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Protein

Putative fructokinase

Gene

gmuE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Seems to be involved in the degradation of glucomannan.1 Publication

Catalytic activityi

ATP + D-fructose = ADP + D-fructose 6-phosphate.

Cofactori

Mg2+Curated

Enzyme regulationi

Inhibited by zinc ions.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301ATP
Metal bindingi153 – 1531Zinc
Metal bindingi168 – 1681Zinc
Metal bindingi171 – 1711Zinc
Metal bindingi174 – 1741Zinc
Binding sitei182 – 1821ATP; via imide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi230 – 2345ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU05860-MONOMER.
BRENDAi2.7.1.4. 658.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative fructokinase (EC:2.7.1.4)
Alternative name(s):
Glucomannan utilization protein E
Gene namesi
Name:gmuE
Synonyms:ydhR
Ordered Locus Names:BSU05860
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Putative fructokinasePRO_0000095681Add
BLAST

Proteomic databases

PaxDbiO05510.

Expressioni

Inductioni

Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by GmuR.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003283.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi9 – 179Combined sources
Beta strandi23 – 308Combined sources
Helixi34 – 4512Combined sources
Beta strandi51 – 577Combined sources
Beta strandi59 – 613Combined sources
Turni68 – 714Combined sources
Turni79 – 813Combined sources
Helixi86 – 949Combined sources
Beta strandi98 – 1025Combined sources
Helixi103 – 11412Combined sources
Turni116 – 1194Combined sources
Beta strandi123 – 13816Combined sources
Beta strandi145 – 1473Combined sources
Helixi151 – 1533Combined sources
Turni169 – 1713Combined sources
Beta strandi172 – 1743Combined sources
Helixi175 – 1795Combined sources
Helixi181 – 1888Combined sources
Helixi192 – 1954Combined sources
Helixi199 – 21921Combined sources
Beta strandi225 – 2306Combined sources
Helixi231 – 2333Combined sources
Helixi236 – 24914Combined sources
Helixi256 – 2583Combined sources
Turni259 – 2613Combined sources
Helixi262 – 2643Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 29218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XC3X-ray2.10A1-299[»]
3LM9X-ray2.45A1-299[»]
3OHRX-ray1.66A1-299[»]
ProteinModelPortaliO05510.
SMRiO05510. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO05510.

Family & Domainsi

Sequence similaritiesi

Belongs to the ROK (NagC/XylR) family.Curated

Phylogenomic databases

eggNOGiENOG4105EVU. Bacteria.
COG1940. LUCA.
HOGENOMiHOG000150085.
InParanoidiO05510.
KOiK00847.
OMAiRHPEDTY.
PhylomeDBiO05510.

Family and domain databases

InterProiIPR000600. ROK.
[Graphical view]
PfamiPF00480. ROK. 1 hit.
[Graphical view]
PROSITEiPS01125. ROK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O05510-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGGIEAGGT KFVCAVGRED GTIIDRIEFP TKMPDETIEK VIQYFSQFSL
60 70 80 90 100
QAIGIGSFGP VDNDKTSQTY GTITATPKAG WRHYPFLQTV KNEMKIPVGF
110 120 130 140 150
STDVNAAALG EFLFGEAKGL DSCLYITIGT GIGAGAIVEG RLLQGLSHPE
160 170 180 190 200
MGHIYIRRHP DDVYQGKCPY HGDCFEGLAS GPAIEARWGK KAADLSDIAQ
210 220 230 240 250
VWELEGYYIA QALAQYILIL APKKIILGGG VMQQKQVFSY IYQYVPKIMN
260 270 280 290
SYLDFSELSD DISDYIVPPR LGSNAGIIGT LVLAHQALQA EAASGEVRS
Length:299
Mass (Da):32,440
Last modified:July 1, 1997 - v1
Checksum:iE384CECFDDF056BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19710.1.
AL009126 Genomic DNA. Translation: CAB12405.1.
PIRiF69785.
RefSeqiNP_388467.1. NC_000964.3.
WP_003234095.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12405; CAB12405; BSU05860.
GeneIDi938016.
KEGGibsu:BSU05860.
PATRICi18972788. VBIBacSub10457_0615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19710.1.
AL009126 Genomic DNA. Translation: CAB12405.1.
PIRiF69785.
RefSeqiNP_388467.1. NC_000964.3.
WP_003234095.1. NZ_JNCM01000031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XC3X-ray2.10A1-299[»]
3LM9X-ray2.45A1-299[»]
3OHRX-ray1.66A1-299[»]
ProteinModelPortaliO05510.
SMRiO05510. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003283.

Proteomic databases

PaxDbiO05510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12405; CAB12405; BSU05860.
GeneIDi938016.
KEGGibsu:BSU05860.
PATRICi18972788. VBIBacSub10457_0615.

Phylogenomic databases

eggNOGiENOG4105EVU. Bacteria.
COG1940. LUCA.
HOGENOMiHOG000150085.
InParanoidiO05510.
KOiK00847.
OMAiRHPEDTY.
PhylomeDBiO05510.

Enzyme and pathway databases

BioCyciBSUB:BSU05860-MONOMER.
BRENDAi2.7.1.4. 658.

Miscellaneous databases

EvolutionaryTraceiO05510.

Family and domain databases

InterProiIPR000600. ROK.
[Graphical view]
PfamiPF00480. ROK. 1 hit.
[Graphical view]
PROSITEiPS01125. ROK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSCRK_BACSU
AccessioniPrimary (citable) accession number: O05510
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: September 7, 2016
This is version 109 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, Reference proteome

Documents

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