Riboflavin kinase
     (EC 2.7.1.26)
     (Flavokinase)
FMN adenylyltransferase
     (EC 2.7.7.2)
     (FAD pyrophosphorylase)
     (FAD synthetase)

Gene name

	Name:	ribF
	OrderedLocusNames:	BUsg_143

From

Buchnera aphidicola subsp. Schizaphis graminum

[TaxID: 98794]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).

Comments

CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN.
CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1 .
PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin: step 1/1 .
SIMILARITY: Belongs to the ribF family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE013218; AAM67711.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660500.1; -.

3D structure databases

HSSP

O74866; 1N08. [HSSP ENTRY / PDB]

ModBase

Q8K9Z1.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG143-MON; -.

Ontologies

GO:0003919;	Molecular function: FMN adenylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008531;	Molecular function: riboflavin kinase activity (inferred from electronic annotation from InterPro).
GO:0009231;	Biological process: riboflavin biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:2.40.30.30; Riboflavin_kinase; 1.
G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.

PANTHER

PTHR22749; Riboflavin_kinase; 1.

Pfam

PF06574; FAD_syn; 1.
PF01687; Flavokinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF004491; FAD_Synth; 1.

ProDom

PD003662; FAD_Synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00083; ribF; 1.

Genome annotation databases

GeneID

1005960; -.

GenomeReviews

AE013218_GR; BUsg_143.

KEGG

bas:BUsg143; -.

Phylogenomic databases

HOGENOM

Q8K9Z1; -.

Genome annotation databases

CMR

Q8K9Z1; BUsg_143.

Other

ProtoNet

Q8K9Z1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; FAD; FMN; Multifunctional enzyme; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 312`	`312`		`Riboflavin biosynthesis protein ribF.`	`PRO_0000194135`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 36139 Da [This is the MW of the unprocessed precursor]

CRC64: AEC2E18F28082DF4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLIRGIHNL KKINSNSAVS IGNFDGVHLG HQKLLSNLYK IGKKNNILTV LILFEPQPLE 

        70         80         90        100        110        120 
FLNNKNSPKR LTTIQNKIKY IQSWKIDIIL CIKFNESFSS LSAEKFIKNI LITKLNIKFI 

       130        140        150        160        170        180 
IIGDDFRFGS KRNGNISLLK EIGYQYNFKV IEISSLLYKN KIKISSTNIR KCLLENKIEL 

       190        200        210        220        230        240 
ARKLLGRPFS ISGRVIHGNK IGRKLGYPTA NISLRKNIPL NNGVYAVKIS CFFNKKFVGI 

       250        260        270        280        290        300 
CNIGIKPSYF SSKKHRLLEV HLFNFNLNLY EEKIEVFLYK KIRNECFFSS KNKLKEQISK 

       310 
DIEIVKKYFN LI

Q8K9Z1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools