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P51831 (FABG_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 104. 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:
3-oxoacyl-[acyl-carrier-protein] reductase FabG

EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
Gene names
Name:fabG
Synonyms:ylpF
Ordered Locus Names:BSU15910
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis By similarity.

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2462463-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054665

Regions

Nucleotide binding11 – 144NADP By similarity
Nucleotide binding62 – 632NADP By similarity
Nucleotide binding154 – 1585NADP By similarity

Sites

Active site1541Proton acceptor By similarity
Binding site361NADP By similarity
Binding site891NADP; via carbonyl oxygen By similarity
Binding site1411Substrate By similarity
Binding site1871NADP; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Sequence conflict231D → A in AAC44307. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51831 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: C6A391167D3237DC

FASTA24626,282
        10         20         30         40         50         60 
MLNDKTAIVT GASRGIGRSI ALDLAKSGAN VVVNYSGNEA KANEVVDEIK SMGRKAIAVK 

        70         80         90        100        110        120 
ADVSNPEDVQ NMIKETLSVF STIDILVNNA GITRDNLIMR MKEDEWDDVI NINLKGVFNC 

       130        140        150        160        170        180 
TKAVTRQMMK QRSGRIINVS SIVGVSGNPG QANYVAAKAG VIGLTKSSAK ELASRNITVN 

       190        200        210        220        230        240 
AIAPGFISTD MTDKLAKDVQ DEMLKQIPLA RFGEPSDVSS VVTFLASEGA RYMTGQTLHI 


DGGMVM 

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes."
Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.
J. Bacteriol. 178:4794-4800(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"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.
[3]"A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
Foulger D., Errington J.
Microbiology 144:801-805(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172.
Strain: 168.
[4]"The effect of Srb, a homologue of the mammalian SRP receptor alpha-subunit, on Bacillus subtilis growth and protein translocation."
Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.
Gene 172:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 230-246.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59433 Genomic DNA. Translation: AAC44307.1.
AL009126 Genomic DNA. Translation: CAB13464.1.
Y13937 Genomic DNA. Translation: CAA74250.1.
D64116 Genomic DNA. Translation: BAA10974.1.
PIRA69621.
RefSeqNP_389473.1. NC_000964.3.

3D structure databases

ProteinModelPortalP51831.
SMRP51831. Positions 1-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP51831. 1 interaction.
MINTMINT-8365890.
STRING224308.BSU15910.

Proteomic databases

PaxDbP51831.
PRIDEP51831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13464; CAB13464; BSU15910.
GeneID938113.
KEGGbsu:BSU15910.
PATRIC18974987. VBIBacSub10457_1685.

Organism-specific databases

GenoListBSU15910. [Micado]

Phylogenomic databases

eggNOGCOG1028.
KOK00059.
OMATGQELHV.
OrthoDBEOG6N3CR8.
ProtClustDBCLSK887295.

Enzyme and pathway databases

BioCycBSUB:BSU15910-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsTIGR01830. 3oxo_ACP_reduc. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABG_BACSU
AccessionPrimary (citable) accession number: P51831
Secondary accession number(s): O31733
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 15, 1998
Last modified: February 19, 2014
This is version 104 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

Bacillus subtilis

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