Difference between revisions of "AcsA"
| Line 14: | Line 14: | ||
|style="background:#ABCDEF;" align="center"|'''Function''' || utilization of acetate, fatty acids | |style="background:#ABCDEF;" align="center"|'''Function''' || utilization of acetate, fatty acids | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU29680 acsA] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' | ||
| Line 24: | Line 24: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytzK]]'', ''[[acuA]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ytzK]]'', ''[[acuA]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU29680 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU29680 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU29680 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:acsA_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:acsA_context.gif]] | ||
Revision as of 13:37, 13 May 2013
- Description: acetyl-CoA synthetase
| Gene name | acsA |
| Synonyms | |
| Essential | no |
| Product | acetyl-CoA synthetase) |
| Function | utilization of acetate, fatty acids |
| Gene expression levels in SubtiExpress: acsA | |
| Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
| MW, pI | 64 kDa, 5.547 |
| Gene length, protein length | 1716 bp, 572 aa |
| Immediate neighbours | ytzK, acuA |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
utilization of specific carbon sources, utilization of lipids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU29680
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA (according to Swiss-Prot)
- Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: acetylated on Lys-549 by AcuA, this results in inactivation PubMed, deacetylated by SrtN and AcuC deacetylates (and thereby activates) AcsA PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P39062
- KEGG entry: [3]
- E.C. number: 6.2.1.1
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- GP1212 (acsA::kan), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Eric L Hegg
Unraveling the structure and mechanism of acetyl-coenzyme A synthase.
Acc Chem Res: 2004, 37(10);775-83
[PubMed:15491124]
[WorldCat.org]
[DOI]
(P p)
V J Starai, J C Escalante-Semerena
Acetyl-coenzyme A synthetase (AMP forming).
Cell Mol Life Sci: 2004, 61(16);2020-30
[PubMed:15316652]
[WorldCat.org]
[DOI]
(P p)
Paul A Lindahl
Acetyl-coenzyme A synthase: the case for a Ni(p)(0)-based mechanism of catalysis.
J Biol Inorg Chem: 2004, 9(5);516-24
[PubMed:15221478]
[WorldCat.org]
[DOI]
(P p)
Original publications
