Difference between revisions of "YumC"
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* '''Modification:''' | * '''Modification:''' | ||
| − | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' FAD, NADPH {{PubMed|20878669}} |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''Interactions:''' dimeric protein {{PubMed|20878669}} |
* '''Localization:''' | * '''Localization:''' | ||
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=== Database entries === | === Database entries === | ||
| − | * '''Structure:''' | + | * '''Structure:''' [http://www.pdb.org/pdb/search/structidSearch.do?structureId=3LZW 3LZW] {{PubMed|20878669}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/O05268 O05268] | * '''UniProt:''' [http://www.uniprot.org/uniprot/O05268 O05268] | ||
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=References= | =References= | ||
| − | <pubmed> 20208166,, 19162251, 15252706 </pubmed> | + | <pubmed> 20208166, 20878669, 19162251, 15252706 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 08:57, 30 September 2010
- Description: ferredoxin-NAD(P)+ oxidoreductase
| Gene name | yumC |
| Synonyms | |
| Essential | yes PubMed |
| Product | ferredoxin-NAD(P)+ oxidoreductase |
| Function | redox reactions that involve ferredoxin |
| MW, pI | 36 kDa, 5.573 |
| Gene length, protein length | 996 bp, 332 aa |
| Immediate neighbours | yumB, yuzG |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU32110
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH (according to Swiss-Prot)
- Protein family: ferredoxin--NADP reductase type 2 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): FAD, NADPH PubMed
- Effectors of protein activity:
- Interactions: dimeric protein PubMed
- Localization:
Database entries
- UniProt: O05268
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Hirofumi Komori, Daisuke Seo, Takeshi Sakurai, Yoshiki Higuchi
Crystal structure analysis of Bacillus subtilis ferredoxin-NADP(+) oxidoreductase and the structural basis for its substrate selectivity.
Protein Sci: 2010, 19(12);2279-90
[PubMed:20878669]
[WorldCat.org]
[DOI]
(I p)
Hirofumi Komori, Daisuke Seo, Takeshi Sakurai, Yoshiki Higuchi
Crystallization and preliminary X-ray studies of ferredoxin-NADP+ oxidoreductase encoded by Bacillus subtilis yumC.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 3);301-3
[PubMed:20208166]
[WorldCat.org]
[DOI]
(I p)
Daisuke Seo, Seisuke Okabe, Mitsuhiro Yanase, Kunishige Kataoka, Takeshi Sakurai
Studies of interaction of homo-dimeric ferredoxin-NAD(P)+ oxidoreductases of Bacillus subtilis and Rhodopseudomonas palustris, that are closely related to thioredoxin reductases in amino acid sequence, with ferredoxins and pyridine nucleotide coenzymes.
Biochim Biophys Acta: 2009, 1794(4);594-601
[PubMed:19162251]
[WorldCat.org]
[DOI]
(P p)
Daisuke Seo, Kei Kamino, Kazuhito Inoue, Hidehiro Sakurai
Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC.
Arch Microbiol: 2004, 182(1);80-9
[PubMed:15252706]
[WorldCat.org]
[DOI]
(P p)
