NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.

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.
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 bacterial cell surface (By similarity).
SIMILARITY: Belongs to the enolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000512; ABM31913.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_969687.1; -.

3D structure databases

ModBase

A1TLS5.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004634;	Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00318; -; 1.
PBIL [Tree]

InterPro

IPR000941; Enolase.
Graphical view of domain structure.

PANTHER

PTHR11902; Enolase; 1.

Pfam

PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001400; Enolase; 1.

PRINTS

PR00148; ENOLASE.

ProDom

PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Genome annotation databases

GeneID

4667611; -.

GenomeReviews

CP000512_GR; Aave_1322.

KEGG

aav:Aave_1322; -.

NMPDR

fig|397945.5.peg.1164; -.

CMR

A1TLS5; Aave_1322.

Other

ProtoNet

A1TLS5.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 428`	`428`	`Enolase.`	`PRO_0000280830`
`REGION`	`365 368`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`205 205`		`Proton donor (By similarity).`
`ACT_SITE`	`338 338`		`Proton acceptor (By similarity).`
`METAL`	`242 242`		`Magnesium (By similarity).`
`METAL`	`286 286`		`Magnesium (By similarity).`
`METAL`	`313 313`		`Magnesium (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`286 286`		`Substrate (By similarity).`
`BINDING`	`313 313`		`Substrate (By similarity).`
`BINDING`	`338 338`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`389 389`		`Substrate (By similarity).`
`MOD_RES`	`280 280`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 45853 Da [This is the MW of the unprocessed precursor]

CRC64: AC94EBFC0B4B07C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSAIVDIVGR EVLDSRGNPT VECDVLLESG VMGRAAVPSG ASTGSREAIE LRDGDKSRYL 

        70         80         90        100        110        120 
GKGVLKAVEH INTEISEAVL GLDASEQAFL DKTLIDLDGT DNKSRLGANA MLAVSMAVAR 

       130        140        150        160        170        180 
AAAEESGLPL YRYLGGMGGL QLPVPMMNVI NGGAHANNSL DLQEFMIIPV GAPSFREAVR 

       190        200        210        220        230        240 
WGAEVFHALK KIINDKGMST AVGDEGGFAP SVENHEAAIQ LILQAIDAAG YTAGEQIALG 

       250        260        270        280        290        300 
LDCAASEFYK DGHYVLEGEG GIRLTAQQWT DMLATWVDKY PIISIEDGMA EGDWDGWKHL 

       310        320        330        340        350        360 
TERLGKNVQL VGDDLFVTNT RILKEGIDKD IGNSILIKIN QIGTLTETFA AIEMAKRAGY 

       370        380        390        400        410        420 
TAVISHRSGE TEDSTIADIA VGTNAGQIKT GSLSRSDRIA KYNQLLRIEE DLGDIAHYPG 


RAAFYNLR

A1TLS5 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools