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Q98ET8 (ACSA_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:mlr4089
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length651 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_0000208380

Regions

Region412 – 4176Substrate binding By similarity

Sites

Active site5181 By similarity
Metal binding5381Magnesium; via carbonyl oxygen By similarity
Metal binding5401Magnesium; via carbonyl oxygen By similarity
Metal binding5431Magnesium; via carbonyl oxygen By similarity
Binding site3121Coenzyme A By similarity
Binding site3361Coenzyme A By similarity
Binding site3881Substrate; via amide nitrogen By similarity
Binding site5011Substrate By similarity
Binding site5161Substrate By similarity
Binding site5241Coenzyme A By similarity
Binding site5271Substrate By similarity
Binding site5851Coenzyme A

Amino acid modifications

Modified residue6101N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98ET8 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: C7A0AC5011C4D43F

FASTA65172,530
        10         20         30         40         50         60 
MSEVHVHRVQ PAWKKNALID NDTYLKWYAD SIKNPDKFWG KHGKRIDWFK PFSKVKNTSF 

        70         80         90        100        110        120 
DGKVSIKWFE DGLTNVSYNC IDRHLKKRGD QTAIIWEGDN PYDDKKITYN ELYERVCRLA 

       130        140        150        160        170        180 
NVMKKHGVKK GDRVTIYMPM IPEAAYAMLA CTRIGAIHSI VFGGFSPDAL AGRIVDCEST 

       190        200        210        220        230        240 
FVITADEGLR GGKSIPLKEN TDKAIDIAAK NFVMVKNVLV VRRTGGKVGW APGRDLWYHD 

       250        260        270        280        290        300 
EVATVKAECK PEKMKAEDPL FILYTSGSTG KPKGVLHTTA GYLVYASMTH QYVFDYHDGD 

       310        320        330        340        350        360 
IYWCTADVGW VTGHSYIVYG PLANGATTLM FEGVPNYPSQ SRFWEVIDKH KVNIFYTAPT 

       370        380        390        400        410        420 
ALRALMGAGN DPVKKTSRKS LRVLGSVGEP INPEAWEWYF NVVGNGKVPI VDTWWQTETG 

       430        440        450        460        470        480 
GILITPLPGA TDLKAGSATR PFFGVKPQLV DGEGKVLEGA ADGNLCITDS WPGQMRTVYG 

       490        500        510        520        530        540 
DHDRFVQTYF STYKGKYFTG DGCRRDADGY YWITGRVDDV INVSGHRMGT AEVESALVSH 

       550        560        570        580        590        600 
DKVSEAAVVG YPHDIKGQGI YSYVTLMKGE EPTEDLRKEL IAHVRKEIGA IASPDKIQFA 

       610        620        630        640        650 
PGLPKTRSGK IMRRILRKIA EDDFSTLGDT STLADPAVVD DLIANRQNKK G 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB50829.1.
RefSeqNP_105043.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98ET8.
SMRQ98ET8. Positions 5-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr4089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB50829; BAB50829; BAB50829.
GeneID1227704.
KEGGmlo:mlr4089.
PATRIC22480693. VBIMesLot2464_3234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAQTAILFE.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-3186-MONOMER.

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 nameACSA_RHILO
AccessionPrimary (citable) accession number: Q98ET8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families