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Protein

Riboflavin biosynthesis protein RibF

Gene

ribF

Organism
Corynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + riboflavin = ADP + FMN.
ATP + FMN = diphosphate + FAD.

Enzyme regulationi

Higher divalent cation concentrations lead to decrease in the turnover of riboflavin and the 5'-phosphotransferase activity, while the adenylyltransferase activity increases. With magnesium ions the highest turnover of riboflavin is observed between pH 6 and 7.5, while that of FAD is between 7.0 and 9.0. With zinc ions a steady increase in riboflavin turnover is observed between pH 4.5 and 10, while FAD is the major product at pH 7.0 and decreases rapidly above pH 8.0.

Pathwayi: FAD biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.
Proteins known to be involved in this subpathway in this organism are:
  1. Riboflavin biosynthesis protein RibF (ribF)
This subpathway is part of the pathway FAD biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FAD from FMN, the pathway FAD biosynthesis and in Cofactor biosynthesis.

Pathwayi: FMN biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FMN from riboflavin (ATP route).
Proteins known to be involved in this subpathway in this organism are:
  1. Riboflavin biosynthesis protein RibF (ribF)
This subpathway is part of the pathway FMN biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FMN from riboflavin (ATP route), the pathway FMN biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.26. 959.
2.7.7.2. 959.
UniPathwayiUPA00276; UER00406.
UPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin biosynthesis protein RibF
Including the following 2 domains:
Riboflavin kinase (EC:2.7.1.26)
Alternative name(s):
Flavokinase
FMN adenylyltransferase (EC:2.7.7.2)
Alternative name(s):
FAD pyrophosphorylase
FAD synthase
Gene namesi
Name:ribF
OrganismiCorynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Taxonomic identifieri1697 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001941361 – 338Riboflavin biosynthesis protein RibFAdd BLAST338

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi7 – 9Combined sources3
Beta strandi17 – 22Combined sources6
Helixi29 – 45Combined sources17
Beta strandi48 – 56Combined sources9
Helixi58 – 62Combined sources5
Beta strandi70 – 72Combined sources3
Helixi74 – 83Combined sources10
Beta strandi87 – 92Combined sources6
Turni94 – 96Combined sources3
Beta strandi97 – 100Combined sources4
Helixi103 – 109Combined sources7
Helixi110 – 114Combined sources5
Beta strandi117 – 123Combined sources7
Beta strandi127 – 129Combined sources3
Helixi130 – 132Combined sources3
Helixi136 – 142Combined sources7
Turni143 – 146Combined sources4
Beta strandi147 – 152Combined sources6
Helixi164 – 172Combined sources9
Helixi176 – 183Combined sources8
Beta strandi188 – 192Combined sources5
Helixi200 – 204Combined sources5
Beta strandi209 – 212Combined sources4
Beta strandi222 – 231Combined sources10
Beta strandi239 – 241Combined sources3
Beta strandi247 – 255Combined sources9
Turni258 – 260Combined sources3
Beta strandi266 – 271Combined sources6
Beta strandi282 – 292Combined sources11
Helixi300 – 324Combined sources25
Turni325 – 327Combined sources3
Helixi329 – 331Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X0KX-ray1.95A/B1-338[»]
3ZUGX-ray2.05A/B1-338[»]
4UZEX-ray2.34A/B1-338[»]
4UZFX-ray2.52A/B1-338[»]
5A88X-ray2.08A/B/C/D183-338[»]
5A89X-ray1.65A/B183-338[»]
5A8AX-ray1.80A/B183-338[»]
ProteinModelPortaliQ59263.
SMRiQ59263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59263.

Family & Domainsi

Sequence similaritiesi

Belongs to the RibF family.Curated

Family and domain databases

Gene3Di2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR015864. FAD_synthase.
IPR023468. Riboflavin_kinase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR22749. PTHR22749. 1 hit.
PfamiPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF004491. FAD_Synth. 1 hit.
SMARTiSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMiSSF82114. SSF82114. 1 hit.
TIGRFAMsiTIGR00083. ribF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIWYGTAAV PKDLDNSAVT IGVFDGVHRG HQKLINATVE KAREVGAKAI
60 70 80 90 100
MVTFDPHPVS VFLPRRAPLG ITTLAERFAL AESFGIDGVL VIDFTRELSG
110 120 130 140 150
TSPEKYVEFL LEDTLHASHV VVGANFTFGE NAAGTADSLR QICQSRLTVD
160 170 180 190 200
VIDLLDDEGV RISSTTVREF LSEGDVARAN WALGRHFYVT GPVVRGAGRG
210 220 230 240 250
GKELGFPTAN QYFHDTVALP ADGVYAGWLT ILPTEAPVSG NMEPEVAYAA
260 270 280 290 300
AISVGTNPTF GDEQRSVESF VLDRDADLYG HDVKVEFVDH VRAMEKFDSV
310 320 330
EQLLEVMAKD VQKTRTLLAQ DVQAHKMAPE TYFLQAES
Length:338
Mass (Da):36,844
Last modified:November 1, 1996 - v1
Checksum:iB714FD885412CC68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37967 Genomic DNA. Translation: BAA07182.1.
PIRiJC4008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37967 Genomic DNA. Translation: BAA07182.1.
PIRiJC4008.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X0KX-ray1.95A/B1-338[»]
3ZUGX-ray2.05A/B1-338[»]
4UZEX-ray2.34A/B1-338[»]
4UZFX-ray2.52A/B1-338[»]
5A88X-ray2.08A/B/C/D183-338[»]
5A89X-ray1.65A/B183-338[»]
5A8AX-ray1.80A/B183-338[»]
ProteinModelPortaliQ59263.
SMRiQ59263.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00276; UER00406.
UPA00277; UER00407.
BRENDAi2.7.1.26. 959.
2.7.7.2. 959.

Miscellaneous databases

EvolutionaryTraceiQ59263.

Family and domain databases

Gene3Di2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR015864. FAD_synthase.
IPR023468. Riboflavin_kinase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR22749. PTHR22749. 1 hit.
PfamiPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF004491. FAD_Synth. 1 hit.
SMARTiSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMiSSF82114. SSF82114. 1 hit.
TIGRFAMsiTIGR00083. ribF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRIBF_CORAM
AccessioniPrimary (citable) accession number: Q59263
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.