Q5PPH0 (ENOPH_RAT) 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
MASA homolog

Gene names

Name:	Enoph1
Synonyms:	Masa

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-methionine salvage from methylthioadenosine Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity Inferred from electronic annotation. Source: InterPro 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity Inferred from electronic annotation. Source: InterPro acireductone synthase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglycolate phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 261	261	Enolase-phosphatase E1		PRO_0000254009
Regions
	Region	150 – 151	2	Substrate binding By similarity
Sites
	Metal binding	16	1	Magnesium By similarity
	Metal binding	18	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	209	1	Magnesium By similarity
	Binding site	184	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PPH0 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 0C51CA857A122BEE	FASTA	261	28,875
	10 20 30 40 50 60 MVVVSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIKENVK EYLQTHWEEE ECQQDVSLLR 70 80 90 100 110 120 KQAEEDAHLD GAVPIPVASG GDVQQMIQAV VDNVSWQMSH DRKTTALKQL QGHMWKAAFT 130 140 150 160 170 180 AGRMKAEVFA DVVPAVRRWR EAGMKVYIYS SGSVEAQKLL FGHSTEGDIL ELIDGHFDTK 190 200 210 220 230 240 IGHKVESDSY RKIADSIGCS TNNILFLTDV TVEASAAEEA DVHVAVVVRP GNAGLTDDEK 250 260 TYYNLISSFS ELYLPSTQSK V

References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC087697 mRNA. Translation: AAH87697.1.
IPI	IPI00363718.
RefSeq	NP_001009391.1. NM_001009391.1.
UniGene	Rn.98105.
3D structure databases
HSSP	HSSP built from PDB template 1YNS based on UniProtKB Q9UHY7.
ProteinModelPortal	Q5PPH0.
SMR	Q5PPH0. Positions 4-254.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PPH0.
Proteomic databases
PRIDE	Q5PPH0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000003083; ENSRNOP00000003083; ENSRNOG00000002262.
GeneID	305177.
KEGG	rno:305177.
NMPDR	fig|10116.3.peg.10040.
UCSC	NM_001009391. rat.
Organism-specific databases
CTD	58478.
RGD	1309016. Enoph1.
Phylogenomic databases
eggNOG	roNOG08406.
GeneTree	ENSGT00440000039914.
HOVERGEN	HBG054539.
InParanoid	Q5PPH0.
OMA	VESAILC.
OrthoDB	EOG405S1X.
PhylomeDB	Q5PPH0.
Gene expression databases
ArrayExpress	Q5PPH0.
Genevestigator	Q5PPH0.
GermOnline	ENSRNOG00000002262. Rattus norvegicus.
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. IPR023943. Enolase-phosphatase_E1. IPR010041. Enolase_ppase. IPR023214. HAD-like_dom. IPR006439. HAD-SF_hydro_IA_v1. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K09880.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01691. Enolase-ppase. 1 hit. TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNet	Search...
Other
NextBio	654183.

Entry information

Entry name

ENOPH_RAT

Accession

Primary (citable) accession number: Q5PPH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 4, 2005
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program