2NPD_NEUCR
ID 2NPD_NEUCR Reviewed; 378 AA.
AC Q01284; Q7RV78;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nitronate monooxygenase;
DE EC=1.13.12.16;
DE AltName: Full=2-nitropropane dioxygenase;
DE Short=2-NPD;
DE AltName: Full=Nitroalkane oxidase;
DE Flags: Precursor;
GN Name=ncd-2; ORFNames=G17A4.200, NCU03949;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=ATCC 10337 / FGSC 1758 / NBRC 6067 / IMI 53239;
RX PubMed=9501443; DOI=10.1128/aem.64.3.1029-1033.1998;
RA Gorlatova N., Tchorzewski M., Kurihara T., Soda K., Esaki N.;
RT "Purification, characterization, and mechanism of a flavin mononucleotide-
RT dependent 2-nitropropane dioxygenase from Neurospora crassa.";
RL Appl. Environ. Microbiol. 64:1029-1033(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP COFACTOR, SUBSTRATE SPECIFICITY, AND REACTION MECHANISM.
RX PubMed=19577534; DOI=10.1016/j.abb.2009.06.018;
RA Gadda G., Francis K.;
RT "Nitronate monooxygenase, a model for anionic flavin semiquinone
RT intermediates in oxidative catalysis.";
RL Arch. Biochem. Biophys. 493:53-61(2010).
CC -!- FUNCTION: Catalyzes the oxidation of alkyl nitronates to produce the
CC corresponding carbonyl compounds and nitrites. Anionic forms of
CC nitroalkanes are much better substrates than are neutral forms.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethylnitronate + O2 = acetaldehyde + chemical entity + H(+) +
CC nitrite; Xref=Rhea:RHEA:28767, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16301, ChEBI:CHEBI:24431,
CC ChEBI:CHEBI:77894; EC=1.13.12.16;
CC Evidence={ECO:0000269|PubMed:9501443};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:19577534, ECO:0000269|PubMed:9501443};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:19577534,
CC ECO:0000269|PubMed:9501443};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for 2-nitropropane {ECO:0000269|PubMed:9501443};
CC KM=6 mM for nitroethane {ECO:0000269|PubMed:9501443};
CC KM=8.3 mM for 1-nitropropane {ECO:0000269|PubMed:9501443};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9501443}.
CC -!- SIMILARITY: Belongs to the nitronate monooxygenase family. NMO class II
CC subfamily. {ECO:0000305}.
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DR EMBL; U22530; AAA64218.1; -; mRNA.
DR EMBL; BX908812; CAF06155.1; -; Genomic_DNA.
DR EMBL; CM002241; EAA28352.1; -; Genomic_DNA.
DR PIR; T46693; T46693.
DR RefSeq; XP_957588.1; XM_952495.3.
DR AlphaFoldDB; Q01284; -.
DR SMR; Q01284; -.
DR STRING; 5141.EFNCRP00000003619; -.
DR EnsemblFungi; EAA28352; EAA28352; NCU03949.
DR GeneID; 3873678; -.
DR KEGG; ncr:NCU03949; -.
DR VEuPathDB; FungiDB:NCU03949; -.
DR HOGENOM; CLU_038732_9_0_1; -.
DR InParanoid; Q01284; -.
DR OMA; NSPLWGP; -.
DR BioCyc; MetaCyc:MON-302; -.
DR BRENDA; 1.13.11.32; 3627.
DR BRENDA; 1.13.12.16; 3627.
DR SABIO-RK; Q01284; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IBA:GO_Central.
DR CDD; cd04730; NPD_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004136; NMO.
DR Pfam; PF03060; NMO; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Reference proteome.
FT PROPEP 1..15
FT /evidence="ECO:0000255"
FT /id="PRO_0000020575"
FT CHAIN 16..378
FT /note="Nitronate monooxygenase"
FT /id="PRO_0000020576"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 37..39
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229..231
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 252..253
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 39916 MW; E453EB43FD23E441 CRC64;
MHFPGHSSKK EESAQAALTK LNSWFPTTKN PVIISAPMYL IANGTLAAEV SKAGGIGFVA
GGSDFRPGSS HLTALSTELA SARSRLGLTD RPLTPLPGIG VGLILTHTIS VPYVTDTVLP
ILIEHSPQAV WLFANDPDFE ASSEPGAKGT AKQIIEALHA SGFVVFFQVG TVKDARKAAA
DGADVIVAQG IDAGGHQLAT GSGIVSLVPE VRDMLDREFK EREVVVVAAG GVADGRGVVG
ALGLGAEGVV LGTRFTVAVE ASTPEFRRKV ILETNDGGLN TVKSHFHDQI NCNTIWHNVY
DGRAVRNASY DDHAAGVPFE ENHKKFKEAA SSGDNSRAVT WSGTAVGLIK DQRPAGDIVR
ELREEAKERI KKIQAFAA
