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A5F3Q8 (A5F3Q8_VIBC3) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acs-1 EMBL ABQ21501.1
Synonyms:acsA HAMAP-Rule MF_01123
Ordered Locus Names:VC0395_A2691 EMBL ABQ21501.1, VC395_0342 EMBL ACP08367.1
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP] EMBL ABQ21501.1
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Protein existenceInferred 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. 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. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region428 – 4336Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5341 By similarity HAMAP-Rule MF_01123
Metal binding5541Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5561Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5591Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3281Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3521Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4041Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5171Substrate By similarity HAMAP-Rule MF_01123
Binding site5321Substrate By similarity HAMAP-Rule MF_01123
Binding site5401Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5431Substrate By similarity HAMAP-Rule MF_01123
Binding site6011Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6261N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
A5F3Q8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: F88F13DB61BB7BE2

FASTA66673,676
        10         20         30         40         50         60 
MKRALSGNLP NSQGEPVMSE AHIYPVKQNI KAHTHADNDT YLAMYQQSIK DPEGFWSEHG 

        70         80         90        100        110        120 
KIVDWIKPFT KVKHTSFDPG HIDIRWFEDG TLNVSANCID RHLATRGDQV AIIWEGDDPT 

       130        140        150        160        170        180 
QDKTLTYKQL HQEVCRFANA LKEQGVRKGD VVCIYMPMVP EAAVAMLACT RIGAVHTIVF 

       190        200        210        220        230        240 
GGFSPEALAG RIIDSNAKLV ITADEGVRGG RAVPLKKNVD EALCNPEVKN ISKVMVLKRT 

       250        260        270        280        290        300 
GGNVAWHEHR DIWWHEATAK ASDNCPPEEM KAEDPLFILY TSGSTGKPKG VLHTTGGYLV 

       310        320        330        340        350        360 
YATMTFKYVF DYQPNEVFWC TADVGWITGH SYLVYGPLAN GAKTILFEGV PNYPTTARMS 

       370        380        390        400        410        420 
EVVDKHKVNI LYTAPTAIRA LMAKGDEAIK GTSRDSLRIM GSVGEPINPE AWEWYYRTIG 

       430        440        450        460        470        480 
NEESPIVDTW WQTETGGILI TPLPGATALK PGSATRPFFG VQPALVDNMG EIVEGATEGN 

       490        500        510        520        530        540 
LVLLDSWPGQ MRTVYGDHDR FEQTYFSTFK GMYFTGDGAR RDEDGYYWIT GRVDDVLNVS 

       550        560        570        580        590        600 
GHRMGTAEIE SALVAFNKIA EAAVVGVPHD IKGQAIYAYI TLNDGVYPSA ELHKEVKDWV 

       610        620        630        640        650        660 
RKEIGAIATP DVLHWTDALP KTRSGKIMRR ILRKIATGDT SNLGDTSTLA DPSVVDRLIA 


EKAQLK 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395 and O395 EMBL ABQ21501.1.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395 and O395 EMBL ACP08367.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ21501.1.
CP001235 Genomic DNA. Translation: ACP08367.1.
RefSeqYP_002818603.1. NC_012582.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A2691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ21501; ABQ21501; VC0395_A2691.
ACP08367; ACP08367; VC395_0342.
GeneID7774414.
KEGGvcr:VC395_0342.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAWIWYRD.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA5F3Q8_VIBC3
AccessionPrimary (citable) accession number: A5F3Q8
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: July 9, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)