TGNA_ACIAD
ID TGNA_ACIAD Reviewed; 310 AA.
AC Q6F9F5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Flavin-dependent trigonelline monooxygenase, reductase component {ECO:0000303|PubMed:29686076};
DE EC=1.5.1.36 {ECO:0000269|PubMed:29686076};
DE AltName: Full=Flavin:NADH reductase {ECO:0000305|PubMed:29686076};
GN Name=tgnA {ECO:0000303|PubMed:29686076};
GN OrderedLocusNames=ACIAD2544 {ECO:0000312|EMBL:CAG69309.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, 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. TgnA catalyzes the reduction
CC of flavin (FMN or FAD) by NADH and supplies the reduced flavin to the
CC oxygenase component TgnB. {ECO:0000269|PubMed:29686076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:31303, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:60531, ChEBI:CHEBI:62787; EC=1.5.1.36;
CC Evidence={ECO:0000269|PubMed:29686076};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31305;
CC Evidence={ECO:0000305|PubMed:29686076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000269|PubMed:29686076};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30149;
CC Evidence={ECO:0000305|PubMed:29686076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:29686076};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21622;
CC Evidence={ECO:0000305|PubMed:29686076};
CC -!- ACTIVITY REGULATION: Maximal reductase activity is achieved only upon
CC trigonelline (TG) binding to the reductase component before interaction
CC with NADH. It seems that TgnA undergoes an allosteric transition upon
CC trigonelline (TG) binding accounting for the positive cooperativity
CC toward NADH oxidation. {ECO:0000269|PubMed:29686076}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=74 uM for NADH {ECO:0000269|PubMed:29686076};
CC Note=kcat is 72 sec(-1) for NADH as substrate.
CC {ECO:0000269|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 non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG69309.1; -; Genomic_DNA.
DR RefSeq; WP_004928626.1; NC_005966.1.
DR AlphaFoldDB; Q6F9F5; -.
DR SMR; Q6F9F5; -.
DR STRING; 62977.ACIAD2544; -.
DR EnsemblBacteria; CAG69309; CAG69309; ACIAD2544.
DR GeneID; 45234828; -.
DR KEGG; aci:ACIAD2544; -.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_896101_0_0_6; -.
DR OMA; WFECSMQ; -.
DR OrthoDB; 1681849at2; -.
DR BioCyc; ASP62977:ACIAD_RS11555-MON; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0036382; F:flavin reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:RHEA.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; FAD; Flavoprotein; FMN; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..310
FT /note="Flavin-dependent trigonelline monooxygenase,
FT reductase component"
FT /id="PRO_0000445258"
FT BINDING 40..43
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q92ZM6"
FT BINDING 57..63
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q92ZM6"
FT BINDING 90..91
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q92ZM6"
FT BINDING 97
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q92ZM6"
SQ SEQUENCE 310 AA; 34415 MW; 3F5DCFBF0338618B CRC64;
MSEMDAVNKI RELRDAFGSF MTGVTVVTTC KDDGTPLGFT ANSFASVSLD PALLLVSIAK
TSSNYHNFAD ASHFAINILA EEQKDVSNIF ARPSDDRFAQ LVWAKSEYQN PLIDGVSAWF
DCTTYQVVDA GDHAILIGKV ENFTSAGFAG LGYYRGAYFT PAKSSTDVIS SMKVMMMALI
GHENKILLEQ TADHKWALPH LMVEKDGAEK ALEKIFATYQ PEASPSFIYS VYDDVTTQQQ
YIAFLCNTPV PTAHKGQFVD LNDLEKLTFT DSALQSMLMR YRKENYLKTY GVYYGNHTSG
TVRQIVKEGV
