ID S5Y682_PARAH Unreviewed; 449 AA.
AC S5Y682;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Monooxygenase {ECO:0000313|EMBL:AGT11155.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:AGT11155.1};
GN ORFNames=JCM7686_pAMI5p089 {ECO:0000313|EMBL:AGT11155.1};
OS Paracoccus aminophilus JCM 7686.
OG Plasmid pAMI5 {ECO:0000313|EMBL:AGT11155.1,
OG ECO:0000313|Proteomes:UP000015480}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT11155.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT11155.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT11155.1};
RC PLASMID=Plasmid pAMI5 {ECO:0000313|Proteomes:UP000015480};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00033748}.
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; CP006653; AGT11155.1; -; Genomic_DNA.
DR RefSeq; WP_020952927.1; NC_022043.1.
DR AlphaFoldDB; S5Y682; -.
DR KEGG; pami:JCM7686_pAMI5p089; -.
DR PATRIC; fig|1367847.3.peg.4122; -.
DR HOGENOM; CLU_022256_1_2_5; -.
DR OrthoDB; 9779442at2; -.
DR Proteomes; UP000015480; Plasmid pAMI5.
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:AGT11155.1};
KW Oxidoreductase {ECO:0000313|EMBL:AGT11155.1};
KW Plasmid {ECO:0000313|EMBL:AGT11155.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT DOMAIN 18..380
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT BINDING 56
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 97
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 147
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 151
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
FT BINDING 222
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000337-1"
SQ SEQUENCE 449 AA; 49190 MW; BBFBFE784F837B95 CRC64;
MSRKIRLGAF LPGGGQHVAA WRHPGSPSDG ATNLAFHIEL AKTAEKGLFD AYFLADGLSA
GFAGGREGGS AKAAGFEPVT LFAALSAHTK RLGFIATAST TYEEPYQLAR KFASLDLVTG
GRAGWNVVTS TGDETARNFS RDTQLPHAER YARAREHVDV VRQLWDSWED DAFLRDKESG
QFFDRDRVHE INYEGEYFKV RGPLNTPRPP QGHPVVVQAG ASEDGRDLAA ATAEVIFTAH
QNLSSAQEFY RDIKARAAAK GRDPREILVM PGVAPFIGRT LGEAQAKYDR LTSLILPEEG
LALLNGLAGG TLDLTGYPLD GPLPPQDVTE GNKSRQVLIR EIADRHGFTI RQLYQYVATA
RGHLTLIGTP KTIVDTLEEW FTSDAADGFN ILPPWLPAGL EDFVGLIVPE LQRRGLFRTE
YEGRTLRENL GLARPENPWT RARSALAAE
//
