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Protein

dTDP-glucose 4,6-dehydratase

Gene

rmlB

Organism
Salmonella choleraesuis
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.UniRule annotation

Cofactori

NAD+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80NAD; via carbonyl oxygenCombined sources1
Binding sitei99NADCombined sources1
Binding sitei131NAD; via carbonyl oxygenCombined sources1
Binding sitei167NADCombined sources1
Binding sitei171NADCombined sources1
Binding sitei197NAD; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 12NADCombined sources3
Nucleotide bindingi32 – 35NADCombined sources4
Nucleotide bindingi58 – 59NADCombined sources2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation

Keywords - Ligandi

NADCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydrataseUniRule annotation (EC:4.2.1.46UniRule annotation)
Gene namesi
Name:rmlBImported
OrganismiSalmonella choleraesuisImported
Taxonomic identifieri28901 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella

Interactioni

Protein-protein interaction databases

STRINGi220341.STY2307.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1AX-ray2.47A/B/C/D3-361[»]
ProteinModelPortaliQ9EU31.
SMRiQ9EU31.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 330NAD(P)-bd_domInterPro annotationAdd BLAST327

Sequence similaritiesi

Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9EU31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQILITGGAG FIGSAVVRHI IKNTQDTVVN IDKLTYAGNL ESLSDISESN
60 70 80 90 100
RYNFEHADIC DSAEITRIFE QYQPDAVMHL AAESHVDRSI TGPAAFIETN
110 120 130 140 150
IVGTYVLLEV ARKYWSALGE DKKNNFRFHH ISTDEVYGDL PHPDEVENSV
160 170 180 190 200
TLPLFTETTA YAPSSPYSAS KASSDHLVRA WRRTYGLPTI VTNCSNNYGP
210 220 230 240 250
YHFPEKLIPL VILNALEGKP LPIYGKGDQI RDWLYVEDHA RALHMVVTEG
260 270 280 290 300
KAGETYNIGG HNEKKNLDVV FTICDLLDEI VPKATSYREQ ITYVADRPGH
310 320 330 340 350
DRRYAIDAGK ISRELGWKPL ETFESGIRKT VEWYLANTQW VNNVKSGAYQ
360
SWIEQNYEGR Q
Length:361
Mass (Da):40,747
Last modified:March 1, 2001 - v1
Checksum:i516F6BC52387E465
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279615 Genomic DNA. Translation: AAG09498.1.
AF279616 Genomic DNA. Translation: AAG09502.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279615 Genomic DNA. Translation: AAG09498.1.
AF279616 Genomic DNA. Translation: AAG09502.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1AX-ray2.47A/B/C/D3-361[»]
ProteinModelPortaliQ9EU31.
SMRiQ9EU31.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi220341.STY2307.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ9EU31_SALCE
AccessioniPrimary (citable) accession number: Q9EU31
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.