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Protein

Protein IolS

Gene

iolS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Pathwayi: myo-inositol degradation into acetyl-CoA

This protein is involved in the pathway myo-inositol degradation into acetyl-CoA, which is part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the pathway myo-inositol degradation into acetyl-CoA and in Polyol metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei531
Active sitei58Proton donor1
Active sitei841

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi204 – 214NADPAdd BLAST11

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU39780-MONOMER.
SABIO-RKP46336.
UniPathwayiUPA00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein IolS (EC:1.1.1.-)
Alternative name(s):
AKR11A
Vegetative protein 147
Short name:
VEG147
Gene namesi
Name:iolS
Synonyms:yxbF
Ordered Locus Names:BSU39780
ORF Names:SS92ER
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000703821 – 310Protein IolSAdd BLAST310

Proteomic databases

PaxDbiP46336.
PRIDEiP46336.

Expressioni

Inductioni

Inositol.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021456.

Structurei

Secondary structure

1310
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni26 – 28Combined sources3
Beta strandi29 – 31Combined sources3
Helixi34 – 46Combined sources13
Beta strandi51 – 53Combined sources3
Turni56 – 61Combined sources6
Helixi62 – 71Combined sources10
Helixi76 – 78Combined sources3
Beta strandi80 – 85Combined sources6
Beta strandi87 – 90Combined sources4
Beta strandi93 – 96Combined sources4
Helixi100 – 114Combined sources15
Beta strandi119 – 124Combined sources6
Beta strandi129 – 131Combined sources3
Helixi133 – 145Combined sources13
Beta strandi148 – 150Combined sources3
Beta strandi152 – 156Combined sources5
Helixi159 – 165Combined sources7
Turni166 – 168Combined sources3
Beta strandi173 – 177Combined sources5
Helixi184 – 186Combined sources3
Helixi189 – 196Combined sources8
Beta strandi199 – 204Combined sources6
Turni205 – 209Combined sources5
Helixi210 – 212Combined sources3
Helixi226 – 229Combined sources4
Helixi231 – 233Combined sources3
Helixi235 – 246Combined sources12
Helixi249 – 254Combined sources6
Helixi259 – 269Combined sources11
Helixi283 – 290Combined sources8
Helixi291 – 294Combined sources4
Helixi299 – 308Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PYFX-ray1.80A1-310[»]
1PZ0X-ray2.35A1-310[»]
ProteinModelPortaliP46336.
SMRiP46336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46336.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CPC. Bacteria.
COG0667. LUCA.
HOGENOMiHOG000250284.
InParanoidiP46336.
KOiK06607.
OMAiIQVIPKI.
PhylomeDBiP46336.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.

Sequencei

Sequence statusi: Complete.

P46336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKAKLGKSD LQVFPIGLGT NAVGGHNLYP NLNEETGKEL VREAIRNGVT
60 70 80 90 100
MLDTAYIYGI GRSEELIGEV LREFNREDVV IATKAAHRKQ GNDFVFDNSP
110 120 130 140 150
DFLKKSVDES LKRLNTDYID LFYIHFPDEH TPKDEAVNAL NEMKKAGKIR
160 170 180 190 200
SIGVSNFSLE QLKEANKDGL VDVLQGEYNL LNREAEKTFF PYTKEHNISF
210 220 230 240 250
IPYFPLVSGL LAGKYTEDTT FPEGDLRNEQ EHFKGERFKE NIRKVNKLAP
260 270 280 290 300
IAEKHNVDIP HIVLAWYLAR PEIDILIPGA KRADQLIDNI KTADVTLSQE
310
DISFIDKLFA
Length:310
Mass (Da):35,168
Last modified:November 1, 1995 - v1
Checksum:iA870F226F8684867
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005554 Genomic DNA. Translation: BAA21607.1.
AL009126 Genomic DNA. Translation: CAB16014.1.
PIRiD69646.
RefSeqiNP_391857.1. NC_000964.3.
WP_003243075.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB16014; CAB16014; BSU39780.
GeneIDi937636.
KEGGibsu:BSU39780.
PATRICi18980020. VBIBacSub10457_4172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005554 Genomic DNA. Translation: BAA21607.1.
AL009126 Genomic DNA. Translation: CAB16014.1.
PIRiD69646.
RefSeqiNP_391857.1. NC_000964.3.
WP_003243075.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PYFX-ray1.80A1-310[»]
1PZ0X-ray2.35A1-310[»]
ProteinModelPortaliP46336.
SMRiP46336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021456.

Proteomic databases

PaxDbiP46336.
PRIDEiP46336.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16014; CAB16014; BSU39780.
GeneIDi937636.
KEGGibsu:BSU39780.
PATRICi18980020. VBIBacSub10457_4172.

Phylogenomic databases

eggNOGiENOG4105CPC. Bacteria.
COG0667. LUCA.
HOGENOMiHOG000250284.
InParanoidiP46336.
KOiK06607.
OMAiIQVIPKI.
PhylomeDBiP46336.

Enzyme and pathway databases

UniPathwayiUPA00076.
BioCyciBSUB:BSU39780-MONOMER.
SABIO-RKP46336.

Miscellaneous databases

EvolutionaryTraceiP46336.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIOLS_BACSU
AccessioniPrimary (citable) accession number: P46336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 126 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, Direct protein sequencing, 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.