ID E0I9L2_9BACL Unreviewed; 448 AA.
AC E0I9L2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Nitrilotriacetate monooxygenase component A/pristinamycin IIA synthase subunit A {ECO:0000313|EMBL:EFM11096.1};
GN ORFNames=PaecuDRAFT_2349 {ECO:0000313|EMBL:EFM11096.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11096.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM11096.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM11096.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00033748}.
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DR EMBL; AEDD01000005; EFM11096.1; -; Genomic_DNA.
DR RefSeq; WP_006038345.1; NZ_AEDD01000005.1.
DR AlphaFoldDB; E0I9L2; -.
DR STRING; 717606.PaecuDRAFT_2349; -.
DR eggNOG; COG2141; Bacteria.
DR OrthoDB; 3265338at2; -.
DR Proteomes; UP000005387; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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 Monooxygenase {ECO:0000313|EMBL:EFM11096.1};
KW Oxidoreductase {ECO:0000313|EMBL:EFM11096.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT DOMAIN 26..384
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT BINDING 59
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 146
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 150
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 220
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 221
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
SQ SEQUENCE 448 AA; 49573 MW; F39D0C4946BACD05 CRC64;
MSQPRKKLHL NVFLMNVGHH EAAWRRKDTS PQHATDIRYF TRLAQIAENA KFDSLFLADV
LSVGKNIRHG SHVGLEPFTL LSALAAVTEH IGLIGTVSTT FNEPFHVARK FASLDHISSG
RAGWNIVTSA SEFEAANFSQ EEHLQHAKRY ERAREFLDVA TKLWDSWQDD AIVFDRESGI
FADDSKVTAI NHAGAYFNVN GPLNVPRAPQ GYPVLVQAGS SEDGKEFAAQ YAEAIFTAQQ
TLAEGQQFYA DVKGRLAKYG RDPDQIKILP GICPIIAPTE SEAKEKEQEL NELTVPAYGL
NQLSGIIGID LSSYPLDGPL PELPPLNEIN GNKSRYQLVT DLAAREHLTI RQLISKLAGG
RGHRVFAGTA IQVADQLEEW FTQGASDGFN VMPPYLPAGL EDFAQLVVPE LQRRGLFRTE
YESRTLRGNY GLARPSNRWA APIVGATR
//
