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Annotation rule MF_00180
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General rule information [?]

Accession MF_00180
Dates 1-JUN-2001 (Created)
18-NOV-2019 (Last updated, Version 22)
Name RibB
Templates P0A7J0 (RIBB_ECOLI); Q60364 (RIBB_METJA): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
Short=DHBP synthase;
Gene name

Comments [?]

Function Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic activity RHEA:18457: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Cofactor Mg(2+)
Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Subunit Homodimer.
Similarity Belongs to the DHBP synthase family.

Keywords [?]

Gene Ontology [?]

GO:0000287; Molecular function: magnesium ion binding.
GO:0008686; Molecular function: 3,4-dihydroxy-2-butanone-4-phosphate synthase activity.
GO:0030145; Molecular function: manganese ion binding.
GO:0009231; Biological process: riboflavin biosynthetic process.

Cross-references [?]

Pfam PF00926; DHBP_synthase; 1;
TIGRFAMs TIGR00506; RibB; 1;

Features [?]

From: RIBB_METJA (Q60364)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     25     26       Substrate binding     R-E  
REGION     161     165       Substrate binding     R-x-x-[HQ]-T  
METAL     26     26       Magnesium or manganese 1     E  
METAL     26     26       Magnesium or manganese 2     E  
METAL     164     164       Magnesium or manganese 2     H  
BINDING     30     30       Substrate     D  
BINDING     185     185       Substrate     E  
SITE     147     147       Essential for catalytic activity     H  
SITE     185     185       Essential for catalytic activity     E  

Additional information [?]

Size range 200-247 amino acids
Related rules MF_01283 (RIBBA supersedes the current rule)
Fusion Nter: None; Cter: <ribA-like>
Comments RibA and RibB are fused in some organisms (see MF_01283 for bifunctional RibBA). Some ribB are followed by a ribA-like domain, which does not seem to code for GTP cyclohydrolase II activity because it lacks all the residues important for activity.