Reviewed, UniProtKB/Swiss-Prot Q2FTN3 (ENO3_METHJ)

Names and origin

Protein names

Recommended name:
    Enolase 3
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 3
    2-phospho-D-glycerate hydro-lyase 3

Gene names

Name:	eno3
Ordered Locus Names:	Mhun_2893

Organism

Methanospirillum hungatei (strain JF-1 / DSM 864) [Complete proteome] [HAMAP]

Taxonomic identifier

323259 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Methanospirillaceae › Methanospirillum

Protein attributes

Sequence length	402 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 – 402	402	Enolase 3		PRO_0000267146
Regions
	Region	352 – 355	4	Substrate binding By similarity
Sites
	Active site	193	1	Proton donor By similarity
	Active site	325	1	Proton acceptor By similarity
	Metal binding	229	1	Magnesium By similarity
	Metal binding	273	1	Magnesium By similarity
	Metal binding	300	1	Magnesium By similarity
	Binding site	143	1	Substrate By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	273	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity
	Binding site	325	1	Substrate (covalent); in inhibited form By similarity
	Binding site	376	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2FTN3-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 3F08AA5C7816B356	FASTA	402	43,282
	10 20 30 40 50 60 MTITRAITLR TILDSRGRKT VEAEVRTEHG FGRAAAPGGA STGIHEAAVR DPLLAIADAQ 70 80 90 100 110 120 GQVIPHLIGI DSSDQIGVDS LLHEIDGTDN FSGIGANVAV ALSLAMAKAA ADATNIPLWQ 130 140 150 160 170 180 HIGGIFVDSA PRPLGNIIGG GAHASHATQF QEFLVVPTGC ERVRDGIFAN AQVHKTVYDL 190 200 210 220 230 240 LKKRGIRAGK GDEGAWAPPI SDPEAFRILA EAISLVSDET GFEISPGIDA AASQLYDPES 250 260 270 280 290 300 GMYRYRDGTV RSPEDQVTYI ADLIDEFDLI YVEDPLYEED YEGFAALNRE AGNRCLICGD 310 320 330 340 350 360 DLFVTNTKRI QEGISHGSAN CVLIKPNQIG TLTDTHEAIH LAKRHGMETV ISHRSGETED 370 380 390 400 TTIAHLGCAF QCIFIKTGVV GGERTAKLNE LIRIEESIYE RK

References

[1]

"Complete sequence of Methanospirillum hungatei JF-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000254 Genomic DNA. Translation: ABD42585.1.
RefSeq	YP_504304.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3924453.
GenomeReviews	Gene locus Mhun_2893 in contig CP000254_GR.
KEGG	mhu:Mhun_2893.
NMPDR	fig|323259.5.peg.3031.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2FTN3.
Enzyme and pathway databases
BioCyc	MHUN323259:MHUN_2893-MON.
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]
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO3_METHJ

Accession

Primary (citable) accession number: Q2FTN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	March 21, 2006
Last modified:	November 25, 2008
This is version 27 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)