ID A0A2N6NQM5_BEABA Unreviewed; 464 AA.
AC A0A2N6NQM5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=6-hydroxynicotinate 3-monooxygenase {ECO:0000313|EMBL:PMB69556.1};
GN Name=nicC_0 {ECO:0000313|EMBL:PMB69556.1};
GN ORFNames=BM221_004200 {ECO:0000313|EMBL:PMB69556.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB69556.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB69556.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB69556.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:PMB69556.1}.
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DR EMBL; MRVG01000004; PMB69556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NQM5; -.
DR OMA; CRNDELG; -.
DR Proteomes; UP000235728; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF215; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:PMB69556.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000235728};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..464
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014679034"
FT DOMAIN 4..355
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 464 AA; 51319 MW; 660CD18AF29A0BDE CRC64;
MLHIVIAGAG IAGLAAAVSL RRAGHHVQLY EQSSLNNEIG AAITIPPNAS RILLAWGVRP
QDWGFVLAEG ASGYDPFTME KTMDFGSKGS AEAIGGAPMY LSHRVDLHNC LKWLATREQG
PGVPAKIHRR SNVAAFFKDP EAPSITLRNG QVIHADLIVG ADGVHSRAAE AVLQHKIEAI
APQHSNICYR FLIPASVLEE DPETRHWNIA NRSRTRVFSH NDTQRRLVTN TVHNFVGLIY
DESARLDAED WQASVKVDEI VDRFKDFHPD IVKVIRKAKD VKRWPLLYRY PLKTWHKDML
VLVGDAAHPM LPHQGQGGAQ SIEDGLVLGI SMLGARSRND IESRFGIYQD VRRDRASVIQ
ILSNIGQDLV QQLQNEVLPY LDKDKIPTNP AQIQQFNFGY DAIQAALEAM RRHEPEFSLP
ANFFDEKVVG VPPKTVLAVH RTGASLPHCG SATTDTGRAA VEIS
//
