UniProtKB - P42848 (ENO_THEMA)
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Protein
Enolase
Gene
eno
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Functioni
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation1 Publication
Catalytic activityi
2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation1 Publication
Cofactori
Mg2+UniRule annotation1 Publication
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 (By similarity). Inhibited by fluoride and phosphate.UniRule annotation1 Publication
Kineticsi
- KM=0.07 mM for 2-phospho-D-glycerate (at 75 degrees Celsius)1 Publication
- KM=0.03 mM for magnesium (at 75 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 7.5.1 Publication
Temperature dependencei
Optimum temperature is 90 degrees Celsius.1 Publication
: glycolysis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotationProteins known to be involved in the 5 steps of the subpathway in this organism are:
- Glyceraldehyde-3-phosphate dehydrogenase (gap)
- Bifunctional PGK/TIM (pgk/tpi), Multifunctional fusion protein (pgk)
- Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM), Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM)
- Enolase (eno), Enolase (eno)
- Pyruvate kinase (pyk), Pyruvate kinase (Tmari_0206)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 156 | SubstrateUniRule annotation | 1 | |
Binding sitei | 165 | SubstrateUniRule annotation | 1 | |
Active sitei | 206 | Proton donorUniRule annotation | 1 | |
Metal bindingi | 243 | MagnesiumUniRule annotation | 1 | |
Metal bindingi | 286 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 286 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 313 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 313 | SubstrateUniRule annotation | 1 | |
Active sitei | 338 | Proton acceptorUniRule annotation | 1 | |
Binding sitei | 338 | Substrate (covalent); in inhibited formUniRule annotation | 1 | |
Binding sitei | 389 | SubstrateUniRule annotation | 1 |
GO - Molecular functioni
- magnesium ion binding Source: InterPro
- phosphopyruvate hydratase activity Source: UniProtKB-EC
GO - Biological processi
- glycolytic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Lyase |
Biological process | Glycolysis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
UniPathwayi | UPA00109; 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:TM_0877 |
Organismi | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Taxonomic identifieri | 243274 [NCBI] |
Taxonomic lineagei | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › |
Proteomesi |
|
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
- cell surface Source: UniProtKB-SubCell
- extracellular region Source: UniProtKB-SubCell
- phosphopyruvate hydratase complex Source: InterPro
Keywords - Cellular componenti
Cytoplasm, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000133994 | 1 – 429 | EnolaseAdd BLAST | 429 |
Proteomic databases
PRIDEi | P42848 |
Interactioni
Subunit structurei
Homooctamer. Forms a ring-shaped particle.1 Publication
Protein-protein interaction databases
STRINGi | 243274.TM0877 |
Structurei
3D structure databases
ProteinModelPortali | P42848 |
SMRi | P42848 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 365 – 368 | Substrate bindingUniRule annotation | 4 |
Sequence similaritiesi
Belongs to the enolase family.UniRule annotation
Phylogenomic databases
eggNOGi | ENOG4105C70 Bacteria COG0148 LUCA |
InParanoidi | P42848 |
KOi | K01689 |
OMAi | EFMIIPV |
Family and domain databases
CDDi | cd03313 enolase, 1 hit |
Gene3Di | 3.20.20.1201 hit 3.30.390.101 hit |
HAMAPi | MF_00318 Enolase, 1 hit |
InterProi | View protein in InterPro IPR000941 Enolase IPR036849 Enolase-like_C_sf IPR029017 Enolase-like_N IPR034390 Enolase-like_superfamily IPR020810 Enolase_C IPR020809 Enolase_CS IPR020811 Enolase_N |
PANTHERi | PTHR11902 PTHR11902, 1 hit |
Pfami | View protein in Pfam PF00113 Enolase_C, 1 hit PF03952 Enolase_N, 1 hit |
PIRSFi | PIRSF001400 Enolase, 1 hit |
PRINTSi | PR00148 ENOLASE |
SFLDi | SFLDG00178 enolase, 1 hit SFLDS00001 Enolase, 1 hit |
SMARTi | View protein in SMART SM01192 Enolase_C, 1 hit SM01193 Enolase_N, 1 hit |
SUPFAMi | SSF51604 SSF51604, 1 hit |
TIGRFAMsi | TIGR01060 eno, 1 hit |
PROSITEi | View protein in PROSITE PS00164 ENOLASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P42848-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MYVEIVDVRA REVLDSRGNP TVEAEVVLED GTMGRAIVPS GASTGKFEAL
60 70 80 90 100
EIRDKDKKRY LGKGVLKAVE NVNETIAPAL IGMNAFDQPL VDKTLIELDG
110 120 130 140 150
TENKSKLGAN AILAVSMAVA RAAANYLGLP LYKYLGGVNA KVLPVPLMNV
160 170 180 190 200
INGGQHADNN LDLQEFMIVP AGFDSFREAL RAGAEIFHTL KKILHEAGHV
210 220 230 240 250
TAVGDEGGFA PNLSSNEEAI KVLIEAIEKA GYKPGEEVFI ALDCAASSFY
260 270 280 290 300
DEEKGVYYVD GEEKSSEVLM GYYEELVAKY PIISIEDPFA EEDWDAFVEF
310 320 330 340 350
TKRVGNKVQI VGDDLYVTNV KRLSKGIELK ATNSILIKLN QIGTVTETLD
360 370 380 390 400
AVEMAQKNNM TAIISHRSGE SEDTFIADLA VATNAGFIKT GSLSRSERIA
410 420
KYNQLLRIEE ELGKVAEFRG LKSFYSIKR
Sequence cautioni
The sequence AAD35958 differs from that shown. Reason: Erroneous initiation.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD35958.1 Different initiation. |
PIRi | G72323 |
RefSeqi | NP_228685.1, NC_000853.1 |
Genome annotation databases
EnsemblBacteriai | AAD35958; AAD35958; TM_0877 |
GeneIDi | 898551 |
KEGGi | tma:TM0877 tmi:THEMA_00250 tmw:THMA_0899 |
PATRICi | fig|243274.18.peg.50 |
Similar proteinsi
Entry informationi
Entry namei | ENO_THEMA | |
Accessioni | P42848Primary (citable) accession number: P42848 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | May 30, 2000 | |
Last modified: | February 28, 2018 | |
This is version 138 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |