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ECOLI:FABF

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fabF (synonyms: fabJ)
Protein Name(s) 3-oxoacyl-[acyl-carrier-protein] synthase 2

3-oxoacyl-[acyl-carrier-protein] synthase II Beta-ketoacyl-ACP synthase II KAS II

External Links
UniProt P0AAI5
EMBL Z34979
U20767
U00096
AP009048
PIR I41060
RefSeq NP_415613.1
YP_489363.1
PDB 1B3N
1KAS
2GFV
2GFW
2GFX
2GFY
3G0Y
3G11
3HNZ
3HO2
3HO9
3I8P
PDBsum 1B3N
1KAS
2GFV
2GFW
2GFX
2GFY
3G0Y
3G11
3HNZ
3HO2
3HO9
3I8P
ProteinModelPortal P0AAI5
SMR P0AAI5
DIP DIP-29377N
IntAct P0AAI5
MINT MINT-1231688
STRING 511145.b1095
DrugBank DB01034
PaxDb P0AAI5
PRIDE P0AAI5
EnsemblBacteria AAC74179
BAA35903
GeneID 12931078
946665
KEGG ecj:Y75_p1065
eco:b1095
PATRIC 32117431
EchoBASE EB2490
EcoGene EG12606
eggNOG COG0304
HOGENOM HOG000060165
InParanoid P0AAI5
KO K09458
OMA MGPNYTT
OrthoDB EOG6DG2SR
PhylomeDB P0AAI5
BioCyc EcoCyc:3-OXOACYL-ACP-SYNTHII-MONOMER
ECOL316407:JW1081-MONOMER
MetaCyc:3-OXOACYL-ACP-SYNTHII-MONOMER
BRENDA 2.3.1.179
SABIO-RK P0AAI5
UniPathway UPA00094
EvolutionaryTrace P0AAI5
PRO PR:P0AAI5
Proteomes UP000000318
UP000000625
Genevestigator P0AAI5
GO GO:0005829
GO:0004315
GO:0033817
GO:0006633
Gene3D 3.40.47.10
InterPro IPR017568
IPR018201
IPR014031
IPR014030
IPR016039
IPR016038
Pfam PF00109
PF02801
PIRSF PIRSF000447
SUPFAM SSF53901
TIGRFAMs TIGR03150
PROSITE PS00606

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0033817

beta-ketoacyl-acyl-carrier-protein synthase II activity

PMID:3549687[1]

ECO:0000314

F

Figures 1, 2, and 3 show that the fabF mutant (fabF1) activity is decreased by expressing F-ACP. The decrease in activity can be seen by the banding pattern seen after running samples through gel electrophoresis. Wild type fabF cells show increased activity by expressing ACP, and the mutants show a lack of activity by expressing F-ACP.

complete
CACAO 7631

enables

GO:0033817

beta-ketoacyl-acyl-carrier-protein synthase II activity

PMID:3549687[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10274
PANTHER:PTN000918584
TAIR:locus:2027252
UniProtKB:P9WQD7
UniProtKB:P9WQD9
UniProtKB:Q9I3B2
UniProtKB:Q9NWU1

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10274
EcoGene:EG12606
PANTHER:PTN000196483
UniProtKB:P9WQD9

C

Seeded From UniProt

complete

enables

GO:0004315

3-oxoacyl-[acyl-carrier-protein] synthase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10274
EcoGene:EG12606
PANTHER:PTN000918584
TAIR:locus:2027252
UniProtKB:P9WQD7
UniProtKB:P9WQD9
UniProtKB:Q9NWU1

F

Seeded From UniProt

complete

enables

GO:0033817

beta-ketoacyl-acyl-carrier-protein synthase II activity

PMID:7002930[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004315

3-oxoacyl-[acyl-carrier-protein] synthase activity

PMID:237914[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016039

F

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017568

P

Seeded From UniProt

complete

enables

GO:0016747

transferase activity, transferring acyl groups other than amino-acyl groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017568

F

Seeded From UniProt

complete

enables

GO:0033817

beta-ketoacyl-acyl-carrier-protein synthase II activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.179

F

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0275
UniPathway:UPA00094

P

Seeded From UniProt

complete

involved_in

GO:0006631

fatty acid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0276

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Jackowski, S & Rock, CO (1987) Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. J. Bacteriol. 169 1469-73 PubMed GONUTS page
  2. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Garwin, JL et al. (1980) Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. J. Biol. Chem. 255 11949-56 PubMed GONUTS page
  5. D'Agnolo, G et al. (1975) Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J. Biol. Chem. 250 5289-94 PubMed GONUTS page