UniProtKB - Q02008 (RIBB_PHOLE)
Protein
3,4-dihydroxy-2-butanone 4-phosphate synthase
Gene
ribB
Organism
Photobacterium leiognathi
Status
Functioni
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.By similarity
Catalytic activityi
- EC:4.1.99.12
Cofactori
Mg2+By similarity, Mn2+By similarityNote: Binds 2 divalent metal cations per subunit. Magnesium or manganese.By similarity
: riboflavin biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate.Proteins known to be involved in this subpathway in this organism are:
- 3,4-dihydroxy-2-butanone 4-phosphate synthase (ribB), 3,4-dihydroxy-2-butanone 4-phosphate synthase (ribB), 3,4-dihydroxy-2-butanone 4-phosphate synthase (ribB), 3,4-dihydroxy-2-butanone 4-phosphate synthase (ribB), 3,4-dihydroxy-2-butanone 4-phosphate synthase (ribB)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 28 | Magnesium or manganese 1By similarity | 1 | |
Metal bindingi | 28 | Magnesium or manganese 2By similarity | 1 | |
Binding sitei | 32 | SubstrateBy similarity | 1 | |
Sitei | 126 | Essential for catalytic activityBy similarity | 1 | |
Metal bindingi | 143 | Magnesium or manganese 2By similarity | 1 | |
Binding sitei | 164 | SubstrateBy similarity | 1 | |
Sitei | 164 | Essential for catalytic activityBy similarity | 1 |
GO - Molecular functioni
- 3,4-dihydroxy-2-butanone-4-phosphate synthase activity Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
- manganese ion binding Source: UniProtKB-UniRule
GO - Biological processi
- riboflavin biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Lyase |
Biological process | Riboflavin biosynthesis |
Ligand | Magnesium, Manganese, Metal-binding |
Enzyme and pathway databases
UniPathwayi | UPA00275;UER00399 |
Names & Taxonomyi
Protein namesi | Recommended name: 3,4-dihydroxy-2-butanone 4-phosphate synthase (EC:4.1.99.12)Short name: DHBP synthase |
Gene namesi | Name:ribB |
Organismi | Photobacterium leiognathi |
Taxonomic identifieri | 553611 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Photobacterium |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000151821 | 1 – 364 | 3,4-dihydroxy-2-butanone 4-phosphate synthaseAdd BLAST | 364 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 201 | DHBP synthaseAdd BLAST | 201 | |
Regioni | 27 – 28 | Substrate bindingBy similarity | 2 | |
Regioni | 140 – 144 | Substrate bindingBy similarity | 5 | |
Regioni | 202 – 364 | GTP cyclohydrolase II-likeAdd BLAST | 163 |
Sequence similaritiesi
In the N-terminal section; belongs to the DHBP synthase family.Curated
In the C-terminal section; belongs to the GTP cyclohydrolase II family.Curated
Family and domain databases
HAMAPi | MF_00180 RibB, 1 hit |
InterProi | View protein in InterPro IPR017945 DHBP_synth_RibB-like_a/b_dom IPR000422 DHBP_synthase_RibB IPR032677 GTP_cyclohydro_II IPR036144 RibA-like_sf |
Pfami | View protein in Pfam PF00926 DHBP_synthase, 1 hit PF00925 GTP_cyclohydro2, 1 hit |
SUPFAMi | SSF142695 SSF142695, 1 hit SSF55821 SSF55821, 1 hit |
TIGRFAMsi | TIGR00506 ribB, 1 hit |
i Sequence
Sequence statusi: Complete.
Q02008-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MALSSAKEII DDIRQGRMVI LMDDESRENE GDLIIASEMV TPEAINFMAT
60 70 80 90 100
HGRGLICLTL SKARCKTLNL PLMVQGNNDN FSTPFTISIE AAKYVTTGIS
110 120 130 140 150
ASDRAKTVLA AVAPNAKSTD IVMPGHIFPL MAQDGGVLIR AGHTEAGCDV
160 170 180 190 200
ARLAGLEPSS VIVEILNEDG SMARRPQLEI FAEKHGLKLG TIADLIEYRT
210 220 230 240 250
QQESHIERIS EYELNTEYGI FTLVTYRDTI DNQAHFALCK GEIQAKAATL
260 270 280 290 300
VRVHVKDTLK DILQVGLSQW SLEAAMQRIQ TEDGVLVIIS QQESPKTLFE
310 320 330 340 350
KLDMYAKEQP NSPHSGIVQS RNIGLGSQIL ADLGVKKIRL LSNSNQGYRA
360
LSGFGLEVVE YIYD
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M90094 Genomic DNA Translation: AAA73229.1 |
PIRi | JC1188 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M90094 Genomic DNA Translation: AAA73229.1 |
PIRi | JC1188 |
3D structure databases
SMRi | Q02008 |
ModBasei | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00275;UER00399 |
Family and domain databases
HAMAPi | MF_00180 RibB, 1 hit |
InterProi | View protein in InterPro IPR017945 DHBP_synth_RibB-like_a/b_dom IPR000422 DHBP_synthase_RibB IPR032677 GTP_cyclohydro_II IPR036144 RibA-like_sf |
Pfami | View protein in Pfam PF00926 DHBP_synthase, 1 hit PF00925 GTP_cyclohydro2, 1 hit |
SUPFAMi | SSF142695 SSF142695, 1 hit SSF55821 SSF55821, 1 hit |
TIGRFAMsi | TIGR00506 ribB, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RIBB_PHOLE | |
Accessioni | Q02008Primary (citable) accession number: Q02008 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | July 1, 1993 | |
Last modified: | September 18, 2019 | |
This is version 88 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Documents
- SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways