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Q44680

- RISA_BACAM

UniProt

Q44680 - RISA_BACAM

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Protein
Riboflavin synthase
Gene
ribE, ribB
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil By similarity.

Catalytic activityi

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine.

Pathwayi

GO - Molecular functioni

  1. oxidoreductase activity Source: InterPro
  2. riboflavin synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. riboflavin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin synthase (EC:2.5.1.9)
Short name:
RS
Gene namesi
Name:ribE
Synonyms:ribB
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Riboflavin synthase
PRO_0000068158Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ44680.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 9696Lumazine-binding 1
Add
BLAST
Repeati97 – 19397Lumazine-binding 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 63Substrate binding By similarity
Regioni47 – 493Substrate binding By similarity
Regioni61 – 666Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR21098. PTHR21098. 1 hit.
PfamiPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMiSSF63380. SSF63380. 2 hits.
TIGRFAMsiTIGR00187. ribE. 1 hit.
PROSITEiPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q44680-1 [UniParc]FASTAAdd to Basket

« Hide

MFTGIVEETG TIQAIKKTGL SMALTIAASK VTSDVRLGDS IAVNGICLTV    50
TGFSDNQFTV DVMPETVKAT SLNGLSKGSK VNLERAMSAN GRFGGHFVSG 100
HVDGTAEITR IEKKSNAVYY DLKLSPELTK TLVLKGSITV DGVSSTIFGL 150
SDESVTVSVI PHTISETIFR TKAVGSIVNI ECDMIGKYLY RFLHKTEQTK 200
SNQTITEAFF SENGF 215
Length:215
Mass (Da):23,089
Last modified:November 1, 1996 - v1
Checksum:i5A5174315DFE0033
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95955 Genomic DNA. Translation: CAA65190.1.
PIRiT50542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95955 Genomic DNA. Translation: CAA65190.1 .
PIRi T50542.

3D structure databases

ProteinModelPortali Q44680.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00275 ; UER00405 .

Family and domain databases

Gene3Di 2.40.30.20. 2 hits.
InterProi IPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
PANTHERi PTHR21098. PTHR21098. 1 hit.
Pfami PF00677. Lum_binding. 2 hits.
[Graphical view ]
PIRSFi PIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMi SSF63380. SSF63380. 2 hits.
TIGRFAMsi TIGR00187. ribE. 1 hit.
PROSITEi PS51177. LUMAZINE_BIND. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Riboflavin biosynthetic genes in Bacillus amyloliquefaciens: primary structure, organization and regulation of activity."
    Gusarov I.I., Kreneva R.A., Podcharniaev D.A., Iomantas I.U.V., Abalakina E.G., Stoinova N.V., Perumov D.A., Kozlov I.U.I.
    Mol. Biol. (Mosk.) 31:446-453(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A 50.

Entry informationi

Entry nameiRISA_BACAM
AccessioniPrimary (citable) accession number: Q44680
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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