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P16657 (FABI_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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
Synonyms:envM
Ordered Locus Names:STM1700
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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.

Miscellaneous

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 262261Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054910

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 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

Experimental info

Mutagenesis931G → S: Diazaborine resistance. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16657 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 185A199EB359F643

FASTA26227,761
        10         20         30         40         50         60 
MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSSIV 

        70         80         90        100        110        120 
LPCDVAEDAS IDAMFAELGN VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKVAHDIS 

       130        140        150        160        170        180 
SYSFVAMAKA CRTMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE 

       190        200        210        220        230        240 
GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI 

       250        260 
SGEVVHVDGG FSIAAMNELE LK 

« Hide

References

« Hide 'large scale' references
[1]"envM genes of Salmonella typhimurium and Escherichia coli."
Turnowsky F., Fuchs K., Jeschek C., Hoegenauer G.
J. Bacteriol. 171:6555-6565(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-93.
Strain: AG701.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Salmonella typhimurium responses to a bactericidal protein from human neutrophils."
Qi S.Y., Li Y., Szyroki A., Giles I.G., Moir A., O'Connor C.D.
Mol. Microbiol. 17:523-531(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Strain: SL1344.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31806 Genomic DNA. Translation: AAA27059.1.
AE006468 Genomic DNA. Translation: AAL20618.1.
PIRB43729.
RefSeqNP_460659.1. NC_003197.1.

3D structure databases

ProteinModelPortalP16657.
SMRP16657. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1700.

Proteomic databases

PaxDbP16657.
PRIDEP16657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20618; AAL20618; STM1700.
GeneID1253219.
KEGGstm:STM1700.
PATRIC32381909. VBISalEnt20916_1794.

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMAKLSIAWA.
OrthoDBEOG6HF644.
PhylomeDBP16657.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1709-MONOMER.
UniPathwayUPA00078.
UPA00094.

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...

Entry information

Entry nameFABI_SALTY
AccessionPrimary (citable) accession number: P16657
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 119 of the entry and version 3 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