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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

Keywordsi

Molecular functionLyaseUniRule annotation
LigandNADCombined 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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1AX-ray2.47A/B/C/D1-361[»]
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

InterProiView protein in InterPro
IPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
IPR036291. NAD(P)-bd_dom_sf.
PfamiView protein in Pfam
PF16363. GDP_Man_Dehyd. 1 hit.
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.

Similar proteinsi

Entry informationi

Entry nameiQ9EU31_SALCE
AccessioniPrimary (citable) accession number: Q9EU31
Entry historyiIntegrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: October 25, 2017
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources