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Protein

2,3-diketo-5-methylthiopentyl-1-phosphate enolase

Gene

mtnW

Organism
Geobacillus kaustophilus (strain HTA426)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P).1 Publication

Catalytic activityi

5-(methylthio)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 3 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (mtnA)
  2. Methylthioribulose-1-phosphate dehydratase (mtnB)
  3. 2,3-diketo-5-methylthiopentyl-1-phosphate enolase (mtnW)
  4. 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (mtnX)
  5. Acireductone dioxygenase (mtnD)
  6. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei98Proton acceptor1
Binding sitei147Substrate1
Metal bindingi173Magnesium; via carbamate group1
Metal bindingi175Magnesium1
Metal bindingi176Magnesium1
Binding sitei264Substrate1
Binding sitei337Substrate; via amide nitrogen1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi5.3.2.5. 8138.
UniPathwayiUPA00904; UER00876.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-diketo-5-methylthiopentyl-1-phosphate enolase (EC:5.3.2.5)
Short name:
DK-MTP-1-P enolase
Alternative name(s):
RuBisCO-like protein
Short name:
RLP
Gene namesi
Name:mtnW
Ordered Locus Names:GK0953
OrganismiGeobacillus kaustophilus (strain HTA426)
Taxonomic identifieri235909 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000001172 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98K → A: Loss of enolase activity. 1 Publication1
Mutagenesisi147K → A: Same activity as the wild-type. 1 Publication1
Mutagenesisi173K → A: Same activity as the wild-type. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626941 – 4132,3-diketo-5-methylthiopentyl-1-phosphate enolaseAdd BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei173N6-carboxylysine1 Publication1

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi235909.GK0953.

Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 14Combined sources12
Helixi16 – 26Combined sources11
Turni27 – 29Combined sources3
Helixi37 – 43Combined sources7
Helixi44 – 46Combined sources3
Beta strandi49 – 55Combined sources7
Helixi60 – 66Combined sources7
Beta strandi71 – 80Combined sources10
Helixi81 – 83Combined sources3
Helixi88 – 96Combined sources9
Helixi98 – 101Combined sources4
Beta strandi102 – 111Combined sources10
Helixi114 – 117Combined sources4
Helixi126 – 134Combined sources9
Beta strandi141 – 145Combined sources5
Helixi154 – 166Combined sources13
Beta strandi170 – 173Combined sources4
Beta strandi182 – 184Combined sources3
Helixi186 – 204Combined sources19
Beta strandi209 – 213Combined sources5
Helixi218 – 220Combined sources3
Helixi221 – 230Combined sources10
Beta strandi234 – 238Combined sources5
Helixi240 – 242Combined sources3
Helixi245 – 253Combined sources9
Turni255 – 257Combined sources3
Beta strandi261 – 263Combined sources3
Helixi268 – 270Combined sources3
Beta strandi275 – 279Combined sources5
Helixi281 – 284Combined sources4
Helixi287 – 292Combined sources6
Beta strandi295 – 300Combined sources6
Beta strandi302 – 306Combined sources5
Helixi310 – 321Combined sources12
Beta strandi325 – 327Combined sources3
Beta strandi331 – 337Combined sources7
Helixi340 – 342Combined sources3
Helixi343 – 350Combined sources8
Beta strandi352 – 359Combined sources8
Helixi360 – 363Combined sources4
Helixi368 – 385Combined sources18
Helixi389 – 393Combined sources5
Helixi397 – 406Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OEJX-ray2.55A/B1-413[»]
2OEKX-ray1.80A/B1-413[»]
2OELX-ray1.80A/B1-413[»]
2OEMX-ray1.70A/B1-413[»]
ProteinModelPortaliQ5L1E2.
SMRiQ5L1E2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5L1E2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 176Substrate binding4
Regioni359 – 360Substrate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230832.
KOiK08965.
OMAiKDDEIFF.
OrthoDBiPOG091H0DKL.

Family and domain databases

CDDicd08209. RLP_DK-MTP-1-P-enolase. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01679. Salvage_MtnW. 1 hit.
InterProiIPR017717. Diketo-Methiopentyl-P_enolase.
IPR033966. RuBisCO.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsiTIGR03332. salvage_mtnW. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5L1E2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVMATYLL HDETDIRKKA EGIALGLTIG TWTDLPALEQ EQLRKHKGEV
60 70 80 90 100
VAIEELGESE RVNAYFGKRL KRAIVKIAYP TVNFSADLPA LLVTTFGKLS
110 120 130 140 150
LDGEVRLLDL EFPDEWKRQF PGPRFGIDGI RDRVGVHNRP LLMSIFKGMI
160 170 180 190 200
GRDLAYLTSE LKKQALGGVD LVKDDEILFD SELLPFEKRI TEGKAALQEV
210 220 230 240 250
YEQTGKRTLY AVNLTGKTFA LKDKAKRAAE LGADVLLFNV FAYGLDVLQA
260 270 280 290 300
LREDEEIAVP IMAHPAFSGA VTPSEFYGVA PSLWLGKLLR LAGADFVLFP
310 320 330 340 350
SPYGSVALER EQALGIARAL TDDQEPFARA FPVPSAGIHP GLVPLIIRDF
360 370 380 390 400
GLDTIVNAGG GIHGHPDGAI GGGRAFRAAI DAVLAGRPLR AAAAENEALQ
410
KAIDRWGVVE VEA
Length:413
Mass (Da):44,906
Last modified:February 1, 2005 - v1
Checksum:i560DBEA2E17E0310
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD75238.1.
RefSeqiWP_011230454.1. NC_006510.1.

Genome annotation databases

EnsemblBacteriaiBAD75238; BAD75238; GK0953.
GeneIDi3185264.
KEGGigka:GK0953.
PATRICi21963143. VBIGeoKau81518_1041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD75238.1.
RefSeqiWP_011230454.1. NC_006510.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OEJX-ray2.55A/B1-413[»]
2OEKX-ray1.80A/B1-413[»]
2OELX-ray1.80A/B1-413[»]
2OEMX-ray1.70A/B1-413[»]
ProteinModelPortaliQ5L1E2.
SMRiQ5L1E2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi235909.GK0953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD75238; BAD75238; GK0953.
GeneIDi3185264.
KEGGigka:GK0953.
PATRICi21963143. VBIGeoKau81518_1041.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230832.
KOiK08965.
OMAiKDDEIFF.
OrthoDBiPOG091H0DKL.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00876.
BRENDAi5.3.2.5. 8138.

Miscellaneous databases

EvolutionaryTraceiQ5L1E2.

Family and domain databases

CDDicd08209. RLP_DK-MTP-1-P-enolase. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01679. Salvage_MtnW. 1 hit.
InterProiIPR017717. Diketo-Methiopentyl-P_enolase.
IPR033966. RuBisCO.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsiTIGR03332. salvage_mtnW. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMTNW_GEOKA
AccessioniPrimary (citable) accession number: Q5L1E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: February 1, 2005
Last modified: November 30, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Has no RuBP-carboxylation activity.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.