Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q31CX3

- ENO_PROM9

UniProt

Q31CX3 - ENO_PROM9

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Enolase

Gene

eno

Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Magnesium.UniRule annotation

Enzyme regulationi

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei159 – 1591SubstrateUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Active sitei209 – 2091Proton donorUniRule annotation
Metal bindingi246 – 2461MagnesiumUniRule annotation
Metal bindingi287 – 2871MagnesiumUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Metal bindingi314 – 3141MagnesiumUniRule annotation
Binding sitei314 – 3141SubstrateUniRule annotation
Active sitei339 – 3391Proton acceptorUniRule annotation
Binding sitei339 – 3391Substrate (covalent); in inhibited formUniRule annotation
Binding sitei390 – 3901SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. phosphopyruvate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciPMAR74546:GHRG-215-MONOMER.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyaseUniRule annotation
2-phosphoglycerate dehydrataseUniRule annotation
Gene namesi
Name:enoUniRule annotation
Ordered Locus Names:PMT9312_0210
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation. Secreted UniRule annotation. Cell surface UniRule annotation
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 cell surface.UniRule annotation

GO - Cellular componenti

  1. cell surface Source: UniProtKB-HAMAP
  2. extracellular region Source: UniProtKB-KW
  3. phosphopyruvate hydratase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430EnolasePRO_0000267072Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi74546.PMT9312_0210.

Structurei

3D structure databases

ProteinModelPortaliQ31CX3.
SMRiQ31CX3. Positions 8-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3694Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072174.
KOiK01689.
OMAiRSEIKGQ.
OrthoDBiEOG65J589.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q31CX3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKETIDFLID TIEARQVLDS RGNPTVEAEV FLECGASGRA IVPSGASTGA
60 70 80 90 100
HEAHELRDGG SKYMGKGVLN AVNKIHETIS PALCGLSALD QTTVDKLMIE
110 120 130 140 150
IDGTFNKSNL GANSILAVSL ATARASANAL DVPLYRYLGD PLSNLLPVPL
160 170 180 190 200
MNVINGGAHA PNSLDFQEFM LVPHGVQNFS ESLRMGTEIF HSLKSLLDKK
210 220 230 240 250
GLSTAVGDEG GFAPNLSSSE EAGDLLLEAI QKAGFIPGEQ VSLALDAAST
260 270 280 290 300
EFYSDGIYKY EGKSLNSSEM ISYLSRLVSN YPIVSIEDGL AEDDWEGWSE
310 320 330 340 350
LNKELGNKVQ LVGDDLFVTN TERLRKGIME KSANSILIKV NQIGTLTETL
360 370 380 390 400
EAIELAKTSG FTSVISHRSG ETEDTTIADL SVATRSGQIK TGSLSRSERI
410 420 430
AKYNRLLKIE EELGNQARFA GALGLGPKNI
Length:430
Mass (Da):46,071
Last modified:December 6, 2005 - v1
Checksum:iD263A14A2578F717
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB49272.1.
RefSeqiYP_396708.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB49272; ABB49272; PMT9312_0210.
GeneIDi3764995.
KEGGipmi:PMT9312_0210.
PATRICi23004038. VBIProMar70153_0214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB49272.1 .
RefSeqi YP_396708.1. NC_007577.1.

3D structure databases

ProteinModelPortali Q31CX3.
SMRi Q31CX3. Positions 8-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74546.PMT9312_0210.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB49272 ; ABB49272 ; PMT9312_0210 .
GeneIDi 3764995.
KEGGi pmi:PMT9312_0210.
PATRICi 23004038. VBIProMar70153_0214.

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072174.
KOi K01689.
OMAi RSEIKGQ.
OrthoDBi EOG65J589.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci PMAR74546:GHRG-215-MONOMER.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiENO_PROM9
AccessioniPrimary (citable) accession number: Q31CX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3