Reviewed, UniProtKB/Swiss-Prot P40370 (ENO11_SCHPO)

Names and origin

Protein names

Recommended name:
    Enolase 1-1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1-1
    2-phospho-D-glycerate hydro-lyase 1-1

Gene names

Name:	eno101
Synonyms:	eno1
ORF Names:	SPBC1815.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: GeneDB_SPombe 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 – 439	439	Enolase 1-1		PRO_0000134058
Regions
	Region	372 – 375	4	Substrate binding By similarity
Sites
	Active site	211	1	Proton donor By similarity
	Active site	345	1	Proton acceptor By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	295	1	Magnesium By similarity
	Metal binding	320	1	Magnesium By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	295	1	Substrate By similarity
	Binding site	320	1	Substrate By similarity
	Binding site	396	1	Substrate By similarity
Amino acid modifications
	Modified residue	85	1	Phosphothreonine Ref.4
	Modified residue	249	1	Phosphoserine Ref.4
	Modified residue	250	1	Phosphoserine Ref.4
	Modified residue	253	1	Phosphotyrosine Ref.4
	Modified residue	351	1	Phosphoserine Ref.4
	Modified residue	353	1	Phosphothreonine Ref.4
	Modified residue	355	1	Phosphoserine Ref.4
	Modified residue	421	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	13 – 15	3	DSR → ALG in AAA70080. Ref.1
	Sequence conflict	191	1	H → Q in AAA70080. Ref.1
	Sequence conflict	248	1	A → T in AAA70080. Ref.1
	Sequence conflict	358	1	A → V in AAA70080. Ref.1
	Sequence conflict	377	1	E → G in AAA70080. Ref.1
	Sequence conflict	422	1	E → R in AAA70080. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40370-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 4CA257CFF4B456E3	FASTA	439	47,436
	10 20 30 40 50 60 MAIQKVFARQ IYDSRGNPTV EVDLTTETGI HRAIVPSGAS TGIWEALEMR DGDKTKWGGK 70 80 90 100 110 120 GVLKAVGNVN NIIAPAVVKA NLDVTDQKAA DEFLLKLDGT ENKSKLGANA ILGVSMAICR 130 140 150 160 170 180 AGAAQKKLPL WKYIAENFGT KGPYVLPVPS FNVLNGGSHA GGDLAFQEFM ILPTGAPSFS 190 200 210 220 230 240 EAMRWGAETY HTLKSIAKKR YGSSAGNVGD EGGIAPDLQT PQEALDLIVE AINKAGYEGK 250 260 270 280 290 300 IKIGLDVASS EFYVDGKYDL DIKAAKPKPE NKLTYQQLTD LYVELSKKYP IVSIEDPFDQ 310 320 330 340 350 360 DDWSAWTHMK AETDFQIVGD DLTVTNVKRL RTAIDKKCAN ALLLKVNQIG SVTESLNAVR 370 380 390 400 410 420 MSYEAGWGVM VSHRSGETAD TFISHLTVGI GAGQLKSGAP CRSERLAKYN ELLRIEEELG 430 SEGVYAGAHA GKYIKAAKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A cDNA from Schizosaccharomyces pombe encoding a putative enolase." Jackson J.C., Lopes J.M. Gene 154:109-113(1995) [PubMed: 7867936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of enolase gene of S. pombe." Park S.-K. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-249; SER-250; TYR-253; SER-351; THR-353; SER-355 AND SER-421, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U13799 mRNA. Translation: AAA70080.1. L37084 mRNA. Translation: AAA51399.2. CU329671 Genomic DNA. Translation: CAB43486.1.
PIR	JC4036. T39737. T45116.
RefSeq	NP_595903.1.
3D structure databases
SMR	P40370. Positions 2-427.
ModBase	Search...
Protein-protein interaction databases
STRING	P40370.
Genome annotation databases
GeneID	2539782.
GenomeReviews	Gene locus eno101 in contig CU329671_GR.
KEGG	spo:SPBC1815.01.
NMPDR	fig|4896.1.peg.1769.
Organism-specific databases
GeneDB_Spombe	SPBC1815.01.
Phylogenomic databases
eggNOG	fuNOG04478.
HOGENOM	HBG726599.
OMA	EYPVVSI.
OrthoDB	EOG91G4M7.
PhylomeDB	P40370.
Enzyme and pathway databases
BRENDA	4.2.1.11. 653.
Gene expression databases
ArrayExpress	P40370.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO11_SCHPO

Accession

Primary (citable) accession number: P40370
Secondary accession number(s): Q12703, Q9Y7J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 11, 2001
Last modified:	February 9, 2010
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)