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ECOLI:FABB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) fabB (synonyms: fabC)
Protein Name(s) 3-oxoacyl-[acyl-carrier-protein] synthase 1

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

External Links
UniProt P0A953
EMBL M24427
AJ012161
AJ012162
AJ012163
U00096
AP009048
PIR A31284
RefSeq NP_416826.1
WP_000817178.1
PDB 1DD8
1EK4
1F91
1FJ4
1FJ8
1G5X
1H4F
2AQ7
2AQB
2BUH
2BUI
2BYW
2BYX
2BYY
2BYZ
2BZ3
2BZ4
2CDH
2CF2
2VB7
2VB8
2VB9
2VBA
5KOF
PDBsum 1DD8
1EK4
1F91
1FJ4
1FJ8
1G5X
1H4F
2AQ7
2AQB
2BUH
2BUI
2BYW
2BYX
2BYY
2BYZ
2BZ3
2BZ4
2CDH
2CF2
2VB7
2VB8
2VB9
2VBA
5KOF
ProteinModelPortal P0A953
SMR P0A953
BioGrid 4260793
DIP DIP-29379N
IntAct P0A953
STRING 316385.ECDH10B_2485
BindingDB P0A953
ChEMBL CHEMBL4913
DrugBank DB08359
DB04519
DB01034
DB03600
DB03017
SwissLipids SLP:000001786
EPD P0A953
jPOST P0A953
PaxDb P0A953
PRIDE P0A953
EnsemblBacteria AAC75383
BAA16180
GeneID 946799
KEGG ecj:JW2320
eco:b2323
PATRIC fig|1411691.4.peg.4409
EchoBASE EB0270
EcoGene EG10274
eggNOG ENOG4105C0Q
COG0304
HOGENOM HOG000060165
InParanoid P0A953
KO K00647
PhylomeDB P0A953
BioCyc EcoCyc:FABB-MONOMER
MetaCyc:FABB-MONOMER
BRENDA 2.3.1.41
UniPathway UPA00094
EvolutionaryTrace P0A953
PRO PR:P0A953
Proteomes UP000000318
UP000000625
GO GO:0005829
GO:0004315
GO:0006633
GO:0008610
Gene3D 3.40.47.10
InterPro IPR018201
IPR014031
IPR014030
IPR020841
IPR016039
Pfam PF00109
PF02801
SMART SM00825
SUPFAM SSF53901
PROSITE PS00606

Annotations

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

part_of

GO:0005829

cytosol

PMID:16858726[1]

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[2]

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[2]

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[2]

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

involved_in

GO:0008610

lipid biosynthetic process

PMID:19679654[3]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:fadD
UniProtKB:Q39473

P

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

PMID:19679654[3]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:fadD
UniProtKB:Q39473

P

Seeded From UniProt

complete

involved_in

GO:0006633

fatty acid biosynthetic process

PMID:11959552[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004315

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

PMID:7002930[7]

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

enables

GO:0004315

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

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.41

F

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

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

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

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

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

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. 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
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. 3.0 3.1 Feng, Y & Cronan, JE (2009) Escherichia coli unsaturated fatty acid synthesis: complex transcription of the fabA gene and in vivo identification of the essential reaction catalyzed by FabB. J. Biol. Chem. 284 29526-35 PubMed GONUTS page
  4. Jackowski, S et al. (2002) A missense mutation in the fabB (beta-ketoacyl-acyl carrier protein synthase I) gene confers tiolactomycin resistance to Escherichia coli. Antimicrob. Agents Chemother. 46 1246-52 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  6. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  7. 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