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Q9HU21 (RMLC_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:rmlC
Ordered Locus Names:PA5164
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose. Ref.3

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181dTDP-4-dehydrorhamnose 3,5-epimerase
PRO_0000395350

Sites

Binding site231Substrate
Binding site281Substrate
Binding site491Substrate
Binding site591Substrate
Binding site621Substrate
Binding site711Substrate
Binding site821Substrate
Binding site1181Substrate
Binding site1681Substrate

Secondary structure

.................................... 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HU21 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F44AA1D59C1772C2

FASTA18120,766
        10         20         30         40         50         60 
MKATRLAIPD VILFEPRVFG DDRGFFFESY NQRAFEEACG HPVSFVQDNH SRSARGVLRG 

        70         80         90        100        110        120 
LHYQIRQAQG KLVRATLGEV FDVAVDLRRG SPTFGQWVGE RLSAENKRQM WIPAGFAHGF 

       130        140        150        160        170        180 
VVLSEYAEFL YKTTDFWAPE HERCIVWNDP ELKIDWPLQD APLLSEKDRQ GKAFADADCF 


P 

« Hide

References

« Hide 'large scale' references
[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]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ298594 Genomic DNA. Translation: CAC82199.1.
AE004091 Genomic DNA. Translation: AAG08549.1.
PIRE83000.
RefSeqNP_253851.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9HU21.
SMRQ9HU21. Positions 1-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5164.

Protocols and materials databases

DNASU879991.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG08549; AAG08549; PA5164.
GeneID879991.
KEGGpae:PA5164.
PATRIC19845171. VBIPseAer58763_5412.

Organism-specific databases

PseudoCAPPA5164.

Phylogenomic databases

eggNOGCOG1898.
HOGENOMHOG000227724.
KOK01790.
OMASERSIIW.
OrthoDBEOG6HTP2V.
PhylomeDBQ9HU21.

Enzyme and pathway databases

UniPathwayUPA00030.
UPA00124.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR21047. PTHR21047. 1 hit.
PfamPF00908. dTDP_sugar_isom. 1 hit.
[Graphical view]
ProDomPD001462. dTDP_sugar_isom. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR01221. rmlC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9HU21.

Entry information

Entry nameRMLC_PSEAE
AccessionPrimary (citable) accession number: Q9HU21
Secondary accession number(s): Q7AYQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways