ID E4TS97_MARTH Unreviewed; 445 AA.
AC E4TS97;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Ftrac_2836 {ECO:0000313|EMBL:ADR22814.1};
OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR22814.1, ECO:0000313|Proteomes:UP000008720};
RN [1] {ECO:0000313|EMBL:ADR22814.1, ECO:0000313|Proteomes:UP000008720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC H-43 {ECO:0000313|Proteomes:UP000008720};
RX PubMed=21677852; DOI=10.4056/sigs.1623941;
RA Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL Stand. Genomic Sci. 4:154-162(2011).
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; CP002349; ADR22814.1; -; Genomic_DNA.
DR RefSeq; WP_013454957.1; NC_014759.1.
DR AlphaFoldDB; E4TS97; -.
DR STRING; 643867.Ftrac_2836; -.
DR KEGG; mtt:Ftrac_2836; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_023210_0_1_10; -.
DR OrthoDB; 9766816at2; -.
DR UniPathway; UPA00253; UER00328.
DR Proteomes; UP000008720; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000008720};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..354
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 445 AA; 51026 MW; D62B594C615A5C12 CRC64;
MKKEIKHIGV LGAGLVGALL SIYLRKRGYK VSLYEKRDDM RKSSADSGRS INLALSRRGI
KALEDIGVIE EVEKIMLPME GRMMHSQDGE LTFQAYGKEG QYINSVSRGN LNKILLEKAE
AAGVEIKFEH TCKSVDLEGT SVTFKTPDAE KTMQFDLLFG SDGAYSKMRQ AMVKKDRFNY
EQYYIPHGYK ELSIPPNEDG DFAIAPNALH IWPRGQYMLI ALPNLDKSFT CTLFFPFEGQ
PSFESLQTPQ QVLNFFKNTF PDSLPHLKNI QEEYFENPTS SLVTVKCEPW VKNNCVLIGD
AAHAIVPFYG QGMNAGFEDC YELNLLLNRH ADDWEMTLDE YQELRKKDGD AIADLALHNF
VEMRDLVADD KFLVQKKIEA KLHEKFPKKW MPLYSMVTFS DLRYSEAFEI GKKQQSIMDD
VMQRPAILEN WESIDLEEIV RKLEE
//
