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Protein

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

Gene

fabI

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 and in the biotin biosynthesis (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.

Pathwayi: biotin biosynthesis

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei13NAD; via carbonyl oxygenBy similarity1
Binding sitei40NADBy similarity1
Binding sitei92NAD; via carbonyl oxygenBy similarity1
Binding sitei95Substrate; via amide nitrogen and carbonyl oxygenBy similarity1
Active sitei146Proton acceptorBy similarity1
Active sitei156Proton acceptorBy similarity1
Binding sitei163NADBy similarity1
Sitei201Involved in acyl-ACP bindingBy similarity1
Sitei204Involved in acyl-ACP bindingBy similarity1
Sitei205Involved in acyl-ACP bindingBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 20NADBy similarity2
Nucleotide bindingi64 – 65NADBy similarity2
Nucleotide bindingi192 – 196NADBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, Biotin biosynthesis, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciECOO157:FABI-MONOMER.
UniPathwayiUPA00078.
UPA00094.

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:Z2512, ECs1861
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000549002 – 262Enoyl-[acyl-carrier-protein] reductase [NADH] FabIAdd BLAST261

Proteomic databases

PRIDEiP0AEK5.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

MINTiMINT-1251192.
STRINGi155864.Z2512.

Structurei

3D structure databases

ProteinModelPortaliP0AEK5.
SMRiP0AEK5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CSJ. Bacteria.
COG0623. LUCA.
KOiK00208.
OMAiSACKREG.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEK5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE
60 70 80 90 100
FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL
110 120 130 140 150
DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE
160 170 180 190 200
RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI
210 220 230 240 250
KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG
260
FSIAAMNELE LK
Length:262
Mass (Da):27,864
Last modified:January 23, 2007 - v2
Checksum:i436A89AF349D1866
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56524.1.
BA000007 Genomic DNA. Translation: BAB35284.1.
PIRiE90861.
H85757.
RefSeqiNP_309888.1. NC_002695.1.
WP_000506490.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG56524; AAG56524; Z2512.
BAB35284; BAB35284; BAB35284.
GeneIDi912787.
KEGGiece:Z2512.
ecs:ECs1861.
PATRICi18353671. VBIEscCol44059_2052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56524.1.
BA000007 Genomic DNA. Translation: BAB35284.1.
PIRiE90861.
H85757.
RefSeqiNP_309888.1. NC_002695.1.
WP_000506490.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliP0AEK5.
SMRiP0AEK5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1251192.
STRINGi155864.Z2512.

Proteomic databases

PRIDEiP0AEK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG56524; AAG56524; Z2512.
BAB35284; BAB35284; BAB35284.
GeneIDi912787.
KEGGiece:Z2512.
ecs:ECs1861.
PATRICi18353671. VBIEscCol44059_2052.

Phylogenomic databases

eggNOGiENOG4105CSJ. Bacteria.
COG0623. LUCA.
KOiK00208.
OMAiSACKREG.

Enzyme and pathway databases

UniPathwayiUPA00078.
UPA00094.
BioCyciECOO157:FABI-MONOMER.

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_ECO57
AccessioniPrimary (citable) accession number: P0AEK5
Secondary accession number(s): P29132
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The antibiotic diazaborine interferes with the activity by binding to the protein.By similarity

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.