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Protein

dTDP-4-dehydrorhamnose 3,5-epimerase

Gene

rmlC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.1 Publication

Catalytic activityi

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose.1 Publication

Pathway:idTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

Pathway:ilipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei23 – 231Substrate1 Publication
Binding sitei28 – 281Substrate1 Publication
Binding sitei49 – 491Substrate1 Publication
Binding sitei59 – 591Substrate1 Publication
Binding sitei62 – 621Substrate1 Publication
Binding sitei71 – 711Substrate1 Publication
Binding sitei82 – 821Substrate1 Publication
Binding sitei118 – 1181Substrate1 Publication
Binding sitei168 – 1681Substrate1 Publication

GO - Molecular functioni

  • dTDP-4-dehydrorhamnose 3,5-epimerase activity Source: UniProtKB

GO - Biological processi

  • dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  • extracellular polysaccharide biosynthetic process Source: UniProtKB
  • lipopolysaccharide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00124.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-4-dehydrorhamnose 3,5-epimerase (EC:5.1.3.13)
Alternative name(s):
Thymidine diphospho-4-keto-rhamnose 3,5-epimerase
dTDP-4-keto-6-deoxyglucose 3,5-epimerase
dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase
dTDP-L-rhamnose synthase
Gene namesi
Name:rmlC
Ordered Locus Names:PA5164
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5164.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181dTDP-4-dehydrorhamnose 3,5-epimerasePRO_0000395350Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5164.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi11 – 155Combined sources
Beta strandi18 – 214Combined sources
Beta strandi24 – 318Combined sources
Helixi32 – 398Combined sources
Beta strandi47 – 548Combined sources
Beta strandi57 – 6711Combined sources
Beta strandi71 – 8616Combined sources
Turni92 – 954Combined sources
Beta strandi97 – 1037Combined sources
Turni104 – 1063Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi116 – 1227Combined sources
Beta strandi124 – 13512Combined sources
Helixi139 – 1413Combined sources
Beta strandi142 – 1454Combined sources
Turni150 – 1523Combined sources
Helixi166 – 1694Combined sources
Helixi174 – 1763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RTVX-ray2.50A1-181[»]
2IXHX-ray2.00A/B1-181[»]
2IXIX-ray1.80A/B1-181[»]
2IXJX-ray2.54A1-181[»]
2IXKX-ray1.70A/B1-181[»]
ProteinModelPortaliQ9HU21.
SMRiQ9HU21. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HU21.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1898.
HOGENOMiHOG000227724.
InParanoidiQ9HU21.
KOiK01790.
OMAiRSILWND.
OrthoDBiEOG6HTP2V.
PhylomeDBiQ9HU21.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR21047. PTHR21047. 1 hit.
PfamiPF00908. dTDP_sugar_isom. 1 hit.
[Graphical view]
ProDomiPD001462. dTDP_sugar_isom. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01221. rmlC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HU21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKATRLAIPD VILFEPRVFG DDRGFFFESY NQRAFEEACG HPVSFVQDNH
60 70 80 90 100
SRSARGVLRG LHYQIRQAQG KLVRATLGEV FDVAVDLRRG SPTFGQWVGE
110 120 130 140 150
RLSAENKRQM WIPAGFAHGF VVLSEYAEFL YKTTDFWAPE HERCIVWNDP
160 170 180
ELKIDWPLQD APLLSEKDRQ GKAFADADCF P
Length:181
Mass (Da):20,766
Last modified:March 1, 2001 - v1
Checksum:iF44AA1D59C1772C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298594 Genomic DNA. Translation: CAC82199.1.
AE004091 Genomic DNA. Translation: AAG08549.1.
PIRiE83000.
RefSeqiNP_253851.1. NC_002516.2.
WP_003096184.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG08549; AAG08549; PA5164.
GeneIDi879991.
KEGGipae:PA5164.
PATRICi19845171. VBIPseAer58763_5412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298594 Genomic DNA. Translation: CAC82199.1.
AE004091 Genomic DNA. Translation: AAG08549.1.
PIRiE83000.
RefSeqiNP_253851.1. NC_002516.2.
WP_003096184.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RTVX-ray2.50A1-181[»]
2IXHX-ray2.00A/B1-181[»]
2IXIX-ray1.80A/B1-181[»]
2IXJX-ray2.54A1-181[»]
2IXKX-ray1.70A/B1-181[»]
ProteinModelPortaliQ9HU21.
SMRiQ9HU21. Positions 1-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5164.

Protocols and materials databases

DNASUi879991.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08549; AAG08549; PA5164.
GeneIDi879991.
KEGGipae:PA5164.
PATRICi19845171. VBIPseAer58763_5412.

Organism-specific databases

PseudoCAPiPA5164.

Phylogenomic databases

eggNOGiCOG1898.
HOGENOMiHOG000227724.
InParanoidiQ9HU21.
KOiK01790.
OMAiRSILWND.
OrthoDBiEOG6HTP2V.
PhylomeDBiQ9HU21.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00124.

Miscellaneous databases

EvolutionaryTraceiQ9HU21.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR21047. PTHR21047. 1 hit.
PfamiPF00908. dTDP_sugar_isom. 1 hit.
[Graphical view]
ProDomiPD001462. dTDP_sugar_isom. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR01221. rmlC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the rmlC gene of Pseudomonas aeruginosa."
    Maeki M.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. "RmlC, a C3' and C5' carbohydrate epimerase, appears to operate via an intermediate with an unusual twist boat conformation."
    Dong C., Major L.L., Srikannathasan V., Errey J.C., Giraud M.F., Lam J.S., Graninger M., Messner P., McNeil M.R., Field R.A., Whitfield C., Naismith J.H.
    J. Mol. Biol. 365:146-159(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry nameiRMLC_PSEAE
AccessioniPrimary (citable) accession number: Q9HU21
Secondary accession number(s): Q7AYQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.