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Reviewed, UniProtKB/Swiss-Prot P49604 (GATA_USTMA)

Last modified November 3, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    4-aminobutyrate aminotransferase
    EC=2.6.1.19
Alternative name(s):
    Gamma-amino-N-butyrate transaminase
      Short name=GABA transaminase
    GABA aminotransferase
      Short name=GABA-AT
Gene names
Name: GATA
ORF Names: UM01080
OrganismUstilago maydis (Smut fungus) [Complete proteome]
Taxonomic identifier5270 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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
Gene Ontology (GO)
   Biological processgamma-aminobutyric acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4-aminobutyrate transaminase activity

Inferred from electronic annotation. Source: 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
P49604-1 [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: 8598057] [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: 17080091] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521.

Cross-references

Sequence databases

U28655 Genomic DNA. Translation: AAA98560.1.
AACP01000037 Genomic DNA. Translation: EAK82039.1.
PIRS68116.
RefSeqXP_757227.1.

3D structure databases

HSSPHSSP built from PDB template 1GTX based on UniProtKB P80147.
ModBaseSearch...

Protein-protein interaction databases

STRINGP49604.

Genome annotation databases

GeneID3629154.
KEGGuma:UM01080.1.

Phylogenomic databases

OMAKERGQRG.

Enzyme and pathway databases

BRENDA2.6.1.19. 2320.

Family and domain databases

InterProIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
[Graphical view]
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF6. GABAtrns_euk. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATA_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 3, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents