Reviewed, UniProtKB/Swiss-Prot Q9Y927 (ENO_AERPE)

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:	APE_2458

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	432 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 + H(2)O.
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.
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 archaeal 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
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: HAMAP extracellular region Inferred from electronic annotation. Source: UniProtKB-KW 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 – 432	432	Enolase		PRO_0000134019
Regions
	Region	367 – 370	4	Substrate binding By similarity
Sites
	Active site	210	1	Proton donor By similarity
	Active site	340	1	Proton acceptor By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	288	1	Magnesium By similarity
	Metal binding	315	1	Magnesium By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	315	1	Substrate By similarity
	Binding site	340	1	Substrate (covalent); in inhibited form By similarity
	Binding site	391	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Y927-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 924E6362F8BDFDDE	FASTA	432	46,344
	10 20 30 40 50 60 MGVNDFAIER VWGLQVLDSR GNPTVKAYVK LAGGSLGWGI APSGASRGER EAVELRDGGG 70 80 90 100 110 120 KWRGKGVSRA VSLLNTVVAP RLEGVDARRQ AQIDRLLIEL DGTPNKSRLG GNTTTALSIA 130 140 150 160 170 180 VSRAAAAQAR LELFQYLGGA GARRLPIPLL NVINGGVHAG NELDFQEFMI IPYGFESFTE 190 200 210 220 230 240 AMRAAVETYG ELKSLLKDRY GASAVNVGDE GGFAPPMRSA EEALKTLVDA VEKAGYQPGS 250 260 270 280 290 300 EIALGIDAAA SQLYSNGRYS VEGKSLSREE LLSLYQRLVE QYPIVYLEDP FSEDDYEGFK 310 320 330 340 350 360 AAVDALSTET IIVGDDLLVT NPQRVKEASA LKAVTGLLVK VNQVGTLTEA LEAIQAARDR 370 380 390 400 410 420 GIVHIVSHRS GDTEDTFIAD LAVATEALMI KTGAPARGER TSKYNRLLEI ENILGYSAEY 430 AGPELRGVMG RR

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA81473.1.
PIR	A72477.
RefSeq	NP_148623.1.
3D structure databases
HSSP	HSSP built from PDB template 4ENL based on UniProtKB P00924.
ModBase	Search...
Genome annotation databases
GeneID	1445431.
GenomeReviews	Gene locus APE_2458 in contig BA000002_GR.
KEGG	ape:APE_2458.
NMPDR	fig|272557.1.peg.1731.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9Y927.
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_AERPE

Accession

Primary (citable) accession number: Q9Y927

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1999
Last modified:	November 25, 2008
This is version 61 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)