ID A0A238U7G5_9FLAO Unreviewed; 470 AA.
AC A0A238U7G5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Kynurenine 3-monooxygenase {ECO:0000256|HAMAP-Rule:MF_01971};
DE EC=1.14.13.9 {ECO:0000256|HAMAP-Rule:MF_01971};
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000256|HAMAP-Rule:MF_01971};
GN Name=kmo {ECO:0000256|HAMAP-Rule:MF_01971,
GN ECO:0000313|EMBL:SNR15139.1};
GN ORFNames=TJEJU_1405 {ECO:0000313|EMBL:SNR15139.1};
OS Tenacibaculum jejuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=584609 {ECO:0000313|EMBL:SNR15139.1, ECO:0000313|Proteomes:UP000215214};
RN [1] {ECO:0000313|EMBL:SNR15139.1, ECO:0000313|Proteomes:UP000215214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: KCTC 22618 {ECO:0000313|Proteomes:UP000215214};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic
CC acid. {ECO:0000256|HAMAP-Rule:MF_01971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine +
CC H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349;
CC EC=1.14.13.9; Evidence={ECO:0000256|ARBA:ARBA00000886,
CC ECO:0000256|HAMAP-Rule:MF_01971};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_01971};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 1/3. {ECO:0000256|HAMAP-Rule:MF_01971}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01971}.
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DR EMBL; LT899436; SNR15139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238U7G5; -.
DR KEGG; tje:TJEJU_1405; -.
DR OrthoDB; 9766816at2; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000215214; Chromosome tjeju.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR HAMAP; MF_01971; Kynurenine_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027545; Kynurenine_monooxygenase.
DR PANTHER; PTHR46028; KYNURENINE 3-MONOOXYGENASE; 1.
DR PANTHER; PTHR46028:SF2; KYNURENINE 3-MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01971};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01971};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01971};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01971};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01971};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_01971};
KW Reference proteome {ECO:0000313|Proteomes:UP000215214}.
FT DOMAIN 6..360
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 470 AA; 53530 MW; 70F9686013114A63 CRC64;
MTKQDKILIV GAGLCGSLLA LRLAQRGYKI EVYESRPDLR KVDISAGRSI NLALSDRGLK
SLRLAGVEEQ AKALCIPMYG RLIHDIEGNT FASNYSGRTG EYINSVSRQD LNALLLDEAE
KHENVNIHFN TKCTRIDIEN TVAHFKSYKT DEEFSVNPDI IFGADGAGSI LRKSYELERK
FLFSYSQDYL THGYKELEIP ADKLGNHQIS KDHLHIWPRG EYMLIALPNL DGSFTVTLFL
SYEEGKFNFE NLTTEEEVTH FFETQFPDAL ALIPNIKDEF FNNPTGALGT VKCSPWMYKN
KTLIIGDAAH AIVPFYGQGM NASFEDVAVF DGVLERFEDD WEQIFKTYQQ ERKKDTDAIA
DLAVDNYYEM RDHVANPLFK QKRKLEMDLE EKFPESYYSK YSMVTFNEDI GYNEAMKKGR
AQDKALLNLI ADAEVSTSEN MSAQELEIVL NKVNHETKEI LTEDKIAGLK
//
