Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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FMN_bind

SMART accession number:	SM00900
Description:	This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins.
Interpro abstract (IPR007329):	This conserved region includes the FMN-binding site of the NqrC protein [(PUBMED:11248234)] as well as the NosR and NirI regulatory proteins.
GO component:	membrane (GO:0016020)
GO function:	FMN binding (GO:0010181)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 1991 FMN_bind domains in 1801 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a FMN_bind domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with FMN_bind domain is also avaliable.

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• Cellular role (predicted cellular role)

• Cellular role: interaction
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Barquera B, Hase CC, Gennis RB
  • Expression and mutagenesis of the NqrC subunit of the NQR respiratoryNa(+) pump from Vibrio cholerae with covalently attached FMN.
  • FEBS Lett. 2001; 492: 45-9
  • Display abstract

  • The Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) is presentin the membranes of a number of marine bacteria and pathogenic bacteria.Two of the six subunits of the Na(+)-NQR, NqrB and NqrC, have beenpreviously shown to contain covalently bound flavin adenine mononucleotide(FMN). In the current work, the cloning of nqrC from Vibrio cholerae isreported. The gene has been expressed in V. cholerae and shown to containone equivalent of covalently bound FMN. In contrast, no covalent flavinwas detected when threonine-225 was replaced by leucine. The data showthat the FMN attachment does not require assembly of the enzyme and areconsistent with the unusual threonine attachment site.

• Structure (3D structures containing this domain)

• 3D Structures of FMN_bind domains in PDB

  PDB code	Main view	Title
  3dcz		Crystal structure of putative rnfg subunit of electron transport complex (tm0246) from thermotoga maritima at 1.65 a resolution

• Links (links to other resources describing this domain)

• PFAM	FMN_bind
  INTERPRO	IPR007329

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