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 | |