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O13837 (GABAT_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-aminobutyrate aminotransferase

EC=2.6.1.19
Alternative name(s):
GABA aminotransferase
Short name=GABA-AT
Gamma-amino-N-butyrate transaminase
Short name=GABA transaminase
Gene names
Name:uga1
ORF Names:SPAC19D5.07
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source. Deaminates GABA to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase. Cannot transaminate beta-alanine (BAL). Ref.3

Catalytic activity

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer. Ref.3

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4744744-aminobutyrate aminotransferase
PRO_0000120380

Amino acid modifications

Modified residue3331N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O13837 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2B92B232BADEF4E4

FASTA47452,945
        10         20         30         40         50         60 
MSSTATVTES THFFPNEPQG PSIKTETIPG PKGKAAAEEM SKYHDISAVK FPVDYEKSIG 

        70         80         90        100        110        120 
NYLVDLDGNV LLDVYSQIAT IPIGYNNPTL LKAAKSDEVA TILMNRPALG NYPPKEWARV 

       130        140        150        160        170        180 
AYEGAIKYAP KGQKYVYFQM SGSDANEIAY KLAMLHHFNN KPRPTGDYTA EENESCLNNA 

       190        200        210        220        230        240 
APGSPEVAVL SFRHSFHGRL FGSLSTTRSK PVHKLGMPAF PWPQADFPAL KYPLEEHVEE 

       250        260        270        280        290        300 
NAKEEQRCID QVEQILTNHH CPVVACIIEP IQSEGGDNHA SPDFFHKLQA TLKKHDVKFI 

       310        320        330        340        350        360 
VDEVQTGVGS TGTLWAHEQW NLPYPPDMVT FSKKFQAAGI FYHDLALRPH AYQHFNTWMG 

       370        380        390        400        410        420 
DPFRAVQSRY ILQEIQDKDL LNNVKSVGDF LYAGLEELAR KHPGKINNLR GKGKGTFIAW 

       430        440        450        460        470 
DCESPAARDK FCADMRINGV NIGGCGVAAI RLRPMLVFQK HHAQILLKKI DELI 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"A gene duplication led to specialized gamma-aminobutyrate and beta-alanine aminotransferase in yeast."
Andersen G., Andersen B., Dobritzsch D., Schnackerz K.D., Piskur J.
FEBS J. 274:1804-1817(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB16717.1.
PIRT37967.
RefSeqNP_594905.1. NM_001020336.2.

3D structure databases

ProteinModelPortalO13837.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278953. 3 interactions.
MINTMINT-4668393.
STRING4896.SPAC19D5.07-1.

Proteomic databases

MaxQBO13837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC19D5.07.1; SPAC19D5.07.1:pep; SPAC19D5.07.
GeneID2542494.
KEGGspo:SPAC19D5.07.

Organism-specific databases

PomBaseSPAC19D5.07.

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020208.
KOK13524.
OMAKLIQQPQ.
OrthoDBEOG744TK4.
PhylomeDBO13837.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803548.
PROO13837.

Entry information

Entry nameGABAT_SCHPO
AccessionPrimary (citable) accession number: O13837
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names