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O13837 (GABAT_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
ORF Names:SPAC19D5.07
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processgamma-aminobutyric acid catabolic process

Inferred from direct assay. Source: GeneDB_Spombe

glutamate metabolic process

Inferred from direct assay. Source: GeneDB_Spombe

nitrogen utilization

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

mitochondrion

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Molecular function4-aminobutyrate transaminase activity

Inferred from direct assay. Source: GeneDB_Spombe

pyridoxal phosphate binding

Inferred from direct assay. Source: GeneDB_Spombe

Complete GO annotation...

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: 11859360] [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: 16823372] [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: 17355287] [Abstract]
Cited for: FUNCTION, SUBUNIT.

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalO13837.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC19D5.07.1; SPAC19D5.07.1:pep; SPAC19D5.07.
GeneID2542494.
KEGGspo:SPAC19D5.07.
NMPDRfig|4896.1.peg.4875.

Organism-specific databases

GeneDB_SpombeSPAC19D5.07.

Phylogenomic databases

eggNOGfuNOG06785.
GeneTreeEFGT00050000003450.
HOGENOMHBG483813.
OMAATGKFWA.
OrthoDBEOG4HX88H.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002971-MONOMER.

Gene expression databases

ArrayExpressO13837.

Family and domain databases

InterProIPR004631. 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]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK13524.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF6. GABAtrns_euk. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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: December 14, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents