GenomeNet

Database: UniProt
Entry: A8UKA8_9FLAO
LinkDB: A8UKA8_9FLAO
Original site: A8UKA8_9FLAO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system