ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q1ISS7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ENO_ACIBL
Primary accession number Q1ISS7
Secondary accession numbers None
Integrated into Swiss-Prot on December 12, 2006
Sequence was last modified on June 13, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 22)
Name and origin of the protein
Protein name Enolase
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase
2-phospho-D-glycerate hydro-lyase
Gene name
Name: eno
OrderedLocusNames: Acid345_1070
From
Acidobacteria bacterium (strain Ellin345) [TaxID: 204669] [HAMAP proteome]
Taxonomy Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Kiss H., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Kuske C., Janssen P.H., Richardson P.;
"Complete sequence of Acidobacteria bacterium Ellin345.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
Comments
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
CP000360; ABF40073.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_590147.1; -.
3D structure databases
ModBase Q1ISS7.
Ontologies
GO
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]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS Q1ISS7.
Genome annotation databases
GeneID 4070030; -.
GenomeReviews CP000360_GR; Acid345_1070.
KEGG aba:Acid345_1070; -.
NMPDR fig|204669.6.peg.1057; -.
Phylogenomic databases
HOGENOM Q1ISS7; -.
Genome annotation databases
CMR Q1ISS7; Acid345_1070.
Other
ProtoNet Q1ISS7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   433  433     Enolase. PRO_0000266991
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: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 46524 Da [This is the MW of the unprocessed precursor] CRC64: 6B268DB6EFA38EC4 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MFDITLVHAR EILDSRGNPT VEAEVTLSGG AVGRAAVPSG ASTGEHEAVE LRDGDNARYL 

        70         80         90        100        110        120 
GKGVLKAVEN VEGEIAQALG GMDASQQRDI DMRMLDLDGT ENKGRLGANA ILAVSMASAR 

       130        140        150        160        170        180 
AVANQLDIPL YRYLGGVNGN ILPVPMMNIL NGGAHADNNV DFQEFMAMPV GAESFSEALR 

       190        200        210        220        230        240 
WGAEVFHTLK GVLKKRGYNT AVGDEGGFAP SLKSNVEAIE VILEAIQQAG YTPGEQIAIA 

       250        260        270        280        290        300 
LDPAASEFFK DGKYIFKKSD KSEKTSEQMV RWWSDWANKY PIVSIEDGLA EDDWEGWKLL 

       310        320        330        340        350        360 
TDELGDKIQL VGDDLFVTNP ERLARGIDNG VANSILIKVN QIGTLSETLD AIEMARRNGY 

       370        380        390        400        410        420 
TAVISHRSGE TEDTFIADLA VATGAGQIKT GSASRTDRVA KYNQLLRIEE QLGAGARFLG 

       430 
IGALNYDGDL SAE
Q1ISS7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!