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Protein
Submitted name:

dTDP-glucose 4,6-dehydratase

Gene

rmlB

Organism
Streptococcus suis
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011NADCombined sources
Binding sitei161 – 1611NADCombined sources
Binding sitei165 – 1651NADCombined sources
Binding sitei191 – 1911NAD; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 163NADCombined sources
Nucleotide bindingi37 – 404NADCombined sources
Nucleotide bindingi62 – 632NADCombined sources
Nucleotide bindingi82 – 865NADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseImported

Keywords - Ligandi

NADCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciSSUI1007064:GHXD-725-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
dTDP-glucose 4,6-dehydrataseImported (EC:4.2.1.46Imported)
Gene namesi
Name:rmlBImported
OrganismiStreptococcus suisImported
Taxonomic identifieri1307 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Interactioni

Protein-protein interaction databases

STRINGi391295.SSU05_1298.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KERX-ray2.20A/B1-348[»]
1OC2X-ray1.50A/B1-348[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GIP9.

Family & Domainsi

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]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8GIP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQFKNIIVT GGAGFIGSNF VHYVYNNHPD VHVTVLDKLT YAGNKANLEA
60 70 80 90 100
ILGDRVELVV GDIADAELVD KLAAKADAIV HYAAESHNDN SLNDPSPFIH
110 120 130 140 150
TNFIGTYTLL EAARKYDIRF HHVSTDEVYG DLPLREDLPG HGEGPGEKFT
160 170 180 190 200
AETNYNPSSP YSSTKAASDL IVKAWVRSFG VKATISNCSN NYGPYQHIEK
210 220 230 240 250
FIPRQITNIL AGIKPKLYGE GKNVRDWIHT NDHSTGVWAI LTKGRMGETY
260 270 280 290 300
LIGADGEKNN KEVLELILEK MGQPKDAYDH VTDRAGHDLR YAIDASKLRD
310 320 330 340
ELGWTPQFTD FSQGLEETIQ WYTDNQDWWK AEKEAVEANY AKTQEVIK
Length:348
Mass (Da):38,932
Last modified:March 1, 2003 - v1
Checksum:iEEA3464D7CBCF2A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ509828 Genomic DNA. Translation: CAD49092.1.
RefSeqiWP_002937117.1. NZ_LDON01000053.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ509828 Genomic DNA. Translation: CAD49092.1.
RefSeqiWP_002937117.1. NZ_LDON01000053.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KERX-ray2.20A/B1-348[»]
1OC2X-ray1.50A/B1-348[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi391295.SSU05_1298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.

Enzyme and pathway databases

BioCyciSSUI1007064:GHXD-725-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8GIP9.

Family and domain databases

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

Publicationsi

  1. Mao Y., Xie Y., Dai J.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: P1/7Imported.
  2. "The high resolution structure of RmlC from S. suis in complex with dTDP-glucose and dTDP-xylose locates the active site of this class of enzyme."
    Dong C.J., Allen A., Blankenfeldt W., Major L.L., Maskell D., Whitfield C., Naismith J.H.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: P1/7Imported.

Entry informationi

Entry nameiQ8GIP9_STRSU
AccessioniPrimary (citable) accession number: Q8GIP9
Secondary accession number(s): F4EEB1
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 88 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.