Acetyl-coenzyme A synthetase - Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

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
Ordered Locus Names:	VC_0298

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length	649 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
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence AAF93472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 sequence or structural similarity Ref.1. Source: TIGR
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 sequence or structural similarity Ref.1. Source: TIGR 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 – 649

649

Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

PRO_0000208392

Regions

Region

411 – 416

6

Substrate binding By similarity

Sites

Active site

517

1

By similarity

Metal binding

537

1

Magnesium; via carbonyl oxygen By similarity

Metal binding

539

1

Magnesium; via carbonyl oxygen By similarity

Metal binding

542

1

Magnesium; via carbonyl oxygen By similarity

Binding site

311

1

Coenzyme A By similarity

Binding site

335

1

Coenzyme A By similarity

Binding site

387

1

Substrate; via amide nitrogen By similarity

Binding site

500

1

Substrate By similarity

Binding site

515

1

Substrate By similarity

Binding site

523

1

Coenzyme A By similarity

Binding site

526

1

Substrate By similarity

Binding site

584

1

Coenzyme A

Amino acid modifications

Modified residue

609

1

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9KV59 [UniParc].

Last modified September 26, 2003. Version 2.
Checksum: A0C7282B14806B6E
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FASTA

649

71,895

        10         20         30         40         50         60 
MSEAHIYPVK QNIKAHTHAD NDTYLAMYQQ SIKDPEGFWS EHGKIVDWIK PFTKVKHTSF 

        70         80         90        100        110        120 
DPGHIDIRWF EDGTLNVSAN CIDRHLATRG DQVAIIWEGD DPTQDKTLTY KQLHQEVCRF 

       130        140        150        160        170        180 
ANALKEQGVR KGDVVCIYMP MVPEAAVAML ACTRIGAVHT IVFGGFSPEA LAGRIIDSNA 

       190        200        210        220        230        240 
KLVITADEGV RGGRAVPLKK NVDEALCNPE VKNISKVMVL KRTGGNVAWH EHRDIWWHEA 

       250        260        270        280        290        300 
TAKASDNCPP EEMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYATMTFK YVFDYQPNEV 

       310        320        330        340        350        360 
FWCTADVGWI TGHSYLVYGP LANGAKTILF EGVPNYPTTA RMSEVVDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRALMAKGDE AIKGTSRDSL RIMGSVGEPI NPEAWEWYYR TIGNEKSPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILITPLPGAT ALKPGSATRP FFGVQPALVD NMGEIVEGAT EGNLVLLDSW PGQMRTVYGD 

       490        500        510        520        530        540 
HDRFEQTYFS TFKGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESALVAFN 

       550        560        570        580        590        600 
KIAEAAVVGV PHDIKGQAIY AYITLNDGVY PSAELHKEVK DWVRKEIGAI ATPDVLHWTD 

       610        620        630        640 
ALPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVDR LIAEKAQLK

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References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S.

Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF93472.1. Different initiation.
PIR	D82339.
RefSeq	NP_229953.2. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KV59.
SMR	Q9KV59. Positions 5-645.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC0298.
Protocols and materials databases
DNASU	2614968.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF93472; AAF93472; VC_0298.
GeneID	2614968.
KEGG	vch:VC0298.
PATRIC	20079643. VBIVibCho83274_0280.
Phylogenomic databases
eggNOG	COG0365.
KO	K01895.
OMA	PPIKRSC.
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_VIBCH

Accession

Primary (citable) accession number: Q9KV59

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	September 26, 2003
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

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