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Q81GI3 (FABI_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 83. 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:BC_1216
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length256 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000407976

Regions

Nucleotide binding19 – 202NAD
Nucleotide binding66 – 672NAD
Nucleotide binding193 – 1975NAD

Sites

Active site1471Proton acceptor By similarity
Active site1571Proton acceptor
Binding site131NAD; via carbonyl oxygen
Binding site941NAD; via carbonyl oxygen
Binding site971Substrate; via amide nitrogen and carbonyl oxygen
Binding site1641NAD
Site2051Involved in acyl-ACP binding By similarity

Secondary structure

................................................ 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q81GI3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 66780350F497CA31

FASTA25627,740
        10         20         30         40         50         60 
MELLQGKTFV VMGVANQRSI AWGIARSLHN AGAKLIFTYA GERLERNVRE LADTLEGQES 

        70         80         90        100        110        120 
LVLPCDVTND EELTACFETI KQEVGTIHGV AHCIAFANRD DLKGEFVDTS RDGFLLAQNI 

       130        140        150        160        170        180 
SAFSLTAVAR EAKKVMTEGG NILTLTYLGG ERVVKNYNVM GVAKASLEAS VKYLANDLGQ 

       190        200        210        220        230        240 
HGIRVNAISA GPIRTLSAKG VGDFNSILRE IEERAPLRRT TTQEEVGDTA VFLFSDLARG 

       250 
VTGENIHVDS GYHILG 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.
[2]"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus."
Kim S.J., Ha B.H., Kim K.H., Hong S.K., Shin K.J., Suh S.W., Kim E.E.
Biochem. Biophys. Res. Commun. 400:517-522(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08201.1.
RefSeqNP_831000.1. NC_004722.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OJEX-ray3.02A1-256[»]
3OJFX-ray2.20A/B/C/D1-256[»]
ProteinModelPortalQ81GI3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC1216.

Proteomic databases

PRIDEQ81GI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP08201; AAP08201; BC_1216.
GeneID1203565.
KEGGbce:BC1216.
PATRIC32598149. VBIBacCer54481_1186.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAGILDMIH.
OrthoDBEOG6HF644.
ProtClustDBPRK08594.

Enzyme and pathway databases

BioCycBCER226900:GJEU-1216-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

EvolutionaryTraceQ81GI3.

Entry information

Entry nameFABI_BACCR
AccessionPrimary (citable) accession number: Q81GI3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 1, 2003
Last modified: January 22, 2014
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways