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Protein

Enoyl-[acyl-carrier-protein] reductase [NADH] FabI

Gene

fabI

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131NAD; via carbonyl oxygenBy similarity
Binding sitei40 – 401NADBy similarity
Binding sitei94 – 941NAD; via carbonyl oxygenBy similarity
Binding sitei97 – 971Substrate; via amide nitrogen and carbonyl oxygenBy similarity
Active sitei149 – 1491Proton acceptorBy similarity
Active sitei159 – 1591Proton acceptorBy similarity
Binding sitei166 – 1661NADBy similarity
Sitei204 – 2041Involved in acyl-ACP bindingBy similarity
Sitei207 – 2071Involved in acyl-ACP bindingBy similarity
Sitei208 – 2081Involved in acyl-ACP bindingBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NADBy similarity
Nucleotide bindingi66 – 672NADBy similarity
Nucleotide bindingi195 – 1995NADBy similarity

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB
  2. enoyl-[acyl-carrier-protein] reductase activity Source: PseudoCAP

GO - Biological processi

  1. fatty acid elongation Source: UniProtKB
  2. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
Short name:
ENR
Alternative name(s):
NADH-dependent enoyl-ACP reductase
Gene namesi
Name:fabI
Ordered Locus Names:PA1806
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 265265Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054904Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi208964.PA1806.

Structurei

Secondary structure

1
265
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Beta strandi8 – 125Combined sources
Beta strandi16 – 194Combined sources
Helixi20 – 3011Combined sources
Beta strandi34 – 418Combined sources
Helixi42 – 5413Combined sources
Helixi59 – 613Combined sources
Beta strandi62 – 643Combined sources
Helixi70 – 8011Combined sources
Turni81 – 833Combined sources
Beta strandi89 – 924Combined sources
Helixi99 – 1024Combined sources
Helixi106 – 1094Combined sources
Helixi112 – 12211Combined sources
Helixi124 – 1329Combined sources
Helixi134 – 1374Combined sources
Turni138 – 1414Combined sources
Beta strandi143 – 1486Combined sources
Helixi150 – 1523Combined sources
Turni157 – 1604Combined sources
Helixi161 – 18020Combined sources
Turni181 – 1844Combined sources
Beta strandi186 – 1927Combined sources
Helixi198 – 2014Combined sources
Helixi206 – 21611Combined sources
Helixi225 – 23511Combined sources
Helixi238 – 2403Combined sources
Beta strandi247 – 2515Combined sources
Helixi254 – 2563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NQZX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-265[»]
4NR0X-ray1.80A/B/C/D1-265[»]
SMRiQ9ZFE4. Positions 2-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623.
InParanoidiQ9ZFE4.
KOiK00208.
OMAiGILDMIH.
OrthoDBiEOG6HF644.
PhylomeDBiQ9ZFE4.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Q9ZFE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFLTGKRAL IVGVASKLSI ASGIAAAMHR EGAELAFTYQ NDKLRGRVEE
60 70 80 90 100
FASGWGSRPE LCFPCDVADD SQIEAVFAAL GKHWDGLDII VHSVGFAPGD
110 120 130 140 150
QLDGDFTAVT TREGFRIAHD ISAYSFIALA KAGREMMKGR NGSLLTLSYL
160 170 180 190 200
GAERTMPNYN VMGMAKASLE AGVRYLAGSL GAEGTRVNAV SAGPIRTLAA
210 220 230 240 250
SGIKSFRKML AANERQTPLR RNVTIEEVGN AGAFLCSDLA SGISGEILYV
260
DGGFNTTAMG PLDDD
Length:265
Mass (Da):28,006
Last modified:April 30, 1999 - v1
Checksum:i3E7A946886DFB293
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104262 Genomic DNA. Translation: AAC95362.1.
AE004091 Genomic DNA. Translation: AAG05195.1.
PIRiC83419.
RefSeqiNP_250497.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG05195; AAG05195; PA1806.
GeneIDi878311.
KEGGipae:PA1806.
PATRICi19837991. VBIPseAer58763_1876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104262 Genomic DNA. Translation: AAC95362.1.
AE004091 Genomic DNA. Translation: AAG05195.1.
PIRiC83419.
RefSeqiNP_250497.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NQZX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-265[»]
4NR0X-ray1.80A/B/C/D1-265[»]
SMRiQ9ZFE4. Positions 2-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA1806.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG05195; AAG05195; PA1806.
GeneIDi878311.
KEGGipae:PA1806.
PATRICi19837991. VBIPseAer58763_1876.

Organism-specific databases

PseudoCAPiPA1806.

Phylogenomic databases

eggNOGiCOG0623.
InParanoidiQ9ZFE4.
KOiK00208.
OMAiGILDMIH.
OrthoDBiEOG6HF644.
PhylomeDBiQ9ZFE4.

Enzyme and pathway databases

UniPathwayiUPA00094.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiFABI_PSEAE
AccessioniPrimary (citable) accession number: Q9ZFE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: April 30, 1999
Last modified: March 31, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.