ID A0A0T1WL68_9MYCO Unreviewed; 483 AA.
AC A0A0T1WL68;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=5,10-methylene tetrahydromethanopterin reductase {ECO:0000313|EMBL:KQY10180.1};
GN ORFNames=ASD37_01485 {ECO:0000313|EMBL:KQY10180.1};
OS Mycobacterium sp. Root135.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY10180.1, ECO:0000313|Proteomes:UP000051127};
RN [1] {ECO:0000313|EMBL:KQY10180.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY10180.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY10180.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY10180.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00033748}.
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:KQY10180.1}.
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DR EMBL; LMEZ01000001; KQY10180.1; -; Genomic_DNA.
DR RefSeq; WP_056549626.1; NZ_LMEZ01000001.1.
DR AlphaFoldDB; A0A0T1WL68; -.
DR STRING; 1736457.ASD37_01485; -.
DR OrthoDB; 8320141at2; -.
DR Proteomes; UP000051127; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT DOMAIN 23..388
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT REGION 436..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 154
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 230
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
SQ SEQUENCE 483 AA; 52807 MW; 56203BEAEECA6DFC CRC64;
MTRPIRFNAF DMNCVAHQSP GLWRHPQDRS SEYKDLSYWA DLARLLERGR FDGLFIADVL
GTYDVYGASD EAAIRQAAQV PVNDPLLLVS AMALVTEHLG FGITTGTGFE HPYPFARRVS
TLDHLTKGRV GWNVVTGYLP SAARNMGQTD QPAHDARYDH ADEYLEVLYK LWEGSWEDDA
VIRDRERGVF TDPDKVHHIG HAGTHFTVPG IHLSEPSPQR TPVMFQAGAS PRGVRFAAEN
AEAIFTAAPT KAILRETVTT IRRELELAGR DPYAAKIYNL STVITAETDE EARAKHAEYL
SYGDPEGALV FMSGWMGVDL ASYGLDEPIG NVDSNAILSA VKAFQSADPD GGEWAVRDIA
NWGKIGGIGP LIVGSGERVA DVLQEWVAET DVDGFNLAYA ITPGTFADFV DHVVPVLTAR
GAYQSEYAPG TLRNKLFGRG DRLPDEHRGS RYRVGGPSST IIERPSTKPS SSSSTASQPT
ASR
//
