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Protein

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

Gene

fabI

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei13NAD; via carbonyl oxygenBy similarity1
Binding sitei40NADBy similarity1
Binding sitei94NAD; via carbonyl oxygenBy similarity1
Binding sitei97Substrate; via amide nitrogen and carbonyl oxygenBy similarity1
Active sitei149Proton acceptorBy similarity1
Active sitei159Proton acceptorBy similarity1
Binding sitei166NADBy similarity1
Sitei204Involved in acyl-ACP bindingBy similarity1
Sitei207Involved in acyl-ACP bindingBy similarity1
Sitei208Involved in acyl-ACP bindingBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 20NADBy similarity2
Nucleotide bindingi66 – 67NADBy similarity2
Nucleotide bindingi195 – 199NADBy similarity5

GO - Molecular functioni

GO - Biological processi

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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000549041 – 265Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST265

Proteomic databases

PaxDbiQ9ZFE4.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi208964.PA1806.

Structurei

Secondary structure

1265
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 6Combined sources4
Beta strandi8 – 12Combined sources5
Beta strandi16 – 19Combined sources4
Helixi20 – 30Combined sources11
Beta strandi34 – 41Combined sources8
Helixi42 – 54Combined sources13
Helixi59 – 61Combined sources3
Beta strandi62 – 64Combined sources3
Helixi70 – 80Combined sources11
Turni81 – 83Combined sources3
Beta strandi89 – 92Combined sources4
Helixi99 – 102Combined sources4
Helixi106 – 109Combined sources4
Helixi112 – 122Combined sources11
Helixi124 – 132Combined sources9
Helixi134 – 137Combined sources4
Turni138 – 141Combined sources4
Beta strandi143 – 148Combined sources6
Helixi150 – 152Combined sources3
Turni157 – 160Combined sources4
Helixi161 – 180Combined sources20
Turni181 – 184Combined sources4
Beta strandi186 – 192Combined sources7
Helixi198 – 201Combined sources4
Helixi206 – 216Combined sources11
Helixi225 – 235Combined sources11
Helixi238 – 240Combined sources3
Beta strandi247 – 251Combined sources5
Helixi254 – 256Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9ZFE4.
SMRiQ9ZFE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CSJ. Bacteria.
COG0623. LUCA.
InParanoidiQ9ZFE4.
KOiK00208.
OMAiAGYCING.
PhylomeDBiQ9ZFE4.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PTHR24322:SF317. PTHR24322:SF317. 2 hits.
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.

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:May 1, 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.
WP_003087936.1. NZ_ASJY01000250.1.

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.
WP_003087936.1. NZ_ASJY01000250.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9ZFE4.
SMRiQ9ZFE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA1806.

Proteomic databases

PaxDbiQ9ZFE4.

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

eggNOGiENOG4105CSJ. Bacteria.
COG0623. LUCA.
InParanoidiQ9ZFE4.
KOiK00208.
OMAiAGYCING.
PhylomeDBiQ9ZFE4.

Enzyme and pathway databases

UniPathwayiUPA00094.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PTHR24322:SF317. PTHR24322:SF317. 2 hits.
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFABI_PSEAE
AccessioniPrimary (citable) accession number: Q9ZFE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 115 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

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 one 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.