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Q59263

- RIBF_CORAM

UniProt

Q59263 - RIBF_CORAM

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Protein

Riboflavin biosynthesis protein RibF

Gene
ribF
Organism
Corynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Status
Reviewed - 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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. FMN adenylyltransferase activity Source: UniProtKB-EC
  3. riboflavin kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. FAD biosynthetic process Source: UniProtKB-UniPathway
  2. FMN biosynthetic process Source: UniProtKB-UniPathway
  3. riboflavin biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.7.2. 1639.
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Riboflavin biosynthesis protein RibFPRO_0000194136Add
BLAST

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi7 – 93
Beta strandi17 – 226
Helixi29 – 4517
Beta strandi48 – 569
Helixi58 – 625
Beta strandi70 – 723
Helixi74 – 8310
Beta strandi87 – 926
Turni94 – 963
Beta strandi97 – 1004
Helixi103 – 1097
Helixi110 – 1145
Beta strandi117 – 1237
Beta strandi127 – 1293
Helixi130 – 1323
Helixi136 – 1427
Turni143 – 1464
Beta strandi147 – 1526
Helixi164 – 1729
Helixi176 – 1838
Beta strandi188 – 1925
Beta strandi200 – 2023
Beta strandi208 – 2136
Beta strandi222 – 23110
Beta strandi239 – 2413
Beta strandi247 – 25711
Turni258 – 2603
Beta strandi264 – 2718
Beta strandi282 – 29211
Helixi300 – 32324
Turni325 – 3273
Beta strandi330 – 3334

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X0KX-ray1.95A/B1-338[»]
3ZUGX-ray2.05A/B1-338[»]
ProteinModelPortaliQ59263.

Miscellaneous databases

EvolutionaryTraceiQ59263.

Family & Domainsi

Sequence similaritiesi

Belongs to the RibF family.

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

MDIWYGTAAV PKDLDNSAVT IGVFDGVHRG HQKLINATVE KAREVGAKAI    50
MVTFDPHPVS VFLPRRAPLG ITTLAERFAL AESFGIDGVL VIDFTRELSG 100
TSPEKYVEFL LEDTLHASHV VVGANFTFGE NAAGTADSLR QICQSRLTVD 150
VIDLLDDEGV RISSTTVREF LSEGDVARAN WALGRHFYVT GPVVRGAGRG 200
GKELGFPTAN QYFHDTVALP ADGVYAGWLT ILPTEAPVSG NMEPEVAYAA 250
AISVGTNPTF GDEQRSVESF VLDRDADLYG HDVKVEFVDH VRAMEKFDSV 300
EQLLEVMAKD VQKTRTLLAQ DVQAHKMAPE TYFLQAES 338
Length:338
Mass (Da):36,844
Last modified:November 1, 1996 - v1
Checksum:iB714FD885412CC68
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D37967 Genomic DNA. Translation: BAA07182.1.
PIRiJC4008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D37967 Genomic DNA. Translation: BAA07182.1 .
PIRi JC4008.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2X0K X-ray 1.95 A/B 1-338 [» ]
3ZUG X-ray 2.05 A/B 1-338 [» ]
ProteinModelPortali Q59263.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00276 ; UER00406 .
UPA00277 ; UER00407 .
BRENDAi 2.7.7.2. 1639.

Miscellaneous databases

EvolutionaryTracei Q59263.

Family and domain databases

Gene3Di 2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProi IPR015864. 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 ]
PANTHERi PTHR22749. PTHR22749. 1 hit.
Pfami PF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF004491. FAD_Synth. 1 hit.
SMARTi SM00904. Flavokinase. 1 hit.
[Graphical view ]
SUPFAMi SSF82114. SSF82114. 1 hit.
TIGRFAMsi TIGR00083. ribF. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli."
    Nakagawa S., Igarashi A., Ohta T., Hagihara T., Fujio T., Aisaka K.
    Biosci. Biotechnol. Biochem. 59:694-702(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6872 / DSM 20305 / KCTC 1019 / NCTC 2399.
  2. "Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes."
    Manstein D.J., Pai E.F.
    J. Biol. Chem. 261:16169-16173(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18, CHARACTERIZATION.
    Strain: ATCC 6872 / DSM 20305 / KCTC 1019 / NCTC 2399.

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: September 3, 2014
This is version 72 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

External Data

Dasty 3

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