HOM6/YJR139C Protein Information

Standard Name	Hom6p
Systematic Name	Yjr139cp
Alias	Thr6p 1
ORF Classification	Verified
Description	Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase), dimeric enzyme that catalyzes the third step in the common pathway for methionine and threonine biosynthesis; enzyme has nucleotide-binding, dimerization and catalytic regions (2, 3, 4)
Name Description	HOMoserine requiring 2

Experimental Data
Molecules/cell	48900 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	359
Molecular Weight (Da)	38,502
Isoelectric Point (pI)	7.75

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 Hom6p (InterPro)
Transmembrane Domains	There are 1 total predicted transmembrane domains (TMHMM)
Signal Peptide(s)	There are 1 total predicted predicted signal peptide(s) (SignalP)
Physical Interactions	There are 12 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000129358 \| P31116 MIPS: YJR139C NCBI: 1015880 \| 3797 \| 38492935 \| 38492936 \| 398365575 \| 399368 \| 51247753 \| 51247754 \| 7245384 \| 7245385 \| 7245386 \| 7245387 \| 7245388 \| 7245389 \| NP_012673.3 GenBank/EMBL/DDBJ: DAA08924.1 \| X64457 \| Z49639
External Classifications	EC: 1.1.1.3 [Homoserine dehydrogenase]

Amino Acid Sequence (or in FASTA format)
1 MSTKVVNVAV IGAGVVGSAF LDQLLAMKST ITYNLVLLAE AERSLISKDF 51 SPLNVGSDWK AALAASTTKT LPLDDLIAHL KTSPKPVILV DNTSSAYIAG 101 FYTKFVENGI SIATPNKKAF SSDLATWKAL FSNKPTNGFV YHEATVGAGL 151 PIISFLREII QTGDEVEKIE GIFSGTLSYI FNEFSTSQAN DVKFSDVVKV 201 AKKLGYTEPD PRDDLNGLDV ARKVTIVGRI SGVEVESPTS FPVQSLIPKP 251 LESVKSADEF LEKLSDYDKD LTQLKKEAAT ENKVLRFIGK VDVATKSVSV 301 GIEKYDYSHP FASLKGSDNV ISIKTKRYTN PVVIQGAGAG AAVTAAGVLG 351 DVIKIAQRL*

Amino Acid Sequence (or in FASTA format)

       1  MSTKVVNVAV IGAGVVGSAF LDQLLAMKST ITYNLVLLAE AERSLISKDF
      51  SPLNVGSDWK AALAASTTKT LPLDDLIAHL KTSPKPVILV DNTSSAYIAG
     101  FYTKFVENGI SIATPNKKAF SSDLATWKAL FSNKPTNGFV YHEATVGAGL
     151  PIISFLREII QTGDEVEKIE GIFSGTLSYI FNEFSTSQAN DVKFSDVVKV
     201  AKKLGYTEPD PRDDLNGLDV ARKVTIVGRI SGVEVESPTS FPVQSLIPKP
     251  LESVKSADEF LEKLSDYDKD LTQLKKEAAT ENKVLRFIGK VDVATKSVSV
     301  GIEKYDYSHP FASLKGSDNV ISIKTKRYTN PVVIQGAGAG AAVTAAGVLG
     351  DVIKIAQRL*

external links for Hom6p

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

References cited on this page View Complete Literature Guide for Hom6p

1)	Robichon-Szulmajster H, et al. (1966) Genetic and biochemical studies of genes controlling the synthesis of threonine and methionine in Saccharomyces. Genetics 53(3):609-19
2)	Thomas D, et al. (1993) Evolutionary relationships between yeast and bacterial homoserine dehydrogenases. FEBS Lett 323(3):289-93
3)	Yumoto N, et al. (1991) Rapid purification and characterization of homoserine dehydrogenase from Saccharomyces cerevisiae. Arch Biochem Biophys 285(2):270-5
4)	DeLaBarre B, et al. (2000) Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases. Nat Struct Biol 7(3):238-44
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41