Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49604 (GABAT_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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
Name:GATA
ORF Names:UM01080
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Deaminates gamma-aminobutyric acid (GABA) to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase By similarity. Not required for the utilization of GABA as nitrogen source. Ref.1

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Induction

Up-regulated by GABA and beta-alanine. Is not subject to nitrogen catabolite repression. Ref.1

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 electronic annotation. Source: EnsemblFungi

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-aminobutyrate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5095094-aminobutyrate aminotransferase
PRO_0000120381

Amino acid modifications

Modified residue3631N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict3371G → GT in AAA98560. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49604 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 9ECAFAE83FE4DD4C

FASTA50955,993
        10         20         30         40         50         60 
MISSKATSAA RACARTSRVM QQQQRRLLAT VVSSSSLFPG EPSSPHVVTS QIPGPKSKEL 

        70         80         90        100        110        120 
SDRIGTFQEN RTHGFVVDYA KSQGNWIADA DGNVLLDMFA QIASIAIGYN NPDLLALAKT 

       130        140        150        160        170        180 
DEFITATMNR AALGSFPPTN WQELVETSFG TVKPDGLNNI FTAMCGSCAN ENAFKASFMA 

       190        200        210        220        230        240 
YRARERGEKA EFTPEEMSSC MKNQSPGSPD LSILSFTSAF HGRLFGSLSA TRSKAIHKLD 

       250        260        270        280        290        300 
IPSFNWPVVE WPDVKYPFAQ NSRENAEAEK VALAAVEEAI VSSKKTGSSY GPVAALIVEP 

       310        320        330        340        350        360 
IQSEGGDNHA SPAFFQGLRD VTKKHGVFMI VDEVQTGVGA TGAFWAHSKW NLTSPPDFVT 

       370        380        390        400        410        420 
FSKKMQAAGF YHNIETRPSL PYRNYNTWMG DPARTLQARQ IIRTIQDHNL IQKTDKVGNY 

       430        440        450        460        470        480 
IYEKLFDLIE NGAGRGKIEK LRGENAGTFL AFDGRTAKVR DQLIMEMRKL GVHMGGCGDK 

       490        500 
ALRLRPMLVF EQKHADIFLD KLETALGQL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the ugatA gene of Ustilago maydis, isolated by homology to the gatA gene of Aspergillus nidulans."
Straffon M.J., Hynes M.J., Davis M.A.
Curr. Genet. 29:360-369(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
Strain: 518.
[2]"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. expand/collapse author list , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28655 Genomic DNA. Translation: AAA98560.1.
AACP01000037 Genomic DNA. Translation: EAK82039.1.
PIRS68116.
RefSeqXP_757227.1. XM_752134.1.

3D structure databases

ProteinModelPortalP49604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5270.UM01080.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM01080T0; UM01080P0; UM01080.
GeneID3629154.
KEGGuma:UM01080.1.

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020208.
KOK13524.
OMALNMLTDY.
OrthoDBEOG744TK4.

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...

Entry information

Entry nameGABAT_USTMA
AccessionPrimary (citable) accession number: P49604
Secondary accession number(s): Q4PFN3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 12, 2006
Last modified: November 13, 2013
This is version 81 of the entry and version 2 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