| General Information |
| MoonProt ID | 119 |
| First appeared in release | 1.0 |
| Name(s) | Lambda-crystallin
L-gulonate 3-dehydrogenase
Gul3DH
GDH
Gene Name: CRYL1 |
| UniProt ID | P14755 (CRYL1_RABIT), Reviewed |
| GO terms | GO:0006631 fatty acid metabolic process
GO:0055114 oxidation-reduction process
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0005212 structural constituent of eye lens
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042803 protein homodimerization activity
GO:0050104 L-gulonate 3-dehydrogenase activity
GO:0050662 coenzyme binding
GO:0070403 NAD+ binding
GO:0005737 cytoplasm
GO:0005829 cytosol
|
| Organisms for which functions have been demonstrated | Oryctolagus cuniculus (Rabbit) |
| Sequence length | 319 |
| FASTA sequence | >sp|P14755|CRYL1_RABIT Lambda-crystallin OS=Oryctolagus cuniculus GN=CRYL1 PE=1 SV=3
MASPAAGDVLIVGSGLVGRSWAMLFASGGFRVKLYDIEPRQITGALENIRKEMKSLQQSGSLKGSLSAEEQLSLISSCTNLAEAVEGVVHIQECVPENLDLKRKIFAQLDSIVDDRVVLSSSSSCLLPSKLFTGLAHVKQCIVAHPVNPPYYIPLVELVPHPETSPATVDRTHALMRKIGQSPVRVLKEIDGFVLNRLQYAIISEAWRLVEEGIVSPSDLDLVMSDGLGMRYAFIGPLETMHLNAEGMLSYCDRYSEGMKRVLKSFGSIPEFSGATVEKVNQAMCKKVPADPEHLAARREWRDECLKRLAKLKRQMQPQ |
| Structure Information |
| PDB ID | 3ADO,
3ADP |
| Quaternary structure | |
| SCOP | NA |
| CATH | 3.40.50.720, 1.10.1040.10 |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1-4, 62-67, 315-319 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | L-gulonate 3 -dehydrogenase, enzyme
L-gulonate + NAD(+) <=> 3-dehydro-L-gulonate + NADH
Catalysis the NAD-linked dehydrogenation of L-gulonate into dehydro-L-gulonate in the urinate cycle.
|
| References for function | Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase. Ishikura S., Usami N., Araki M., Hara A.
J. Biochem. 137:303-314(2005). PMID: 15809331.
Dimeric crystal structure of rabbit L-gulonate 3-dehydrogenase/lambda-crystallin: insights into the catalytic mechanism. Asada Y, Kuroishi C, Ukita Y, Sumii R, Endo S, Matsunaga T, Hara A, Kunishima N.J Mol Biol. 2010 Sep 3;401(5):906-20. doi: 10.1016/j.jmb.2010.06.069. Epub 2010 Jul 8. PMID: 20620150. |
| E.C. number | 1.1.1.45 |
| Location of functional site(s) | |
| Cellular location of function | Mitochondria |
| Comments | |
| Function 2 |
| Function description | Lambda crystallin
|
| References for function | Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases. Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H., de Jong W.W. J. Biol. Chem. 263:15462-15466(1988).
PMID: 3170592. |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | lens of the eye |
| Comments | |