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Protein

Methylthioribose-1-phosphate isomerase

Gene

mtnA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).UniRule annotation1 Publication

Catalytic activityi

S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate.UniRule annotation

Kineticsi

  1. KM=138 µM for methylthioribose-1-phosphate (at pH 8.5 and 35 degrees Celsius)1 Publication
  1. Vmax=20.4 µmol/min/mg enzyme (at pH 8.5 and 35 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8.1.1 Publication

Temperature dependencei

Optimum temperature is 35 degrees Celsius.1 Publication

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 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. 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. Transaminase MtnE (mtnE)
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
Binding sitei94 – 941Substrate
Sitei160 – 1601Transition state stabilizer
Binding sitei199 – 1991Substrate
Active sitei240 – 2401Proton donor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU13550-MONOMER.
BRENDAi5.3.1.23. 658.
UniPathwayiUPA00904; UER00874.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylthioribose-1-phosphate isomeraseUniRule annotation (EC:5.3.1.23UniRule annotation)
Short name:
M1PiUniRule annotation
Short name:
MTR-1-P isomeraseUniRule annotation
Alternative name(s):
S-methyl-5-thioribose-1-phosphate isomeraseUniRule annotation
Gene namesi
Name:mtnAUniRule annotation
Synonyms:ykrS
Ordered Locus Names:BSU13550
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Methylthioribose-1-phosphate isomerasePRO_0000156092Add
BLAST

Proteomic databases

PaxDbiO31662.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

IntActiO31662. 1 interaction.
MINTiMINT-8365263.
STRINGi224308.Bsubs1_010100007511.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 65Combined sources
Beta strandi10 – 134Combined sources
Beta strandi18 – 214Combined sources
Helixi23 – 253Combined sources
Turni26 – 283Combined sources
Beta strandi32 – 354Combined sources
Helixi38 – 469Combined sources
Helixi53 – 6816Combined sources
Helixi76 – 9116Combined sources
Helixi98 – 11013Combined sources
Turni111 – 1133Combined sources
Helixi117 – 14630Combined sources
Helixi147 – 1493Combined sources
Beta strandi155 – 1584Combined sources
Turni164 – 1663Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi172 – 1743Combined sources
Helixi175 – 1828Combined sources
Beta strandi188 – 1925Combined sources
Turni195 – 1984Combined sources
Helixi199 – 2024Combined sources
Helixi204 – 2096Combined sources
Turni210 – 2123Combined sources
Beta strandi214 – 2185Combined sources
Helixi220 – 2223Combined sources
Helixi223 – 2297Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi248 – 2514Combined sources
Helixi254 – 26310Combined sources
Beta strandi268 – 2714Combined sources
Helixi274 – 2763Combined sources
Helixi284 – 2863Combined sources
Helixi295 – 2984Combined sources
Beta strandi315 – 3206Combined sources
Helixi322 – 3243Combined sources
Beta strandi326 – 3305Combined sources
Beta strandi333 – 3353Combined sources
Helixi339 – 3468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRFX-ray2.70A/B1-353[»]
2YVKX-ray2.40A/B/C/D1-353[»]
ProteinModelPortaliO31662.
SMRiO31662. Positions 1-349.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31662.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 533Substrate binding
Regioni250 – 2512Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C35. Bacteria.
COG0182. LUCA.
HOGENOMiHOG000224730.
InParanoidiO31662.
KOiK08963.
OMAiHIYACET.
PhylomeDBiO31662.

Family and domain databases

Gene3Di1.20.120.420. 1 hit.
HAMAPiMF_01678. Salvage_MtnA. 1 hit.
InterProiIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.

Sequencei

Sequence statusi: Complete.

O31662-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHSFAVPRS VEWKETAITI LNQQKLPDET EYLELTTKED VFDAIVTLKV
60 70 80 90 100
RGAPAIGITA AFGLALAAKD IETDNVTEFR RRLEDIKQYL NSSRPTAINL
110 120 130 140 150
SWALERLSHS VENAISVNEA KTNLVHEAIQ IQVEDEETCR LIGQNALQLF
160 170 180 190 200
KKGDRIMTIC NAGSIATSRY GTALAPFYLA KQKDLGLHIY ACETRPVLQG
210 220 230 240 250
SRLTAWELMQ GGIDVTLITD SMAAHTMKEK QISAVIVGAD RIAKNGDTAN
260 270 280 290 300
KIGTYGLAIL ANAFDIPFFV AAPLSTFDTK VKCGADIPIE ERDPEEVRQI
310 320 330 340 350
SGVRTAPSNV PVFNPAFDIT PHDLISGIIT EKGIMTGNYE EEIEQLFKGE

KVH
Length:353
Mass (Da):38,860
Last modified:January 1, 1998 - v1
Checksum:iD8866535BE127DC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13228.1.
PIRiC69863.
RefSeqiNP_389238.1. NC_000964.3.
WP_003232498.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13228; CAB13228; BSU13550.
GeneIDi939341.
KEGGibsu:BSU13550.
PATRICi18974478. VBIBacSub10457_1431.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13228.1.
PIRiC69863.
RefSeqiNP_389238.1. NC_000964.3.
WP_003232498.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRFX-ray2.70A/B1-353[»]
2YVKX-ray2.40A/B/C/D1-353[»]
ProteinModelPortaliO31662.
SMRiO31662. Positions 1-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO31662. 1 interaction.
MINTiMINT-8365263.
STRINGi224308.Bsubs1_010100007511.

Proteomic databases

PaxDbiO31662.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13228; CAB13228; BSU13550.
GeneIDi939341.
KEGGibsu:BSU13550.
PATRICi18974478. VBIBacSub10457_1431.

Phylogenomic databases

eggNOGiENOG4105C35. Bacteria.
COG0182. LUCA.
HOGENOMiHOG000224730.
InParanoidiO31662.
KOiK08963.
OMAiHIYACET.
PhylomeDBiO31662.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00874.
BioCyciBSUB:BSU13550-MONOMER.
BRENDAi5.3.1.23. 658.

Miscellaneous databases

EvolutionaryTraceiO31662.

Family and domain databases

Gene3Di1.20.120.420. 1 hit.
HAMAPiMF_01678. Salvage_MtnA. 1 hit.
InterProiIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMTNA_BACSU
AccessioniPrimary (citable) accession number: O31662
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a translation initiation factor.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.