NasF

• Description: uroporphyrinogen methyltransferase
  
  

Gene name	nasF
Synonyms	nasBE
Essential	no
Product	uroporphyrinogen methyltransferase
Function	nitrate respiration
Gene expression levels in SubtiExpress: nasF
Metabolic function and regulation of this protein in SubtiPathways: nasF
MW, pI	53 kDa, 6.523
Gene length, protein length	1449 bp, 483 aa
Immediate neighbours	ycgT, nasE
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

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

• Expression browser: 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)