4-aminobutyrate aminotransferase, mitochondrial precursor

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P80404 (GABT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	ABAT
Synonyms:	GABAT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate. (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer; disulfide-linked. Ref.6
Subcellular location	Mitochondrion matrix.
Tissue specificity	Liver > pancreas > brain > kidney > heart > placenta.
Involvement in disease	Defects in ABAT are a cause of GABA transaminase deficiency (GABATD) [MIM:613163]. The phenotype of this deficiency includes psychomotor retardation, hypotonia, hyperreflexia, lethargy, refractory seizures, and EEG abnormalities. Ref.7
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	behavioral response to cocaine Inferred from sequence or structural similarity. Source: UniProtKB gamma-aminobutyric acid catabolic process Non-traceable author statement Ref.6. Source: UniProtKB neurotransmitter catabolic process Non-traceable author statement Ref.6. Source: UniProtKB neurotransmitter secretion Traceable author statement. Source: Reactome
Cellular component	4-aminobutyrate transaminase complex Inferred from direct assay Ref.6. Source: UniProtKB mitochondrial matrix Traceable author statement. Source: Reactome
Molecular function	(S)-3-amino-2-methylpropionate transaminase activity Inferred from electronic annotation. Source: EC 4-aminobutyrate transaminase activity Traceable author statement. Source: Reactome protein homodimerization activity Inferred from physical interaction Ref.6. Source: UniProtKB pyridoxal phosphate binding Inferred from direct assay. Source: UniProtKB succinate-semialdehyde dehydrogenase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	1	EBI-1753838,EBI-886

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

Mitochondrion

Chain

29 – 500

472

4-aminobutyrate aminotransferase, mitochondrial

PRO_0000001249

Amino acid modifications

Modified residue

318

N6-acetyllysine By similarity

Modified residue

357

N6-(pyridoxal phosphate)lysine

Disulfide bond

163 ↔ 166

By similarity

Disulfide bond

321

Interchain Ref.6

Natural variations

Natural variant

Q → R. Ref.4
Corresponds to variant rs1731017 [ dbSNP | Ensembl ].

VAR_018979

Natural variant

220

R → K in GABATD; 25% reduction in activity. Ref.7

VAR_008883

Experimental info

Mutagenesis

321

C → M, S, A, G or K: Loss of activity. Ref.6

Sequence conflict

S → T in AAA74449. Ref.1

Sequence conflict

109

H → D in AAA74449. Ref.1

Sequence conflict

113

L → V in AAA74449. Ref.1

Sequence conflict

132

G → E in AAA74449. Ref.1

Sequence conflict

155 – 171

MSQLI…SNENA → CPSSSPWPACPAPMKTT in AAB38510. Ref.2

Sequence conflict

191

Q → K in AAA74449. Ref.1

Sequence conflict

204

G → W in AAA74449. Ref.1

Sequence conflict

216

A → S in AAA74449. Ref.1

Sequence conflict

247

P → T in AAB38510. Ref.2

Sequence conflict

268

R → G in AAA74449. Ref.1

Sequence conflict

320

G → C in AAA74449. Ref.1

Sequence conflict

366

H → L in AAA74449. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P80404 [UniParc].

Last modified June 7, 2004. Version 3.
Checksum: F990B0B6B77BD3F5
Show »

FASTA

500

56,439

        10         20         30         40         50         60 
MASMLLAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGPLMKTEV PGPRSQELMK 

        70         80         90        100        110        120 
QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYSHP ALLKLIQQPQ 

       130        140        150        160        170        180 
NASMFVNRPA LGILPPENFV EKLRQSLLSV APKGMSQLIT MACGSCSNEN ALKTIFMWYR 

       190        200        210        220        230        240 
SKERGQRGFS QEELETCMIN QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS 

       250        260        270        280        290        300 
FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG 

       310        320        330        340        350        360 
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM 

       370        380        390        400        410        420 
TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNAAH AGKALLTGLL 

       430        440        450        460        470        480 
DLQARYPQFI SRVRGRGTFC SFDTPDDSIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF 

       490        500 
RDHHAHLFLN IFSDILADFK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase." Osei Y.D., Churchich J.E. Gene 155:185-187(1995) [PubMed: 7721088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	Medina-Kauwe L.K., Gibson K.M., Nyhan W.L., Tobin A.J. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pancreatic islet.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-56. Tissue: Brain and Eye.
[5]	"Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase." de Biase D., Barra D., Simmaco M., John R.A., Bossa F. Eur. J. Biochem. 227:476-480(1995) [PubMed: 7851425] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-485, PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[6]	"Cysteine-321 of human brain GABA transaminase is involved in intersubunit cross-linking." Yoon C.S., Kim D.W., Jang S.H., Lee B.R., Choi H.S., Choi S.H., Kim S.Y., An J.J., Kwon O.S., Kang T.C., Won M.H., Cho S.W., Lee K.S., Park J., Eum W.S., Choi S.Y. Mol. Cells 18:214-219(2004) [PubMed: 15528998] [Abstract] Cited for: SUBUNIT, INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF CYS-321.
[7]	"4-aminobutyrate aminotransferase (GABA-transaminase) deficiency." Medina-Kauwe L.K., Tobin A.J., De Meirleir L., Jaeken J., Jakobs C., Nyhan W.L., Gibson K.M. J. Inherit. Metab. Dis. 22:414-427(1999) [PubMed: 10407778] [Abstract] Cited for: VARIANT GABATD LYS-220.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00009532.
PIR	JC4022. S67470.
RefSeq	NP_000654.2. NM_000663.4. NP_001120920.1. NM_001127448.1. NP_065737.2. NM_020686.5.
UniGene	Hs.336768.
3D structure databases
ProteinModelPortal	P80404.
SMR	P80404. Positions 39-499.
ModBase	Search...
Protein-protein interaction databases
IntAct	P80404. 1 interaction.
MINT	MINT-3023444.
STRING	P80404.
PTM databases
PhosphoSite	P80404.
Polymorphism databases
DMDM	48429239.
Proteomic databases
PeptideAtlas	P80404.
PRIDE	P80404.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000268251; ENSP00000268251; ENSG00000183044. ENST00000396600; ENSP00000379845; ENSG00000183044. ENST00000425191; ENSP00000411916; ENSG00000183044.
GeneID	18.
KEGG	hsa:18.
UCSC	uc002czc.2. human.
Organism-specific databases
CTD	18.
GeneCards	GC16P008768.
H-InvDB	HIX0012805.
HGNC	HGNC:23. ABAT.
HPA	HPA041528. HPA041690.
MIM	137150. gene. 613163. phenotype.
neXtProt	NX_P80404.
Orphanet	2066. Gamma aminobutyric acid transaminase deficiency.
PharmGKB	PA24372.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10497.
GeneTree	ENSGT00550000074885.
HOVERGEN	HBG000634.
InParanoid	P80404.
OMA	ATGKFWA.
OrthoDB	EOG441QB6.
PhylomeDB	P80404.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11538.
Reactome	REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	P80404.
Bgee	P80404.
CleanEx	HS_ABAT.
Genevestigator	P80404.
Family and domain databases
InterPro	IPR004631. 4NH2But_aminotransferase_euk. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K13524.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF6. GABAtrns_euk. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00699. GABAtrns_euk. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00510. Divalproex sodium. DB00951. Isoniazid. DB00160. L-Alanine. DB00142. L-Glutamic Acid. DB00114. Pyridoxal Phosphate. DB00119. Pyruvic acid. DB00906. Tiagabine. DB00313. Valproic Acid. DB01080. Vigabatrin.
NextBio	45.
SOURCE	Search...

Entry information

Entry name

GABT_HUMAN

Accession

Primary (citable) accession number: P80404
Secondary accession number(s): A8K386

Q99800

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 7, 2004
Last modified:	January 25, 2012
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Relevant documents

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Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents