Reviewed, UniProtKB/Swiss-Prot Q0A7K4 (ENO_ALHEH)

Names and origin

Protein names

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

Gene names

Name:	eno
Ordered Locus Names:	Mlg_1839

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP MF_00318
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer By similarity.
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.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP MF_00318
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.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete 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 MF_00318		PRO_0000266993
Regions
	Region	364 – 367	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	337	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	285	1	Magnesium By similarity
	Metal binding	312	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	285	1	Substrate By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	337	1	Substrate (covalent); in inhibited form By similarity
	Binding site	388	1	Substrate By similarity
Amino acid modifications
	Modified residue	279	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0A7K4-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 65E5BA96EBF84536	FASTA	429	46,083
	10 20 30 40 50 60 MGTIKQIKAR EILDSRGNPT VEADVILDSG VMGRAAVPSG ASTGTREAVE LRDGDAGRYL 70 80 90 100 110 120 GKGVRKAVEN VNTVIADALC GMDASGQRAL DDRMRELDGT DNKGKLGANA LLAVSLAAAR 130 140 150 160 170 180 ATAAERGQSL FRYLNPEGPW SLPVPMMNIL NGGEHADNSV DIQEFMVMPT GFDRFSEALR 190 200 210 220 230 240 CGTEIFHALK KVLQDRGLNT GVGDEGGFAP DLPSNEAALE VILEAIDRAG YKAGENVWLA 250 260 270 280 290 300 LDAASSEFYQ DGVYRLASEG REFSAEAFAD YLADLCARYP ILSIEDGMDE SDWVGWKALT 310 320 330 340 350 360 DKLGDRVQLV GDDLFVTNTR ILKRGIDEGV GNSILIKFNQ IGTLSETLDA IAMAHEAGFT 370 380 390 400 410 420 SVVSHRSGET EDTTIADLAV ATTATQIKTG SLSRSDRVAK YNQLLRIEEE LGEQADYPGL AAFPQLRRG

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000453 Genomic DNA. Translation: ABI57183.1.
RefSeq	YP_742673.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4269207.
GenomeReviews	Gene locus Mlg_1839 in contig CP000453_GR.
KEGG	aeh:Mlg_1839.
NMPDR	fig|187272.6.peg.1750.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0A7K4.
OMA	Q0A7K4. DIAVGTN.
Family and domain databases
HAMAP	MF_00318. [Tree]
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

ENO_ALHEH

Accession

Primary (citable) accession number: Q0A7K4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	October 17, 2006
Last modified:	June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)