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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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 sitei316Coenzyme AUniRule annotation1
Binding sitei510ATPUniRule annotation1
Binding sitei525ATPUniRule annotation1
Binding sitei533Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei536ATPUniRule annotation1
Metal bindingi547Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi549Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi552Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi392 – 394ATPUniRule annotation3
Nucleotide bindingi416 – 421ATPUniRule 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
Synonyms:acs
Ordered Locus Names:sll0542
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083911 – 653Acetyl-coenzyme A synthetaseAdd BLAST653

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei619N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ55404.

Structurei

3D structure databases

ProteinModelPortaliQ55404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 200Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
InParanoidiQ55404.
KOiK01895.
OMAiPMASEDR.
PhylomeDBiQ55404.

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.

Q55404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDTIESILQ EERLFDPPTE FSERAYVRSG REYEQLYSRA ASNPEKFWGE
60 70 80 90 100
LAEQELHWFK KWDQVLDWQP PFAKWFVGGQ LNISHNCLDR HLTTWRRNKA
110 120 130 140 150
AIIWEGEPGD SRIITYAQLH REVCQFANAL KSLGVQKGDR VAIYLPMIPE
160 170 180 190 200
AAITMLACSR IGAPHSVVFG GFSAEALRDR LVDAEAKLVI TADGGFRKDK
210 220 230 240 250
AIALKQEVDK ALEHGAPSVE NVIVVQRTKA DVTMTAGRDH WWHELQPQQS
260 270 280 290 300
AHCPAEPIDS EDMLFILYTS GSTGKPKGVV HTTGGYNLYT HMTTKWIFDL
310 320 330 340 350
KDTDVYWCTA DVGWITGHSY IVYGPLSNGA TTVMYEGVPR PSNPGCFWDV
360 370 380 390 400
IERYGVNIFY TAPTAIRAFI RMGEAVPNAR DLSSLRLLGT VGEPINPEAW
410 420 430 440 450
MWYHRVIGGG KCPIVDTWWQ TETGGIMLTP LPGAIPTKPG SCTKPFPGIV
460 470 480 490 500
AEIVDLDGNP VESDQGGFLV IKQPWPSMIR DVYGDTDRFR HTYWEHIQPK
510 520 530 540 550
EGQYLYFAGD GARRDKDGYF WVMGRVDDVI NVSGHRLGTM EIESALVSHP
560 570 580 590 600
LVAEAAVVGR PDELTGEAIF AFVSLEGNAE PSEELKKDLV KHVTEEIGAI
610 620 630 640 650
ARPAEIRFTD VLPKTRSGKI MRRLLRSLAS GQEISGDTST LEDRTVLDKL

REG
Length:653
Mass (Da):73,052
Last modified:November 1, 1996 - v1
Checksum:i5EBCAD430EEFFA03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10498.1.
PIRiS75763.

Genome annotation databases

EnsemblBacteriaiBAA10498; BAA10498; BAA10498.
KEGGisyn:sll0542.
PATRICi23842556. VBISynSp132158_2817.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10498.1.
PIRiS75763.

3D structure databases

ProteinModelPortaliQ55404.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ55404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10498; BAA10498; BAA10498.
KEGGisyn:sll0542.
PATRICi23842556. VBISynSp132158_2817.

Phylogenomic databases

HOGENOMiHOG000229981.
InParanoidiQ55404.
KOiK01895.
OMAiPMASEDR.
PhylomeDBiQ55404.

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_SYNY3
AccessioniPrimary (citable) accession number: Q55404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 109 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
  2. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.