NasF

• Description: uroporphyrinogen methyltransferase
  
  

Gene name	nasF
Synonyms	nasBE
Essential	no
Product	uroporphyrinogen methyltransferase
Function	nitrate respiration
Metabolic function and regulation of this protein in SubtiPathways: Alternative nitrogen sources
MW, pI	53 kDa, 6.523
Gene length, protein length	1449 bp, 483 aa
Immediate neighbours	ycgT, nasE
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

respiration, utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

Fur regulon, NsrR regulon, ResD regulon, TnrA regulon

The gene

Basic information

• Locus tag: BSU03280

Expression

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1 (according to Swiss-Prot)

• Protein family: precorrin methyltransferase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P42437

• KEGG entry: [3]

• E.C. number: 2.1.1.107

Expression and regulation

• Operon: nasB-nasC-nasD-nasE-nasF PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • expressed under anaerobic conditions (ResD) PubMed
  • induced by nitric oxide under anaerobic conditions (NsrR) PubMed
  • induced by iron starvation (Fur) PubMed

• Regulatory mechanism:
  • TnrA: transcription activation PubMed
  • ResD: transcription activation PubMed
  • NsrR: transcription repression PubMed
  • Fur: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Sushma Kommineni, Erik Yukl, Takahiro Hayashi, Jacob Delepine, Hao Geng, Pierre Moënne-Loccoz, Michiko M Nakano
Nitric oxide-sensitive and -insensitive interaction of Bacillus subtilis NsrR with a ResDE-controlled promoter.
Mol Microbiol: 2010, 78(5);1280-93
[PubMed:21091510] [WorldCat.org] [DOI] (I p)

Michiko M Nakano, Hao Geng, Shunji Nakano, Kazuo Kobayashi
The nitric oxide-responsive regulator NsrR controls ResDE-dependent gene expression.
J Bacteriol: 2006, 188(16);5878-87
[PubMed:16885456] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

M M Nakano, Y Zhu, M Lacelle, X Zhang, F M Hulett
Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilis.
Mol Microbiol: 2000, 37(5);1198-207
[PubMed:10972836] [WorldCat.org] [DOI] (P p)

Per Johansson, Lars Hederstedt
Organization of genes for tetrapyrrole biosynthesis in gram--positive bacteria.
Microbiology (Reading): 1999, 145 ( Pt 3);529-538
[PubMed:10217486] [WorldCat.org] [DOI] (P p)

M M Nakano, T Hoffmann, Y Zhu, D Jahn
Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE.
J Bacteriol: 1998, 180(20);5344-50
[PubMed:9765565] [WorldCat.org] [DOI] (P p)

L V Wray, A E Ferson, K Rohrer, S H Fisher
TnrA, a transcription factor required for global nitrogen regulation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(17);8841-5
[PubMed:8799114] [WorldCat.org] [DOI] (P p)

K Ogawa, E Akagawa, K Yamane, Z W Sun, M LaCelle, P Zuber, M M Nakano
The nasB operon and nasA gene are required for nitrate/nitrite assimilation in Bacillus subtilis.
J Bacteriol: 1995, 177(5);1409-13
[PubMed:7868621] [WorldCat.org] [DOI] (P p)