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P51831

- FABG_BACSU

UniProt

P51831 - FABG_BACSU

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Protein

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Gene

fabG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361NADPBy similarity
Binding sitei89 – 891NADP; via carbonyl oxygenBy similarity
Binding sitei141 – 1411SubstrateBy similarity
Active sitei154 – 1541Proton acceptorBy similarity
Binding sitei187 – 1871NADP; via amide nitrogen and carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADPBy similarity
Nucleotide bindingi62 – 632NADPBy similarity
Nucleotide bindingi154 – 1585NADPBy similarity

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU15910-MONOMER.
RETL1328306-WGS:GSTH-1078-MONOMER.
RETL1328306-WGS:GSTH-2417-MONOMER.
RETL1328306-WGS:GSTH-5994-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:fabG
Synonyms:ylpF
Ordered Locus Names:BSU15910
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU15910. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2462463-oxoacyl-[acyl-carrier-protein] reductase FabGPRO_0000054665Add
BLAST

Proteomic databases

PaxDbiP51831.
PRIDEiP51831.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiP51831. 1 interaction.
MINTiMINT-8365890.
STRINGi224308.BSU15910.

Structurei

3D structure databases

ProteinModelPortaliP51831.
SMRiP51831. Positions 1-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
InParanoidiP51831.
KOiK00059.
OMAiDEFGAID.
OrthoDBiEOG6N3CR8.
PhylomeDBiP51831.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFiPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsiTIGR01830. 3oxo_ACP_reduc. 1 hit.

Sequencei

Sequence statusi: Complete.

P51831-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNDKTAIVT GASRGIGRSI ALDLAKSGAN VVVNYSGNEA KANEVVDEIK
60 70 80 90 100
SMGRKAIAVK ADVSNPEDVQ NMIKETLSVF STIDILVNNA GITRDNLIMR
110 120 130 140 150
MKEDEWDDVI NINLKGVFNC TKAVTRQMMK QRSGRIINVS SIVGVSGNPG
160 170 180 190 200
QANYVAAKAG VIGLTKSSAK ELASRNITVN AIAPGFISTD MTDKLAKDVQ
210 220 230 240
DEMLKQIPLA RFGEPSDVSS VVTFLASEGA RYMTGQTLHI DGGMVM
Length:246
Mass (Da):26,282
Last modified:December 15, 1998 - v3
Checksum:iC6A391167D3237DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231D → A in AAC44307. (PubMed:8759840)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59433 Genomic DNA. Translation: AAC44307.1.
AL009126 Genomic DNA. Translation: CAB13464.1.
Y13937 Genomic DNA. Translation: CAA74250.1.
D64116 Genomic DNA. Translation: BAA10974.1.
PIRiA69621.
RefSeqiNP_389473.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13464; CAB13464; BSU15910.
GeneIDi938113.
KEGGibsu:BSU15910.
PATRICi18974987. VBIBacSub10457_1685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59433 Genomic DNA. Translation: AAC44307.1 .
AL009126 Genomic DNA. Translation: CAB13464.1 .
Y13937 Genomic DNA. Translation: CAA74250.1 .
D64116 Genomic DNA. Translation: BAA10974.1 .
PIRi A69621.
RefSeqi NP_389473.1. NC_000964.3.

3D structure databases

ProteinModelPortali P51831.
SMRi P51831. Positions 1-246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51831. 1 interaction.
MINTi MINT-8365890.
STRINGi 224308.BSU15910.

Proteomic databases

PaxDbi P51831.
PRIDEi P51831.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13464 ; CAB13464 ; BSU15910 .
GeneIDi 938113.
KEGGi bsu:BSU15910.
PATRICi 18974987. VBIBacSub10457_1685.

Organism-specific databases

GenoListi BSU15910. [Micado ]

Phylogenomic databases

eggNOGi COG1028.
InParanoidi P51831.
KOi K00059.
OMAi DEFGAID.
OrthoDBi EOG6N3CR8.
PhylomeDBi P51831.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci BSUB:BSU15910-MONOMER.
RETL1328306-WGS:GSTH-1078-MONOMER.
RETL1328306-WGS:GSTH-2417-MONOMER.
RETL1328306-WGS:GSTH-5994-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR011284. 3oxo_ACP_reduc.
IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PIRSFi PIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsi TIGR01830. 3oxo_ACP_reduc. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFABG_BACSU
AccessioniPrimary (citable) accession number: P51831
Secondary accession number(s): O31733
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 15, 1998
Last modified: October 29, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3