Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3,4-dihydroxy-2-butanone 4-phosphate synthase

Gene

ribB

Organism
Sphaerobacter thermophilus (strain DSM 20745 / S 6022)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.UniRule annotationSAAS annotation

Catalytic activityi

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Magnesium or manganese.UniRule annotation
  • Mn2+SAAS annotation

Pathwayi: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate.UniRule annotationSAAS annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 3,4-dihydroxy-2-butanone 4-phosphate synthase (ribB)
This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi28Magnesium or manganese 1UniRule annotation1
Metal bindingi28Magnesium or manganese 2UniRule annotation1
Binding sitei32SubstrateUniRule annotation1
Sitei128Essential for catalytic activityUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Sitei166Essential for catalytic activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Riboflavin biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, ManganeseUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00275; UER00399.

Names & Taxonomyi

Protein namesi
Recommended name:
3,4-dihydroxy-2-butanone 4-phosphate synthaseUniRule annotation (EC:4.1.99.12UniRule annotation)
Short name:
DHBP synthaseUniRule annotation
Gene namesi
Name:ribBUniRule annotation
Ordered Locus Names:Sthe_1970Imported
OrganismiSphaerobacter thermophilus (strain DSM 20745 / S 6022)Imported
Taxonomic identifieri479434 [NCBI]
Taxonomic lineageiBacteriaChloroflexiSphaerobacteridaeSphaerobacteralesSphaerobacterineaeSphaerobacteraceaeSphaerobacter
Proteomesi
  • UP000002027 Componenti: Chromosome 1

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi479434.Sthe_1970.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 28Substrate bindingUniRule annotation2
Regioni142 – 146Substrate bindingUniRule annotation5

Sequence similaritiesi

Belongs to the DHBP synthase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4107QZQ. Bacteria.
COG0108. LUCA.
HOGENOMiHOG000115444.
KOiK14652.
OMAiQMAKLIR.
OrthoDBiPOG091H008U.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00180. RibB. 1 hit.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00506. ribB. 1 hit.

Sequencei

Sequence statusi: Complete.

D1C584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLATIEQAI AALRAGRFVI IVDGPDRENE GDLCIAGQFI TPEAVNFIVR
60 70 80 90 100
EARGLLCAAM APEWVDRLRL PLMVDPASNS APFGTAFTVS VEARQGVTTG
110 120 130 140 150
ISAHDRARTI RTLADPASTP ADFAMPGHVF PLRARPGGVL ERPGQTEAAV
160 170 180 190 200
DLARLAGLHP VVAICEIMAD DGTMARLPEL ERFATRHDIP IISVADLAAV
210 220 230
RRAQADRHPA GVADHSPAGT AAREGTAYGC
Length:230
Mass (Da):24,299
Last modified:January 19, 2010 - v1
Checksum:i3E5AC3CC147F1D70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001823 Genomic DNA. Translation: ACZ39401.1.

Genome annotation databases

EnsemblBacteriaiACZ39401; ACZ39401; Sthe_1970.
KEGGisti:Sthe_1970.
PATRICi32426755. VBISphThe120955_1990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001823 Genomic DNA. Translation: ACZ39401.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi479434.Sthe_1970.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACZ39401; ACZ39401; Sthe_1970.
KEGGisti:Sthe_1970.
PATRICi32426755. VBISphThe120955_1990.

Phylogenomic databases

eggNOGiENOG4107QZQ. Bacteria.
COG0108. LUCA.
HOGENOMiHOG000115444.
KOiK14652.
OMAiQMAKLIR.
OrthoDBiPOG091H008U.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00399.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00180. RibB. 1 hit.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00506. ribB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiD1C584_SPHTD
AccessioniPrimary (citable) accession number: D1C584
Entry historyi
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: November 30, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.