SALTY:ACSA

Species (Taxon ID)	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). (99287)
Gene Name(s)	acs (ECO:0000255 with HAMAP-Rule:MF_01123)
Protein Name(s)	Acetyl-coenzyme A synthetase (ECO:0000255 with HAMAP-Rule:MF_01123) AcCoA synthetase (ECO:0000255 with HAMAP-Rule:MF_01123) Acs (ECO:0000255 with HAMAP-Rule:MF_01123) Acetate--CoA ligase (ECO:0000255 with HAMAP-Rule:MF_01123) Acyl-activating enzyme (ECO:0000255 with HAMAP-Rule:MF_01123)
External Links
UniProt	Q8ZKF6
EMBL	AE006468
RefSeq	NP_463140.1 WP_000083882.1
PDB	1PG3 1PG4 2P20 2P2B 2P2F 2P2J 2P2M 2P2Q
PDBsum	1PG3 1PG4 2P20 2P2B 2P2F 2P2J 2P2M 2P2Q
ProteinModelPortal	Q8ZKF6
SMR	Q8ZKF6
STRING	99287.STM4275
PaxDb	Q8ZKF6
PRIDE	Q8ZKF6
EnsemblBacteria	AAL23099
GeneID	1255801
KEGG	stm:STM4275
PATRIC	32387457
eggNOG	ENOG4108IQF COG0365
HOGENOM	HOG000229981
KO	K01895
OMA	EGAPNWP
PhylomeDB	Q8ZKF6
EvolutionaryTrace	Q8ZKF6
Proteomes	UP000001014
GO	GO:0003987 GO:0016208 GO:0005524 GO:0046872 GO:0019427 GO:0006935
CDD	cd05966
HAMAP	MF_01123
InterPro	IPR011904 IPR032387 IPR025110 IPR020845 IPR000873
Pfam	PF16177 PF00501 PF13193
TIGRFAMs	TIGR02188
PROSITE	PS00455

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0003987	acetate-CoA ligase activity	PMID:27974467	ECO:0000314			F		Organism: Salmonella enterica (Salmonella typhimurium). Protein Name: Acetyl-coenzyme A synthetase (Acs). The control of Figure 1C shows that when molecules such as cAMP inhibit Acetyl-coenzyme A Synthetase, Acetate-CoA ligase activity is downregulated. Thus, SeAcs is involved with Acetate-CoA ligase activity.	complete CACAO 12268
	GO:0051591	response to cAMP	PMID:27974467	ECO:0000314			P		Organism: Salmonella enterica (Salmonella typhimurium). Protein Name: Acetyl-coenzyme A synthetase (Acs). "The potential inhibitory effect of cAMP on Acs was tested using a subsaturated concentration for each of the substrates. cAMP substantially inhibited SeAcs activity only in an enzymatic reaction system with a low concentration of ATP (Fig. 1C), suggesting cAMP inhibits SeAcs via an ATP-competitive mechanism."	complete CACAO 12318
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000873	F		Seeded From UniProt	complete
enables	GO:0003987	acetate-CoA ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011904	F		Seeded From UniProt	complete
enables	GO:0016208	AMP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011904	F		Seeded From UniProt	complete
involved_in	GO:0019427	acetyl-CoA biosynthetic process from acetate	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011904	P		Seeded From UniProt	complete
enables	GO:0003987	acetate-CoA ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.2.1.1	F		Seeded From UniProt	complete
involved_in	GO:0006935	chemotaxis	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100676	P		Seeded From UniProt	complete
involved_in	GO:0019427	acetyl-CoA biosynthetic process from acetate	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100676	P		Seeded From UniProt	complete
enables	GO:0003987	acetate-CoA ligase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100676	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	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
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F		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
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References

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