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Reviewed, UniProtKB/Swiss-Prot Q9RPT1 (RHLG_PSEAE)

Last modified November 3, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-oxoacyl-[acyl-carrier-protein] reductase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

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
Q9RPT1-1 [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: 9721281] [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: 10984043] [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

AF148964 Genomic DNA. Translation: AAD53514.1.
AE004091 Genomic DNA. Translation: AAG06775.1.
PIRF83221.
RefSeqNP_252077.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2B4QX-ray2.30A/B1-256[»]
ModBaseSearch...

Genome annotation databases

GeneID880033.
GenomeReviewsGene locus PA3387 in contig AE004091_GR.
KEGGpae:PA3387.
NMPDRfig|208964.1.peg.3387.

Organism-specific databases

PseudoCAPPA3387.
CMRSearch...

Phylogenomic databases

HOGENOMQ9RPT1.
OMANVIAPGR.

Enzyme and pathway databases

BioCycPAER208964:PA3387-MON.
BRENDA1.1.1.100. 354.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

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: November 3, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents