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Information on EC 1.5.99.B2 - proline dehydrogenase (acceptor)

for references in articles please use BRENDA:EC1.5.99.B2
preliminary BRENDA-supplied EC number
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UNIPROT: O59089 not found.
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
Synonyms
prodh2, pro dehydrogenase, l-prodh, more
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-proline:acceptor oxidoreductase
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
the beta subunit of the L-proline dehydrogenase complex is the catalytic component containing FAD as a cofactor
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
beta-subunit of the L-proline dehydrogenase complex
SwissProt
Manually annotated by BRENDA team
beta-subunit of the L-proline dehydrogenase complex
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O59089_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
382
0
42686
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of PDH1, which is a heterooctameric complex containing three different cofactors: FAD, FMN, and ATP. The structure is determined by x-ray crystallography to a resolution of 2.86 A. The structure of the beta subunit, which is an L-proline dehydrogenase catalytic component containing FAD as a cofactor, is similar to that of monomeric sarcosine oxidase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsuge, H.; Kawakami, R.; Sakuraba, H.; Ago, H.; Miyano, M.; Aki, K.; Katunuma, N.; Ohshima, T.
Crystal structure of a novel FAD-, FMN-, and ATP-containing L-proline dehydrogenase complex from Pyrococcus horikoshii
J. Biol. Chem.
280
31045-31049
2005
Pyrococcus horikoshii, Pyrococcus horikoshii (O59089), Pyrococcus horikoshii OT-3 (O59089)
Manually annotated by BRENDA team