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Protein

Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase

Gene

iolG

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

Functioni

Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively. Can also use D-glucose and D-xylose, and shows a trace of activity with D-ribose and D-fructose.2 Publications

Catalytic activityi

Myo-inositol + NAD+ = 2,4,6/3,5-pentahydroxycyclohexanone + NADH.1 Publication
1D-chiro-inositol + NAD+ = 2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH.1 Publication

Kineticsi

  1. KM=0.036 mM for NADH (in the presence of 5 mM 2-inosose at 25 degrees Celsius and pH 7)1 Publication
  2. KM=0.23 mM for NAD (in the presence of 40 mM myo-inositol at 25 degrees Celsius and pH 9)1 Publication
  3. KM=1.61 mM for 2-inosose (in the presence of 0.1 mM NADH at 25 degrees Celsius and pH 7)1 Publication
  4. KM=18.2 mM for myo-inositol (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)1 Publication
  5. KM=55.6 mM for alpha-D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)1 Publication
  6. KM=167 mM for D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)1 Publication
  7. KM=190 mM for D-xylose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)1 Publication
  1. Vmax=42 µmol/min/mg enzyme for 2-inosose reduction reaction (at 25 degrees Celsius and pH 7)1 Publication
  2. Vmax=21 µmol/min/mg enzyme for myo-inositol oxidation reaction (at 25 degrees Celsius and pH 9)1 Publication
  3. Vmax=13.5 µmol/min/mg enzyme with for alpha-D-glucose oxidation reaction (at 25 degrees Celsius and pH 9)1 Publication
  4. Vmax=7.3 µmol/min/mg enzyme for D-glucose oxidation reaction (at 25 degrees Celsius and pH 9)1 Publication
  5. Vmax=6.7 µmol/min/mg enzyme for D-xylose oxidation reaction (at 25 degrees Celsius and pH 9)1 Publication

pH dependencei

Optimum pH is 9.5 for inositol 2-dehydrogenase activity.1 Publication

Pathwayi: myo-inositol degradation into acetyl-CoA

This protein is involved in step 1 of the subpathway that synthesizes acetyl-CoA from myo-inositol.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase (iolG)
  2. Inosose dehydratase (iolE)
  3. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase (iolD)
  4. 5-deoxy-glucuronate isomerase (iolB)
  5. 5-dehydro-2-deoxygluconokinase (iolC)
  6. 6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase (iolJ)
  7. Methylmalonate semialdehyde dehydrogenase [acylating] (iolA)
This subpathway is part of the pathway myo-inositol degradation into acetyl-CoA, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from myo-inositol, the pathway myo-inositol degradation into acetyl-CoA and in Polyol metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBSUB:BSU39700-MONOMER.
MetaCyc:BSU39700-MONOMER.
BRENDAi1.1.1.18. 658.
1.1.1.369. 658.
SABIO-RKP26935.
UniPathwayiUPA00076; UER00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase (EC:1.1.1.18, EC:1.1.1.369)
Alternative name(s):
Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
Short name:
MI 2-dehydrogenase/DCI 3-dehydrogenase
Gene namesi
Name:iolG
Synonyms:idh
Ordered Locus Names:BSU39700
ORF Names:E83G
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenasePRO_0000091774Add
BLAST

Proteomic databases

PaxDbiP26935.

Expressioni

Inductioni

By inositol. Subjected to catabolite repression.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021411.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi12 – 2312Combined sources
Beta strandi26 – 349Combined sources
Helixi38 – 4710Combined sources
Beta strandi53 – 575Combined sources
Helixi58 – 636Combined sources
Beta strandi69 – 724Combined sources
Helixi76 – 783Combined sources
Helixi79 – 8810Combined sources
Beta strandi92 – 954Combined sources
Helixi103 – 11614Combined sources
Beta strandi121 – 1233Combined sources
Helixi126 – 1294Combined sources
Helixi131 – 14111Combined sources
Turni142 – 1454Combined sources
Beta strandi146 – 15611Combined sources
Helixi168 – 1714Combined sources
Turni172 – 1743Combined sources
Helixi175 – 18511Combined sources
Beta strandi189 – 1957Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi210 – 2178Combined sources
Beta strandi222 – 2287Combined sources
Beta strandi236 – 24510Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi263 – 2664Combined sources
Helixi272 – 2754Combined sources
Helixi277 – 29418Combined sources
Helixi302 – 32120Combined sources
Beta strandi323 – 3264Combined sources
Helixi334 – 3363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MZ0X-ray1.54A1-344[»]
3NT2X-ray2.30A/B1-344[»]
3NT4X-ray2.50A/B1-344[»]
3NT5X-ray2.90A/B1-344[»]
3NTOX-ray1.91A1-344[»]
3NTQX-ray2.60A/B1-344[»]
3NTRX-ray2.65A/B1-344[»]
4L8VX-ray2.09A/B/C/D1-337[»]
4L9RX-ray1.95A1-337[»]
ProteinModelPortaliP26935.
SMRiP26935. Positions 1-337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26935.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Phylogenomic databases

eggNOGiENOG4105DRI. Bacteria.
COG0673. LUCA.
HOGENOMiHOG000227439.
InParanoidiP26935.
KOiK00010.
OMAiDIQCEIV.
PhylomeDBiP26935.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01671. IolG. 1 hit.
InterProiIPR023794. MI/DCI_dehydrogenase.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

P26935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRIGVIGT GAIGKEHINR ITNKLSGAEI VAVTDVNQEA AQKVVEQYQL
60 70 80 90 100
NATVYPNDDS LLADENVDAV LVTSWGPAHE SSVLKAIKAQ KYVFCEKPLA
110 120 130 140 150
TTAEGCMRIV EEEIKVGKRL VQVGFMRRYD SGYVQLKEAL DNHVIGEPLM
160 170 180 190 200
IHCAHRNPTV GDNYTTDMAV VDTLVHEIDV LHWLVNDDYE SVQVIYPKKS
210 220 230 240 250
KNALPHLKDP QIVVIETKGG IVINAEIYVN CKYGYDIQCE IVGEDGIIKL
260 270 280 290 300
PEPSSISLRK EGRFSTDILM DWQRRFVAAY DVEIQDFIDS IQKKGEVSGP
310 320 330 340
TAWDGYIAAV TTDACVKAQE SGQKEKVELK EKPEFYQSFT TVQN
Length:344
Mass (Da):38,351
Last modified:July 28, 2009 - v2
Checksum:i92464EDEC3A735F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451I → N in AAA22543 (PubMed:1761221).Curated
Sequence conflicti145 – 1451I → N in BAA03296 (PubMed:7952181).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76431 Genomic DNA. Translation: AAA22543.1.
D14399 Genomic DNA. Translation: BAA03296.1.
AY676876 Genomic DNA. Translation: AAT78431.1.
AL009126 Genomic DNA. Translation: CAB16006.2.
PIRiJH0511.
RefSeqiNP_391849.2. NC_000964.3.
WP_003244482.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB16006; CAB16006; BSU39700.
GeneIDi937615.
KEGGibsu:BSU39700.
PATRICi18980004. VBIBacSub10457_4164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76431 Genomic DNA. Translation: AAA22543.1.
D14399 Genomic DNA. Translation: BAA03296.1.
AY676876 Genomic DNA. Translation: AAT78431.1.
AL009126 Genomic DNA. Translation: CAB16006.2.
PIRiJH0511.
RefSeqiNP_391849.2. NC_000964.3.
WP_003244482.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MZ0X-ray1.54A1-344[»]
3NT2X-ray2.30A/B1-344[»]
3NT4X-ray2.50A/B1-344[»]
3NT5X-ray2.90A/B1-344[»]
3NTOX-ray1.91A1-344[»]
3NTQX-ray2.60A/B1-344[»]
3NTRX-ray2.65A/B1-344[»]
4L8VX-ray2.09A/B/C/D1-337[»]
4L9RX-ray1.95A1-337[»]
ProteinModelPortaliP26935.
SMRiP26935. Positions 1-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021411.

Proteomic databases

PaxDbiP26935.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16006; CAB16006; BSU39700.
GeneIDi937615.
KEGGibsu:BSU39700.
PATRICi18980004. VBIBacSub10457_4164.

Phylogenomic databases

eggNOGiENOG4105DRI. Bacteria.
COG0673. LUCA.
HOGENOMiHOG000227439.
InParanoidiP26935.
KOiK00010.
OMAiDIQCEIV.
PhylomeDBiP26935.

Enzyme and pathway databases

UniPathwayiUPA00076; UER00143.
BioCyciBSUB:BSU39700-MONOMER.
MetaCyc:BSU39700-MONOMER.
BRENDAi1.1.1.18. 658.
1.1.1.369. 658.
SABIO-RKP26935.

Miscellaneous databases

EvolutionaryTraceiP26935.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01671. IolG. 1 hit.
InterProiIPR023794. MI/DCI_dehydrogenase.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIOLG_BACSU
AccessioniPrimary (citable) accession number: P26935
Secondary accession number(s): Q6B6R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 28, 2009
Last modified: September 7, 2016
This is version 124 of the entry and version 2 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. 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.