Difference between revisions of "CitZ"
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+ | <pubmed>10348849,8045899,,10656796,12850135 17218307 12100558 9642180 8045898 8655569 4211224 4980242 20525796 20933603 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:14, 9 January 2013
- Description: citrate synthase
Gene name | citZ |
Synonyms | citA2 |
Essential | no |
Product | citrate synthase II |
Function | TCA cycle |
Gene expression levels in SubtiExpress: citZ | |
Interactions involving this protein in SubtInteract: CitZ | |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 41 kDa, 5.451 |
Gene length, protein length | 1116 bp, 372 aa |
Immediate neighbours | icd, ytwI |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
carbon core metabolism, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU29140
Phenotypes of a mutant
glutamate auxotrophy and a defect in sporulation PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Acetyl-CoA + H2O + oxaloacetate = citrate + CoA (according to Swiss-Prot)
- Protein family: citrate synthase family (according to Swiss-Prot)
Extended information on the protein
- Kinetic information: Michaelis-Menten (Random Sequential Reaction Mechanism) PubMed
- Domains:
- Modification: phosphorylation on Ser-284 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Inhibited by acetyl-CoA, 2-oxoglutarate and NADH PubMed FEBS Letters
- Inhibited by citrate and CoA (competitively against acetyl-CoA and non-competitively against oxaloacetate) PubMed
- Inhibited by ATP competitively in B. subtilis strain 168 and HS 1A17 PubMed PubMed
- In B. subtilis strain HS 2A2, ATP inhibits a non-competitive fashion PubMed
- Activated by AMP PubMed
Database entries
- Structure:
- UniProt: P39120
- KEGG entry: [3]
- E.C. number: 2.3.3.1
Additional information
- extensive information on the structure and enzymatic properties of CitZ can be found at Proteopedia
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
Biological materials
- Expression vector:
- pGP1120 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Stülke lab)
- pGP1776 (for expression, purification in E. coli with N-terminal Strep-tag, in pGP172, available in Stülke lab)
- pGP1761 (expression with N-terminal His-tag from E. coli, in pWH844), available in Jörg Stülke's lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Linc Sonenshein lab
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Original publications
Additional publications: PubMed