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O67505 (FABI_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 96. 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:aq_1552
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 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.

Subunit structure

Homotetramer. Ref.2

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Sequence caution

The sequence AAC07465.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054894

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 site921NAD; via carbonyl oxygen By similarity
Binding site951Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1631NAD By similarity

Secondary structure

.............................................. 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67505 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 2ACD6C85EE16DC68

FASTA27029,725
        10         20         30         40         50         60 
MGLLEGKRAL ITGVANERSI AYGIAKSFHR EGAQLAFTYA TPKLEKRVRE IAKGFGSDLV 

        70         80         90        100        110        120 
VKCDVSLDED IKNLKKFLEE NWGSLDIIVH SIAYAPKEEF KGGVIDTSRE GFKIAMDISV 

       130        140        150        160        170        180 
YSLIALTREL LPLMEGRNGA IVTLSYYGAE KVVPHYNVMG IAKAALESTV RYLAYDIAKH 

       190        200        210        220        230        240 
GHRINAISAG PVKTLAAYSI TGFHLLMEHT TKVNPFGKPI TIEDVGDTAV FLCSDWARAI 

       250        260        270 
TGEVVHVDNG YHIMGVFGRE EEIKKEVYGD 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5."
Southeast collaboratory for structural genomics (SECSG)
Submitted (APR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07465.1. Different initiation.
PIRG70434.
RefSeqNP_214070.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P91X-ray2.00A/B/C/D1-270[»]
ProteinModelPortalO67505.
SMRO67505. Positions 2-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07465; AAC07465; aq_1552.
GeneID1193128.
KEGGaae:aq_1552.
PATRIC20960182. VBIAquAeo85532_1204.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAGILDMIH.
OrthoDBEOG6HF644.
ProtClustDBCLSK2299749.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1112-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Other

EvolutionaryTraceO67505.

Entry information

Entry nameFABI_AQUAE
AccessionPrimary (citable) accession number: O67505
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: January 22, 2014
This is version 96 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways