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P45273 (RISA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin synthase alpha chain

EC=2.5.1.9
Gene names
Name:ribE
Synonyms:ribC
Ordered Locus Names:HI_1613
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione By similarity.

Catalytic activity

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

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2.

Subunit structure

Oligomer that consist of 3 alpha subunits and 60 beta subunits By similarity.

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   DomainRepeat
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

riboflavin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Riboflavin synthase alpha chain
PRO_0000068167

Regions

Repeat1 – 9797Lumazine-binding 1
Repeat98 – 19598Lumazine-binding 2

Sequences

Sequence LengthMass (Da)Tools
P45273 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B7C2172F88BC1DA4

FASTA20422,590
        10         20         30         40         50         60 
MFTGIVQGTA PIHSIKEKAN FRTQVVKLLP EMRKDLEIGA SIANNGVCLT VTEINGDLVS 

        70         80         90        100        110        120 
FDLMQETLKI TNLGTVKVGD YVNIERAMQM GTEIGGHLLS GHIYCTAKIS DIIASENNRQ 

       130        140        150        160        170        180 
IWFELPSADV MKYILTKGFV AVDGISLTIG EVRDTQFCVN LIPETLQRTL MGRRKVGDIV 

       190        200 
NIEIDPQTQA IVDTVENYLQ SKNF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC23257.1.
PIRE64132.
RefSeqNP_439755.1. NC_000907.1.

3D structure databases

ProteinModelPortalP45273.
SMRP45273. Positions 1-202.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID950465.
GenomeReviewsGene locus HI_1613 in contig L42023_GR.
KEGGhin:HI1613.
NMPDRfig|71421.1.peg.1529.
PATRIC20191957. VBIHaeInf48452_1686.
TIGRHI_1613.

Phylogenomic databases

HOGENOMHBG289809.
OMAHILSGHV.
PhylomeDBP45273.
ProtClustDBPRK09289.

Enzyme and pathway databases

BioCycHINF71421:HI_1613-MONOMER.

Family and domain databases

InterProIPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR001783. Lumazine-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:2.40.30.20. G3DSA:2.40.30.20. 2 hits.
KOK00793.
PANTHERPTHR21098. Lumazine_bd. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 2 hits.
TIGRFAMsTIGR00187. RibE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRISA_HAEIN
AccessionPrimary (citable) accession number: P45273
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families