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Protein

4-aminobutyrate aminotransferase

Gene

gatA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Deaminates gamma-aminobutyric acid (GABA) to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase (By similarity). Required for the degradation of GABA, which is important for utilization of GABA as nitrogen source.By similarity

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei222 – 2221SubstrateBy similarity
Binding sitei381 – 3811Pyridoxal phosphate; shared with dimeric partnerBy similarity

GO - Molecular functioni

  1. 4-aminobutyrate transaminase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular amide catabolic process Source: ASPGD
  2. gamma-aminobutyric acid catabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

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:gatA
ORF Names:AN2248
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VII

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4984984-aminobutyrate aminotransferasePRO_0000120379Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei356 – 3561N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP14010.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi162425.CADANIAP00008938.

Structurei

3D structure databases

ProteinModelPortaliP14010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 1652Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020208.
InParanoidiP14010.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG744TK4.

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.

P14010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAFRSSLK LRASARLPAV RTITTTPRLR AAEKPYFPNE PTAPKLATAI
60 70 80 90 100
PGPKNKAASE QLNEVFDVRS LNMLADYTKS VGNYIADLDG NMLLDVYAQI
110 120 130 140 150
ASIPVGYNNP HLLKVAASPE MATSLINRPA LGNFPSADWA HILKTGILKV
160 170 180 190 200
APKGLDQVFT AMAGSDANET AYKAAFMYYR QQQRGGPEKE FTEEEIQSSM
210 220 230 240 250
LNQTPGSPQL SIMSFKAGFH GRLFGSLSTT RSKPIHKLDI PAFDWPQAPF
260 270 280 290 300
PSLKYPLEEH AKENAEEEQR CLQEAERLIK EWHNPVAAII VEPIQSEGGD
310 320 330 340 350
NHASPAFFRG LREITKRNNV LFIVDEVQTG VGATGKFWAH DHWNLETPPD
360 370 380 390 400
MVTFSKKAQT AGYYFGNPAL RPNKPYRQFN TWMGDPSRAL IFRGIIEEIE
410 420 430 440 450
RLFLVENTAA TGDYLYSGLE RLAKQYPEHL QNLRGKGQGT FIAWDTPKRD
460 470 480 490
EFLVKGKGVG INIGGSGQNA VRLRPMLIFQ KHHADILLES IEKIIKQL
Length:498
Mass (Da):55,489
Last modified:January 1, 1990 - v1
Checksum:i97013EF39D66D5E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15647 Genomic DNA. Translation: CAA33674.1.
AACD01000036 Genomic DNA. Translation: EAA63933.1.
BN001307 Genomic DNA. Translation: CBF86462.1.
PIRiJQ0197.
RefSeqiXP_659852.1. XM_654760.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008938; CADANIAP00008938; CADANIAG00008938.
GeneIDi2875488.
KEGGiani:AN2248.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15647 Genomic DNA. Translation: CAA33674.1.
AACD01000036 Genomic DNA. Translation: EAA63933.1.
BN001307 Genomic DNA. Translation: CBF86462.1.
PIRiJQ0197.
RefSeqiXP_659852.1. XM_654760.1.

3D structure databases

ProteinModelPortaliP14010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00008938.

Proteomic databases

PRIDEiP14010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00008938; CADANIAP00008938; CADANIAG00008938.
GeneIDi2875488.
KEGGiani:AN2248.2.

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020208.
InParanoidiP14010.
KOiK13524.
OMAiKLIQQPQ.
OrthoDBiEOG744TK4.

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. "Cloning and molecular characterisation of the amdR controlled gatA gene of Aspergillus nidulans."
    Richardson I.B., Hurley S.K., Hynes M.J.
    Mol. Gen. Genet. 217:118-125(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MH 3010.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiGABAT_EMENI
AccessioniPrimary (citable) accession number: P14010
Secondary accession number(s): C8VMU4, Q5BB32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: March 4, 2015
This is version 102 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. 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.