1.5.5.2: proline dehydrogenase

This is an abbreviated version!
For detailed information about proline dehydrogenase, go to the full flat file.

Word Map on EC 1.5.5.2

Reaction

L-proline
+
a quinone
=
(S)-1-pyrroline-5-carboxylate
+
a quinol

Synonyms

bifunctional dye-linked L-proline/NADH dehydrogenase complex, dye-linked L-proline dehydrogenase, FAD-dependent L-proline oxidoreductase, JcProDH, L-proline dehydrogenase, L-proline:FAD oxidoreductase, PdhB, PDHbeta, PF1246, PF1798, PH1364, PH1751, PRODH, proDH-B1, proDH-B2, PRODH/POX, ProDH1, proline dehydrogenase, proline dehydrogenase 1, proline dehydrogenase/oxidase, proline oxidase, proline/P5C dehydrogenase, prub, PutA, PutA flavoprotein, PutA proline dehydrogenase, Tc00.1047053506411.30, TcPRODH, TK0117, TK0122, TPpdhbeta, TtProDH

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.5 With a quinone or similar compound as acceptor
                1.5.5.2 proline dehydrogenase

Cofactor

Cofactor on EC 1.5.5.2 - proline dehydrogenase

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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme Q1
phenazine methosulfate
-
-
[4Fe-4S]-center
O59088; O59089
-
additional information
-
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit
-