (S)-3-amino-2-methylpropionate transaminase activity Source: UniProtKB-EC
  2. 4-aminobutyrate transaminase activity Source: UniProtKB-EC
  3. protein homodimerization activity Source: UniProtKB
  4. pyridoxal phosphate binding Source: UniProtKB
  5. succinate-semialdehyde dehydrogenase binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Neurotransmitter degradation

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_219022. Degradation of GABA.
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
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. 4-aminobutyrate transaminase complex Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: Ensembl
  4. mitochondrial matrix Source: UniProtKB
  5. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828Mitochondrion1 PublicationAdd
BLAST
Chaini29 – 5004724-aminobutyrate aminotransferase, mitochondrialPRO_0000001251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi163 ↔ 166
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)lysine
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

PaxDbiP80147.
PRIDEiP80147.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

BioGridi1149627. 1 interaction.
STRINGi9823.ENSSSCP00000008445.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 6513
Helixi77 – 793
Beta strandi84 – 874
Beta strandi92 – 976
Helixi98 – 1014
Helixi110 – 1178
Helixi119 – 1213
Helixi122 – 1265
Turni131 – 1333
Helixi139 – 1457
Helixi147 – 1504
Beta strandi157 – 1637
Helixi164 – 18421
Helixi191 – 1988
Turni202 – 2043
Beta strandi209 – 2135
Helixi222 – 2276
Helixi232 – 2354
Helixi255 – 2573
Helixi259 – 28224
Beta strandi287 – 2926
Beta strandi294 – 2963
Turni298 – 3003
Helixi306 – 31813
Beta strandi322 – 3265
Turni328 – 3358
Beta strandi336 – 3394
Helixi340 – 3445
Beta strandi351 – 3555
Helixi357 – 3593
Beta strandi360 – 3667
Helixi368 – 3703
Beta strandi381 – 3844
Helixi386 – 40116
Helixi404 – 42522
Turni427 – 4293
Beta strandi431 – 4366
Beta strandi439 – 4435
Helixi447 – 45913
Beta strandi465 – 4673
Turni468 – 4703
Beta strandi471 – 4744
Helixi482 – 49716

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OHVX-ray2.30A/B/C/D29-500[»]
1OHWX-ray2.30A/B/C/D29-500[»]
1OHYX-ray2.80A/B/C/D29-500[»]
ProteinModelPortaliP80147.
SMRiP80147. Positions 39-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80147.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020208.
HOVERGENiHBG000634.
InParanoidiP80147.
KOiK13524.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti454 – 4541I → N in AAA96981. (PubMed:1559966)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M84802 mRNA. Translation: AAA96981.1 .
RefSeqi NP_999428.1. NM_214263.1.
UniGenei Ssc.16251.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OHV X-ray 2.30 A/B/C/D 29-500 [» ]
1OHW X-ray 2.30 A/B/C/D 29-500 [» ]
1OHY X-ray 2.80 A/B/C/D 29-500 [» ]
ProteinModelPortali P80147.
SMRi P80147. Positions 39-499.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1149627. 1 interaction.
STRINGi 9823.ENSSSCP00000008445.

Chemistry

BindingDBi P80147.
ChEMBLi CHEMBL2266.

Proteomic databases

PaxDbi P80147.
PRIDEi P80147.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397500.
KEGGi ssc:397500.

Organism-specific databases

CTDi 18.

Phylogenomic databases

eggNOGi COG0160.
HOGENOMi HOG000020208.
HOVERGENi HBG000634.
InParanoidi P80147.
KOi K13524.

Enzyme and pathway databases

Reactomei REACT_219022. Degradation of GABA.
SABIO-RK P80147.

Miscellaneous databases

EvolutionaryTracei P80147.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProi IPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR00699. GABAtrns_euk. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Brain 4-aminobutyrate aminotransferase. Isolation and sequence of a cDNA encoding the enzyme."
    Kwon O.S., Park J., Churchich J.E.
    J. Biol. Chem. 267:7215-7216(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Protein structure of pig liver 4-aminobutyrate aminotransferase and comparison with a cDNA-deduced sequence."
    de Biase D., Maras B., Bossa F., Barra D., John R.A.
    Eur. J. Biochem. 208:351-357(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-500.
    Tissue: Liver.
  3. "Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy."
    Storici P., Capitani G., De Biase D., Moser M., John R.A., Jansonius J.N., Schirmer T.
    Biochemistry 38:8628-8634(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    Tissue: Liver.

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: October 29, 2014
This is version 114 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

External Data

Dasty 3