HIS7/YBR248C Protein Information

Standard Name	His7p 1, 2
Systematic Name	Ybr248cp
ORF Classification	Verified
Description	Imidazole glycerol phosphate synthase (glutamine amidotransferase:cyclase), catalyzes the fifth step of histidine biosynthesis and also produces 5-aminoimidazole-4-carboxamide ribotide (AICAR), a purine precursor (1, 3, 4)
Name Description	HIStidine requiring 1

Experimental Data
Molecules/cell	11800 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	552
Molecular Weight (Da)	61,068
Isoelectric Point (pI)	5.24

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Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with His7p (InterPro)
Physical Interactions	There are 5 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012C815 \| P33734 MIPS: YBR248C NCBI: 16975311 \| 16975312 \| 33357789 \| 33357790 \| 33357791 \| 33357792 \| 33357793 \| 33357794 \| 395155 \| 398365721 \| 536663 \| 585255 \| NP_009807.3 \| NM_001178596.3 GenBank/EMBL/DDBJ: DAA07364.1 \| X69815 \| Z36117
External Classifications	EC: 2.4.2.- [Pentosyltransferases] EC: 4.1.3.- [Oxo-Acid-Lyases]

Amino Acid Sequence (or in FASTA format)
1 MPVVHVIDVE SGNLQSLTNA IEHLGYEVQL VKSPKDFNIS GTSRLILPGV 51 GNYGHFVDNL FNRGFEKPIR EYIESGKPIM GICVGLQALF AGSVESPKST 101 GLNYIDFKLS RFDDSEKPVP EIGWNSCIPS ENLFFGLDPY KRYYFVHSFA 151 AILNSEKKKN LENDGWKIAK AKYGSEEFIA AVNKNNIFAT QFHPEKSGKA 201 GLNVIENFLK QQSPPIPNYS AEEKELLMND YSNYGLTRRI IACLDVRTND 251 QGDLVVTKGD QYDVREKSDG KGVRNLGKPV QLAQKYYQQG ADEVTFLNIT 301 SFRDCPLKDT PMLEVLKQAA KTVFVPLTVG GGIKDIVDVD GTKIPALEVA 351 SLYFRSGADK VSIGTDAVYA AEKYYELGNR GDGTSPIETI SKAYGAQAVV 401 ISVDPKRVYV NSQADTKNKV FETEYPGPNG EKYCWYQCTI KGGRESRDLG 451 VWELTRACEA LGAGEILLNC IDKDGSNSGY DLELIEHVKD AVKIPVIASS 501 GAGVPEHFEE AFLKTRADAC LGAGMFHRGE FTVNDVKEYL LEHGLKVRMD 551 EE*

Amino Acid Sequence (or in FASTA format)

       1  MPVVHVIDVE SGNLQSLTNA IEHLGYEVQL VKSPKDFNIS GTSRLILPGV
      51  GNYGHFVDNL FNRGFEKPIR EYIESGKPIM GICVGLQALF AGSVESPKST
     101  GLNYIDFKLS RFDDSEKPVP EIGWNSCIPS ENLFFGLDPY KRYYFVHSFA
     151  AILNSEKKKN LENDGWKIAK AKYGSEEFIA AVNKNNIFAT QFHPEKSGKA
     201  GLNVIENFLK QQSPPIPNYS AEEKELLMND YSNYGLTRRI IACLDVRTND
     251  QGDLVVTKGD QYDVREKSDG KGVRNLGKPV QLAQKYYQQG ADEVTFLNIT
     301  SFRDCPLKDT PMLEVLKQAA KTVFVPLTVG GGIKDIVDVD GTKIPALEVA
     351  SLYFRSGADK VSIGTDAVYA AEKYYELGNR GDGTSPIETI SKAYGAQAVV
     401  ISVDPKRVYV NSQADTKNKV FETEYPGPNG EKYCWYQCTI KGGRESRDLG
     451  VWELTRACEA LGAGEILLNC IDKDGSNSGY DLELIEHVKD AVKIPVIASS
     501  GAGVPEHFEE AFLKTRADAC LGAGMFHRGE FTVNDVKEYL LEHGLKVRMD
     551  EE*

external links for His7p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
YGOB	CYC2008 (complexes)	Pfam domains
YOGY	Complexome	YeastRC Structure Prediction (Seattle)
	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for His7p

1)	Kuenzler M, et al. (1993) Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae. J Bacteriol 175(17):5548-58
2)	Plotkin, D.J. (1978) Commitment to meiotic recombination: a temporal analysis. Ph.D Thesis
3)	Chittur SV, et al. (2000) Expression and purification of imidazole glycerol phosphate synthase from Saccharomyces cerevisiae. Protein Expr Purif 18(3):366-77
4)	Alifano P, et al. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60(1):44-69
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41