ID   DMFAA_PARAH             Reviewed;         141 AA.
AC   C9DQ22;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=N,N-dimethylformamidase alpha subunit {ECO:0000250|UniProtKB:Q9LCC1};
DE            EC=3.5.1.56;
DE   AltName: Full=N,N-dimethylformamidase light chain {ECO:0000250|UniProtKB:Q9LCC1};
GN   Name=dmfA1 {ECO:0000312|EMBL:ACV81785.1};
OS   Paracoccus aminophilus.
OG   Plasmid pAMI2 {ECO:0000312|EMBL:ACV81785.1}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=34003;
RN   [1] {ECO:0000312|EMBL:ACV81785.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49673 / DSM 8538 / JCM 7686 / NBRC 16710;
RX   PubMed=17158670; DOI=10.1128/jb.01610-06;
RA   Dziewit L., Jazurek M., Drewniak L., Baj J., Bartosik D.;
RT   "The SXT conjugative element and linear prophage N15 encode toxin-
RT   antitoxin-stabilizing systems homologous to the tad-ata module of the
RT   Paracoccus aminophilus plasmid pAMI2.";
RL   J. Bacteriol. 189:1983-1997(2007).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:ACV81785.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 49673 / DSM 8538 / JCM 7686 / NBRC 16710;
RX   PubMed=20118371; DOI=10.1128/aem.01926-09;
RA   Dziewit L., Dmowski M., Baj J., Bartosik D.;
RT   "Plasmid pAMI2 of Paracoccus aminophilus JCM 7686 carries N,N-
RT   dimethylformamide degradation-related genes whose expression is activated
RT   by a LuxR family regulator.";
RL   Appl. Environ. Microbiol. 76:1861-1869(2010).
CC   -!- FUNCTION: Hydrolyzes N,N-dimethylformamide, and to a lesser extent N,N-
CC       dimethylacetamide and N,N-diethylacetamide. Has no activity against the
CC       substituted amides N-methylformamide, N-ethylformamide, N-
CC       ethylformamide and N-methylacetamide or the unsubstituted amides
CC       formamide, nicotinamide, acetoamide, benzamide, acetamide and
CC       acrylamide (By similarity). {ECO:0000250|UniProtKB:Q9LCC1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N,N-dimethylformamide = dimethylamine + formate;
CC         Xref=Rhea:RHEA:19517, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:17741, ChEBI:CHEBI:58040; EC=3.5.1.56;
CC         Evidence={ECO:0000250|UniProtKB:Q9LCC1};
CC   -!- SUBUNIT: Heterotetramer of two DmfA1 (alpha) and two DmfA2 (beta)
CC       subunits. {ECO:0000250}.
CC   -!- INDUCTION: By N,N-dimethylformamide. {ECO:0000269|PubMed:20118371}.
CC   -!- CAUTION: It is not known which subunit of DmfA1 or DmfA2 possesses
CC       catalytic activity. {ECO:0000305}.
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DR   EMBL; GQ410978; ACV81785.1; -; Genomic_DNA.
DR   RefSeq; WP_012476891.1; NC_010847.2.
DR   RefSeq; YP_003208119.1; NC_010847.2.
DR   AlphaFoldDB; C9DQ22; -.
DR   SMR; C9DQ22; -.
DR   GO; GO:0050116; F:N,N-dimethylformamidase activity; IEA:UniProtKB-EC.
PE   2: Evidence at transcript level;
KW   Hydrolase; Plasmid.
FT   CHAIN           1..141
FT                   /note="N,N-dimethylformamidase alpha subunit"
FT                   /id="PRO_0000404195"
SQ   SEQUENCE   141 AA;  17220 MW;  2F4C9CDFDF5936DA CRC64;
     MNQRRENYVS DPSAYPDRSA DWYEYFDRKR REEIIEIIDS HPEIIDEHER NPFGYRNHPS
     PHLQRVHNYF RMQPTFGKYY IYTEREWSSY RIAEIREFGK LPVLTDDSFA TEEEAMHAVF
     LKRIEDVRNE LSQAEQREIA N