Reviewed, UniProtKB/Swiss-Prot P0AG40 (RIBF_ECOLI)

Names and origin

Protein names

Recommended name:
    Riboflavin biosynthesis protein ribF
Including the following 2 domains:
    1- Recommended name:
            Riboflavin kinase
              EC=2.7.1.26
        Alternative name(s):
            Flavokinase
    2- Recommended name:
            FMN adenylyltransferase
              EC=2.7.7.2
        Alternative name(s):
            FAD pyrophosphorylase
            FAD synthetase

Gene names

Name:	ribF
Synonyms:	yaaC
Ordered Locus Names:	b0025, JW0023

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + riboflavin = ADP + FMN. ATP + FMN = diphosphate + FAD.
Pathway	Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
Sequence similarities	Belongs to the ribF family.

Ontologies

Keywords
Ligand	ATP-binding FAD FMN Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FMN adenylyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct riboflavin kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
aceE	P0AFG8	1	EBI-542969,EBI-542683

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 313	313	Riboflavin biosynthesis protein ribF		PRO_0000194137
Experimental info
	Sequence conflict	108	1	I → V Ref.1
	Sequence conflict	108	1	I → V Ref.2
	Sequence conflict	128 – 169	42	RFGAG…SSTAV → PLALVVKAISCYYRKLAWNT ASISPVRKLFAEVACASAAR L Ref.1
	Sequence conflict	128 – 169	42	RFGAG…SSTAV → PLALVVKAISCYYRKLAWNT ASISPVRKLFAEVACASAAR L Ref.2
	Sequence conflict	214	1	L → P Ref.1
	Sequence conflict	214	1	L → P Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0AG40-1 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: C0B2EF5499CD30FE	FASTA	313	34,734
	10 20 30 40 50 60 MKLIRGIHNL SQAPQEGCVL TIGNFDGVHR GHRALLQGLQ EEGRKRNLPV MVMLFEPQPL 70 80 90 100 110 120 ELFATDKAPA RLTRLREKLR YLAECGVDYV LCVRFDRRFA ALTAQNFISD LLVKHLRVKF 130 140 150 160 170 180 LAVGDDFRFG AGREGDFLLL QKAGMEYGFD ITSTQTFCEG GVRISSTAVR QALADDNLAL 190 200 210 220 230 240 AESLLGHPFA ISGRVVHGDE LGRTIGFPTA NVPLRRQVSP VKGVYAVEVL GLGEKPLPGV 250 260 270 280 290 300 ANIGTRPTVA GIRQQLEVHL LDVAMDLYGR HIQVVLRKKI RNEQRFASLD ELKAQIARDE 310 LTAREFFGLT KPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Kamio Y., Lin C.-K., Regue M., Wu H.C. J. Biol. Chem. 260:5616-5620(1985) [PubMed: 2985604] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 108; 128-169 AND 214. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M10428 Genomic DNA. Translation: AAA24605.1. U00096 Genomic DNA. Translation: AAC73136.1. AP009048 Genomic DNA. Translation: BAB96594.2.
PIR	QQECIL. A64723.
RefSeq	AP_000689.1. NP_414566.1.
3D structure databases
HSSP	HSSP built from PDB template 1N08 based on UniProtKB O74866.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AG40. 10 interactions.
Genome annotation databases
GeneID	949129.
GenomeReviews	Gene locus JW0023 in contig AP009048_GR. Gene locus b0025 in contig U00096_GR.
KEGG	ecj:JW0023. eco:b0025.
Organism-specific databases
EchoBASE	EB1071.
EcoGene	EG11079. ribF.
CMR	Search...
Phylogenomic databases
HOGENOM	P0AG40.
OMA	P0AG40. GVHLGHR.
Enzyme and pathway databases
BioCyc	EcoCyc:RIBF-MON. MetaCyc:RIBF-MON.
Family and domain databases
InterPro	IPR015864. FAD_synthase. IPR015865. Riboflavin_kinase. IPR002606. Riboflavin_kinase/FAD_synth. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:2.40.30.30. Riboflavin_kinase. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR22749. Riboflavin_kinase. 1 hit.
Pfam	PF06574. FAD_syn. 1 hit. PF01687. Flavokinase. 1 hit. [Graphical view]
PIRSF	PIRSF004491. FAD_Synth. 1 hit.
ProDom	PD003662. FAD_Synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00083. ribF. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RIBF_ECOLI

Accession

Primary (citable) accession number: P0AG40
Secondary accession number(s): P08391, P75621

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	December 20, 2005
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)