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G0F1A2

- G0F1A2_CUPNN

UniProt

G0F1A2 - G0F1A2_CUPNN

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA3, acsA, CNE_1c24100
Organism
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei317 – 3171Coenzyme A By similarityUniRule annotation
Binding sitei397 – 3971Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei512 – 5121Substrate By similarityUniRule annotation
Binding sitei528 – 5281Substrate By similarityUniRule annotation
Active sitei530 – 5301 By similarityUniRule annotation
Binding sitei536 – 5361Coenzyme A By similarityUniRule annotation
Binding sitei539 – 5391Substrate By similarityUniRule annotation
Metal bindingi550 – 5501Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi555 – 5551Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei600 – 6001Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  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 ligase
Acyl-activating enzyme
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-acetyllysine By similarityUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliG0F1A2.

Family & Domainsi

Sequence similaritiesi

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

MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYRALCDEAE RDYEGFWARH    50
ARELLHWNKP FTKVLDESNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV 100
AIVFEADDGT VTRVTYRELH GKVCRFANGL KALGIKKGDR VVIYMPMSVE 150
GVVAMQACAR LGATHSVVFG GFSAKSLQER LVDVGAVALI TADEQMRGGK 200
ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD RWMEDVSAGQ 250
PDICEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWSFD 300
IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD 350
MIARHKVSIF YTAPTAIRSL IKAAEADDKI HPKQYDLSSL RLLGTVGEPI 400
NPEAWMWYYK NIGNERCPIV DTFWQTETGG HMITPLPGAT PLVPGSCTLP 450
LPGIMAAIVD ETGHDVPNGN GGILVVKRPW PAMIRTIWGD PERFRKSYFP 500
EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM GTMEIESALV 550
SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG 600
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP 650
AILEQLKQAQ 660
Length:660
Mass (Da):72,614
Last modified:October 19, 2011 - v1
Checksum:i3381FFD2F26F1B3B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002877 Genomic DNA. Translation: AEI77733.1.
RefSeqiYP_004686214.1. NC_015726.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002877 Genomic DNA. Translation: AEI77733.1 .
RefSeqi YP_004686214.1. NC_015726.1.

3D structure databases

ProteinModelPortali G0F1A2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEI77733 ; AEI77733 ; CNE_1c24100 .
GeneIDi 10918801.
KEGGi cnc:CNE_1c24100.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci CNEC1042878:GH0Z-2410-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

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-1.

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: June 11, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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