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Protein

dTDP-glucose 4,6-dehydratase

Gene

desIV

Organism
Streptomyces venezuelae
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831NAD; via carbonyl oxygenCombined sources
Binding sitei87 – 871NADCombined sources
Binding sitei151 – 1511NADCombined sources
Binding sitei155 – 1551NADCombined sources
Binding sitei181 – 1811NAD; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 123NADCombined sources
Nucleotide bindingi37 – 404NADCombined sources
Nucleotide bindingi63 – 642NADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation

Keywords - Ligandi

NADCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16952.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydrataseUniRule annotation (EC:4.2.1.46UniRule annotation)
Gene namesi
Name:desIVImported
OrganismiStreptomyces venezuelaeImported
Taxonomic identifieri54571 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R66X-ray1.44A1-337[»]
1R6DX-ray1.35A1-337[»]
ProteinModelPortaliQ9ZGH3.
SMRiQ9ZGH3. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZGH3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 306303NAD(P)-bd_domInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZGH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLVTGGAG FIGSHFVRQL LAGAYPDVPA DEVIVLDSLT YAGNRANLAP
60 70 80 90 100
VDADPRLRFV HGDIRDAGLL ARELRGVDAI VHFAAESHVD RSIAGASVFT
110 120 130 140 150
ETNVQGTQTL LQCAVDAGVG RVVHVSTDEV YGSIDSGSWT ESSPLEPNSP
160 170 180 190 200
YAASKAGSDL VARAYHRTYG LDVRITRCCN NYGPYQHPEK LIPLFVTNLL
210 220 230 240 250
DGGTLPLYGD GANVREWVHT DDHCRGIALV LAGGRAGEIY HIGGGLELTN
260 270 280 290 300
RELTGILLDS LGADWSSVRK VADRKGHDLR YSLDGGEIER ELGYRPQVSF
310 320 330
ADGLARTVRW YRENRGWWEP LKATAPQLPA TAVEVSA
Length:337
Mass (Da):36,457
Last modified:May 1, 1999 - v1
Checksum:i753443EFCE3A128C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079762 Genomic DNA. Translation: AAC68681.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079762 Genomic DNA. Translation: AAC68681.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R66X-ray1.44A1-337[»]
1R6DX-ray1.35A1-337[»]
ProteinModelPortaliQ9ZGH3.
SMRiQ9ZGH3. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16952.

Miscellaneous databases

EvolutionaryTraceiQ9ZGH3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ9ZGH3_STRVZ
AccessioniPrimary (citable) accession number: Q9ZGH3
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: April 13, 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.