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Q89AM1 (FABI_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:bbp_246
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [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 caution

The sequence AAO26973.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054898

Regions

Nucleotide binding19 – 202NAD By similarity
Nucleotide binding64 – 652NAD By similarity
Nucleotide binding192 – 1943NAD By similarity

Sites

Active site1461Proton acceptor By similarity
Active site1561Proton acceptor By similarity
Binding site131NAD; via carbonyl oxygen By similarity
Binding site921NAD; via carbonyl oxygen By similarity
Binding site951Substrate; via amide nitrogen and 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
Q89AM1 [UniParc].

Last modified May 30, 2003. Version 1.
Checksum: 34E231597C22B560

FASTA26028,500
        10         20         30         40         50         60 
MGFLEEKKIL VTGISNKYSI AFGIAKALHK QNATLAFSYH TDRLKNKVYE LAKELGVKIV 

        70         80         90        100        110        120 
IPCDVSDDNS IKRLFFNISK KWITFDGFIH SIAFAPKNQL SGDYVSSITR LDFSNVLDVS 

       130        140        150        160        170        180 
SYSFVGMAKA CRSILKKGSS LLTLSYIGSK KVVPNYNVMG IAKASLESNV RYMASCMGLN 

       190        200        210        220        230        240 
GIRVNAISSS PIKTLSSYHI KNFKKILNHT TSRSLNNNLT TVEDVGNTAA FLCSDLSKGI 

       250        260 
TGQIIYVDGG FNITAMSNSE 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26973.1. Different initiation.
RefSeqNP_777868.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AM1.
SMRQ89AM1. Positions 2-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26973; AAO26973; bbp_246.
GeneID1058250.
KEGGbab:bbp246.
PATRIC21245273. VBIBucAph80364_0239.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAGISGEIM.
OrthoDBEOG6HF644.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-246-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_BUCBP
AccessionPrimary (citable) accession number: Q89AM1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 30, 2003
Last modified: May 14, 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