Q2OB_COMTE
ID Q2OB_COMTE Reviewed; 10 AA.
AC P80465;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 11-DEC-2019, entry version 43.
DE RecName: Full=Quinoline 2-oxidoreductase beta chain;
DE EC=1.3.99.17 {ECO:0000269|PubMed:7556204};
DE Flags: Fragment;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=63;
RX PubMed=7556204; DOI=10.1111/j.1432-1033.1995.tb20841.x;
RA Schach S., Tshisuaka B., Fetzner S., Lingens F.;
RT "Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase
RT from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-
RT methylquinoline degradation.";
RL Eur. J. Biochem. 232:536-544(1995).
CC -!- FUNCTION: Converts (3-methyl-)-quinoline to (3-methyl-)2-oxo-1,2-
CC dihydroquinoline. {ECO:0000269|PubMed:7556204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + quinoline = AH2 + quinolin-2(1H)-one;
CC Xref=Rhea:RHEA:17749, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17362, ChEBI:CHEBI:17499, ChEBI:CHEBI:18289;
CC EC=1.3.99.17; Evidence={ECO:0000269|PubMed:7556204};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:7556204};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:7556204};
CC -!- PATHWAY: Xenobiotic degradation; quinoline degradation.
CC -!- SUBUNIT: Heterohexamer of two alpha chains, two beta chains, and two
CC gamma chains. {ECO:0000305}.
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DR UniPathway; UPA00239; -.
DR GO; GO:0018523; F:quinoline 2-oxidoreductase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..>10
FT /note="Quinoline 2-oxidoreductase beta chain"
FT /id="PRO_0000097130"
FT NON_TER 10
SQ SEQUENCE 10 AA; 1242 MW; C2E2C25DD9CDC769 CRC64;
MKFPAFAYXR