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Q885J3 (RISB2_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
6,7-dimethyl-8-ribityllumazine synthase 2

Short name=DMRL synthase 2
Short name=Lumazine synthase 2
EC=2.5.1.9
Alternative name(s):
Riboflavin synthase 2 beta chain
Gene names
Name:ribH2
Synonyms:ribH-2
Ordered Locus Names:PSPTO_1839
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length170 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 beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine By similarity. HAMAP MF_00178

Catalytic activity

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. HAMAP MF_00178

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2. HAMAP MF_00178

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1701706,7-dimethyl-8-ribityllumazine synthase 2 HAMAP MF_00178
PRO_0000134790

Sequences

Sequence LengthMass (Da)Tools
Q885J3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CED60719A95553C4

FASTA17018,805
        10         20         30         40         50         60 
MQPTAIDSKS KSHPNERVAF IQACWHKDIV DQSRKGFVAE MAKQGYAESD IDIFEVGGAF 

        70         80         90        100        110        120 
EIPLHAKLLA NTGRYAGIVG AALVVDGGIY RHEFVAQSVV SALMQVQLET EVPVFSVVLT 

       130        140        150        160        170 
PHHFHAGEEH QKFFFDHFSH KGEEAAKTCA DTLNKVRSLR RLDAQQKAAC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO55358.1.
RefSeqNP_791663.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ885J3.
SMRQ885J3. Positions 17-146.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1183480.
GenomeReviewsGene locus PSPTO_1839 in contig AE016853_GR.
KEGGpst:PSPTO_1839.
NMPDRfig|223283.1.peg.1801.
PATRIC19994944. VBIPseSyr93040_1869.
TIGRPSPTO_1839.

Phylogenomic databases

HOGENOMHBG311126.
OMARRYTAIV.
ProtClustDBPRK12419.

Enzyme and pathway databases

BioCycPSYR223283:PSPTO_1839-MONOMER.

Family and domain databases

HAMAPMF_00178. Lumazine_synth.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
KOK00794.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB2_PSESM
AccessionPrimary (citable) accession number: Q885J3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families