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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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 sitei312Coenzyme AUniRule annotation1
Binding sitei501ATPUniRule annotation1
Binding sitei516ATPUniRule annotation1
Binding sitei524Coenzyme A; via carbonyl oxygenUniRule annotation1
Metal bindingi538Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi540Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi543Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi388 – 390ATPUniRule annotation3
Nucleotide bindingi412 – 417ATPUniRule 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:SCO3563
ORF Names:SCH5.26
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083891 – 651Acetyl-coenzyme A synthetaseAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei610N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ9X928.

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO3563.

Structurei

3D structure databases

ProteinModelPortaliQ9X928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni193 – 196Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
InParanoidiQ9X928.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.
PhylomeDBiQ9X928.

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.

Q9X928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNESLANLL KEERRFAPPA DLAANANVTA EAYEQAKADR LGFWAEQARR
60 70 80 90 100
LTWAKEPTET LDWSNPPFAK WFKDGTLNVA YNCVDRHVEA GNGDRVAIHF
110 120 130 140 150
EGESGDSRAL TYAQLKDEVS KAANALLELG VQKGDRVAIY MPMIPETAIA
160 170 180 190 200
MLACARIGAA HSVVFGGFSS DALATRIQDA DARVVITADG GYRRGKPSAL
210 220 230 240 250
KPAVDEAVER AGIVEHVLVV RRTGQDVAWD DSRDKWWHET VDGQSAEHTP
260 270 280 290 300
EAFDAEHPLF ILYTSGTTGK PKGILHTSGG YLTQTAYTHW AVFDLKPETD
310 320 330 340 350
VFWCTADVGW VTGHSYIVYG PLANGATQVM YEGTPDTPHQ GRFWEIVQKY
360 370 380 390 400
GVTILYTAPT AIRTFMKWGD DIPAKFDLSS LRVLGSVGEP INPEAWIWYR
410 420 430 440 450
KNIGADATPV VDTWWQTETG AMMITPLPGV THAKPGSAQR PLPGISATVV
460 470 480 490 500
DDEANEVPNG GGGYLVLTEP WPSMLRTIWG DDQRFIDTYW SRFEGKYFAG
510 520 530 540 550
DGAKKDDDGD IWLLGRVDDV MLVSGHNIST TEVESALVSH PSVAEAAVVG
560 570 580 590 600
ATDETTGQAI VAFVILRGTT AESEDLVAEL RNHVGATLGP IAKPKRILPV
610 620 630 640 650
SELPKTRSGK IMRRLLRDVA ENRQVGDVTT LADSTVMDLI QTKLPAAPSE

D
Length:651
Mass (Da):71,045
Last modified:November 1, 1999 - v1
Checksum:i3A04CFD3ED436EC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939117 Genomic DNA. Translation: CAB38500.1.
PIRiT36684.
RefSeqiNP_627761.1. NC_003888.3.
WP_003975373.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB38500; CAB38500; CAB38500.
GeneIDi1098999.
KEGGisco:SCO3563.
PATRICi23736870. VBIStrCoe124346_3619.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939117 Genomic DNA. Translation: CAB38500.1.
PIRiT36684.
RefSeqiNP_627761.1. NC_003888.3.
WP_003975373.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9X928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO3563.

Proteomic databases

PRIDEiQ9X928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB38500; CAB38500; CAB38500.
GeneIDi1098999.
KEGGisco:SCO3563.
PATRICi23736870. VBIStrCoe124346_3619.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
InParanoidiQ9X928.
KOiK01895.
OMAiEGAPNWP.
OrthoDBiPOG091H059D.
PhylomeDBiQ9X928.

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_STRCO
AccessioniPrimary (citable) accession number: Q9X928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 1, 1999
Last modified: October 5, 2016
This is version 92 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.