Reviewed, UniProtKB/Swiss-Prot B0C9F0 (ENO_ACAM1)

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:	AM1_3978

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	426 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 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 – 426	426	Enolase HAMAP MF_00318		PRO_1000079119
Regions
	Region	364 – 367	4	Substrate binding By similarity
Sites
	Active site	207	1	Proton donor By similarity
	Active site	337	1	Proton acceptor By similarity
	Metal binding	244	1	Magnesium By similarity
	Metal binding	285	1	Magnesium By similarity
	Metal binding	312	1	Magnesium By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	166	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)
	B0C9F0-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: A603741875A0D897	FASTA	426	45,337
	10 20 30 40 50 60 MHETEIAAIE AREILDSRGR PTVEAEVILS CGAFGLAQVP SGASTGSFEA HELRDGDAQR 70 80 90 100 110 120 YGGKGVLTAV TNIKDHIQPE LVGLNALDQA DIDQTMIDLD GSTNKSKLGA NAILAVSLAT 130 140 150 160 170 180 AKAASEVLNL ELYRYLGGPL ANLLPVPLMN VINGGAHANN NVDIQEFMIV PHGADSFKEA 190 200 210 220 230 240 LRWGAEVFAS LSQVLAAQNL LTGVGDEGGY APNLASNQAA LELLVEAIEK AGYQPGAQIS 250 260 270 280 290 300 LALDVAASEF YKDGQYTYDG AAHSPKELID YLDGLASKYP IVSIEDPLHE EDWESWGNLT 310 320 330 340 350 360 AQLGDRVQLV GDDLFVTNPI RLQKGIEQQS ANSILIKLNQ IGTLTETLET IDLAKRNSFT 370 380 390 400 410 420 SIISHRSGET EDTTIADLAV ATRAGQIKTG SLCRSERVAK YNRLLRIEDE LGSQASYAGA VGLGPG

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000828 Genomic DNA. Translation: ABW28963.1.
RefSeq	YP_001518280.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5682782.
GenomeReviews	Gene locus AM1_3978 in contig CP000828_GR.
KEGG	amr:AM1_3978.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	B0C9F0. 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_ACAM1

Accession

Primary (citable) accession number: B0C9F0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 12 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)