Difference between revisions of "NifZ"
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|style="background:#ABCDEF;" align="center"|'''Function''' || thiamine biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || thiamine biosynthesis | ||
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+ | |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/thiamin.html Thiamin]''' | ||
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 41 kDa, 6.34 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 41 kDa, 6.34 |
Revision as of 11:03, 16 February 2010
- Description: NifS protein homolog, putative cysteine desulfurase
Gene name | nifZ |
Synonyms | iscSB |
Essential | no |
Product | putative cysteine desulfurase |
Function | thiamine biosynthesis |
Metabolic function and regulation of this protein in SubtiPathways: Thiamin | |
MW, pI | 41 kDa, 6.34 |
Gene length, protein length | 1143 bp, 381 aa |
Immediate neighbours | ytbJ, braB |
Gene sequence (+200bp) | Protein sequence |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU29590
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: O34874
- 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
Reviews
Christopher T Jurgenson, Tadhg P Begley, Steven E Ealick
The structural and biochemical foundations of thiamin biosynthesis.
Annu Rev Biochem: 2009, 78;569-603
[PubMed:19348578]
[WorldCat.org]
[DOI]
(I p)
Original publications
J T Kaiser, T Clausen, G P Bourenkow, H D Bartunik, S Steinbacher, R Huber
Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly.
J Mol Biol: 2000, 297(2);451-64
[PubMed:10715213]
[WorldCat.org]
[DOI]
(P p)