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Q8K9Q6 (FABI_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_255
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length260 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 and in the biotin biosynthesis 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.

Cofactor biosynthesis; biotin 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 – 260260Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054897

Regions

Nucleotide binding19 – 202NAD By similarity
Nucleotide binding64 – 652NAD By similarity
Nucleotide binding192 – 1965NAD By similarity

Sites

Active site1461Proton acceptor By similarity
Active site1561Proton acceptor By similarity
Binding site131NAD; via carbonyl oxygen By similarity
Binding site401NAD By similarity
Binding site921NAD; via carbonyl oxygen By similarity
Binding site1631NAD By similarity
Site2011Involved in acyl-ACP binding By similarity
Site2041Involved in acyl-ACP binding By similarity
Site2051Involved in acyl-ACP binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9Q6 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: B97D1279FEFD3C71

FASTA26029,268
        10         20         30         40         50         60 
MGILKGKKIL ITGILNEKSI AFGIAKSMYK QEAELIFVCQ NKKIINKIKY LIKSINYNTI 

        70         80         90        100        110        120 
FFCDVSHDEN IKELFFNIKK VWNNFDGLVH SIAYCPKKQM HEDFVESSSR KSFNICHEIS 

       130        140        150        160        170        180 
SYSFLSMARE CKNMLNKFSS LVTLSYLGSQ KIVSNYNMMG LAKSSLEANV RYMANSLGKN 

       190        200        210        220        230        240 
NIRVNAISSG PIKTTSSYQI KNFNKIQKIH KLFSLTKNHV SSEEIGNVAA FLCSDLSIGI 

       250        260 
TGSIINVDHG FNLNGINSII 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67813.1.
RefSeqNP_660602.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Q6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67813; AAM67813; BUsg_255.
GeneID1005457.
KEGGbas:BUsg255.
PATRIC21247315. VBIBucAph100086_0267.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMADCDVGSD.
OrthoDBEOG6HF644.
ProtClustDBCLSK315843.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-269-MONOMER.
UniPathwayUPA00078.
UPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFPIRSF000094. Enoyl-ACP_rdct. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABI_BUCAP
AccessionPrimary (citable) accession number: Q8K9Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: January 22, 2014
This is version 80 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names