[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=White leghorn; TISSUE=Muscle; PubMed=7629021 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka M., Maeda K., Nakashima K.; "Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis."; J. Biochem. 117:554-559(1995).
[2]	PROTEIN SEQUENCE OF 2-434. PubMed=3539098 [NCBI, ExPASy, EBI, Israel, Japan] Russell G.A., Dunbar B., Fothergill-Gilmore L.A.; "The complete amino acid sequence of chicken skeletal-muscle enolase."; Biochem. J. 236:115-126(1986).
[3]	ACETYLATION AT SER-2. DOI=10.1016/0003-2697(88)90277-1; PubMed=2898218 [NCBI, ExPASy, EBI, Israel, Japan] Gibson B.W., Daley D.J., Williams D.H.; "Structural elucidation of N-terminal post-translational modifications by mass spectrometry: application to chicken enolase and the alpha- and beta-subunits of bovine mitochondrial F1-ATPase."; Anal. Biochem. 169:217-226(1988).

Comments

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: Homodimer. Interacts with PNKD (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the enolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D37901; BAA07133.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23850; A23850.
JC4187; JC4187.

RefSeq

NP_990450.1; -.

UniGene

Gga.4297

3D structure databases

HSSP

Q9NDH8; 1OEP. [HSSP ENTRY / PDB]

SMR

P07322; 2-431.

ModBase

P07322.

Family and domain databases

InterPro

IPR000941; Enolase.
Graphical view of domain structure.

PANTHER

PTHR11902; Enolase; 1.

Pfam

PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001400; Enolase; 1.

PRINTS

PR00148; ENOLASE.

ProDom

PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Genome annotation databases

GeneID

396016; -.

KEGG

gga:396016; -.

Phylogenomic databases

HOVERGEN

P07322; -.

Other

ProtoNet

P07322.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 434`	`433`	`Beta-enolase.`	`PRO_0000134111`
`REGION`	`370 373`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`210 210`		`Proton donor (By similarity).`
`ACT_SITE`	`343 343`		`Proton acceptor (By similarity).`
`METAL`	`245 245`		`Magnesium (By similarity).`
`METAL`	`293 293`		`Magnesium (By similarity).`
`METAL`	`318 318`		`Magnesium (By similarity).`
`BINDING`	`158 158`		`Substrate (By similarity).`
`BINDING`	`167 167`		`Substrate (By similarity).`
`BINDING`	`293 293`		`Substrate (By similarity).`
`BINDING`	`318 318`		`Substrate (By similarity).`
`BINDING`	`394 394`		`Substrate (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine.`
`CONFLICT`	`17 17`		`E -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`49 49`		`P -> L (in Ref. 2; AA sequence).`
`CONFLICT`	`94 94`		`M -> V (in Ref. 2; AA sequence).`
`CONFLICT`	`119 120`		`CK -> SH (in Ref. 2; AA sequence).`
`CONFLICT`	`209 209`		`G -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`258 258`		`H -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`266 267`		`HT -> DP (in Ref. 2; AA sequence).`
`CONFLICT`	`270 270`		`Y -> L (in Ref. 2; AA sequence).`
`CONFLICT`	`309 309`		`F -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`323 323`		`T -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`331 331`		`G -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`343 343`		`K -> G (in Ref. 2; AA sequence).`
`CONFLICT`	`394 395`		`KT -> EQ (in Ref. 2; AA sequence).`

Sequence information

Length: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 47196 Da [This is the MW of the unprocessed precursor]

CRC64: 892D1BE4B6342F44 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIQKIHARE ILDSRGEPTV EVDLHTAKGH FRAAVPSGAS TGIHEALEPR DGDKKRFLGK 

        70         80         90        100        110        120 
GVLKAVEHIN KTIGPALIEK KISVVEQEKI DKVMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN TELILPVPAF NVINGGSHAG NKLAMQEFMV LPVGAASFHD 

       190        200        210        220        230        240 
AMRVGAEVYH SLKGVIKAKY GKDATNVGGE GGFAPNILDN HEALELLKAA IAQAGYTDKV 

       250        260        270        280        290        300 
VIGMDVAASE FCRDGRYHLD FKSPPHTKRY ITGEQLGEIY RGFIKDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WEAWKRFVFH VDIQVVGDDL TVTNPKRIAH GAEQHACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSHGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AKFAGRKFRN PKAK

P07322 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools