HAMAP annotation rule: MF_01283
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Accession MF_01283
Dates 16-NOV-2007 (Created)
27-SEP-2010 (Last updated, Version 7)
Data class Protein
Names RibBA



Identifier RIBBA
Protein name
RecName: Full=Riboflavin biosynthesis protein ribBA;
RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
Short=DHBP synthase;
EC=4.1.99.12;
RecName: Full=GTP cyclohydrolase-2;
EC=3.5.4.25;
AltName: Full=GTP cyclohydrolase II;
Gene name ribBA
FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate (By similarity).
CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.
CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or manganese (By similarity).
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
SIMILARITY: In the N-terminal section; belongs to the DHBP synthase family.
SIMILARITY: In the C-terminal section; belongs to the GTP cyclohydrolase II family.
Pfam PF00926; DHBP_synthase; 1;
PF00925; GTP_cyclohydro2; 1;
TIGRFAMs TIGR00505; ribA; 1;
TIGR00506; ribB; 1;
GO:0000287; Molecular function: magnesium ion binding.
GO:0003935; Molecular function: GTP cyclohydrolase II activity.
GO:0008270; Molecular function: zinc 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.
From: RIBBA_BACSU (P17620)
Key     From     To       Description   Condition   FTGroup
NP_BIND     251     255       GTP (By similarity)      
NP_BIND     294     296       GTP (By similarity)   E-G-R  
REGION     Nter     199       DHBP synthase      
REGION     26     27       D-ribulose 5-phosphate binding (By similarity)   R-E  
REGION     138     142       D-ribulose 5-phosphate binding (By similarity)   R-x-x-H-T  
REGION     200     Cter       GTP cyclohydrolase II      
ACT_SITE     328     328       Proton acceptor; for GTP cyclohydrolase activity (Potential)   D  
ACT_SITE     330     330       Nucleophile; for GTP cyclohydrolase activity (By similarity)   R  
METAL     27     27       Magnesium or manganese 1 (By similarity)   E  
METAL     27     27       Magnesium or manganese 2 (By similarity)   E  
METAL     141     141       Magnesium or manganese 2 (By similarity)   H  
METAL     256     256       Zinc; catalytic (By similarity)   C  
METAL     267     267       Zinc; catalytic (By similarity)   C  
METAL     269     269       Zinc; catalytic (By similarity)   C  
BINDING     31     31       D-ribulose 5-phosphate (By similarity)   D  
BINDING     162     162       D-ribulose 5-phosphate (By similarity)   E  
BINDING     272     272       GTP (By similarity)   Q  
BINDING     316     316       GTP (By similarity)   T  
BINDING     351     351       GTP (By similarity)   [TS]  
BINDING     356     356       GTP (By similarity)   K  
SITE     124     124       Essential for DHBP synthase activity (By similarity)   H  
SITE     162     162       Essential for DHBP synthase activity (By similarity)   E  



Size range: 388-425 amino acids
Related UniRules: MF_00178 (RISB); MF_00179 (RIBA)
Template: P50855 (RIBBA_ACTPL)
Scope: Bacteria
Fusion: Nter: None; Cter: <Unknown>
Duplicate: None
Plasmid encoded: None
Comments: RibA and RibB are not fused in some organisms (see MF_00179 for RibA and MF_00180 for RibB). Fused with an unknown C-terminal domain in SYNY3.

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