Q9NDH8 (Q9NDH8_TRYBB) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Recommended name: Enolase RuleBase RU000654 EC=4.2.1.11 RuleBase RU000654
Organism	Trypanosoma brucei brucei EMBL AAF73201.1
Taxonomic identifier	5702 [NCBI]
Taxonomic lineage	Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. RuleBase RU000654
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer By similarity. RuleBase RU000654
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. RuleBase RU000654
Sequence similarities	Belongs to the enolase family. RuleBase RU000654

Ontologies

Keywords
Biological process	Glycolysis RuleBase RU000654
Ligand	Magnesium RuleBase RU000654 Metal-binding PDB 1OEP PDB 2PU1 Zinc PDB 1OEP PDB 2PU1
Molecular function	Lyase RuleBase RU000654 EMBL AAF73201.1
Technical term	3D-structure PDB 1OEP PDB 2PU1
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	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
Sites
	Metal binding	156	1	Zinc 1; via tele nitrogen PDB 1OEP
	Metal binding	164	1	Zinc 1 PDB 1OEP
	Metal binding	165	1	Zinc 1 PDB 1OEP
	Metal binding	208	1	Zinc 1 PDB 1OEP
	Metal binding	243	1	Zinc 2 PDB 2PU1
	Metal binding	291	1	Zinc 2 PDB 2PU1
	Metal binding	318	1	Zinc 2 PDB 2PU1

Sequences

	Sequence		Length	Mass (Da)
	Q9NDH8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2573F8AF223ED360	FASTA	429	46,592
	10 20 30 40 50 60 MTIQKVHGRE VLDSRGNPTV EVEVTTERGV FRSAVPSGAS TGVYEACELR DGDKKRYVGK 70 80 90 100 110 120 GCLQAVKNVN EVIGPALIGR DELKQEELDT LMLRLDGTPN KGKLGANAIL GCSMAISKAA 130 140 150 160 170 180 AAAKGVPLYR YLASLAGTKE LRLPVPCFNV INGGKHAGNA LPFQEFMIAP VKATSFSEAL 190 200 210 220 230 240 RMGSEVYHSL RGIIKKKYGQ DAVNVGDEGG FAPPIKDINE PLPILMEAIE EAGHRGKFAI 250 260 270 280 290 300 CMDCAASETY DEKKQQYNLT FKSPEPTWVT AEQLRETYCK WAHDYPIVSI EDPYDQDDFA 310 320 330 340 350 360 GFAGITEALK GKTQIVGDDL TVTNTERIKM AIEKKACNSL LLKINQIGTI SEAIASSKLC 370 380 390 400 410 420 MENGWSVMVS HRSGETEDTY IADLVVALGS GQIKTGAPCR GERTAKLNQL LRIEEELGAH AKFGFPGWS

References

[1]	"Enolase from Trypanosoma brucei, from the amitochondriate protist Mastigamoeba balamuthi, and from the chloroplast and cytosol of Euglena gracilis: pieces in the evolutionary puzzle of the eukaryotic glycolytic pathway." Hannaert V., Brinkmann H., Nowitzki U., Lee J.A., Albert M.A., Sensen C.W., Gaasterland T., Muller M., Michels P., Martin W. Mol. Biol. Evol. 17:989-1000(2000) [PubMed: 10889212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 427 EMBL AAF73201.1.
[2]	"Compartment-specific forms of the glycolytic enzyme enolase from Trypanosoma brucei and Euglena gracilis and a surprising evolutionary history of the genes." Hannaert V., Albert M.-A., Brinkmann H., Nowitzki U., Michels P.A.M., Martin W. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 427 EMBL AAF73201.1.
[3]	"Structural flexibility in Trypanosoma brucei enolase revealed by X-ray crystallography and molecular dynamics." de A S Navarro M.V., Gomes Dias S.M., Mello L.V., da Silva Giotto M.T., Gavalda S., Blonski C., Garratt R.C., Rigden D.J. FEBS J. 274:5077-5089(2007) [PubMed: 17822439] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC.
[4]	"The crystal structure of Trypanosoma brucei enolase: visualisation of the inhibitory metal binding site III and potential as target for selective, irreversible inhibition." da Silva Giotto M.T., Hannaert V., Vertommen D., de A S Navarro M.V., Rider M.H., Michels P.A., Garratt R.C., Rigden D.J. J. Mol. Biol. 331:653-665(2003) [PubMed: 12899835] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF152348 Genomic DNA. Translation: AAF73201.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OEP	X-ray	2.30	A	1-429	[»]
2PU1	X-ray	1.80	A	1-429	[»]

ProteinModelPortal

Q9NDH8.

SMR

Q9NDH8. Positions 1-429.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

OMA

GELYKNF.

Enzyme and pathway databases

BRENDA

4.2.1.11. 409.

Family and domain databases

HAMAP

MF_00318. Enolase.
[Tree]

InterPro

IPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[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.

TIGRFAMs

TIGR01060. Eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9NDH8_TRYBB

Accession

Primary (citable) accession number: Q9NDH8

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2000
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)