P31638 (ACSA_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-coenzyme A synthetase
Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1

Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme

Gene names

Name:	acsA
Synonyms:	acoE
Ordered Locus Names:	H16_A2525

Organism

Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › Cupriavidus necator

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA. Although acetate is the preferred substrate of AcsA, propionate is also used, but at a diminished rate compared with that of acetate. Fatty acids with more than three carbon atoms are usually not accepted as substrates by AcsA. Ref.1
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123
Cofactor	Magnesium By similarity.
Pathway	Ketone degradation; acetoin degradation. HAMAP-Rule MF_01123
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	acetoin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway acetyl-CoA biosynthetic process from acetate Inferred from electronic annotation. Source: InterPro
Molecular_function	AMP binding Inferred from electronic annotation. Source: InterPro ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 660	660	Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123		PRO_0000208353
Sites
	Active site	530	1	By similarity
	Metal binding	550	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	555	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	317	1	Coenzyme A By similarity
	Binding site	397	1	Substrate; via amide nitrogen By similarity
	Binding site	512	1	Substrate By similarity
	Binding site	528	1	Substrate By similarity
	Binding site	536	1	Coenzyme A By similarity
	Binding site	539	1	Substrate By similarity
	Binding site	600	1	Coenzyme A
Amino acid modifications
	Modified residue	625	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31638 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: EA03022F82C5C502	FASTA	660	72,602
	10 20 30 40 50 60 MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYQALCDEAE RDYEGFWARH ARELLHWTKP 70 80 90 100 110 120 FTKVLDQSNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV AIVFEADDGS VTRVTYRELH 130 140 150 160 170 180 GKVCRFANGL KALGIRKGDR VVIYMPMSVE GVVAMQACAR LGATHSVVFG GFSAKSLQER 190 200 210 220 230 240 LVDVGAVALI TADEQMRGGK ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD 250 260 270 280 290 300 RWMEDVSAGQ PDTCEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD 310 320 330 340 350 360 IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD MIARHKVSIF 370 380 390 400 410 420 YTAPTAIRSL IKAAEADEKI HPKQYDLSSL RLLGTVGEPI NPEAWMWYYK NIGNERCPIV 430 440 450 460 470 480 DTFWQTETGG HMITPLPGAT PLVPGSCTLP LPGIMAAIVD ETGHDVPNGN GGILVVKRPW 490 500 510 520 530 540 PAMIRTIWGD PERFRKSYFP EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM 550 560 570 580 590 600 GTMEIESALV SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG 610 620 630 640 650 660 KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP AILEQLKQAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and molecular characterization of the acetyl coenzyme A synthetase gene (acoE) of Alcaligenes eutrophus." Priefert H., Steinbuechel A. J. Bacteriol. 174:6590-6599(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY.
[2]	"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M97217 Genomic DNA. Translation: AAA21945.1. AM260479 Genomic DNA. Translation: CAJ93612.1.
PIR	A45736.
RefSeq	YP_726980.1. NC_008313.1.
3D structure databases
ProteinModelPortal	P31638.
ModBase	Search...
Protein-protein interaction databases
STRING	381666.H16_A2525.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ93612; CAJ93612; H16_A2525.
GeneID	4247141.
KEGG	reh:H16_A2525.
PATRIC	35234555. VBIRalEut6770_2916.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0365.
HOGENOM	HOG000229981.
KO	K01895.
OMA	ENAPFFK.
ProtClustDB	PRK00174.
Enzyme and pathway databases
BioCyc	CNEC381666:GJUJ-2492-MONOMER. MetaCyc:MONOMER-13637.
UniPathway	UPA00040.
Family and domain databases
HAMAP	MF_01123. Ac_CoA_synth.
InterPro	IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. PF13193. DUF4009. 1 hit. [Graphical view]
TIGRFAMs	TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSA_CUPNH

Accession

Primary (citable) accession number: P31638
Secondary accession number(s): Q0K8Q9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program