ECOLI:FADI

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	fadI (synonyms: yfcY)
Protein Name(s)	3-ketoacyl-CoA thiolase ACSs Acetyl-CoA acyltransferase Acyl-CoA ligase Beta-ketothiolase Fatty acid oxidation complex subunit beta
External Links
UniProt	P76503
EMBL	U00096 AP009048
PIR	D65007
RefSeq	NP_416844.1 YP_490584.1
ProteinModelPortal	P76503
SMR	P76503
DIP	DIP-11991N
IntAct	P76503
STRING	511145.b2342
PaxDb	P76503
PRIDE	P76503
EnsemblBacteria	AAC75402 BAA16197
GeneID	12931540 948823
KEGG	ecj:Y75_p2308 eco:b2342
PATRIC	32120057
EchoBASE	EB3880
EcoGene	EG14128
eggNOG	COG0183
HOGENOM	HOG000012240
InParanoid	P76503
KO	K00632
OMA	IDVWEDM
OrthoDB	EOG68SVWR
PhylomeDB	P76503
BioCyc	EcoCyc:G7213-MONOMER ECOL316407:JW2339-MONOMER MetaCyc:G7213-MONOMER
UniPathway	UPA00659
PRO	PR:P76503
Proteomes	UP000000318 UP000000625
Genevestigator	P76503
GO	GO:0005737 GO:0003857 GO:0003988 GO:0004300 GO:0033542
Gene3D	3.40.47.10
HAMAP	MF_01618
InterPro	IPR012806 IPR002155 IPR016039 IPR016038 IPR020615 IPR020610 IPR020617 IPR020613 IPR020616
Pfam	PF02803 PF00108
PIRSF	PIRSF000429
SUPFAM	SSF53901
TIGRFAMs	TIGR01930 TIGR02446
PROSITE	PS00098 PS00737 PS00099

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG14128 FB:FBgn0025352 PANTHER:PTN000432120 RGD:620482 RGD:620513	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG14128 PANTHER:PTN001823166	C	Seeded From UniProt	complete
enables	GO:0003988	acetyl-CoA C-acyltransferase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13097 EcoGene:EG14128 MGI:MGI:2136381 PANTHER:PTN000432120 RGD:620482 RGD:620513	F	Seeded From UniProt	complete
enables	GO:0003985	acetyl-CoA C-acetyltransferase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11672 MGI:MGI:87870 PANTHER:PTN000432120 RGD:1359366 RGD:2016 SGD:S000005949 TAIR:locus:2164778 UniProtKB:P24752 UniProtKB:Q9BWD1 UniProtKB:Q9FIK7 dictyBase:DDB_G0271544	F	Seeded From UniProt	complete
involved_in	GO:0033542	fatty acid beta-oxidation, unsaturated, even number	PMID:12535077^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12270828^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004300	enoyl-CoA hydratase activity	PMID:12270828^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003988	acetyl-CoA C-acyltransferase activity	PMID:12270828^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003857	3-hydroxyacyl-CoA dehydrogenase activity	PMID:12270828^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:12535077^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P21151	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	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:0003988	acetyl-CoA C-acyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012806	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012806	C	Seeded From UniProt	complete
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012806	P	Seeded From UniProt	complete
involved_in	GO:0016042	lipid catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012806	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:IPR002155 InterPro:IPR020610 InterPro:IPR020613 InterPro:IPR020615 InterPro:IPR020616 InterPro:IPR020617	F	Seeded From UniProt	complete
enables	GO:0003988	acetyl-CoA C-acyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.16	F	Seeded From UniProt	complete
enables	GO:0003988	acetyl-CoA C-acyltransferase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000079272	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000079272	C	Seeded From UniProt	complete
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000079272	P	Seeded From UniProt	complete
involved_in	GO:0016042	lipid catabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000079272	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
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
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
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: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
involved_in	GO:0016042	lipid catabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0442	P	Seeded From UniProt	complete
involved_in	GO:0006635	fatty acid beta-oxidation	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00659	P	Seeded From UniProt	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^2.0 ^2.1 Campbell, JW et al. (2003) A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway. Mol. Microbiol. 47 793-805 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Snell, KD et al. (2002) YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains. J. Bacteriol. 184 5696-705 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:21873635-1] 1.0 ^1.1 ^1.2 ^1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:12535077-2] 2.0 ^2.1 Campbell, JW et al. (2003) A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway. Mol. Microbiol. 47 793-805 PubMed GONUTS page

[PMID:12270828-3] 3.0 ^3.1 ^3.2 ^3.3 Snell, KD et al. (2002) YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains. J. Bacteriol. 184 5696-705 PubMed GONUTS page

[PMID:18304323-4] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[1]

[2]

[3]

[4]

ECOLI:FADI

Contents

Annotations

Notes

References

(

a

b

c

e

f

g

l

p

t

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools