Reviewed, UniProtKB/Swiss-Prot Q55F83 (ENOB_DICDI)

Names and origin

Protein names

Recommended name:
    Enolase B
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase B
    2-phospho-D-glycerate hydro-lyase B

Gene names

Name:	enoB
ORF Names:	DDB_G0268214

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 443	443	Enolase B		PRO_0000330351
Regions
	Region	375 – 378	4	Substrate binding By similarity
Sites
	Active site	208	1	Proton donor By similarity
	Active site	348	1	Proton acceptor By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	296	1	Magnesium By similarity
	Metal binding	323	1	Magnesium By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	323	1	Substrate By similarity
	Binding site	399	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55F83-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 5ADDB5C1D18AC051	FASTA	443	48,820
	10 20 30 40 50 60 MSIESIKARE ILDSRGNPTL EVEVWTSEGM FSAKVPSGAS TGIHEAFELR DGDKSRYFGY 70 80 90 100 110 120 GVLNAIVNVN NLISPTLKGM RVDNQKAIDD KMIELDGTKN KSKLGSNAIV GVSMAVARAA 130 140 150 160 170 180 ASIKGVPLYR YISQLAGNSN IRLPVPCFNV INGGKHAGNR LPFQEFMLVP IGAPKFKEAL 190 200 210 220 230 240 RYGSEVYHSL KEIIKERYGL DATNVGDEGG FAPNLTSPEE ALTLLVDAIN HSGYQDVIKI 250 260 270 280 290 300 GIDSAASEFW NPKTSKYDMD FKNIGSSHLK SSLNSGEQLM SRYLEILKKY PIAFFEDPFG 310 320 330 340 350 360 EDDWENHGKI TAAIGNKIQI IGDDLLCTNP ERIKKAISEK TVNSLLLKIN QIGTLTETIE 370 380 390 400 410 420 AAKLAKEAGW GCLVSHRSGE TDDHFIADLV VGLGTGEIKS GAPCRFERLS KYNRLMKIEE 430 440 ELEKLHRSNG NSFEYAGEEF YHF

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
EMBLGenBankDDBJ	AAFI02000003 Genomic DNA. Translation: EAL73560.1.
RefSeq	XP_647650.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q55F83.
Genome annotation databases
GeneID	3398602.
GenomeReviews	Gene locus enoB in contig CM000150_GR.
KEGG	ddi:DDB_0231356.
Organism-specific databases
dictyBase	DDB_G0268214. enoB.
Phylogenomic databases
OMA	VYHTLKA.
Family and domain databases
InterPro	IPR000941. Enolase. [Graphical view]
PANTHER	PTHR11902. Enolase. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENOB_DICDI

Accession

Primary (citable) accession number: Q55F83

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)