Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

dTDP-4-dehydrorhamnose 3,5-epimerase

Gene

rmlC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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

Pathwayi: dTDP-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.

Pathwayi: lipopolysaccharide 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)DescriptionActionsGraphical viewLength
Binding sitei23Substrate1 Publication1
Binding sitei28Substrate1 Publication1
Binding sitei49Substrate1 Publication1
Binding sitei59Substrate1 Publication1
Binding sitei62Substrate1 Publication1
Binding sitei71Substrate1 Publication1
Binding sitei82Substrate1 Publication1
Binding sitei118Substrate1 Publication1
Binding sitei168Substrate1 Publication1

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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5164.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003953501 – 181dTDP-4-dehydrorhamnose 3,5-epimeraseAdd BLAST181

Proteomic databases

PaxDbiQ9HU21.
PRIDEiQ9HU21.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5164.

Structurei

Secondary structure

1181
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi11 – 15Combined sources5
Beta strandi18 – 21Combined sources4
Beta strandi24 – 31Combined sources8
Helixi32 – 39Combined sources8
Beta strandi47 – 54Combined sources8
Beta strandi57 – 67Combined sources11
Beta strandi71 – 86Combined sources16
Turni92 – 95Combined sources4
Beta strandi97 – 103Combined sources7
Turni104 – 106Combined sources3
Beta strandi109 – 112Combined sources4
Beta strandi116 – 122Combined sources7
Beta strandi124 – 135Combined sources12
Helixi139 – 141Combined sources3
Beta strandi142 – 145Combined sources4
Turni150 – 152Combined sources3
Helixi166 – 169Combined sources4
Helixi174 – 176Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HU21.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108URP. Bacteria.
COG1898. LUCA.
HOGENOMiHOG000227724.
InParanoidiQ9HU21.
KOiK01790.
OMAiPMEQGKL.
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. NZ_ASJY01000811.1.

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. NZ_ASJY01000811.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5164.

Proteomic databases

PaxDbiQ9HU21.
PRIDEiQ9HU21.

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

eggNOGiENOG4108URP. Bacteria.
COG1898. LUCA.
HOGENOMiHOG000227724.
InParanoidiQ9HU21.
KOiK01790.
OMAiPMEQGKL.
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...

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: November 2, 2016
This is version 97 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

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.