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Q8TT89 (RIBB_METAC) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:MA_0548
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifier188937 [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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2472473,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_0000151824

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
Q8TT89 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 214C3716BFDD17EE

FASTA24727,396
        10         20         30         40         50         60 
MNESTVYECL KYGNENINRA LEVLRAGKMI QIYDSDSREG ETDLVIPAKA VTYKDVKWMR 

        70         80         90        100        110        120 
KDAGGLICVA VDPVASKQLK LPFMADLVRE ASRTSESLGE VVEKDGDLKY DSHSSFSIWV 

       130        140        150        160        170        180 
NHRDTRTGIP DLERALTIRK IGEITEKSLS GNGIRFGNEF RTPGHVALLR AAEGLLDERM 

       190        200        210        220        230        240 
GQTELSVALA RMAGITPAMV VCEMLDDESG RALSKENSKD YGKDHGLVFL EGQEILEAYM 


LWTGSEC 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010299 Genomic DNA. Translation: AAM03992.1.
RefSeqNP_615512.1. NC_003552.1.

3D structure databases

ProteinModelPortalQ8TT89.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1472440.
GenomeReviewsGene locus MA_0548 in contig AE010299_GR.
KEGGmac:MA0548.
NMPDRfig|188937.1.peg.538.

Phylogenomic databases

HOGENOMHBG735778.
OMAGDMIFAA.
ProtClustDBCLSK634377.

Enzyme and pathway databases

BioCycMACE188937:MA0548-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_METAC
AccessionPrimary (citable) accession number: Q8TT89
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 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