P14742 (GFA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
Short name=GFAT
EC=2.6.1.16

Alternative name(s):
D-fructose-6-phosphate amidotransferase
Hexosephosphate aminotransferase

Gene names

Name:	GFA1
Ordered Locus Names:	YKL104C
ORF Names:	YKL457

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	717 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Catalytic activity	L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
Induction	The activity of this enzyme increases in presence of mating pheromone (transcriptional regulation).
Miscellaneous	Present with 14300 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 glutamine amidotransferase type-2 domain. Contains 2 SIS domains.

Ontologies

Keywords
Domain	Glutamine amidotransferase Repeat
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway fungal-type cell wall chitin biosynthetic process Inferred from genetic interaction PubMed 11895440. Source: SGD glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro glutamine-fructose-6-phosphate transaminase (isomerizing) activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRR1	P28708	1	EBI-7557,EBI-9782

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 717	716	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		PRO_0000135289
Regions
	Domain	2 – 318	317	Glutamine amidotransferase type-2
	Domain	390 – 529	140	SIS 1
	Domain	562 – 707	146	SIS 2
Sites
	Active site	2	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	199	1	Phosphoserine Ref.7 Ref.8
	Modified residue	238	1	Phosphoserine Ref.8
	Modified residue	253	1	Phosphoserine Ref.8
	Modified residue	332	1	Phosphoserine Ref.6 Ref.8
	Modified residue	334	1	Phosphothreonine Ref.8
Experimental info
	Sequence conflict	453 – 454	2	QS → HC in AAA34643. Ref.1
	Sequence conflict	534	1	Missing in AAA34643. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14742 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 27E5F0D24BDC451A	FASTA	717	80,047
	10 20 30 40 50 60 MCGIFGYCNY LVERSRGEII DTLVDGLQRL EYRGYDSTGI AIDGDEADST FIYKQIGKVS 70 80 90 100 110 120 ALKEEITKQN PNRDVTFVSH CGIAHTRWAT HGRPEQVNCH PQRSDPEDQF VVVHNGIITN 130 140 150 160 170 180 FRELKTLLIN KGYKFESDTD TECIAKLYLH LYNTNLQNGH DLDFHELTKL VLLELEGSYG 190 200 210 220 230 240 LLCKSCHYPN EVIATRKGSP LLIGVKSEKK LKVDFVDVEF PEENAGQPEI PLKSNNKSFG 250 260 270 280 290 300 LGPKKAREFE AGSQNANLLP IAANEFNLRH SQSRAFLSED GSPTPVEFFV SSDAASVVKH 310 320 330 340 350 360 TKKVLFLEDD DLAHIYDGEL HIHRSRREVG ASMTRSIQTL EMELAQIMKG PYDHFMQKEI 370 380 390 400 410 420 YEQPESTFNT MRGRIDYENN KVILGGLKAW LPVVRRARRL IMIACGTSYH SCLATRAIFE 430 440 450 460 470 480 ELSDIPVSVE LASDFLDRKC PVFRDDVCVF VSQSGETADT MLALNYCLER GALTVGIVNS 490 500 510 520 530 540 VGSSISRVTH CGVHINAGPE IGVASTKAYT SQYIALVMFA LSLSDDRVSK IDRRIEIIQG 550 560 570 580 590 600 LKLIPGQIKQ VLKLEPRIKK LCATELKDQK SLLLLGRGYQ FAAALEGALK IKEISYMHSE 610 620 630 640 650 660 GVLAGELKHG VLALVDENLP IIAFGTRDSL FPKVVSSIEQ VTARKGHPII ICNENDEVWA 670 680 690 700 710 QKSKSIDLQT LEVPQTVDCL QGLINIIPLQ LMSYWLAVNK GIDVDFPRNL AKSVTVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, MASS SPECTROMETRY. Strain: YAL6B.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, MASS SPECTROMETRY.
[8]	"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-199; SER-238; SER-253; SER-332 AND THR-334, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04719 Genomic DNA. Translation: AAA34643.1. X71133 Genomic DNA. Translation: CAA50453.1. Z28104 Genomic DNA. Translation: CAA81944.1. BK006944 Genomic DNA. Translation: DAA09054.1.
PIR	XNBYGM. S37931.
RefSeq	NP_012818.1. NM_001179670.1.
3D structure databases
ProteinModelPortal	P14742.
SMR	P14742. Positions 2-205, 278-717.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5224N.
IntAct	P14742. 124 interactions.
MINT	MINT-566761.
STRING	4932.YKL104C.
Protein family/group databases
MEROPS	C44.971.
Proteomic databases
PaxDb	P14742.
PeptideAtlas	P14742.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL104C; YKL104C; YKL104C.
GeneID	853757.
KEGG	sce:YKL104C.
Organism-specific databases
SGD	S000001587. GFA1.
Phylogenomic databases
eggNOG	COG0449.
GeneTree	ENSGT00390000010049.
HOGENOM	HOG000258898.
KO	K00820.
OMA	HLVHWEL.
OrthoDB	EOG4JDMFX.
Enzyme and pathway databases
BioCyc	YEAST:YKL104C-MONOMER.
UniPathway	UPA00113; UER00528.
Gene expression databases
Genevestigator	P14742.
GermOnline	YKL104C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR005855. GlmS_trans. IPR001347. SIS. [Graphical view]
PANTHER	PTHR10937:SF0. PTHR10937:SF0. 1 hit.
Pfam	PF00310. GATase_2. 2 hits. PF01380. SIS. 2 hits. [Graphical view]
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS51464. SIS. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P14742.
NextBio	974834.

Entry information

Entry name

GFA1_YEAST

Accession

Primary (citable) accession number: P14742
Secondary accession number(s): D6VXI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 128 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program