Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P54616 (FABI_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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):
Cold shock-induced protein 15
Short name=CSI15
NADH-dependent enoyl-ACP reductase
Vegetative protein 241
Short name=VEG241
Gene names
Name:fabI
Synonyms:yjbW
Ordered Locus Names:BSU11720
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length258 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. Ref.4

Catalytic activity

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH. Ref.4

Enzyme regulation

Inhibited by triclosan and acrylamide. Ref.4 Ref.5

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer. Ref.5

Induction

By cold shock. Ref.2 Ref.4 Ref.5

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=7 µM for NADH Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054895

Regions

Nucleotide binding20 – 212NAD
Nucleotide binding67 – 682NAD
Nucleotide binding194 – 1985NAD

Sites

Active site1481Proton acceptor By similarity
Active site1581Proton acceptor
Binding site141NAD; via carbonyl oxygen
Binding site951NAD; via carbonyl oxygen
Binding site981Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1651NAD
Site2061Involved in acyl-ACP binding By similarity

Experimental info

Sequence conflict201S → Q AA sequence Ref.2

Secondary structure

.................................................. 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54616 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 097667168B3F0470

FASTA25827,874
        10         20         30         40         50         60 
MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH ELAGTLDRND 

        70         80         90        100        110        120 
SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK EELVGEYLNT NRDGFLLAHN 

       130        140        150        160        170        180 
ISSYSLTAVV KAARPMMTEG GSIVTLTYLG GELVMPNYNV MGVAKASLDA SVKYLAADLG 

       190        200        210        220        230        240 
KENIRVNSIS AGPIRTLSAK GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR 

       250 
GITGENLHVD SGFHITAR 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Cold shock stress-induced proteins in Bacillus subtilis."
Graumann P., Schroeder K., Schmid R., Marahiel M.A.
J. Bacteriol. 178:4611-4619(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21, INDUCTION.
Strain: 168 / JH642.
[3]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15.
Strain: 168 / IS58.
[4]"The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis."
Heath R.J., Su N., Murphy C.K., Rock C.O.
J. Biol. Chem. 275:40128-40133(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ENOYL-ACP REDUCTASE AND IN FATTY ACID BIOSYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[5]"Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis."
Kim K.H., Ha B.H., Kim S.J., Hong S.K., Hwang K.Y., Kim E.E.
J. Mol. Biol. 406:403-415(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB13029.2.
PIRG69845.
RefSeqNP_389054.2. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OIFX-ray2.60A/B/C/D1-258[»]
3OIGX-ray1.25A1-258[»]
ProteinModelPortalP54616.
SMRP54616. Positions 1-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP54616. 1 interaction.
MINTMINT-8366040.
STRING224308.BSU11720.

Chemistry

ChEMBLCHEMBL1075044.

Proteomic databases

PaxDbP54616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13029; CAB13029; BSU11720.
GeneID939379.
KEGGbsu:BSU11720.
PATRIC18974061. VBIBacSub10457_1224.

Organism-specific databases

GenoListBSU11720. [Micado]

Phylogenomic databases

eggNOGCOG0623.
KOK00208.
OMATGEIHHV.
OrthoDBEOG6HF644.
PhylomeDBP54616.

Enzyme and pathway databases

BioCycBSUB:BSU11720-MONOMER.
SABIO-RKP54616.
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

EvolutionaryTraceP54616.

Entry information

Entry nameFABI_BACSU
AccessionPrimary (citable) accession number: P54616
Secondary accession number(s): O31621
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 111 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList