GUA1/YMR217W Protein Information

Standard Name	Gua1p
Systematic Name	Ymr217wp
ORF Classification	Verified
Description	GMP synthase; highly conserved enzyme that catalyzes the second step in the biosynthesis of GMP from inosine 5'-phosphate (IMP); transcription is not subject to regulation by guanine but is negatively regulated by nutrient starvation; reduction-of-function mutation gua1-G388D causes changes in cellular guanine nucleotide pools, defects in general protein synthesis, and impaired translation of GCN4 mRNA (1, 2, 3, 4, 5)
Name Description	GUanine Auxotroph 3

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	525
Molecular Weight (Da)	58,482
Isoelectric Point (pI)	6.47

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Gua1p (InterPro)
Physical Interactions	There are 12 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00001683E1 \| P38625 MIPS: YMR217W NCBI: 1708073 \| 460064 \| 6323873 \| 854469 \| NP_013944.1 GenBank/EMBL/DDBJ: DAA10116.1 \| X70397 \| Z49809
External Classifications	EC: 6.3.5.2 [GMP synthase (glutamine-hydrolyzing)]

Amino Acid Sequence (or in FASTA format)
1 MAAGEQVSNM FDTILVLDFG SQYSHLITRR LREFNIYAEM LPCTQKISEL 51 GWTPKGVILS GGPYSVYAED APHVDHAIFD LNVPILGICY GMQELAWING 101 KQVGRGDKRE YGPATLKVID DSNSLFKGMN DSTVWMSHGD KLHGLPTGYK 151 TIATSDNSPY CGIVHETKPI YGIQFHPEVT HSTQGKTLLK NFAVDLCHAK 201 QNWTMENFID TEINRIRKLV GPTAEVIGAV SGGVDSTVAS KLMTEAIGDR 251 FHAILVDNGV LRLNEAANVK KTLVEGLGIN LMVVDASEEF LSKLKGVTDP 301 EKKRKIIGNT FIHVFEREAE KIKPKDGKEI QFLLQGTLYP DVIESISFKG 351 PSQTIKTHHN VGGLLENMKL KLIEPLRELF KDEVRHLGEL LGIPHDLVWR 401 HPFPGPGIAI RVLGEVTKEQ VEIARKADNI YIEEIKKAGL YNQISQAFAC 451 LLPVKSVGVM GDQRTYDQVI ALRAIETTDF MTADWFPFEH SFLKKVASRI 501 VNEVDGVARV TYDITSKPPA TVEWE*

Amino Acid Sequence (or in FASTA format)

       1  MAAGEQVSNM FDTILVLDFG SQYSHLITRR LREFNIYAEM LPCTQKISEL
      51  GWTPKGVILS GGPYSVYAED APHVDHAIFD LNVPILGICY GMQELAWING
     101  KQVGRGDKRE YGPATLKVID DSNSLFKGMN DSTVWMSHGD KLHGLPTGYK
     151  TIATSDNSPY CGIVHETKPI YGIQFHPEVT HSTQGKTLLK NFAVDLCHAK
     201  QNWTMENFID TEINRIRKLV GPTAEVIGAV SGGVDSTVAS KLMTEAIGDR
     251  FHAILVDNGV LRLNEAANVK KTLVEGLGIN LMVVDASEEF LSKLKGVTDP
     301  EKKRKIIGNT FIHVFEREAE KIKPKDGKEI QFLLQGTLYP DVIESISFKG
     351  PSQTIKTHHN VGGLLENMKL KLIEPLRELF KDEVRHLGEL LGIPHDLVWR
     401  HPFPGPGIAI RVLGEVTKEQ VEIARKADNI YIEEIKKAGL YNQISQAFAC
     451  LLPVKSVGVM GDQRTYDQVI ALRAIETTDF MTADWFPFEH SFLKKVASRI
     501  VNEVDGVARV TYDITSKPPA TVEWE*

external links for Gua1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Gua1p

1)	Dujardin G, et al. (1994) Cloning and sequencing of the GMP synthetase-encoding gene of Saccharomyces cerevisiae. Gene 139(1):127-32
2)	Escobar-Henriques M and Daignan-Fornier B (2001) Transcriptional regulation of the yeast gmp synthesis pathway by its end products. J Biol Chem 276(2):1523-30
3)	Gardner WJ and Woods RA (1979) Isolation and characterisation of guanine auxotrophs in Saccharomyces cerevisiae. Can J Microbiol 25(3):380-9
4)	Escobar-Henriques M, et al. (2003) Transcription initiation of the yeast IMD2 gene is abolished in response to nutrient limitation through a sequence in its coding region. Mol Cell Biol 23(17):6279-90
5)	Iglesias-Gato D, et al. (2011) Guanine Nucleotide Pool Imbalance Impairs Multiple Steps of Protein Synthesis and Disrupts GCN4 Translational Control in Saccharomyces cerevisiae. Genetics 187(1):105-22