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Q8PW86 (RIBB_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3,4-dihydroxy-2-butanone 4-phosphate synthase

Short name=DHBP synthase
EC=4.1.99.12
Gene names
Name:ribB
Ordered Locus Names:MM_1710
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. HAMAP MF_00180

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_00180

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180

Subunit structure

Homodimer By similarity. HAMAP MF_00180

Sequence similarities

Belongs to the DHBP synthase family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3,4-dihydroxy-2-butanone-4-phosphate synthase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2472473,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_0000151826

Regions

Region38 – 392Substrate binding By similarity
Region179 – 1835Substrate binding By similarity

Sites

Metal binding391Magnesium or manganese 1 By similarity
Metal binding391Magnesium or manganese 2 By similarity
Binding site431Substrate By similarity
Binding site2031Substrate By similarity
Site1651Essential for catalytic activity By similarity
Site2031Essential for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PW86 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: BDF2C89BC08D5138

FASTA24727,268
        10         20         30         40         50         60 
MSENMAYECL KYSNENINRA LEALRAGKMI QIYDSDSREG ETDLVIPAKA VTYTDVKWMR 

        70         80         90        100        110        120 
KDAGGLICVA VDPVASKQLK LPFMADLVRE ASKTSDSLGE VVEKDGDLKY DAHSSFSLWV 

       130        140        150        160        170        180 
NHRDTRTGIP DIERALTIRK IGEITEESLS GNGVRFGNEF RTPGHVALLR AAEGLLDERM 

       190        200        210        220        230        240 
GQTELSVALA RMAGITPAMV VCEMLDDDSG KALSKEKSKE YGKEHGLVFL EGREIVEAYL 


LWAGTDC 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM31406.1.
RefSeqNP_633734.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PW86.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1480052.
GenomeReviewsGene locus MM_1710 in contig AE008384_GR.
KEGGmma:MM_1710.
NMPDRfig|192952.1.peg.1710.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG735778.
OMAGDMIFAA.
ProtClustDBCLSK634377.

Enzyme and pathway databases

BioCycMMAZ192952:MM1710-MONOMER.

Family and domain databases

HAMAPMF_00180. RibB.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
KOK02858.
PfamPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMSSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMsTIGR00506. RibB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBB_METMA
AccessionPrimary (citable) accession number: Q8PW86
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2002
Last modified: November 16, 2011
This is version 51 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