ID A8UKA8_9FLAO Unreviewed; 466 AA.
AC A8UKA8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ORFNames=FBALC1_03662 {ECO:0000313|EMBL:EDP71550.1};
OS Flavobacteriales bacterium ALC-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP71550.1, ECO:0000313|Proteomes:UP000003630};
RN [1] {ECO:0000313|EMBL:EDP71550.1, ECO:0000313|Proteomes:UP000003630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALC-1 {ECO:0000313|EMBL:EDP71550.1,
RC ECO:0000313|Proteomes:UP000003630};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP71550.1}.
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DR EMBL; ABHI01000002; EDP71550.1; -; Genomic_DNA.
DR AlphaFoldDB; A8UKA8; -.
DR STRING; 391603.FBALC1_03662; -.
DR eggNOG; COG0654; Bacteria.
DR OrthoDB; 9766816at2; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000003630; Unassembled WGS sequence.
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:UP000003630}.
FT DOMAIN 7..360
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 466 AA; 52831 MW; 1C1C7E2092C9CBB3 CRC64;
MSNKQQNILI IGAGLCGSLL ALRLGQRGYN VTVYEMRPDL RSTDISAGRS INLAFSDRGN
KAMKLVGIED KVKDLCIPMN GRMLHDKEGN TFLSNYSGRD HEYINSISRG ELNGLLLTEA
EKHDNVTIHF NKKCKSVDFE KTTALFKDYH TKDEFIEDAD CIIATDGAGS ALRKSYYLEK
KFLFSFSQDY LTHGYKELSI LPAEDGGYKT YKNALHIWPR GDFMVIALPN LDGSFTVTLF
LSYDEGEYNF NNLTTPEIVT EFFQKEFPDA LELMPNLVED FFENPTAPLG TVKCSPWHYK
GNTLLMGDSA HAIVPFYGQG MNASFEDVVE FDKVLDQNLE NWEATFEAYE KNRKKDTDAI
ADLAVDNFHE MKSHVGQAIF KEKRKIEMEL ENKFPEDYSS KYSLVTFNED IGYREAMLRG
RAQDKAILNM LSDGVISTED DITAILDKVK TETEAILEDD KIAGLR
//