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Protein

4-aminobutyrate aminotransferase

Gene

uga1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei199 – 1991SubstrateBy similarity
Binding sitei357 – 3571Pyridoxal phosphate; shared with dimeric partnerBy similarity

GO - Molecular functioni

  1. 4-aminobutyrate transaminase activity Source: PomBase
  2. pyridoxal phosphate binding Source: PomBase

GO - Biological processi

  1. gamma-aminobutyric acid catabolic process Source: PomBase
  2. glutamate metabolic process Source: PomBase
  3. nitrogen utilization Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_188603. Degradation of GABA.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:uga1
ORF Names:SPAC19D5.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC19D5.07.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4744744-aminobutyrate aminotransferasePRO_0000120380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei333 – 3331N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiO13837.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi278953. 3 interactions.
MINTiMINT-4668393.
STRINGi4896.SPAC19D5.07-1.

Structurei

3D structure databases

ProteinModelPortaliO13837.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1432Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020208.
InParanoidiO13837.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG744TK4.
PhylomeDBiO13837.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13837-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTATVTES THFFPNEPQG PSIKTETIPG PKGKAAAEEM SKYHDISAVK
60 70 80 90 100
FPVDYEKSIG NYLVDLDGNV LLDVYSQIAT IPIGYNNPTL LKAAKSDEVA
110 120 130 140 150
TILMNRPALG NYPPKEWARV AYEGAIKYAP KGQKYVYFQM SGSDANEIAY
160 170 180 190 200
KLAMLHHFNN KPRPTGDYTA EENESCLNNA APGSPEVAVL SFRHSFHGRL
210 220 230 240 250
FGSLSTTRSK PVHKLGMPAF PWPQADFPAL KYPLEEHVEE NAKEEQRCID
260 270 280 290 300
QVEQILTNHH CPVVACIIEP IQSEGGDNHA SPDFFHKLQA TLKKHDVKFI
310 320 330 340 350
VDEVQTGVGS TGTLWAHEQW NLPYPPDMVT FSKKFQAAGI FYHDLALRPH
360 370 380 390 400
AYQHFNTWMG DPFRAVQSRY ILQEIQDKDL LNNVKSVGDF LYAGLEELAR
410 420 430 440 450
KHPGKINNLR GKGKGTFIAW DCESPAARDK FCADMRINGV NIGGCGVAAI
460 470
RLRPMLVFQK HHAQILLKKI DELI
Length:474
Mass (Da):52,945
Last modified:January 1, 1998 - v1
Checksum:i2B92B232BADEF4E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16717.1.
PIRiT37967.
RefSeqiNP_594905.1. NM_001020336.2.

Genome annotation databases

EnsemblFungiiSPAC19D5.07.1; SPAC19D5.07.1:pep; SPAC19D5.07.
GeneIDi2542494.
KEGGispo:SPAC19D5.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16717.1.
PIRiT37967.
RefSeqiNP_594905.1. NM_001020336.2.

3D structure databases

ProteinModelPortaliO13837.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278953. 3 interactions.
MINTiMINT-4668393.
STRINGi4896.SPAC19D5.07-1.

Proteomic databases

MaxQBiO13837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC19D5.07.1; SPAC19D5.07.1:pep; SPAC19D5.07.
GeneIDi2542494.
KEGGispo:SPAC19D5.07.

Organism-specific databases

PomBaseiSPAC19D5.07.

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020208.
InParanoidiO13837.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG744TK4.
PhylomeDBiO13837.

Enzyme and pathway databases

ReactomeiREACT_188603. Degradation of GABA.

Miscellaneous databases

NextBioi20803548.
PROiO13837.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGABAT_SCHPO
AccessioniPrimary (citable) accession number: O13837
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: March 4, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.