2NPD_CYBMR
ID 2NPD_CYBMR Reviewed; 374 AA.
AC Q12723;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
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;
OS Cyberlindnera mrakii (Yeast) (Williopsis mrakii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=1004253;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 0895 / NCYC 2251 / VTT C-01434;
RX PubMed=7813473; DOI=10.1111/j.1432-1033.1994.00841.x;
RA Tchorzewski M., Kurihara T., Esaki N., Soda K.;
RT "Unique primary structure of 2-nitropropane dioxygenase from Hansenula
RT mrakii.";
RL Eur. J. Biochem. 226:841-846(1994).
RN [2]
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. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:19577534};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:19577534};
CC -!- SIMILARITY: Belongs to the nitronate monooxygenase family. NMO class I
CC subfamily. {ECO:0000305}.
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DR EMBL; U13900; AAA64484.1; -; Genomic_DNA.
DR PIR; S50891; S50891.
DR PDB; 6BKA; X-ray; 1.65 A; A=1-374.
DR PDBsum; 6BKA; -.
DR AlphaFoldDB; Q12723; -.
DR SMR; Q12723; -.
DR BioCyc; MetaCyc:MON-12527; -.
DR BRENDA; 1.13.11.32; 2586.
DR BRENDA; 1.13.12.16; 2586.
DR SABIO-RK; Q12723; -.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:UniProtKB-EC.
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 3D-structure; Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT CHAIN 1..374
FT /note="Nitronate monooxygenase"
FT /id="PRO_0000064361"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 22..24
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238..240
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 261..262
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:6BKA"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:6BKA"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6BKA"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6BKA"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6BKA"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:6BKA"
SQ SEQUENCE 374 AA; 41467 MW; 63F82BA7453E43F0 CRC64;
MRSQIQSFLK TFEVRYPIIQ APMAGASTLE LAATVTRLGG IGSIPMGSLS EKCDAIETQL
ENFDELVGDS GRIVNLNFFA HKEPRSGRAD VNEEWLKKYD KIYGKAGIEF DKKELKLLYP
SFRSIVDPQH PTVRLLKNLK PKIVSFHFGL PHEAVIESLQ ASDIKIFVTV TNLQEFQQAY
ESKLDGVVLQ GWEAGGHRGN FKANDVEDGQ LKTLDLVSTI VDYIDSASIS NPPFIIAAGG
IHDDESIKEL LQFNIAAVQL GTVWLPSSQA TISPEHLKMF QSPKSDTMMT AAISGRNLRT
ISTPFLRDLH QSSPLASIPD YPLPYDSFKS LANDAKQSGK GPQYSAFLAG SNYHKSWKDT
RSTEEIFSIL VQDL
