Skip Header

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

P31638

- ACSA_CUPNH

UniProt

P31638 - ACSA_CUPNH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 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. Although acetate is the preferred substrate of AcsA, propionate is also used, but at a diminished rate compared with that of acetate. Fatty acids with more than three carbon atoms are usually not accepted as substrates by AcsA.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Pathwayi

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. acetoin catabolic process Source: UniProtKB-UniPathway
  2. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-2492-MONOMER.
MetaCyc:MONOMER-13637.
UniPathwayiUPA00040.

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
Synonyms:acoE
Ordered Locus Names:H16_A2525
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Acetyl-coenzyme A synthetasePRO_0000208353Add
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

Interactioni

Protein-protein interaction databases

STRINGi381666.H16_A2525.

Structurei

3D structure databases

ProteinModelPortaliP31638.
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

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAHERYEN.
OrthoDBiEOG68WR2H.

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.

P31638-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYQALCDEAE RDYEGFWARH
60 70 80 90 100
ARELLHWTKP FTKVLDQSNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV
110 120 130 140 150
AIVFEADDGS VTRVTYRELH GKVCRFANGL KALGIRKGDR 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
PDTCEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD
310 320 330 340 350
IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD
360 370 380 390 400
MIARHKVSIF YTAPTAIRSL IKAAEADEKI 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):72,602
Last modified:July 1, 1993 - v1
Checksum:iEA03022F82C5C502
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97217 Genomic DNA. Translation: AAA21945.1.
AM260479 Genomic DNA. Translation: CAJ93612.1.
PIRiA45736.
RefSeqiWP_011615709.1. NC_008313.1.
YP_726980.1. NC_008313.1.

Genome annotation databases

EnsemblBacteriaiCAJ93612; CAJ93612; H16_A2525.
GeneIDi4247141.
KEGGireh:H16_A2525.
PATRICi35234555. VBIRalEut6770_2916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97217 Genomic DNA. Translation: AAA21945.1 .
AM260479 Genomic DNA. Translation: CAJ93612.1 .
PIRi A45736.
RefSeqi WP_011615709.1. NC_008313.1.
YP_726980.1. NC_008313.1.

3D structure databases

ProteinModelPortali P31638.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 381666.H16_A2525.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ93612 ; CAJ93612 ; H16_A2525 .
GeneIDi 4247141.
KEGGi reh:H16_A2525.
PATRICi 35234555. VBIRalEut6770_2916.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi AHERYEN.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

UniPathwayi UPA00040 .
BioCyci CNEC381666:GJUJ-2492-MONOMER.
MetaCyc:MONOMER-13637.

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

« Hide 'large scale' publications
  1. "Identification and molecular characterization of the acetyl coenzyme A synthetase gene (acoE) of Alcaligenes eutrophus."
    Priefert H., Steinbuechel A.
    J. Bacteriol. 174:6590-6599(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Entry informationi

Entry nameiACSA_CUPNH
AccessioniPrimary (citable) accession number: P31638
Secondary accession number(s): Q0K8Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 26, 2014
This is version 100 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3