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Q9ZFE4 (FABI_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Short name=ENR
EC=1.3.1.9
Alternative name(s):
NADH-dependent enoyl-ACP reductase
Gene names
Name:fabI
Ordered Locus Names:PA1806
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity.

Catalytic activity

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 265265Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054904

Regions

Nucleotide binding19 – 202NAD By similarity
Nucleotide binding66 – 672NAD By similarity
Nucleotide binding195 – 1995NAD By similarity

Sites

Active site1491Proton acceptor By similarity
Active site1591Proton acceptor By similarity
Binding site131NAD; via carbonyl oxygen By similarity
Binding site401NAD By similarity
Binding site941NAD; via carbonyl oxygen By similarity
Binding site971Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1661NAD By similarity
Site2041Involved in acyl-ACP binding By similarity
Site2071Involved in acyl-ACP binding By similarity
Site2081Involved in acyl-ACP binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZFE4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 3E7A946886DFB293

FASTA26528,006
        10         20         30         40         50         60 
MGFLTGKRAL IVGVASKLSI ASGIAAAMHR EGAELAFTYQ NDKLRGRVEE FASGWGSRPE 

        70         80         90        100        110        120 
LCFPCDVADD SQIEAVFAAL GKHWDGLDII VHSVGFAPGD QLDGDFTAVT TREGFRIAHD 

       130        140        150        160        170        180 
ISAYSFIALA KAGREMMKGR NGSLLTLSYL GAERTMPNYN VMGMAKASLE AGVRYLAGSL 

       190        200        210        220        230        240 
GAEGTRVNAV SAGPIRTLAA SGIKSFRKML AANERQTPLR RNVTIEEVGN AGAFLCSDLA 

       250        260 
SGISGEILYV DGGFNTTAMG PLDDD 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis."
Hoang T.T., Schweizer H.P.
J. Bacteriol. 181:5489-5497(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
AF104262 Genomic DNA. Translation: AAC95362.1.
AE004091 Genomic DNA. Translation: AAG05195.1.
PIRC83419.
RefSeqNP_250497.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9ZFE4.
SMRQ9ZFE4. Positions 2-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA1806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID878311.
KEGGpae:PA1806.
PATRIC19837991. VBIPseAer58763_1876.

Organism-specific databases

PseudoCAPPA1806.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAWGKLDFI.
OrthoDBEOG6HF644.
ProtClustDBCLSK866795.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Entry information

Entry nameFABI_PSEAE
AccessionPrimary (citable) accession number: Q9ZFE4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 98 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

PATHWAY comments

Index of metabolic and biosynthesis pathways