Acetyl-coenzyme A synthetase - Helicobacter pylori (strain ATCC 700392 / 26695)

Preferred order of sections

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:	acs
Ordered Locus Names:	HP_1045

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length	662 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 By similarity. HAMAP-Rule MF_01123
Catalytic activity	ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123
Cofactor	Magnesium By similarity.
Post-translational modification	Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123
Miscellaneous	There is no ortholog for acsA in strain J99. 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 Reference proteome
Gene Ontology (GO)
Biological_process	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 – 662

662

Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

PRO_0000208365

Regions

Region

417 – 422

6

Substrate binding By similarity

Sites

Active site

527

1

By similarity

Metal binding

549

1

Magnesium; via carbonyl oxygen By similarity

Metal binding

552

1

Magnesium; via carbonyl oxygen By similarity

Binding site

317

1

Coenzyme A By similarity

Binding site

393

1

Substrate; via amide nitrogen By similarity

Binding site

510

1

Substrate By similarity

Binding site

525

1

Substrate By similarity

Binding site

533

1

Coenzyme A By similarity

Binding site

536

1

Substrate By similarity

Binding site

598

1

Coenzyme A

Amino acid modifications

Modified residue

623

1

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O25686 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A83E0F9A34F021F3
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FASTA

662

74,948

        10         20         30         40         50         60 
MQLDEDLEFA KKIFNPNRAF AKQARIKNMC EYKDLVHEAN EDYEHFWGDL AKQKLTWFKP 

        70         80         90        100        110        120 
FDKVLNSDNA PFFKWFENGK INVSYNCIDR HLKDKKNKVA IIFEGEMGDY NVITYRKLHS 

       130        140        150        160        170        180 
EVNKTANLLK NEFNVKKGDR VIIYMPMIVE SVYMMLACTR IGAIHSIVFA GFSPEALRDR 

       190        200        210        220        230        240 
INDAQAKLVI TADGTFRKGK PYMLKPALDK ALENNACPSV EKALIVIRNA KEIDYVRGRD 

       250        260        270        280        290        300 
FVYNEMVNYQ SDKCEPEMMD SEDPLFLLYT SGSTGKPKGV QHSSAGYLLW AQMTMEWVFD 

       310        320        330        340        350        360 
IRDNDNFWCT ADIGWITGHT YVVYGPLACG ATTLILEGTM SYPDYGRWWR MIEEYRVDKF 

       370        380        390        400        410        420 
YTSPTAIRML HAKGENEPSK YNLESLKVLG TVGEPINPTA WKWFYEKIGN SKCSIVDTWW 

       430        440        450        460        470        480 
QTETGGHIIS PLPGATPIRA SCATLPLPGI HAEVLNEDGT KTKPGEQGFL CITKPWPSMI 

       490        500        510        520        530        540 
RNIWGDEKRY IDSYFSQIKL NGEYVYLSGD GAIVDENGYI TIIGRTDDIV NVSGHRIGTA 

       550        560        570        580        590        600 
EVESAISKHE MVAECAVVGI PDAIKGEGLF AFVVLCDGAK CNLGESLELL KEMNHILSIE 

       610        620        630        640        650        660 
IGKIAKLDNV MYVPGLPKTR SGKIMRRLLK SIAKKEPITQ DLSTLEDVNV VKEIMSIAQM 


EE

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References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J.

Venter J.C.
Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD08090.1.
PIR	E64650.
RefSeq	NP_207835.1. NC_000915.1. YP_006934961.1. NC_018939.1.
3D structure databases
ProteinModelPortal	O25686.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3168N.
MINT	MINT-164557.
STRING	85962.HP1045.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD08090; AAD08090; HP_1045.
GeneID	13870238. 899580.
KEGG	heo:C694_05405. hpy:HP1045.
PATRIC	20593427. VBIHelPyl33062_1094.
Phylogenomic databases
eggNOG	COG0365.
KO	K01895.
OMA	AISKHEM.
ProtClustDB	PRK00174.
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_HELPY

Accession

Primary (citable) accession number: O25686

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents