ID Q8NSF8_CORGL Unreviewed; 438 AA.
AC Q8NSF8; Q6M762;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE SubName: Full=Coenzyme F420-dependent N5,N10-methylene tetrahydromethanopterin reductase and related flavin-dependent oxidoreductases {ECO:0000313|EMBL:BAB98110.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:BAB98110.1};
GN OrderedLocusNames=Cgl0717 {ECO:0000313|EMBL:BAB98110.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB98110.1, ECO:0000313|Proteomes:UP000000582};
RN [1] {ECO:0000313|Proteomes:UP000000582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00033748}.
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DR EMBL; BA000036; BAB98110.1; -; Genomic_DNA.
DR RefSeq; NP_599949.1; NC_003450.3.
DR RefSeq; WP_011013841.1; NC_006958.1.
DR AlphaFoldDB; Q8NSF8; -.
DR STRING; 196627.cg0823; -.
DR KEGG; cgl:Cgl0717; -.
DR PATRIC; fig|196627.13.peg.704; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_022256_1_2_11; -.
DR OMA; DIKGRME; -.
DR OrthoDB; 8320141at2; -.
DR BioCyc; CORYNE:G18NG-10279-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016215; NTA_MOA.
DR NCBIfam; TIGR03860; FMN_nitrolo; 1.
DR PANTHER; PTHR30011; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR30011:SF16; C2H2 FINGER DOMAIN TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PIRSF; PIRSF000337; NTA_MOA; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000337-1};
KW FMN {ECO:0000256|PIRSR:PIRSR000337-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAB98110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000582}.
FT DOMAIN 39..380
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT BINDING 57
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 149
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 218
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 219
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
SQ SEQUENCE 438 AA; 47757 MW; 8DE1F583569CAE47 CRC64;
MTPKEIHLNL FAFGAGHHAA AWRAVEGSVE KLGLISWWEE LARTAERGKL DAVFLADGQA
INPVGLENGP GWFLEPVTAL TAMARATNNI GLISTISSTF WQPFHAARMI ASLDHISGGR
AGINVVTSMT DAEARNHGMD ALPGHDVRYA RAAEFIETIT ALWDSWPAES LVMDRAGKFA
DSSLIKSIDH DGEFFQVAGP LNIPSPPQGR PVLFQAGSSP QGREIAAKYA EAIYSVAWDL
EQAQDYRSDI HARATAQGRE PMPVLPGLVT FVGTTVEEAR AKQQALNALL PVKDSLNQLS
FFVGQDCSTW DLDAPPPPLP PLEEFSGPKG RYETVLRIIE SKSPTVRELL GYLAAGGGHA
TFIGTPESIA DEIERWIDEG GADGFNLMPP MLPHSLDDFV DLVVPELQRR GRFRTEYSHT
TLRGHLFNQV AYSARSLV
//