Q9RPT1 (RHLG_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 256

256

Rhamnolipids biosynthesis 3-oxoacyl-[acyl-carrier-protein] reductase

PRO_0000054755

Regions

Nucleotide binding

14 – 38

25

NADP By similarity

Sites

Active site

162

1

Proton acceptor By similarity

Binding site

148

1

Substrate By similarity

Secondary structure

1

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256

Helix Strand Turn

Details...

Turn

3 – 5

3

Beta strand

11 – 15

5

Turn

16 – 18

3

Helix

20 – 31

12

Beta strand

35 – 39

5

Helix

43 – 53

11

Beta strand

59 – 61

3

Helix

69 – 82

14

Beta strand

87 – 91

5

Helix

107 – 116

10

Helix

118 – 134

17

Beta strand

137 – 139

3

Beta strand

141 – 146

6

Helix

149 – 151

3

Helix

162 – 180

19

Helix

181 – 183

3

Beta strand

185 – 192

8

Turn

198 – 200

3

Helix

201 – 205

5

Helix

207 – 215

9

Helix

225 – 236

12

Helix

238 – 240

3

Beta strand

247 – 251

5

Turn

252 – 255

4

Sequences

	Sequence		Length	Mass (Da)
	Q9RPT1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3DB7B481F34C89A3	FASTA	256	26,831
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

F83221.

RefSeq

NP_252077.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B4Q	X-ray	2.30	A/B	1-256	[»]

ProteinModelPortal

Q9RPT1.

SMR

Q9RPT1. Positions 1-256.

ModBase

Search...

Protein-protein interaction databases

STRING

208964.PA3387.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

880033.

KEGG

pae:PA3387.

PATRIC

19841377. VBIPseAer58763_3546.

Organism-specific databases

PseudoCAP

PA3387.

Phylogenomic databases

eggNOG

COG1028.

OMA

GEHINVN.

ProtClustDB

CLSK787429.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15945.

UniPathway

UPA00657.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

PROSITE

PS00061. ADH_SHORT. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9RPT1.

Entry information

Entry name

RHLG_PSEAE

Accession

Primary (citable) accession number: Q9RPT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program