NFDA_ARTPS
ID NFDA_ARTPS Reviewed; 542 AA.
AC Q68AP4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=N-substituted formamide deformylase {ECO:0000303|PubMed:15358859, ECO:0000312|EMBL:BAD37143.1};
DE EC=3.5.1.91;
DE Flags: Precursor;
GN Name=nfdA {ECO:0000312|EMBL:BAD37143.1};
OS Arthrobacter pascens.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1677;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD37143.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-12 AND 347-354,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, AND MASS SPECTROMETRY.
RC STRAIN=F164 {ECO:0000312|EMBL:BAD37143.1};
RX PubMed=15358859; DOI=10.1073/pnas.0405082101;
RA Fukatsu H., Hashimoto Y., Goda M., Higashibata H., Kobayashi M.;
RT "Amine-synthesizing enzyme N-substituted formamide deformylase: screening,
RT purification, characterization, and gene cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13726-13731(2004).
RN [2] {ECO:0000305}
RP INDUCTION.
RX PubMed=15665493; DOI=10.1271/bbb.69.228;
RA Fukatsu H., Goda M., Hashimoto Y., Higashibata H., Kobayashi M.;
RT "Optimum culture conditions for the production of N-substituted formamide
RT deformylase by Arthrobacter pascens F164.";
RL Biosci. Biotechnol. Biochem. 69:228-230(2005).
CC -!- FUNCTION: Hydrolyzes N-substituted formamides, but not amides. N-
CC benzylformamide is the preferred substrate, while N-butylformamide is
CC hydrolyzed at a much lower rate. Has very low activity towards
CC allylformamide, N-(2-cyclohex-1-enylethyl)formamide and N-(alpha-
CC methylbenzyl)formamide. {ECO:0000269|PubMed:15358859}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-benzylformamide = benzylamine + formate;
CC Xref=Rhea:RHEA:12096, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:41117, ChEBI:CHEBI:225238; EC=3.5.1.91;
CC Evidence={ECO:0000269|PubMed:15358859};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15358859};
CC -!- ACTIVITY REGULATION: Completely inhibited by HgCl(2), CuCl, CuCl(2) and
CC AgNO(3). Partially inhibited by ZnCl(2) and SnCl(2). Almost completely
CC inhibited by the reducing reagent DTT. Partially inhibited by
CC phenylhydrazine. Moderately inhibited by phenanthroline and 8-
CC hydroxyquinoline. Completely inhibited by the thiol-specific inhibitors
CC N-ethylmaleimide and p-chloromercuribenzoate. Not inhibited by the
CC carbonyl-specific inhibitors aminoguanidine and semicarbazide, the
CC chelating agents alpha,alpha'-dipyridyl, KCN, diethyldithiocarbamate
CC and EDTA, or the oxidizing reagents and serine-modifying reagents such
CC as H(2)O(2), ammonium persulfate, phenylmethanesulfonyl fluoride and
CC diisopropyl fluorophosphates. {ECO:0000269|PubMed:15358859}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.075 mM for N-benzylformamide {ECO:0000269|PubMed:15358859};
CC KM=7.5 mM for N-butylformamide {ECO:0000269|PubMed:15358859};
CC Vmax=52.7 mmol/min/mg enzyme with N-benzylformamide as substrate
CC {ECO:0000269|PubMed:15358859};
CC Vmax=6.3 mmol/min/mg enzyme with N-butylformamide as substrate
CC {ECO:0000269|PubMed:15358859};
CC pH dependence:
CC Optimum pH is 7.0. Stable from pH 7.5 to 8.5.
CC {ECO:0000269|PubMed:15358859};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. Inactive following 30
CC minutes incubation at 50 degrees Celsius or above, no loss of
CC activity following 30 minutes incubation at 25 degrees Celsius or
CC below. Little loss of activity following 30 minutes incubation at 35
CC or 30 degrees Celsius. {ECO:0000269|PubMed:15358859};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15358859}.
CC -!- INDUCTION: Induced by N-benzylformamide. Repressed by glucose.
CC {ECO:0000269|PubMed:15358859, ECO:0000269|PubMed:15665493}.
CC -!- MASS SPECTROMETRY: Mass=58556; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15358859};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; AB164325; BAD37143.1; -; Genomic_DNA.
DR AlphaFoldDB; Q68AP4; -.
DR SMR; Q68AP4; -.
DR PRIDE; Q68AP4; -.
DR KEGG; ag:BAD37143; -.
DR BioCyc; MetaCyc:MON-15822; -.
DR BRENDA; 3.5.1.91; 452.
DR SABIO-RK; Q68AP4; -.
DR GO; GO:0033966; F:N-substituted formamide deformylase activity; IDA:UniProtKB.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:15358859"
FT /id="PRO_0000400093"
FT CHAIN 3..542
FT /note="N-substituted formamide deformylase"
FT /evidence="ECO:0000269|PubMed:15358859"
FT /id="PRO_0000400094"
SQ SEQUENCE 542 AA; 58828 MW; FCCD92635E300FA7 CRC64;
MTQMRDLMII NANVRTVDAR NSCAQAVLVS GGRIAIVGTE TEVRGAAAPD AEVLDVSGKT
VVPGFIDAHN HLSVAAFAPD SVDCSTPPLA TLDEVLEVIE RHCRNIPPGQ WVRGINFHAS
HIREQRNPTR YELDEVAPNN PFFLIDASCH AGFANSAALD LVGIGAHTPE PWGGEIERDL
SGKPTGTLLE AAANLLHSAS WNDYAERDWD RAVELLHSKM NDYLAVGLTG VGDAMVTAKS
AELYRRADAA GKMPFTLQQL HGGDHFFSMQ DLGRSDTVDR IMEPESYLLR GGAMKIFVDR
AYPSPAIDQI HDGCKTHVGA NFYSKSEVHD LAVRASKLGI NLAIHGMGNC AIDIVLDAYE
AVRRQSNADT VLRLEHAFIA ETGQGQRMAD LGIDLVANPG LAFGWGEVFN MWRGENQEHL
KLFPVRSMLD AGVRVSLASD HPCGTYSPAE IMWTAVARET MAGAPLEPDE AVTADEALRM
YTINPAHASG RGSEEGSIEA GKRANLLVLD RDPVDCATGE LRELQVLRTY VDGVLRYERT
GS
