ID   TGNB_ACIAD              Reviewed;         360 AA.
AC   Q6F9F6;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Flavin-dependent trigonelline monooxygenase, oxygenase component {ECO:0000303|PubMed:29686076};
DE            EC=1.14.14.- {ECO:0000269|PubMed:29686076};
GN   Name=tgnB {ECO:0000303|PubMed:29686076};
GN   OrderedLocusNames=ACIAD2543 {ECO:0000312|EMBL:CAG69308.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000312|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=29686076; DOI=10.1073/pnas.1722368115;
RA   Perchat N., Saaidi P.L., Darii E., Pelle C., Petit J.L., Besnard-Gonnet M.,
RA   de Berardinis V., Dupont M., Gimbernat A., Salanoubat M., Fischer C.,
RA   Perret A.;
RT   "Elucidation of the trigonelline degradation pathway reveals previously
RT   undescribed enzymes and metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E4358-E4367(2018).
CC   -!- FUNCTION: Involved in the degradation of the pyridine ring of
CC       trigonelline (TG; N-methylnicotinate) into succinate and methylamine as
CC       carbon and nitrogen sources, respectively. Catalyzes the insertion of
CC       two oxygens, followed by a ring cleavage of trigonelline to yield (Z)-
CC       2-((N-methylformamido)methylene)-5-hydroxybutyrolactone (MFMB). It is
CC       able to use reduced FMN or FAD. {ECO:0000269|PubMed:29686076}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + N-methylnicotinate + O2 = (Z)-2-((N-
CC         methylformamido)methylene)-5-hydroxybutanolactone + FMN + H(+);
CC         Xref=Rhea:RHEA:17109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:18123, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:141413; Evidence={ECO:0000269|PubMed:29686076};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17110;
CC         Evidence={ECO:0000305|PubMed:29686076};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FADH2 + N-methylnicotinate + O2 = (Z)-2-((N-
CC         methylformamido)methylene)-5-hydroxybutanolactone + FAD + H(+);
CC         Xref=Rhea:RHEA:57028, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:18123, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:141413; Evidence={ECO:0000269|PubMed:29686076};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57029;
CC         Evidence={ECO:0000305|PubMed:29686076};
CC   -!- SUBUNIT: Homodimer. The trigonelline monooxygenase is composed of a
CC       reductase component TgnA and an oxygenase component TgnB.
CC       {ECO:0000269|PubMed:29686076}.
CC   -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; CR543861; CAG69308.1; -; Genomic_DNA.
DR   RefSeq; WP_004928624.1; NC_005966.1.
DR   AlphaFoldDB; Q6F9F6; -.
DR   SMR; Q6F9F6; -.
DR   STRING; 62977.ACIAD2543; -.
DR   EnsemblBacteria; CAG69308; CAG69308; ACIAD2543.
DR   GeneID; 45234827; -.
DR   KEGG; aci:ACIAD2543; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_3_0_6; -.
DR   OMA; FRYHDTF; -.
DR   OrthoDB; 1434838at2; -.
DR   BioCyc; ASP62977:ACIAD_RS11550-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..360
FT                   /note="Flavin-dependent trigonelline monooxygenase,
FT                   oxygenase component"
FT                   /id="PRO_0000445260"
SQ   SEQUENCE   360 AA;  41152 MW;  7FB97EFB6F235F5B CRC64;
     MRFSLFVHME RVSDQQTQKQ LYDEMIELCQ IADRGGMHAI WTGEHHAMNF TIAPNPFLNI
     ADLANKTKHV RLGTGTVVAP FWHPIKLAGE AAMTDIISNG RLDIGIARGA YSFEYERMVP
     GMDAWSAGQR LREMIPAIKN LWKGDYEHNG EFWQFPKTTS APQPLQQPNP PIWVAARDPN
     SHEFAVQNGC NVQVTPLHLG DEEVEKLMGH FNSACEKFQD IERPEIMLLR HTYVADSEED
     AQVAANEMNV FYNYFGAWFK NEREINQGLI APLSDEEIAA HPFYTPEAMR KNNVIGQAQE
     VIDRLKAYEA MGYDEYSFWI DTGMSFERKK ASLERMINEV MPAFSESKVD RRHATISAVY