NAO_PODAN
ID NAO_PODAN Reviewed; 430 AA.
AC B2AM55;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Nitroalkane oxidase {ECO:0000303|PubMed:20481475};
DE Short=NAO {ECO:0000303|PubMed:20481475};
DE EC=1.7.3.1 {ECO:0000269|PubMed:20481475};
GN OrderedLocusNames=Pa_5_6340; ORFNames=PODANS_5_6340;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR,
RP SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVE SITE, AND MUTAGENESIS OF SER-273; ASP-399 AND ARG-406.
RX PubMed=20481475; DOI=10.1021/bi100610e;
RA Tormos J.R., Taylor A.B., Daubner S.C., Hart P.J., Fitzpatrick P.F.;
RT "Identification of a hypothetical protein from Podospora anserina as a
RT nitroalkane oxidase.";
RL Biochemistry 49:5035-5041(2010).
CC -!- FUNCTION: Nitroalkane oxidase (NAO) catalyzes the oxidation of
CC nitroalkanes to the corresponding aldehydes or ketones with the release
CC of nitrite and the consumption of molecular oxygen to yield hydrogen
CC peroxide (PubMed:20481475). NAO is unusual, since it catalyzes
CC substrate oxidation by removing a substrate proton to form a carbanion
CC intermediate (PubMed:20481475). Prefers longer nitroalkanes, with 1-
CC nitrohexane having the highest activity (PubMed:20481475).
CC {ECO:0000269|PubMed:20481475}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary nitroalkane + H2O + O2 = an aldehyde + H(+) + H2O2 +
CC nitrite; Xref=Rhea:RHEA:20976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:133972; EC=1.7.3.1;
CC Evidence={ECO:0000269|PubMed:20481475};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary nitroalkane + H2O + O2 = a ketone + H(+) + H2O2 +
CC nitrite; Xref=Rhea:RHEA:26490, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17087, ChEBI:CHEBI:139218; EC=1.7.3.1;
CC Evidence={ECO:0000269|PubMed:20481475};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20481475};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.0 mM for nitroethane {ECO:0000269|PubMed:20481475};
CC KM=0.39 mM for O(2) {ECO:0000269|PubMed:20481475};
CC pH dependence:
CC Optimally active at alkaline pHs. {ECO:0000269|PubMed:20481475};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20481475}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CU633870; CAP65043.1; -; Genomic_DNA.
DR EMBL; FO904940; CDP29865.1; -; Genomic_DNA.
DR RefSeq; XP_001905136.1; XM_001905101.1.
DR PDB; 3MKH; X-ray; 2.00 A; A/B/C/D=1-430.
DR PDBsum; 3MKH; -.
DR AlphaFoldDB; B2AM55; -.
DR SMR; B2AM55; -.
DR STRING; 5145.XP_001905136.1; -.
DR EnsemblFungi; CAP65043; CAP65043; PODANS_5_6340.
DR GeneID; 6189407; -.
DR KEGG; pan:PODANSg2158; -.
DR VEuPathDB; FungiDB:PODANS_5_6340; -.
DR eggNOG; KOG0140; Eukaryota.
DR HOGENOM; CLU_018204_3_0_1; -.
DR OrthoDB; 589058at2759; -.
DR BRENDA; 1.7.3.1; 4930.
DR EvolutionaryTrace; B2AM55; -.
DR Proteomes; UP000001197; Chromosome 5.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050141; F:nitroethane oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..430
FT /note="Nitroalkane oxidase"
FT /id="PRO_0000437677"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:20481475"
FT BINDING 132..135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT BINDING 140..142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT BINDING 170..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT BINDING 301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT BINDING 372..376
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT BINDING 397..401
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20481475"
FT MUTAGEN 273
FT /note="S->A: Slightly decreases the catalytic activity."
FT /evidence="ECO:0000269|PubMed:20481475"
FT MUTAGEN 399
FT /note="D->N: Strongly decreases the catalytic activity."
FT /evidence="ECO:0000269|PubMed:20481475"
FT MUTAGEN 406
FT /note="R->K: Slightly decreases the catalytic activity."
FT /evidence="ECO:0000269|PubMed:20481475"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:3MKH"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 90..109
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3MKH"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3MKH"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3MKH"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 262..298
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 311..340
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 345..374
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:3MKH"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3MKH"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:3MKH"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:3MKH"
SQ SEQUENCE 430 AA; 45482 MW; F6CB9DF2890B82D5 CRC64;
MPIDFHLSAS QKGTYQAARS LARNLLMPAR QTYLQHPPNS PLRFQSTQPT YAAAVSAGIL
KGQISPAHGG TGGTLIESAI LVEECYSVEP SAALTIFATG LGLTPINLAA GPQHAEFLAP
FLSGEGSPLA SLVFSEPGGV ANALEKGAPG FQTTARLEGD EWVINGEKMW ATNCAGWDFK
GCDLACVVCR DATTPLEEGQ DPENKVMIIL VTRADLDRNG EGSFEVLRHV ATPGHTSVSG
PHVRYTNVRV PTKNVLCPAG QGAKVAFGAF DGSAVLVGAM GVGLMRAAFD AALKFAKEDN
RGGAVPLLER QAFADLLSGV KIQTEAARAL TWKAAHAMEN GPGDYDARRE LALAAKVFCS
EAAVKACTDV INAVGISAYD LQRPFSDLLN TAVVLPIFDG GNVGIRRRHL QQLMLKPTYD
AWSSTYGSFP
