ID   TGND_ACIAD              Reviewed;         263 AA.
AC   Q6F9F4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=(E)-2-((N-methylformamido)methylene)succinate hydrolase {ECO:0000303|PubMed:29686076};
DE            Short=MFMS hydrolase {ECO:0000303|PubMed:29686076};
DE            EC=3.5.1.- {ECO:0000269|PubMed:29686076};
GN   Name=tgnD {ECO:0000303|PubMed:29686076};
GN   OrderedLocusNames=ACIAD2545 {ECO:0000312|EMBL:CAG69310.1};
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 hydrolysis of
CC       (E)-2-((N-methylformamido)methylene)succinate (MFMS) into formic acid,
CC       succinate semialdehyde (SSA), methylamine and carbon dioxide.
CC       {ECO:0000269|PubMed:29686076}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-2-((N-methylformamido) methylene)succinate + H(+) + 2 H2O
CC         = CO2 + formate + methylamine + succinate semialdehyde;
CC         Xref=Rhea:RHEA:57032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57706,
CC         ChEBI:CHEBI:59338, ChEBI:CHEBI:141414;
CC         Evidence={ECO:0000269|PubMed:29686076};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=222 uM for (E)-2-((N-methylformamido)methylene)succinate (MFMS)
CC         {ECO:0000269|PubMed:29686076};
CC         Note=kcat is 112.3 sec(-1) for (E)-2-((N-
CC         methylformamido)methylene)succinate (MFMS) as substrate.
CC         {ECO:0000269|PubMed:29686076};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29686076}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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; CR543861; CAG69310.1; -; Genomic_DNA.
DR   RefSeq; WP_004928629.1; NC_005966.1.
DR   AlphaFoldDB; Q6F9F4; -.
DR   SMR; Q6F9F4; -.
DR   STRING; 62977.ACIAD2545; -.
DR   ESTHER; aciad-q6f9f4; 6_AlphaBeta_hydrolase.
DR   EnsemblBacteria; CAG69310; CAG69310; ACIAD2545.
DR   GeneID; 45234829; -.
DR   KEGG; aci:ACIAD2545; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_50_3_6; -.
DR   OMA; EAWAPQI; -.
DR   OrthoDB; 1196738at2; -.
DR   BioCyc; ASP62977:ACIAD_RS11560-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..263
FT                   /note="(E)-2-((N-methylformamido)methylene)succinate
FT                   hydrolase"
FT                   /id="PRO_0000445261"
FT   ACT_SITE        96
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q988D4"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000250|UniProtKB:Q988D4"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000250|UniProtKB:Q988D4"
SQ   SEQUENCE   263 AA;  29206 MW;  1FF241428DCBB701 CRC64;
     MISKTLQLSN NRTAHYFEQG EGEPLVLIHG VGMQAEAWYP QIEYFSKHYH VISLDMPGHG
     QSTALAADAQ LQDFVDWAIE CIHTLNLGPV NLAGHSMGSL ITTGVSVTRP DLVKRMAVLN
     GVYKRTHAAR EAVIQRAEAL KQGHLDIETP LQRWFGQSEI EKIASERVKL WLENVNMSGY
     TTAYRAFAQG DLVYADGWSD IECPALVLTG TDDPNSTAEM TIQMAHQAKH GTAIVIENER
     HMVNLTAPEK VNQAMQAWLE TTP