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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei311Coenzyme AUniRule annotation1
Binding sitei335Coenzyme AUniRule annotation1
Binding sitei500ATPUniRule annotation1
Binding sitei515ATPUniRule annotation1
Binding sitei523Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei526ATPUniRule annotation1
Metal bindingi537Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi539Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei584Coenzyme A1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi387 – 389ATPUniRule annotation3
Nucleotide bindingi411 – 416ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:Arad_4932
OrganismiAgrobacterium radiobacter (strain K84 / ATCC BAA-868)
Taxonomic identifieri311403 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
Proteomesi
  • UP000001600 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001640461 – 652Acetyl-coenzyme A synthetaseAdd BLAST652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei609N6-acetyllysineUniRule annotation1

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi311403.Arad_4932.

Structurei

3D structure databases

ProteinModelPortaliB9JEV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni189 – 192Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9JEV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKIHPVTK PVKARALIDQ AKYQKWYRQS VEDPDKFWGK HGQRIDWFKP
60 70 80 90 100
YTKVKNTSFT GKVSIKWFED GLTNVSYNCI DRHLKKHGDR VAFIWEGDNP
110 120 130 140 150
YIDKKVTYNE LYEHVCRLAN VLKKHGVKKG DRVTIYMPMI PEAAYAMLAC
160 170 180 190 200
ARIGAVHSVV FGGFSPEALG GRIVDCQSTF VITCDEGLRG GKPIPLKENT
210 220 230 240 250
DTAIHIAAKQ FVTVEKVLVV RRTGGKTGWA PGRDLWYHEE TAKVKADCPP
260 270 280 290 300
VKMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAAMTHE YTFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYIVYGP LANAATSLMF EGVPNYPDQG RFWDIIDKHK
360 370 380 390 400
VNIFYTAPTA IRSLMGAGDH FVKRSSRSSL RLLGTVGEPI NPEAWEWYYK
410 420 430 440 450
VVGDSRSPIV DTWWQTETGG HMITPLPGAT DLKPGSATLP FFGVQPELVD
460 470 480 490 500
SEGKVLEGAA DGNLVIADSW PGQMRTVYGD HERFIQTYFS TYKGKYFTGD
510 520 530 540 550
GCRRDEDGYY WITGRVDDVL NVSGHRLGTA EVESALVSHK HVSEAAVVGY
560 570 580 590 600
PHSIKGQGIY CYVTLMVGQE GSDALRQELV KHVRAEIGPI ASPDKIQFTP
610 620 630 640 650
GLPKTRSGKI MRRILRKIAE DDFGALGDTS TLADPAVVDD LIANRQNKAD

AA
Length:652
Mass (Da):72,557
Last modified:March 24, 2009 - v1
Checksum:i1C18D8BC403B12B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000628 Genomic DNA. Translation: ACM28523.1.
RefSeqiWP_012652997.1. NC_011985.1.

Genome annotation databases

EnsemblBacteriaiACM28523; ACM28523; Arad_4932.
KEGGiara:Arad_4932.
PATRICi20808580. VBIAgrRad129173_6354.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000628 Genomic DNA. Translation: ACM28523.1.
RefSeqiWP_012652997.1. NC_011985.1.

3D structure databases

ProteinModelPortaliB9JEV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi311403.Arad_4932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM28523; ACM28523; Arad_4932.
KEGGiara:Arad_4932.
PATRICi20808580. VBIAgrRad129173_6354.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACSA_AGRRK
AccessioniPrimary (citable) accession number: B9JEV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.