Skip Header

Contribute Send feedback
Read comments (?) or add your own

O54438 (FABG_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] reductase FabG
EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
Gene names
Name:fabG
Ordered Locus Names:PA2967
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis By similarity.

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2472473-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054678

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding62 – 632NADP By similarity
Nucleotide binding154 – 1585NADP By similarity

Sites

Active site1541Proton acceptor By similarity
Binding site371NADP By similarity
Binding site891NADP; via carbonyl oxygen By similarity
Binding site1411Substrate By similarity
Binding site1871NADP; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

1 .......................................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O54438 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AB83A2B95027445B

FASTA24725,585
        10         20         30         40         50         60 
MSLQGKVALV TGASRGIGQA IALELGRLGA VVIGTATSAS GAEKIAETLK ANGVEGAGLV 

        70         80         90        100        110        120 
LDVSSDESVA ATLEHIQQHL GQPLIVVNNA GITRDNLLVR MKDDEWFDVV NTNLNSLYRL 

       130        140        150        160        170        180 
SKAVLRGMTK ARWGRIINIG SVVGAMGNAG QTNYAAAKAG LEGFTRALAR EVGSRAITVN 

       190        200        210        220        230        240 
AVAPGFIDTD MTRELPEAQR EALLGQIPLG RLGQAEEIAK VVGFLASDGA AYVTGATVPV 


NGGMYMS

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme A:ACP transacylase (fabD)."
Kutchma A.J., Hoang T.T., Schweizer H.P.
J. Bacteriol. 181:5498-5504(1999) [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U91631 Genomic DNA. Translation: AAB94395.1.
AE004091 Genomic DNA. Translation: AAG06355.1.
PIRT12020.
RefSeqNP_251657.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AFNX-ray2.30A/B/C/D1-247[»]
4AG3X-ray1.80A/B/C/D1-247[»]
ProteinModelPortalO54438.
SMRO54438. Positions 1-246.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA2967.

Protocols and materials databases

DNASU880433.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880433.
KEGGpae:PA2967.
PATRIC19840487. VBIPseAer58763_3113.

Organism-specific databases

PseudoCAPPA2967.

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMAQSNYCAA.
ProtClustDBPRK05653.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_PSEAE
AccessionPrimary (citable) accession number: O54438
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents