P42848 (ENO_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase

Gene names

Name:	eno
Ordered Locus Names:	TM_0877

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis By similarity. HAMAP-Rule MF_00318
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318
Cofactor	Magnesium.
Enzyme regulation	The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity. HAMAP-Rule MF_00318
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318
Subunit structure	Homooctamer. Forms a ring-shaped particle. Ref.2
Subcellular location	Cytoplasm. Secreted. Cell surface. Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface By similarity. HAMAP-Rule MF_00318
Sequence similarities	Belongs to the enolase family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 90 degrees Celsius. Ref.2
Sequence caution	The sequence AAD35958.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	Enolase HAMAP-Rule MF_00318		PRO_0000133994
Regions
	Region	365 – 368	4	Substrate binding By similarity
Sites
	Active site	206	1	Proton donor By similarity
	Active site	338	1	Proton acceptor By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	286	1	Magnesium By similarity
	Metal binding	313	1	Magnesium By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity
	Binding site	313	1	Substrate By similarity
	Binding site	338	1	Substrate (covalent); in inhibited form By similarity
	Binding site	389	1	Substrate By similarity
Amino acid modifications
	Modified residue	280	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42848 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 35D65899D3AE56CB	FASTA	429	46,870
	10 20 30 40 50 60 MYVEIVDVRA REVLDSRGNP TVEAEVVLED GTMGRAIVPS GASTGKFEAL EIRDKDKKRY 70 80 90 100 110 120 LGKGVLKAVE NVNETIAPAL IGMNAFDQPL VDKTLIELDG TENKSKLGAN AILAVSMAVA 130 140 150 160 170 180 RAAANYLGLP LYKYLGGVNA KVLPVPLMNV INGGQHADNN LDLQEFMIVP AGFDSFREAL 190 200 210 220 230 240 RAGAEIFHTL KKILHEAGHV TAVGDEGGFA PNLSSNEEAI KVLIEAIEKA GYKPGEEVFI 250 260 270 280 290 300 ALDCAASSFY DEEKGVYYVD GEEKSSEVLM GYYEELVAKY PIISIEDPFA EEDWDAFVEF 310 320 330 340 350 360 TKRVGNKVQI VGDDLYVTNV KRLSKGIELK ATNSILIKLN QIGTVTETLD AVEMAQKNNM 370 380 390 400 410 420 TAIISHRSGE SEDTFIADLA VATNAGFIKT GSLSRSERIA KYNQLLRIEE ELGKVAEFRG LKSFYSIKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing." Schurig H., Rutkat K., Rachel R., Jaenicke R. Protein Sci. 4:228-236(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-24, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35958.1. Different initiation.
PIR	G72323.
RefSeq	NP_228685.1. NC_000853.1.
3D structure databases
ProteinModelPortal	P42848.
SMR	P42848. Positions 5-428.
ModBase	Search...
Protein-protein interaction databases
STRING	243274.TM0877.
Proteomic databases
PRIDE	P42848.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD35958; AAD35958; TM_0877.
GeneID	898551.
KEGG	tma:TM0877.
PATRIC	23936685. VBITheMar51294_0891.
Phylogenomic databases
eggNOG	COG0148.
KO	K01689.
OMA	EYMIMPL.
ProtClustDB	PRK00077.
Enzyme and pathway databases
UniPathway	UPA00109; UER00187.
Family and domain databases
HAMAP	MF_00318. Enolase.
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. PTHR11902. 1 hit.
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

ENO_THEMA

Accession

Primary (citable) accession number: P42848

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program