TGNC_ACIAD
ID TGNC_ACIAD Reviewed; 488 AA.
AC Q6F9F7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=(Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone dehydrogenase {ECO:0000303|PubMed:29686076};
DE Short=MFMB dehydrogenase {ECO:0000303|PubMed:29686076};
DE EC=1.2.1.- {ECO:0000269|PubMed:29686076};
GN Name=tgnC {ECO:0000303|PubMed:29686076};
GN OrderedLocusNames=ACIAD2542 {ECO:0000312|EMBL:CAG69307.1};
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, 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 NAD(+)-
CC dependent oxidation of (Z)-2-((N-methylformamido)methylene)-5-
CC hydroxybutyrolactone (MFMB) to yield (E)-2-((N-
CC methylformamido)methylene)succinate (MFMS).
CC {ECO:0000269|PubMed:29686076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-2-((N-methylformamido)methylene)-5-hydroxybutanolactone +
CC H2O + NAD(+) = (E)-2-((N-methylformamido) methylene)succinate + 3
CC H(+) + NADH; Xref=Rhea:RHEA:56912, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:141413, ChEBI:CHEBI:141414;
CC Evidence={ECO:0000269|PubMed:29686076};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for (Z)-2-((N-methylformamido)methylene)-5-
CC hydroxybutyrolactone (MFMB) {ECO:0000269|PubMed:29686076};
CC KM=900 uM for NAD {ECO:0000269|PubMed:29686076};
CC Note=kcat is 2.5 sec(-1) for NAD as substrate.
CC {ECO:0000269|PubMed:29686076};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29686076}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CR543861; CAG69307.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F9F7; -.
DR SMR; Q6F9F7; -.
DR STRING; 62977.ACIAD2542; -.
DR EnsemblBacteria; CAG69307; CAG69307; ACIAD2542.
DR KEGG; aci:ACIAD2542; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_6; -.
DR OMA; WINLSQA; -.
DR OrthoDB; 744602at2; -.
DR BioCyc; ASP62977:ACIAD_RS11545-MON; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..488
FT /note="(Z)-2-((N-methylformamido)methylene)-5-
FT hydroxybutyrolactone dehydrogenase"
FT /id="PRO_0000445262"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT ACT_SITE 282
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 149..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 226..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
FT BINDING 380
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25526"
SQ SEQUENCE 488 AA; 52515 MW; 1A46638494126540 CRC64;
MQQFQLYING KFEDGAAQFD SINPATGEIW AKMPEARTDQ VNRAVDAAEQ AFYDSSWSGL
TASQRGKLLY KLADLVEKSA PRLAALETTD TGKIIRETSS QIAYVAEYYR YYAGLADKIE
GSFIPVDKPD MQAWLVREPV GVVAAIVPWN SQLFLSAVKV GPALAAGCTV VLKASEEAPA
PLLEFAKLID EAGFPAGVVN VITGFGPECG AVLSAHPKVA HIAFTGGPET AKHIVRNSAE
NLAKVSLELG GKSPFIVFAD TDINSALNAQ IAAIFAATGQ SCVAGSRLLI EESIKDEFLQ
RLAERVQSIK MGLPDDMQTE YGPLCTLKQR EKIQQVVQRS VEQGAKLITG GQVCDGAGYY
YPPTILDCSG VSDAQSIHTE LFGPVLSVDT FSTEAEAIQK ANSTPYGLAS GVFTSNLTRA
HRMTRAIRSG IVWLNTYRVV SPLAPFGGYG LSGHGREGGL SAALEYTTTK TVWLRMSDQP
IDDPFVMR
