| General Information |
| MoonProt ID | 493 |
| First appeared in release | 3.0 |
| Name(s) | Riboflavin biosynthesis protein RibD
Gene: ribD Synonyms:ribG
Recommended name:
Riboflavin biosynthesis protein RibD
Including the following 2 domains:
Diaminohydroxyphosphoribosylaminopyrimidine deaminase (EC:3.5.4.26)
Short name:
DRAP deaminase
Alternative name(s):
Riboflavin-specific deaminase
5-amino-6-(5-phosphoribosylamino)uracil reductase (EC:1.1.1.193)
Alternative name(s):
HTP reductase |
| UniProt ID | P17618 (RIBD_BACSU) |
| GO terms | GO:0055114 oxidation-reduction process
GO:0046872 metal ion binding
GO:0008152 metabolic process
GO:0016787 hydrolase activity
GO:0009231 riboflavin biosynthetic process
GO:0016491 oxidoreductase activity
GO:0003824 catalytic activity
GO:0008835 diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
GO:0008703 5-amino-6-(5-phosphoribosylamino)uracil reductase activity |
| Organisms for which functions have been demonstrated | Bacillus subtilis (strain 168) |
| Sequence length | 361 amino acids |
| FASTA sequence | >sp|P17618|RIBD_BACSU Riboflavin biosynthesis protein RibD OS=Bacillus subtilis (strain 168) OX=224308 GN=ribD PE=1 SV=1
MEEYYMKLALDLAKQGEGQTESNPLVGAVVVKDGQIVGMGAHLKYGEAHAEVHAIHMAGAHAEGADIYVTLEPCSHYGKTPPCAELIINSGIKRVFVAMRDPNPLVAGRGISMMKEAGIEVREGILADQAERLNEKFLHFMRTGLPYVTLKAAASLDGKIATSTGDSKWITSEAARQDAQQYRKTHQSILVGVGTVKADNPSLTCRLPNVTKQPVRVILDTVLSIPEDAKVICDQIAPTWIFTTARADEEKKKRLSAFGVNIFTLETERIQIPDVLKILAEEGIMSVYVEGGSAVHGSFVKEGCFQEIIFYFAPKLIGGTHAPSLISGEGFQSMKDVPLLQFTDITQIGRDIKLTAKPTKE |
| Structure Information |
| PDB ID | 2B3Z,
2D5N,
3EX8,
4G3M. |
| Quaternary structure | tetramer |
| SCOP | 2 domains.
Domain 1:
class 1000002 Alpha and beta proteins (a/b);
fold 2001124 Cytidine deaminase-like;
superfamily 3001838 Cytidine deaminase-like;
family 4000564 Deoxycytidylate deaminase-like;
domain 8025228 2B3Z A:1-145 Riboflavin biosynthesis protein RibD. Species Bacillus subtilis subsp. subtilis str. 168.
Domain 2:
class 1000002 Alpha and beta proteins (a/b);
fold 2000773 Dihydrofolate reductase-like;
superfamily 3001255 Dihydrofolate reductase-like;
family 4003207 RibD C-terminal domain-like;
domain 8025226 2B3Z A:146-359 Riboflavin biosynthesis protein RibD. Species Bacillus subtilis subsp. subtilis str. 168. |
| CATH | 2 Matching CATH Superfamilies.
Superfamily: 3.40.140.10. Cytidine Deaminase, domain 2.
Superfamily: 3.40.430.10. Dihydrofolate Reductase, subunit A.
8 Matching CATH Domains.
Domain: 2b3zA01 PDB code 2b3z, chain A, domain 01. Superfamily: 3.40.140.10.
Domain: 2b3zA02 PDB code 2b3z, chain A, domain 02. Superfamily: 3.40.430.10.
Domain: 2b3zB01 PDB code 2b3z, chain B, domain 01. Superfamily: 3.40.140.10.
Domain: 2b3zB02 PDB code 2b3z, chain B, domain 02. Superfamily: 3.40.430.10.
Domain: 2b3zC01 PDB code 2b3z, chain C, domain 01. Superfamily: 3.40.140.10.
Domain: 2b3zC02 PDB code 2b3z, chain C, domain 02. Superfamily: 3.40.430.10.
Domain: 2b3zD01 PDB code 2b3z, chain D, domain 01. Superfamily: 3.40.140.10.
Domain: 2b3zD02 PDB code 2b3z, chain D, domain 02. Superfamily: 3.40.430.10. |
| TM Helix Prediction | no TM helices
# sp|P17618|RIBD_BACSU Number of predicted TMHs: 0
# sp|P17618|RIBD_BACSU Exp number of AAs in TMHs: 0.01593
# sp|P17618|RIBD_BACSU Exp number, first 60 AAs: 0.00023
# sp|P17618|RIBD_BACSU Total prob of N-in: 0.00995
sp|P17618|RIBD_BACSU TMHMM2.0 outside 1 361 |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
spP17618RIBD_BACSU_Ribof is 361 residues long, with 0 residues (0.00 %) predicted as disordered. The protein has 0 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | deaminase |
| References for function | Chen SC, Chang YC, Lin CH, Lin CH, Liaw SH. Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis. J Biol Chem. 2006 Mar 17;281(11):7605-13. doi: 10.1074/jbc.M510254200. Epub 2005 Nov 24. PMID: 16308316. |
| E.C. number | 3.5.4.26 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | reductase |
| References for function | Chen SC, Chang YC, Lin CH, Lin CH, Liaw SH. Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis. J Biol Chem. 2006 Mar 17;281(11):7605-13. doi: 10.1074/jbc.M510254200. Epub 2005 Nov 24. PMID: 16308316. |
| E.C. number | 1.1.1.193 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |