ID   DMFAB_ALCSP             Reviewed;         762 AA.
AC   Q9LCC0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=N,N-dimethylformamidase beta subunit {ECO:0000303|PubMed:10664842, ECO:0000312|EMBL:BAA90664.1};
DE            EC=3.5.1.56;
DE   AltName: Full=N,N-dimethylformamidase heavy chain {ECO:0000303|Ref.2};
GN   Name=dmfA2 {ECO:0000312|EMBL:BAA90664.1};
OS   Alcaligenes sp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=512;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA90664.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=KUFA-1 {ECO:0000312|EMBL:BAA90664.1};
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 with N,N-dimethylformamide as substrate
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; BAA90664.1; -; Genomic_DNA.
DR   PIR; JC7174; JC7174.
DR   AlphaFoldDB; Q9LCC0; -.
DR   SMR; Q9LCC0; -.
DR   PRIDE; Q9LCC0; -.
DR   KEGG; ag:BAA90664; -.
DR   GO; GO:0050116; F:N,N-dimethylformamidase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           1..762
FT                   /note="N,N-dimethylformamidase beta subunit"
FT                   /id="PRO_0000403316"
SQ   SEQUENCE   762 AA;  84700 MW;  CD7F63B891399ECB CRC64;
     MKDIAIRGYC DRPSVATGET IRFYVSANET RGTFDAELVR LIHGDSNPAG PGYKEEAIKS
     DLEGQYPARF QRTQFGSYVE VADPDAGLQP DGAFSVHLFL WSTTPSRGRQ GIASRWNDER
     QSGWNLAIED GRVVFTIGDG SGATSSVVSD RPLFQQIWYS ITGVYDPEKK QLRLYQKSVV
     NRTNSRFGLV VPLDSDCAVS ADATVKAADS ETSLLIAGLG EAAAQDGRTW CIAHYNGKVD
     APKIYGCALG QDDAEKLSRG EIVRPISRLA HWDFSAGIGL NGIPTDHVVD ASGNGHHGRC
     MNQPDRGSTG WNWDGHEENF IHCPEQYGAL WFHEDCLDDC RWEKDFEFTV PEGLKSDFYA
     VKIRYEDTED YIPFFVLPPR GTATAPILVI ASTLSYLAYA NEQIMHKADI GQAVAGHTPV
     LNENDVELHK NLSYYGLSTY DGHIDGRGVQ YTSWRRPIMN LRPKHRQGFG SIWELPADLH
     LIDWLNHNGF EYDVATEHDL NDQGAELLRR YKVVLTGSHP EYQTWANADA WEDYLADGGR
     GMYLAANGMY WIVEVHPEKP WVMEVRKELG VTAWEAPPGE YHYSTNGRRG GRFRGRARAT
     QKIWGTGMSS FGFDHSGYFV QMPDSQDERV AWIMEGIDPE ERIGDGGLVG GGAGGYELDR
     YDLALGTPPN TLLLASSVEH SVVYTVIPDD KAFPHPGMNG GEHPFVRADI TYFSTANGGG
     MFATSSISWL GSLSWNDYDN NVSKMTKNVL NQFIKDEPAP RV