A6ZQR2 (ENOPH_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase-phosphatase E1
EC=3.1.3.77

Alternative name(s):
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Unknown transcript 4 protein

Gene names

Name:	UTR4
ORF Names:	SCY_1459

Organism

Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]

Taxonomic identifier

307796 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) By similarity.
Catalytic activity	5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. MasA/mtnC family.
Sequence caution	The sequence EDN62932.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acireductone synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 227	227	Enolase-phosphatase E1		PRO_0000377658
Regions
	Region	118 – 119	2	Substrate binding By similarity
Sites
	Metal binding	11	1	Magnesium By similarity
	Metal binding	13	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	186	1	Magnesium By similarity
	Binding site	161	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6ZQR2 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 3DACD0C5B908E7D3	FASTA	227	25,179
	10 20 30 40 50 60 MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TNKVPQLVQQ DTRDSPVSNI LSQFHIDDKE 70 80 90 100 110 120 QLQAHILELV AKDVKDPILK QLQGYVWAQG YESGQIKAPV YADAIDFIKR KKRVFIYSSG 130 140 150 160 170 180 SVKAQKLLFG YVQDPNAPAH DSLDLNSYID GYFDINTSGK KTETQSYANI LRDIGAKASE 190 200 210 220 VLFLSDNPLE LDAAAGVGIA TGLASRPGNA PVPDGQKYQV YKNFETL

References

[1]

"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789." Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M. Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed: 17652520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YJM789.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFW02000048 Genomic DNA. Translation: EDN62932.1. Different initiation.
3D structure databases
ProteinModelPortal	A6ZQR2.
ModBase	Search...
Proteomic databases
PRIDE	A6ZQR2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. IPR010041. Enolase_ppase. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01691. Enolase-ppase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ENOPH_YEAS7

Accession

Primary (citable) accession number: A6ZQR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	November 16, 2011
This is version 25 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program