Skip Header

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

Methylthioribulose-1-phosphate dehydratase

Gene

mtnB

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).UniRule annotation

Catalytic activityi

S-methyl-5-thio-D-ribulose 1-phosphate = 5-(methylthio)-2,3-dioxopentyl phosphate + H2O.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 2 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
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. Enolase-phosphatase E1 (mtnC)
  4. Enolase-phosphatase E1 (mtnC)
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991ZincUniRule annotation
Metal bindingi101 – 1011ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-1418-MONOMER.
UniPathwayiUPA00904; UER00875.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylthioribulose-1-phosphate dehydrataseUniRule annotation (EC:4.2.1.109UniRule annotation)
Short name:
MTRu-1-P dehydrataseUniRule annotation
Gene namesi
Name:mtnBUniRule annotation
Ordered Locus Names:aq_1979
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208Methylthioribulose-1-phosphate dehydratasePRO_0000162933Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_1979.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2521Combined sources
Helixi30 – 323Combined sources
Beta strandi35 – 395Combined sources
Beta strandi41 – 488Combined sources
Helixi54 – 563Combined sources
Helixi59 – 613Combined sources
Beta strandi62 – 665Combined sources
Helixi79 – 9012Combined sources
Beta strandi96 – 1005Combined sources
Helixi103 – 1119Combined sources
Beta strandi114 – 1185Combined sources
Helixi122 – 1254Combined sources
Beta strandi139 – 1435Combined sources
Helixi149 – 16214Combined sources
Beta strandi169 – 1713Combined sources
Turni172 – 1743Combined sources
Beta strandi175 – 1828Combined sources
Helixi183 – 20321Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IRPX-ray2.40A/B1-208[»]
ProteinModelPortaliO67788.
SMRiO67788. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67788.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldolase class II family. MtnB subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CR5. Bacteria.
COG0235. LUCA.
HOGENOMiHOG000086153.
InParanoidiO67788.
KOiK08964.
OMAiIRGHGLY.
OrthoDBiEOG6Z3KJ6.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_01677. Salvage_MtnB.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR017714. MethylthioRu-1-P_deHdtase_MtnB.
[Graphical view]
PANTHERiPTHR10640. PTHR10640. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR03328. salvage_mtnB. 1 hit.

Sequencei

Sequence statusi: Complete.

O67788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVELFKKFS EKVEEIIEAG RILHSRGWVP ATSGNISAKV SEEYIAITAS
60 70 80 90 100
GKHKGKLTPE DILLIDYEGR PVGGGKPSAE TLLHTTVYKL FPEVNAVVHT
110 120 130 140 150
HSPNATVISI VEKKDFVELE DYELLKAFPD IHTHEVKIKI PIFPNEQNIP
160 170 180 190 200
LLAKEVENYF KTSEDKYGFL IRGHGLYTWG RSMEEALIHT EALEFIFECE

LKLLSFHS
Length:208
Mass (Da):23,550
Last modified:August 1, 1998 - v1
Checksum:i3295652C5ED17344
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07751.1.
PIRiH70469.
RefSeqiNP_214357.1. NC_000918.1.
WP_010881293.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07751; AAC07751; aq_1979.
GeneIDi1193685.
KEGGiaae:aq_1979.
PATRICi20960866. VBIAquAeo85532_1528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07751.1.
PIRiH70469.
RefSeqiNP_214357.1. NC_000918.1.
WP_010881293.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IRPX-ray2.40A/B1-208[»]
ProteinModelPortaliO67788.
SMRiO67788. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07751; AAC07751; aq_1979.
GeneIDi1193685.
KEGGiaae:aq_1979.
PATRICi20960866. VBIAquAeo85532_1528.

Phylogenomic databases

eggNOGiENOG4105CR5. Bacteria.
COG0235. LUCA.
HOGENOMiHOG000086153.
InParanoidiO67788.
KOiK08964.
OMAiIRGHGLY.
OrthoDBiEOG6Z3KJ6.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00875.
BioCyciAAEO224324:GJBH-1418-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO67788.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_01677. Salvage_MtnB.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR017714. MethylthioRu-1-P_deHdtase_MtnB.
[Graphical view]
PANTHERiPTHR10640. PTHR10640. 1 hit.
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.
TIGRFAMsiTIGR03328. salvage_mtnB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Crystal structure of the L-fuculose-1-phosphate aldolase (aq_1979) from Aquifex aeolicus VF5."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiMTNB_AQUAE
AccessioniPrimary (citable) accession number: O67788
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 93 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

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.