ID   DMFAA_ALCSP             Reviewed;         132 AA.
AC   Q9LCC1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=N,N-dimethylformamidase alpha subunit {ECO:0000303|PubMed:10664842, ECO:0000312|EMBL:BAA90663.1};
DE            EC=3.5.1.56;
DE   AltName: Full=N,N-dimethylformamidase light chain {ECO:0000303|Ref.2};
GN   Name=dmfA1 {ECO:0000312|EMBL:BAA90663.1};
OS   Alcaligenes sp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=512;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA90663.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=KUFA-1 {ECO:0000312|EMBL:BAA90663.1};
RX   PubMed=10664842; DOI=10.1271/bbb.63.2091;
RA   Hasegawa Y., Tokuyama T., Iwaki H.;
RT   "Cloning and expression of the N,N-dimethylformamidase gene from
RT   Alcaligenes sp. strain KUFA-1.";
RL   Biosci. Biotechnol. Biochem. 63:2091-2096(1999).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RA   Hasegawa Y., Matsuo M., Sigemoto Y., Sakai T., Tokuyama T.;
RT   "Purification and characterization of N,N-dimethylformamidase from
RT   Alcaligenes sp. KUFA-1.";
RL   J. Ferment. Bioeng. 63:2091-2096(1999).
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. {ECO:0000269|PubMed:10664842, ECO:0000269|Ref.2}.
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:0000269|PubMed:10664842, ECO:0000269|Ref.2};
CC   -!- ACTIVITY REGULATION: Activity is slightly inhibited by Mg(2+) and
CC       Mn(2+), and slightly increased by Cu(2+). Activity is slightly
CC       inhibited by the chelating agents 8-hydroxyquinoline,
CC       ethylenediaminetetraacetate, o-phenanthroline and 2,2'-bipyridyl.
CC       {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.28 mM for N,N-dimethylformamide {ECO:0000269|PubMed:10664842,
CC         ECO:0000269|Ref.2};
CC         Vmax=83.3 umol/min/mg enzyme toward N,N-dimethylformamide
CC         {ECO:0000269|PubMed:10664842, ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:10664842,
CC         ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 50-55 degrees Celsius. Stable up to 50 degrees
CC         Celsius, inactivated after incubation at 60 degrees Celsius for 30
CC         minutes. Activity decreases below 50 degrees Celsius, with 20% of
CC         activity retained at 25 degrees Celsius.
CC         {ECO:0000269|PubMed:10664842, ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Heterotetramer of two DmfA1 (alpha) and two DmfA2 (beta)
CC       subunits. {ECO:0000269|PubMed:10664842, ECO:0000269|Ref.2}.
CC   -!- CAUTION: It is not known which subunit of DmfA1 or DmfA2 possesses
CC       catalytic activity. {ECO:0000305}.
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DR   EMBL; AB028874; BAA90663.1; -; Genomic_DNA.
DR   PIR; JC7173; JC7173.
DR   AlphaFoldDB; Q9LCC1; -.
DR   SMR; Q9LCC1; -.
DR   KEGG; ag:BAA90663; -.
DR   GO; GO:0050116; F:N,N-dimethylformamidase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10664842"
FT   CHAIN           2..132
FT                   /note="N,N-dimethylformamidase alpha subunit"
FT                   /evidence="ECO:0000269|PubMed:10664842"
FT                   /id="PRO_0000403315"
SQ   SEQUENCE   132 AA;  16031 MW;  099F783002EB99E2 CRC64;
     MTEASESCVR DPSNYRDRSA DWYAFYDERR RKEIIDIIDE HPEIVEEHAA NPFGYRKHPS
     PYLQRVHNYF RMQPTFGKYY IYSEREWDAY RIATIREFGE LPELGDERFK TEEEAMHAVF
     LRRIEDVRAE LA