Q55FM6 (ENOPH_DICDI) 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

Gene names

Name:	enoph1
ORF Names:	DDB_G0268036

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	267 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.

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	acireductone synthase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – 267	267	Enolase-phosphatase E1		PRO_0000327574
Regions
	Region	155 – 156	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	215	1	Magnesium By similarity
	Binding site	189	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55FM6 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 17DF886B003933B9	FASTA	267	30,594
	10 20 30 40 50 60 MTPNIHTVIL DIEGTTTPIS FVHDVLFPYI RDNLVRHINQ KWGSEELKQD IKELYKLYLE 70 80 90 100 110 120 DNKASELVVN NQFNTPEILN PDDESTDKEK LIESVIRNVI YQMDNDRKST PLKQLQGHMW 130 140 150 160 170 180 LEGYENELVK GVVFPEVPKA FENWNLNHID IYIYSSGSIA AQKLLFNYSN FGSLLPYIKG 190 200 210 220 230 240 HFDTTIGGKL HPSSYEKILS TINNGSPNSY LFVTDSILEA KAARESGLNV CLSIRDGNPP 250 260 IVDRELLNTF DQVSSFDQLF NKFNFKN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000003 Genomic DNA. Translation: EAL73471.1.
RefSeq	XP_647507.1. XM_642415.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZS9 based on UniProtKB Q9UHY7.
ProteinModelPortal	Q55FM6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q55FM6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0230999; DDB0230999; DDB_G0268036.
GeneID	8616314.
GenomeReviews	Gene locus enoph1 in contig CM000150_GR.
KEGG	ddi:DDB_G0268036.
Organism-specific databases
dictyBase	DDB_G0268036.
Phylogenomic databases
eggNOG	KOG2630.
GeneTree	EPrGT00050000005300.
HOGENOM	HBG294242.
OMA	TTDLNFI.
PhylomeDB	Q55FM6.
ProtClustDB	CLSZ2431550.
Family and domain databases
InterPro	IPR010041. Enolase_ppase. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01691. Enolase-ppase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ENOPH_DICDI

Accession

Primary (citable) accession number: Q55FM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	September 21, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)