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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)DescriptionActionsGraphical viewLength
Binding sitei94Substrate1
Sitei160Transition state stabilizer1
Binding sitei199Substrate1
Active sitei240Proton donor1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001560921 – 353Methylthioribose-1-phosphate isomeraseAdd BLAST353

Proteomic databases

PaxDbiO31662.
PRIDEiO31662.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 6Combined sources5
Beta strandi10 – 13Combined sources4
Beta strandi18 – 21Combined sources4
Helixi23 – 25Combined sources3
Turni26 – 28Combined sources3
Beta strandi32 – 35Combined sources4
Helixi38 – 46Combined sources9
Helixi53 – 68Combined sources16
Helixi76 – 91Combined sources16
Helixi98 – 110Combined sources13
Turni111 – 113Combined sources3
Helixi117 – 146Combined sources30
Helixi147 – 149Combined sources3
Beta strandi155 – 158Combined sources4
Turni164 – 166Combined sources3
Beta strandi167 – 170Combined sources4
Beta strandi172 – 174Combined sources3
Helixi175 – 182Combined sources8
Beta strandi188 – 192Combined sources5
Turni195 – 198Combined sources4
Helixi199 – 202Combined sources4
Helixi204 – 209Combined sources6
Turni210 – 212Combined sources3
Beta strandi214 – 218Combined sources5
Helixi220 – 222Combined sources3
Helixi223 – 229Combined sources7
Beta strandi234 – 237Combined sources4
Beta strandi240 – 243Combined sources4
Beta strandi248 – 251Combined sources4
Helixi254 – 263Combined sources10
Beta strandi268 – 271Combined sources4
Helixi274 – 276Combined sources3
Helixi284 – 286Combined sources3
Helixi295 – 298Combined sources4
Beta strandi315 – 320Combined sources6
Helixi322 – 324Combined sources3
Beta strandi326 – 330Combined sources5
Beta strandi333 – 335Combined sources3
Helixi339 – 346Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO31662.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 53Substrate binding3
Regioni250 – 251Substrate binding2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YRFX-ray2.70A/B1-353[»]
2YVKX-ray2.40A/B/C/D1-353[»]
ProteinModelPortaliO31662.
SMRiO31662.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiO31662.
PRIDEiO31662.

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: November 2, 2016
This is version 120 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.