Difference between revisions of "NifZ"

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=== Database entries ===
=== Database entries ===
* '''Structure:'''
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1EG5 1EG5] (NifS-like protein from Thermotoga maritima, 35% identity, 55% similarity) {{PubMed|10715213}}
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34874 O34874]
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34874 O34874]
Line 120: Line 120:
<pubmed>19348578 </pubmed>
<pubmed>19348578 </pubmed>
==Original publications==
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 17:25, 3 February 2010

  • Description: NifS protein homolog, putative cysteine desulfurase

Gene name nifZ
Synonyms iscSB
Essential no
Product putative cysteine desulfurase
Function thiamine biosynthesis
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
NifZ context.gif
This image was kindly provided by SubtiList

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

  • Structure: 1EG5 (NifS-like protein from Thermotoga maritima, 35% identity, 55% similarity) PubMed
  • 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



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)