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Q9RPT1 (RHLG_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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:
Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase

EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Gene names
Name:rhlG
Ordered Locus Names:PA3387
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the synthesis of the beta-hydroxy acid moiety of rhamnolipids.

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; rhamnolipid biosynthesis.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase
PRO_0000054755

Regions

Nucleotide binding14 – 3825NADP By similarity

Sites

Active site1621Proton acceptor By similarity
Binding site1481Substrate By similarity

Secondary structure

............................................. 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9RPT1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3DB7B481F34C89A3

FASTA25626,831
        10         20         30         40         50         60 
MHPYFSLAGR IALVTGGSRG IGQMIAQGLL EAGARVFICA RDAEACADTA TRLSAYGDCQ 

        70         80         90        100        110        120 
AIPADLSSEA GARRLAQALG ELSARLDILV NNAGTSWGAA LESYPVSGWE KVMQLNVTSV 

       130        140        150        160        170        180 
FSCIQQLLPL LRRSASAENP ARVINIGSVA GISAMGEQAY AYGPSKAALH QLSRMLAKEL 

       190        200        210        220        230        240 
VGEHINVNVI APGRFPSRMT RHIANDPQAL EADSASIPMG RWGRPEEMAA LAISLAGTAG 

       250 
AYMTGNVIPI DGGFHL 

« Hide

References

« Hide 'large scale' references
[1]"The Pseudomonas aeruginosa rhlG gene encodes an NADPH-dependent beta-ketoacyl reductase which is specifically involved in rhamnolipid synthesis."
Campos-Garcia J., Caro A.D., Najera R., Miller-Maier R.M., Al-Tahhan R.A., Soberon-Chavez G.
J. Bacteriol. 180:4442-4451(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF148964 Genomic DNA. Translation: AAD53514.1.
AE004091 Genomic DNA. Translation: AAG06775.1.
PIRF83221.
RefSeqNP_252077.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B4QX-ray2.30A/B1-256[»]
ProteinModelPortalQ9RPT1.
SMRQ9RPT1. Positions 1-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA3387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG06775; AAG06775; PA3387.
GeneID880033.
KEGGpae:PA3387.
PATRIC19841377. VBIPseAer58763_3546.

Organism-specific databases

PseudoCAPPA3387.

Phylogenomic databases

eggNOGCOG1028.
OMAWGREEEM.
OrthoDBEOG6N3CR8.
PhylomeDBQ9RPT1.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15945.
UniPathwayUPA00657.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
ProtoNetSearch...

Other

EvolutionaryTraceQ9RPT1.

Entry information

Entry nameRHLG_PSEAE
AccessionPrimary (citable) accession number: Q9RPT1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 89 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