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Protein

Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

Gene

GFA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).1 Publication

Catalytic activityi

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.1 Publication

Pathway:iUDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative glutamine--fructose-6-phosphate aminotransferase [isomerizing] (YMR084W), Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (GFA1)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activity1 Publication

GO - Molecular functioni

GO - Biological processi

  • fungal-type cell wall chitin biosynthetic process Source: SGD
  • glutamine metabolic process Source: UniProtKB-KW
  • UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YKL104C-MONOMER.
ReactomeiREACT_329028. Synthesis of UDP-N-acetyl-glucosamine.
UniPathwayiUPA00113; UER00528.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC:2.6.1.16)
Short name:
GFAT
Alternative name(s):
D-fructose-6-phosphate amidotransferase
Hexosephosphate aminotransferase
Gene namesi
Name:GFA1
Ordered Locus Names:YKL104C
ORF Names:YKL457
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL104C.
SGDiS000001587. GFA1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 717716Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531Phosphoserine2 Publications
Modified residuei334 – 3341Phosphothreonine1 Publication
Modified residuei336 – 3361Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14742.
PaxDbiP14742.
PeptideAtlasiP14742.

Expressioni

Inductioni

The activity of this enzyme increases in presence of mating pheromone (transcriptional regulation).

Interactioni

Protein-protein interaction databases

BioGridi34030. 96 interactions.
DIPiDIP-5224N.
IntActiP14742. 119 interactions.
MINTiMINT-566761.

Structurei

3D structure databases

ProteinModelPortaliP14742.
SMRiP14742. Positions 2-205, 278-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 318317Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini390 – 529140SIS 1PROSITE-ProRule annotationAdd
BLAST
Domaini562 – 707146SIS 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation
Contains 2 SIS domains.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiCOG0449.
GeneTreeiENSGT00390000010049.
HOGENOMiHOG000258898.
InParanoidiP14742.
KOiK00820.
OMAiLSVYCEI.
OrthoDBiEOG7034RG.

Family and domain databases

Gene3Di3.60.20.10. 2 hits.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 2 hits.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIFGYCNY LVERSRGEII DTLVDGLQRL EYRGYDSTGI AIDGDEADST
60 70 80 90 100
FIYKQIGKVS ALKEEITKQN PNRDVTFVSH CGIAHTRWAT HGRPEQVNCH
110 120 130 140 150
PQRSDPEDQF VVVHNGIITN FRELKTLLIN KGYKFESDTD TECIAKLYLH
160 170 180 190 200
LYNTNLQNGH DLDFHELTKL VLLELEGSYG LLCKSCHYPN EVIATRKGSP
210 220 230 240 250
LLIGVKSEKK LKVDFVDVEF PEENAGQPEI PLKSNNKSFG LGPKKAREFE
260 270 280 290 300
AGSQNANLLP IAANEFNLRH SQSRAFLSED GSPTPVEFFV SSDAASVVKH
310 320 330 340 350
TKKVLFLEDD DLAHIYDGEL HIHRSRREVG ASMTRSIQTL EMELAQIMKG
360 370 380 390 400
PYDHFMQKEI YEQPESTFNT MRGRIDYENN KVILGGLKAW LPVVRRARRL
410 420 430 440 450
IMIACGTSYH SCLATRAIFE ELSDIPVSVE LASDFLDRKC PVFRDDVCVF
460 470 480 490 500
VSQSGETADT MLALNYCLER GALTVGIVNS VGSSISRVTH CGVHINAGPE
510 520 530 540 550
IGVASTKAYT SQYIALVMFA LSLSDDRVSK IDRRIEIIQG LKLIPGQIKQ
560 570 580 590 600
VLKLEPRIKK LCATELKDQK SLLLLGRGYQ FAAALEGALK IKEISYMHSE
610 620 630 640 650
GVLAGELKHG VLALVDENLP IIAFGTRDSL FPKVVSSIEQ VTARKGHPII
660 670 680 690 700
ICNENDEVWA QKSKSIDLQT LEVPQTVDCL QGLINIIPLQ LMSYWLAVNK
710
GIDVDFPRNL AKSVTVE
Length:717
Mass (Da):80,047
Last modified:January 23, 2007 - v4
Checksum:i27E5F0D24BDC451A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti453 – 4542QS → HC in AAA34643 (PubMed:2656689).Curated
Sequence conflicti534 – 5341Missing in AAA34643 (PubMed:2656689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04719 Genomic DNA. Translation: AAA34643.1.
X71133 Genomic DNA. Translation: CAA50453.1.
Z28104 Genomic DNA. Translation: CAA81944.1.
BK006944 Genomic DNA. Translation: DAA09054.1.
PIRiS37931. XNBYGM.
RefSeqiNP_012818.1. NM_001179670.1.

Genome annotation databases

EnsemblFungiiYKL104C; YKL104C; YKL104C.
GeneIDi853757.
KEGGisce:YKL104C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04719 Genomic DNA. Translation: AAA34643.1.
X71133 Genomic DNA. Translation: CAA50453.1.
Z28104 Genomic DNA. Translation: CAA81944.1.
BK006944 Genomic DNA. Translation: DAA09054.1.
PIRiS37931. XNBYGM.
RefSeqiNP_012818.1. NM_001179670.1.

3D structure databases

ProteinModelPortaliP14742.
SMRiP14742. Positions 2-205, 278-717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34030. 96 interactions.
DIPiDIP-5224N.
IntActiP14742. 119 interactions.
MINTiMINT-566761.

Chemistry

BindingDBiP14742.

Proteomic databases

MaxQBiP14742.
PaxDbiP14742.
PeptideAtlasiP14742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL104C; YKL104C; YKL104C.
GeneIDi853757.
KEGGisce:YKL104C.

Organism-specific databases

EuPathDBiFungiDB:YKL104C.
SGDiS000001587. GFA1.

Phylogenomic databases

eggNOGiCOG0449.
GeneTreeiENSGT00390000010049.
HOGENOMiHOG000258898.
InParanoidiP14742.
KOiK00820.
OMAiLSVYCEI.
OrthoDBiEOG7034RG.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00528.
BioCyciYEAST:YKL104C-MONOMER.
ReactomeiREACT_329028. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

NextBioi974834.
PROiP14742.

Family and domain databases

Gene3Di3.60.20.10. 2 hits.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 2 hits.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the glutamine:fructose-6-phosphate amidotransferase gene from yeast. Pheromonal regulation of its transcription."
    Watzele G., Tanner W.
    J. Biol. Chem. 264:8753-8758(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  2. "The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of Saccharomyces cerevisiae suggests the presence of a second aspartate aminotransferase gene in yeast."
    Cheret G., Pallier C., Valens M., Daignan-Fornier B., Fukuhara H., Bolotin-Fukuhara M., Sor F.
    Yeast 9:1259-1265(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Yeast glutamine-fructose-6-phosphate aminotransferase (Gfa1) requires methionine aminopeptidase activity for proper function."
    Dummitt B., Micka W.S., Chang Y.H.
    J. Biol. Chem. 280:14356-14360(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND THR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGFA1_YEAST
AccessioniPrimary (citable) accession number: P14742
Secondary accession number(s): D6VXI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 14300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.