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Reviewed, UniProtKB/Swiss-Prot Q9ZFE4 (FABI_PSEAE)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
Alternative name(s):
    NADH-dependent enoyl-ACP reductase
Gene names
Name: fabI
Ordered Locus Names: PA1806
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length265 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Cell inner membrane; Peripheral membrane protein By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

enoyl-[acyl-carrier-protein] reductase (NADH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Nucleotide binding10 – 3627NAD By similarity

Sites

Active site1591Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZFE4-1 [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: 10464225] [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.

Cross-references

Sequence databases

AF104262 Genomic DNA. Translation: AAC95362.1.
AE004091 Genomic DNA. Translation: AAG05195.1.
PIRC83419.
RefSeqNP_250497.1.

3D structure databases

HSSPHSSP built from PDB template 1C14 based on UniProtKB P29132.
SMRQ9ZFE4. Positions 2-263.
ModBaseSearch...

Genome annotation databases

GeneID878311.
GenomeReviewsGene locus PA1806 in contig AE004091_GR.
KEGGpae:PA1806.
NMPDRfig|208964.1.peg.1807.

Organism-specific databases

PseudoCAPPA1806.
CMRSearch...

Phylogenomic databases

HOGENOMQ9ZFE4.
OMAQ9ZFE4. LVHCLAF.

Enzyme and pathway databases

BioCycPAER208964:PA1806-MON.
BRENDA1.3.1.9. 354.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR014358. Enoyl-ACP_Rdtase_NADH.
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.
PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
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: June 16, 2009
This is version 62 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

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