Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Burkholderia pseudomallei (strain 1106a)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei317 – 3171Coenzyme AUniRule annotation
Binding sitei512 – 5121ATPUniRule annotation
Binding sitei528 – 5281ATPUniRule annotation
Binding sitei536 – 5361Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei539 – 5391ATPUniRule annotation
Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi552 – 5521Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi397 – 3993ATPUniRule annotation
Nucleotide bindingi421 – 4266ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciBPSE357348:GHVF-4616-MONOMER.

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:BURPS1106A_A0530
OrganismiBurkholderia pseudomallei (strain 1106a)
Taxonomic identifieri357348 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000006738 Componenti: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Acetyl-coenzyme A synthetasePRO_1000065281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei625 – 6251N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliA3P2K7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni197 – 2004Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.

Family and domain databases

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.

A3P2K7-1 [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
CP000573 Genomic DNA. Translation: ABN93453.1.
RefSeqiWP_004188376.1. NC_009078.1.

Genome annotation databases

EnsemblBacteriaiABN93453; ABN93453; BURPS1106A_A0530.
KEGGibpl:BURPS1106A_A0530.
PATRICi19227376. VBIBurPse14980_4308.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000573 Genomic DNA. Translation: ABN93453.1.
RefSeqiWP_004188376.1. NC_009078.1.

3D structure databases

ProteinModelPortaliA3P2K7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN93453; ABN93453; BURPS1106A_A0530.
KEGGibpl:BURPS1106A_A0530.
PATRICi19227376. VBIBurPse14980_4308.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiPMASEDR.

Enzyme and pathway databases

BioCyciBPSE357348:GHVF-4616-MONOMER.

Family and domain databases

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_BURP0
AccessioniPrimary (citable) accession number: A3P2K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: September 7, 2016
This is version 56 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.