ECOLI:ACCA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	accA (ECO:0000255 with HAMAP-Rule:MF_00823)
Protein Name(s)	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (ECO:0000255 with HAMAP-Rule:MF_00823) ACCase subunit alpha (ECO:0000255 with HAMAP-Rule:MF_00823) Acetyl-CoA carboxylase carboxyltransferase subunit alpha (ECO:0000255 with HAMAP-Rule:MF_00823)
External Links
UniProt	P0ABD5
EMBL	M96394 D49445 U70214 U00096 AP009048 D87518 M19334
PIR	A43452
RefSeq	NP_414727.1 YP_488487.1
PDB	2F9Y
PDBsum	2F9Y
ProteinModelPortal	P0ABD5
SMR	P0ABD5
DIP	DIP-35897N
IntAct	P0ABD5
MINT	MINT-1228651
STRING	511145.b0185
PaxDb	P0ABD5
PRIDE	P0ABD5
EnsemblBacteria	AAC73296 BAA77860
GeneID	12930759 944895
KEGG	ecj:Y75_p0181 eco:b0185
PATRIC	32115481
EchoBASE	EB1600
EcoGene	EG11647
eggNOG	COG0825
HOGENOM	HOG000273832
InParanoid	P0ABD5
KO	K01962
OMA	HSVYTVA
OrthoDB	EOG6HQSSF
PhylomeDB	P0ABD5
BioCyc	EcoCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER ECOL316407:JW0180-MONOMER MetaCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER
SABIO-RK	P0ABD5
UniPathway	UPA00655
EvolutionaryTrace	P0ABD5
PRO	PR:P0ABD5
Proteomes	UP000000318 UP000000625
Genevestigator	P0ABD5
GO	GO:0009329 GO:0005737 GO:0003989 GO:0005524 GO:0042802 GO:0006633 GO:0042759 GO:2001295
Gene3D	3.90.226.10
HAMAP	MF_00823
InterPro	IPR001095 IPR029045 IPR011763
Pfam	PF03255
PRINTS	PR01069
SUPFAM	SSF52096
TIGRFAMs	TIGR00513
PROSITE	PS50989

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0009329	acetate CoA-transferase complex	PMID:9668099^[1]	ECO:0000314			C	Fig 3. Lane 3 of SDS-PAGE of acetate CoA-transferase complex purified by affinity purification on a nickel column resulted in alpha sub-unit (ECOLI:ACCA) and a beta sub-unit of carboxyltransferase.	complete
enables	GO:0042802	identical protein binding	PMID:24561554^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ABD5	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23582331^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0ABD5	F	Seeded From UniProt	complete
involved_in	GO:0042759	long-chain fatty acid biosynthetic process	PMID:18156466^[4]	ECO:0000303	author statement without traceable support used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006633	fatty acid biosynthetic process	PMID:10893421^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	EcoliWiki:accB EcoliWiki:accC EcoliWiki:accD	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10893421^[5]	ECO:0000305	curator inference used in manual assertion	GO:0006633	C	Seeded From UniProt	complete
part_of	GO:0009329	acetate CoA-transferase complex	PMID:1355089^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006633	fatty acid biosynthetic process	PMID:10893421^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:17309111^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003989	acetyl-CoA carboxylase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001095	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:IPR001095	P	Seeded From UniProt	complete
part_of	GO:0009317	acetyl-CoA carboxylase complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001095	C	Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011763	F	Seeded From UniProt	complete
enables	GO:0016743	carboxyl- or carbamoyltransferase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000031345	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:UR000031345	C	Seeded From UniProt	complete
involved_in	GO:0006633	fatty acid biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000031345	P	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	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0275	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	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
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	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
involved_in	GO:2001295	malonyl-CoA biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00655	P	Seeded From UniProt	complete
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Notes

References

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

↑ Blanchard, CZ & Waldrop, GL (1998) Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase. J. Biol. Chem. 273 19140-5 PubMed GONUTS page
↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
↑ Marsh, JA et al. (2013) Protein complexes are under evolutionary selection to assemble via ordered pathways. Cell 153 461-70 PubMed GONUTS page
↑ Benson, BK et al. (2008) DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: implications for active site communication. Protein Sci. 17 34-42 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Davis, MS et al. (2000) Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli. J. Biol. Chem. 275 28593-8 PubMed GONUTS page
↑ Li, SJ & Cronan, JE Jr (1992) The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267 16841-7 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
↑ 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

[PMID:9668099-1] Blanchard, CZ & Waldrop, GL (1998) Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase. J. Biol. Chem. 273 19140-5 PubMed GONUTS page

[PMID:24561554-2] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:23582331-3] Marsh, JA et al. (2013) Protein complexes are under evolutionary selection to assemble via ordered pathways. Cell 153 461-70 PubMed GONUTS page

[PMID:18156466-4] Benson, BK et al. (2008) DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: implications for active site communication. Protein Sci. 17 34-42 PubMed GONUTS page

[PMID:10893421-5] 5.0 ^5.1 ^5.2 Davis, MS et al. (2000) Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli. J. Biol. Chem. 275 28593-8 PubMed GONUTS page

[PMID:1355089-6] Li, SJ & Cronan, JE Jr (1992) The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267 16841-7 PubMed GONUTS page

[PMID:18304323-7] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:17309111-8] Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page

[PMID:15911532-9] 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

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ECOLI:ACCA

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