Reviewed, UniProtKB/Swiss-Prot P19140 (ENOA_ANAPL)

Names and origin

Protein names

Recommended name:
    Alpha-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Tau-crystallin

Gene names

Name:

ENO1

Organism

Anas platyrhynchos (Domestic duck) (Anas boschas)

Taxonomic identifier

8839 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anas

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Eye lens protein
Ligand	Magnesium Metal-binding
Molecular function	Lyase
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 structural constituent of eye lens 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 434	433	Alpha-enolase		PRO_0000134100
Regions
	Region	370 – 373	4	Substrate binding By similarity
Sites
	Active site	210	1	Proton donor By similarity
	Active site	343	1	Proton acceptor By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	293	1	Magnesium By similarity
	Metal binding	318	1	Magnesium By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	318	1	Substrate By similarity
	Binding site	394	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19140-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0802980B8542055D	FASTA	434	47,240
	10 20 30 40 50 60 MSILKIHARE IFDSRGNPTV EVDLYTNKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK 70 80 90 100 110 120 GVSKAVEHIN KTIAPALISK NVNVVEQDKI DKLMLDMDGS ENKSKFGANA ILGVSLAVCK 130 140 150 160 170 180 AGAAEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI PPCGADSFKE 190 200 210 220 230 240 AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA IGKAGYSDKV 250 260 270 280 290 300 VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ISPDQLADLY KGFVKNYPVV SIEDPFDQDD 310 320 330 340 350 360 WGAWKKFTGS VGIQVVGDDL TVTNPKRIAK AVEEKACNCL LLKVNQIGSV TESLQACKLA 370 380 390 400 410 420 QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 430 ARFAGRNFRN PRIN

References

[1]

"Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein." Wistow G.J., Lietman T., Williams L.A., Stapel S.O., de Jong W.W., Horwitz J., Piatigorsky J. J. Cell Biol. 107:2729-2736(1988) [PubMed: 2462567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Embryonic lens.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M20749 mRNA. Translation: AAA49218.1. X14195 mRNA. Translation: CAA32409.1.
PIR	A32132.
3D structure databases
HSSP	HSSP built from PDB template 1PDZ based on UniProtKB P56252.
SMR	P19140. Positions 2-433.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P19140.
Enzyme and pathway databases
BRENDA	4.2.1.11. 3217.
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

ENOA_ANAPL

Accession

Primary (citable) accession number: P19140

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)