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Escherichia coli K-12 substr. MG1655 Enzyme: bifunctional riboflavin kinase / FMN adenylyltransferase



Gene: ribF Accession Numbers: EG11079 (EcoCyc), b0025, ECK0026

Synonyms: yaaC

Regulation Summary Diagram: ?

Summary:
It is thought that ribF encodes a bifunctional protein with riboflavin kinase and FMN adenylyltransferase activities. These enzymes transform riboflavin into the coenzyme forms of FMN and FAD, respectively [Neidhardt96].

A published patent contains experimental evidence that partial deletions or point mutations in the N-terminal domain of RibF ("protein X") selectively affect the FMN adenylyltransferase activity of the enzyme [Kitatsuji93].

ribF can complement the lethal defect of a ribC mutant (lacking riboflavin kinase and FMN adenylyltransferase activities) in Bacillus subtilis [Mack98]. The G23 residue appears to be essential for the FMN adenylyltrasferase, but not the riboflavin kinase activity [Kitatsuji93]. ribF is likely essential for growth in E. coli [Gerdes02, Baba06].

Gene Citations: [Miller87, Brissette91, Miller87a]

Locations: cytosol

Map Position: [21,407 -> 22,348] (0.46 centisomes)
Length: 942 bp / 313 aa

Molecular Weight of Polypeptide: 34.734 kD (from nucleotide sequence), 35 kD (experimental) [Kamio85 ]

Unification Links: ASAP:ABE-0000091 , CGSC:35833 , DIP:DIP-35789N , EchoBASE:EB1071 , EcoGene:EG11079 , EcoliWiki:b0025 , Mint:MINT-1256514 , ModBase:P0AG40 , OU-Microarray:b0025 , PortEco:ribF , PR:PRO_000023754 , Pride:P0AG40 , Protein Model Portal:P0AG40 , RefSeq:NP_414566 , RegulonDB:EG11079 , SMR:P0AG40 , String:511145.b0025 , UniProt:P0AG40

Relationship Links: InterPro:IN-FAMILY:IPR002606 , InterPro:IN-FAMILY:IPR014729 , InterPro:IN-FAMILY:IPR015864 , InterPro:IN-FAMILY:IPR015865 , InterPro:IN-FAMILY:IPR023465 , InterPro:IN-FAMILY:IPR023468 , Panther:IN-FAMILY:PTHR22749 , Pfam:IN-FAMILY:PF01687 , Pfam:IN-FAMILY:PF06574 , Smart:IN-FAMILY:SM00904

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006747 - FAD biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0009231 - riboflavin biosynthetic process Inferred by computational analysis [GOA01a]
GO:0009398 - FMN biosynthetic process Inferred by computational analysis [UniProtGOA12]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003919 - FMN adenylyltransferase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Mack98]
GO:0008531 - riboflavin kinase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Mack98]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks cofactors, small molecule carriers riboflavin

Essentiality data for ribF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Last-Curated ? 10-Apr-2007 by Keseler I , SRI International


Enzymatic reaction of: riboflavin kinase

Synonyms: flavokinase, ATP:riboflavin 5'-phosphotransferase

EC Number: 2.7.1.26

riboflavin + ATP <=> ADP + FMN + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Alternative Substrates [Comment 2]:

In Pathways: flavin biosynthesis I (bacteria and plants)


Enzymatic reaction of: FMN adenylyltransferase

Synonyms: FMN adenylyltransferase, FAD pyrophosphorylase, ATP:FMN adenylyltransferase, FAD synthetase

EC Number: 2.7.7.2

ATP + FMN + H+ <=> FAD + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: flavin biosynthesis I (bacteria and plants)


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 108
[Kamio85, Yura92, UniProt10]
Alternate sequence: I → V; UniProt: (in Ref. 1 and 2);
Sequence-Conflict 128 -> 169
[Kamio85, Yura92, UniProt10]
Alternate sequence: RFGAGREGDFLLLQKAGMEYGFDITSTQTFCEGGVRISSTAV → PLALVVKAISCYYRKLAWNTASISPVRKLFAEVACASAARL; UniProt: (in Ref. 1 and 2);
Sequence-Conflict 214
[Kamio85, Yura92, UniProt10]
Alternate sequence: L → P; UniProt: (in Ref. 1 and 2);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0025 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11079; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Brissette91: Brissette JL, Weiner L, Ripmaster TL, Model P (1991). "Characterization and sequence of the Escherichia coli stress-induced psp operon." J Mol Biol 220(1);35-48. PMID: 1712397

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes02: Gerdes SY, Scholle MD, D'Souza M, Bernal A, Baev MV, Farrell M, Kurnasov OV, Daugherty MD, Mseeh F, Polanuyer BM, Campbell JW, Anantha S, Shatalin KY, Chowdhury SA, Fonstein MY, Osterman AL (2002). "From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways." J Bacteriol 184(16);4555-72. PMID: 12142426

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Kamio85: Kamio Y, Lin CK, Regue M, Wu HC (1985). "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon." J Biol Chem 260(9);5616-20. PMID: 2985604

Kitatsuji93: Kitatsuji K, Ishino S, Teshiba S, Arimoto M (1993). "Process for producing flavine nucleotides." European Patent Application number 92119308.

Mack98: Mack M, van Loon AP, Hohmann HP (1998). "Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC." J Bacteriol 180(4);950-5. PMID: 9473052

Miller87: Miller KW, Bouvier J, Stragier P, Wu HC (1987). "Identification of the genes in the Escherichia coli ileS-lsp operon. Analysis of multiple polycistronic mRNAs made in vivo." J Biol Chem 262(15);7391-7. PMID: 3294831

Miller87a: Miller KW, Wu HC (1987). "Cotranscription of the Escherichia coli isoleucyl-tRNA synthetase (ileS) and prolipoprotein signal peptidase (lsp) genes. Fine-structure mapping of the lsp internal promoter." J Biol Chem 262(1);389-93. PMID: 2432063

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Yura92: Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 1992;20(13);3305-8. PMID: 1630901

Other References Related to Gene Regulation

Bouvier91a: Bouvier J, Stragier P (1991). "Nucleotide sequence of the lsp-dapB interval in Escherichia coli." Nucleic Acids Res 19(1);180. PMID: 2011499


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Nov 21, 2014, biocyc14.