Q9PQV9 (ENO_UREPA) 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:	UU184

Organism

Ureaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]

Taxonomic identifier

273119 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Ureaplasma

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
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. HAMAP MF_00318
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. HAMAP MF_00318
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. HAMAP MF_00318
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: UniProtKB-KW
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: InterPro phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 440	440	Enolase HAMAP MF_00318		PRO_0000134002
Regions
	Region	378 – 381	4	Substrate binding By similarity
Sites
	Active site	210	1	Proton donor By similarity
	Active site	351	1	Proton acceptor By similarity
	Metal binding	249	1	Magnesium By similarity
	Metal binding	300	1	Magnesium By similarity
	Metal binding	326	1	Magnesium By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity
	Binding site	326	1	Substrate By similarity
	Binding site	351	1	Substrate (covalent); in inhibited form By similarity
	Binding site	402	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PQV9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 5F32F530B7A2B7FA	FASTA	440	49,301
	10 20 30 40 50 60 MKIINLLAYQ ILDSRGQPTV AVKLFLENDQ SVIAMVPSGA STGAKEALEL RDGDVNYFFN 70 80 90 100 110 120 KSVKLAIQNI NNIIRPHLIN KNVLNFFELD NLLINLDGTE NKSKLGANAL LGVSIAIVKA 130 140 150 160 170 180 GAIAASKPLY QYIKEDLMHN YDVNYYAPIP LMNFINGGAH ADNDLDIQEF MIVPLNAISF 190 200 210 220 230 240 SQAIQIGSEI FHQLDKLLKS NHLSTTKGDE GGFAPMLKNN YVTLELLVHA IKKAHYLPSK 250 260 270 280 290 300 TQGVCLALDV AASELYENGK YFFKKSSSHN ITLEQTSFSS DEWIKYWSKL VSMFPIISIE 310 320 330 340 350 360 DCFEENDWNS FALFLKNNPH IQVVGDDLYC TNLKYLQKGI DFKATNAILI KPNQIGTISE 370 380 390 400 410 420 TLDVIKFAQK NNINTIISHR SGETEDTFIA DLAIGVGAGQ IKTGSLSRSE RIAKYNRILE 430 440 IEQELKDKLI YEPSKFFKFR

References

[1]	"The complete sequence of the mucosal pathogen Ureaplasma urealyticum." Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H. Nature 407:757-762(2000) [PubMed: 11048724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700970.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF222894 Genomic DNA. Translation: AAF30591.1.
RefSeq	NP_078016.1. NC_002162.1.
3D structure databases
ProteinModelPortal	Q9PQV9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	875866.
GenomeReviews	Gene locus UU184 in contig AF222894_GR.
KEGG	uur:UU184.
PATRIC	20533910. VBIUrePar45146_0191.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG726599.
OMA	KTMMSHR.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	UURE95667:UU184-MONOMER.
Family and domain databases
HAMAP	MF_00318. Enolase. [Tree]
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
KO	K01689.
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.
TIGRFAMs	TIGR01060. Eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO_UREPA

Accession

Primary (citable) accession number: Q9PQV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program