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0ACSA_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameACSS2
DescriptionAcetyl-coenzyme a synthetase, cytoplasmic (ec 6.2.1.1) (acetate--coa ligase) (acyl-activating enzyme) (acetyl-coa synthetase) (acs) (acecs) (acyl-coa synthetase short-chain family member 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (IC)
0003987 acetate-CoA ligase activity (IDA)
0016208 AMP binding (IC)
0005515 protein binding (IPI)
0008610 lipid biosynthesis (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
A number of prokaryotic and eukaryotic enzymes.hich appear to act via an ATP-dependent covalent binding of AMP to their substrate.hare a region of sequence similarity . This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes luciferase.ong chain fatty acid Co-A ligase.cetyl-CoA synthetase and various other closely-related synthetases.
  IPR000873:AMP-dependent synthetase and ligase
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme) is a ubiquitous enzyme.ound in both prokaryotes and eukaryotes.hich catalyses the formation of acetyl-CoA from acetate.oenzyme A (CoA) and ATP as shown below :ATP + acetate + CoA = AMP + diphosphate + acetyl-CoAThe activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA. key intermediate in many important biosynthetic and catabolic processes. It is especially important in eukayotic species as it is the only route for the activation of acetate to acetyl-CoA in these organisms (some prokaryotic species can also activate acetate by either acetate kinase/phosphotransacetylase or by ADP-forming acetyl-CoA synthase). Eukaryotes typically have two isoforms of acetyl-CoA synthase. cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.The crystal structures of a eukaryotic (.rom yeast) and bacterial (.rom Salmonella) form of this enzyme have been determined . The yeast enzyme is trimeric.hile the bacterial enzyme is monomeric. The trimeric state of the yeast protein may be unique to this organism however.s the residues involved in the trimer interface are poorly conserved in other sequences. Despite differences in the oligomeric state of the two enzyme.he structures of the monomers are almost identical. A large N-terminal domain (~ 500 residues) containing two parallel beta sheets is followed by a small (~ 110 residues) C-terminal domain containing a three-stranded beta sheet with helices. The active site occurs at the domain interface.ith its contents determining the orientation of the C-terminal domain.
  IPR011904:Acetate--CoA ligase
IPR000873:AMP-binding 
Evalue:-131 
Location:137-599
SequencesProtein: ACSA_HUMAN (701 aa)
mRNA: AK092281 NM_018677
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01895
  Level 3 annotation:
    acetyl-CoA synthetase
  Level 2 annotation:
    Glycolysis / Gluconeogenesis
    Pyruvate metabolism
    Propanoate metabolism
    Reductive carboxylate cycle (CO2 fixation)
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 85 residues, 32928035-32928287Exon2: 67 residues, 32934257-32934453Exon3: 32 residues, 32964559-32964651Exon4: 36 residues, 32964856-32964960Exon5: 26 residues, 32965216-32965289Exon6: 27 residues, 32965559-32965635Exon7: 40 residues, 32965786-32965901Exon8: 48 residues, 32970898-32971036Exon9: 59 residues, 32972002-32972173Exon10: 46 residues, 32972469-32972603Exon11: 46 residues, 32972793-32972926Exon12: 21 residues, 32973007-32973064Exon13: 29 residues, 32973249-32973330Exon14: 38 residues, 32974786-32974895Exon15: 25 residues, 32977161-32977230Exon16: 61 residues, 32977568-32977745Exon17: 27 residues, 32978340-32978415Exon18: 292 residues, 32978550-32979421Exon19: 2 residues, -Jump to ACSA_HUMANExon1: 71 residues, 32928077-32928287Exon2: 67 residues, 32934257-32934453Exon3: 32 residues, 32964559-32964651Exon4: 36 residues, 32964856-32964960Exon5: 26 residues, 32965216-32965289Exon6: 27 residues, 32965559-32965635Exon7: 40 residues, 32965786-32965901Exon8: 15 residues, 32966681-32966720Exon9: 48 residues, 32970898-32971036Exon10: 59 residues, 32972002-32972173Exon11: 46 residues, 32972469-32972603Exon12: 46 residues, 32972793-32972926Exon13: 21 residues, 32973007-32973064Exon14: 29 residues, 32973249-32973330Exon15: 38 residues, 32974786-32974895Exon16: 25 residues, 32977161-32977230Exon17: 61 residues, 32977568-32977745Exon18: 27 residues, 32978340-32978415Exon19: 293 residues, 32978550-32979424Exon20: 2 residues, -Jump to ACSA_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3249 32610179-32611810 ~-2K 22943(MAP1LC3A)(+)Loci: 4518 32766239-32877094 ~-111K 22948(NCOA6)(-)Loci: 3250 32928035-32979424 ~-51K 22955(ACSS2)(+)Loci: 3248 32567864-32592422 ~-25K 22941(DNCL2A)(+)Link out to UCSC