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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Burkholderia pseudomallei (strain 668)
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 sitei317Coenzyme AUniRule annotation1
Binding sitei512ATPUniRule annotation1
Binding sitei528ATPUniRule annotation1
Binding sitei536Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei539ATPUniRule annotation1
Metal bindingi550Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi552Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi555Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi397 – 399ATPUniRule annotation3
Nucleotide bindingi421 – 426ATPUniRule 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:BURPS668_A0628
OrganismiBurkholderia pseudomallei (strain 668)
Taxonomic identifieri320373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000002153 Componenti: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000652831 – 660Acetyl-coenzyme A synthetaseAdd BLAST660

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei625N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliA3NH07.
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.
KOiK01895.
OMAiPMASEDR.

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.

A3NH07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAIESVLHE RRQFAPPAAV EKAAAISGMA AYRALAEEAE RDYEGFWARL
60 70 80 90 100
ARETLEWRKP FGKVLDETNA PFYKWFEDGE LNASYNCLDR HVAAGLGERV
110 120 130 140 150
AVIFEADDGT VTRVTYADLL ARVSRFANAL KKRGVGRGDR VVIYIPMSVE
160 170 180 190 200
GIVAMQACAR IGATHSVVFG GFSSKSLHER IVDVGATALV TADEQMRGGK
210 220 230 240 250
TLPLKSIADE ALAMGGCDAV KTVVVYRRTG GNVDWHAGRD VWMHEMVANE
260 270 280 290 300
SDACEPEWVG AEHPLFILYT SGSTGKPKGV QHSTAGYLLW VAQTMKWTFD
310 320 330 340 350
WKPDDVFWCT ADIGWVTGHS YITYGPLAVG ATQVVFEGVP TYPNAGRFWK
360 370 380 390 400
MIGDHKVTVF YTAPTAIRSL IKAAEADDRV HPRSYDLSSL RIIGTVGEPI
410 420 430 440 450
NPEAWIWYHK NVGQARCPIV DTWWQTETGG HMITPLPGAT PTVPGSCTLP
460 470 480 490 500
LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW PAMARTIWGD PERFKKSYFP
510 520 530 540 550
EELGGRLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL GTMEIESALV
560 570 580 590 600
SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGEEAAA LAKTLRDWVG
610 620 630 640 650
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP
660
AILEQLAEVR
Length:660
Mass (Da):72,282
Last modified:April 3, 2007 - v1
Checksum:iB067B10A94777DF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000571 Genomic DNA. Translation: ABN87579.1.
RefSeqiWP_004188376.1. NC_009075.1.

Genome annotation databases

EnsemblBacteriaiABN87579; ABN87579; BURPS668_A0628.
KEGGibpd:BURPS668_A0628.
PATRICi19254726. VBIBurPse82117_4270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000571 Genomic DNA. Translation: ABN87579.1.
RefSeqiWP_004188376.1. NC_009075.1.

3D structure databases

ProteinModelPortaliA3NH07.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN87579; ABN87579; BURPS668_A0628.
KEGGibpd:BURPS668_A0628.
PATRICi19254726. VBIBurPse82117_4270.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.

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_BURP6
AccessioniPrimary (citable) accession number: A3NH07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: November 2, 2016
This is version 57 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

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.