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

acsA3

Organism
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha)
Status
Unreviewed-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 bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation

Regions

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

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciCNEC1042878:GH0Z-2410-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:acsA3Imported
Synonyms:acsAUniRule annotation
Ordered Locus Names:CNE_1c24100Imported
OrganismiCupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha)Imported
Taxonomic identifieri1042878 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000006798: Chromosome 1

PTM / Processingi

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

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliG0F1A2.
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

KOiK01895.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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.

G0F1A2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYRALCDEAE RDYEGFWARH
60 70 80 90 100
ARELLHWNKP FTKVLDESNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV
110 120 130 140 150
AIVFEADDGT VTRVTYRELH GKVCRFANGL KALGIKKGDR VVIYMPMSVE
160 170 180 190 200
GVVAMQACAR LGATHSVVFG GFSAKSLQER LVDVGAVALI TADEQMRGGK
210 220 230 240 250
ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD RWMEDVSAGQ
260 270 280 290 300
PDICEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWSFD
310 320 330 340 350
IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD
360 370 380 390 400
MIARHKVSIF YTAPTAIRSL IKAAEADDKI HPKQYDLSSL RLLGTVGEPI
410 420 430 440 450
NPEAWMWYYK NIGNERCPIV DTFWQTETGG HMITPLPGAT PLVPGSCTLP
460 470 480 490 500
LPGIMAAIVD ETGHDVPNGN GGILVVKRPW PAMIRTIWGD PERFRKSYFP
510 520 530 540 550
EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM GTMEIESALV
560 570 580 590 600
SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG
610 620 630 640 650
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP
660
AILEQLKQAQ
Length:660
Mass (Da):72,614
Last modified:October 19, 2011 - v1
Checksum:i3381FFD2F26F1B3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002877 Genomic DNA. Translation: AEI77733.1.
RefSeqiWP_013957336.1. NC_015726.1.
YP_004686214.1. NC_015726.1.

Genome annotation databases

EnsemblBacteriaiAEI77733; AEI77733; CNE_1c24100.
GeneIDi10918801.
KEGGicnc:CNE_1c24100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002877 Genomic DNA. Translation: AEI77733.1.
RefSeqiWP_013957336.1. NC_015726.1.
YP_004686214.1. NC_015726.1.

3D structure databases

ProteinModelPortaliG0F1A2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEI77733; AEI77733; CNE_1c24100.
GeneIDi10918801.
KEGGicnc:CNE_1c24100.

Phylogenomic databases

KOiK01895.

Enzyme and pathway databases

BioCyciCNEC1042878:GH0Z-2410-MONOMER.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. 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...

Publicationsi

  1. "Complete genome sequence of the type strain Cupriavidus necator N-1."
    Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.
    J. Bacteriol. 193:5017-5017(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43291 / DSM 13513 / N-1Imported.

Entry informationi

Entry nameiG0F1A2_CUPNN
AccessioniPrimary (citable) accession number: G0F1A2
Entry historyi
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: January 7, 2015
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.