G4WJD3 · COLC_YERPU
- ProteinGDP-L-colitose synthase
- GenecolC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in the biosynthesis of the L-colitose (3,6-dideoxyl-L-xylo-hexose) present in the O-antigen region of lipopolysaccharides (LPS) where it serves as antigenic determinant and are vital for bacterial defense and survival. Catalyzes the two-step NADP-dependent conversion of GDP-4-keto-3,6-dideoxy-D-mannose to GDP-L-colitose. ColC is a bifunctional enzyme catalyzing the C-5 epimerization of GDP-4-keto-3,6-dideoxy-D-mannose and the subsequent C-4 keto reduction of the resulting L-epimer to give GDP-L-colitose. It can use both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+.
Catalytic activity
- GDP-beta-L-colitose + NAD+ = GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NADH + H+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
75 μM | GDP-4-keto-3,6-dideoxy-D-mannose | 7.5 | 37 | with NADP | ||
139 μM | GDP-4-keto-3,6-dideoxy-D-mannose | 7.5 | 37 | with NAD |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.037 μmol/min/mg | 7.5 | 37 | toward GDP-4-keto-3,6-dideoxy-D-mannose, with NADP | ||
0.015 μmol/min/mg | 7.5 | 37 | toward GDP-4-keto-3,6-dideoxy-D-mannose, with NAD |
Pathway
Nucleotide-sugar metabolism; GDP-L-colitose biosynthesis.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7-13 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GAGGMVG | ||||||
Binding site | 101-104 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: LGSS | ||||||
Site | 103 | Important for catalytic activity | ||||
Sequence: S | ||||||
Site | 105 | Important for catalytic activity | ||||
Sequence: C | ||||||
Active site | 132 | Proton donor/acceptor | ||||
Sequence: Y | ||||||
Binding site | 136 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 160-163 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: PCNL | ||||||
Binding site | 176 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 184 | substrate | ||||
Sequence: K | ||||||
Binding site | 199 | substrate | ||||
Sequence: W | ||||||
Binding site | 206 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | GDP-L-fucose synthase activity | |
Molecular Function | isomerase activity | |
Molecular Function | NADP+ binding | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | |
Biological Process | 'de novo' GDP-L-fucose biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGDP-L-colitose synthase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Yersinia
Accessions
- Primary accessionG4WJD3
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435689 | 1-308 | GDP-L-colitose synthase | |||
Sequence: MKILLTGAGGMVGKNILAHTKSKDYEFITPSSKELDLLEKKHITTYLKHHKPNFIIHAAGIVGGIHANINNPVKFLVENMQMGINLLTAAKDNNIRKLLNLGSSCMYPKDCDSGLTEDMILTGELESTNEGYALAKITSAKLCEYINREDSEFQYKTAIPCNLYGKYDKFDENNSHMIPAVIKKIVTAIETGKSEVEIWGDGEARREFMYAEDLADFIFYTINNFTKMPQNINVGLGQDYTITEYYKVIAKILGYKGTFVYDKSKPVGMRRKLIDNTLLSEFGWSNKVDLESGISKTCQYFLNEKNND |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence similarities
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length308
- Mass (Da)34,768
- Last updated2011-12-14 v1
- ChecksumE4B53BB5F487D54E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HQ456392 EMBL· GenBank· DDBJ | AEP25495.1 EMBL· GenBank· DDBJ | Genomic DNA |