Reviewed, UniProtKB/Swiss-Prot P22990 (RIBF_PSEFL)

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

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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	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 riboflavin kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 311	311	Riboflavin biosynthesis protein ribF		PRO_0000194141

Sequences

	Sequence		Length	Mass (Da)
	P22990-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: E4ED0EF97C064D60	FASTA	311	33,898
	10 20 30 40 50 60 MQLVRGLHNL RPEHRGCVAT IGNFDGVHRG HQAILARLRE RAVELGVPSC VVIFEPQPRE 70 80 90 100 110 120 FFTPETAPAR LALARQAATA GGEGVDRVLC LAFNQRLRSL SAAEFVDRIL VDGLGVQHLE 130 140 150 160 170 180 VGDDFHFGCD RVGDFDFLQH AGVNQGFTVE AAQTVELDGL RVSSTQVRNA LAAADFDLAE 190 200 210 220 230 240 RLLGRPFRIA GRVLHGQKLA RQLGTPTANV QLKRRRVPLT GVYLVSVDID GQSWPGVANI 250 260 270 280 290 300 GVRPTVAGDG KAHLEVHLLD FAGDLYDRRL TVVFHQKLRE EQRFASLEAL KTAINADVAA 310 ARALAAPSAH R

References

[1]	"Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes." Isaki L., Beers R., Wu H.C. J. Bacteriol. 172:6512-6517(1990) [PubMed: 2121716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 49323 / NCIMB 10586.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M35367 Genomic DNA. Translation: AAA26021.1.
PIR	E37152.
3D structure databases
HSSP	HSSP built from PDB template 1NB9 based on UniProtKB Q969G6.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.26. 329. 2.7.7.2. 329.
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_PSEFL

Accession

Primary (citable) accession number: P22990

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 47 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)