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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531
Active sitei58 – 581Proton donor
Active sitei84 – 841

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 21411NADPAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Protein IolSPRO_0000070382Add
BLAST

Proteomic databases

PaxDbiP46336.

Expressioni

Inductioni

Inositol.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021456.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni26 – 283Combined sources
Beta strandi29 – 313Combined sources
Helixi34 – 4613Combined sources
Beta strandi51 – 533Combined sources
Turni56 – 616Combined sources
Helixi62 – 7110Combined sources
Helixi76 – 783Combined sources
Beta strandi80 – 856Combined sources
Beta strandi87 – 904Combined sources
Beta strandi93 – 964Combined sources
Helixi100 – 11415Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi129 – 1313Combined sources
Helixi133 – 14513Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi152 – 1565Combined sources
Helixi159 – 1657Combined sources
Turni166 – 1683Combined sources
Beta strandi173 – 1775Combined sources
Helixi184 – 1863Combined sources
Helixi189 – 1968Combined sources
Beta strandi199 – 2046Combined sources
Turni205 – 2095Combined sources
Helixi210 – 2123Combined sources
Helixi226 – 2294Combined sources
Helixi231 – 2333Combined sources
Helixi235 – 24612Combined sources
Helixi249 – 2546Combined sources
Helixi259 – 26911Combined sources
Helixi283 – 2908Combined sources
Helixi291 – 2944Combined sources
Helixi299 – 30810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PYFX-ray1.80A1-310[»]
1PZ0X-ray2.35A1-310[»]
ProteinModelPortaliP46336.
SMRiP46336. Positions 2-310.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1PYFX-ray1.80A1-310[»]
1PZ0X-ray2.35A1-310[»]
ProteinModelPortaliP46336.
SMRiP46336. Positions 2-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021456.

Proteomic databases

PaxDbiP46336.

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: September 7, 2016
This is version 124 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.