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Q01284 (2NPD_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nitronate monooxygenase
EC=1.13.12.16
Alternative name(s):
2-nitropropane dioxygenase
Short name=2-NPD
Nitroalkane oxidase
Gene names
Name:ncd-2
ORF Names:G17A4.200, NCU03949
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of alkyl nitronates to produce the corresponding carbonyl compounds and nitrites. Anionic forms of nitroalkanes are much better substrates than are neutral forms.

Catalytic activity

Ethylnitronate + O2 = acetaldehyde + nitrite + other products. Ref.1

Cofactor

Binds 1 FMN per subunit. Ref.1 Ref.4

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the nitronate monooxygenase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.1 mM for 2-nitropropane Ref.1

KM=6 mM for nitroethane

KM=8.3 mM for 1-nitropropane

Ontologies

Keywords
   LigandFMN
Flavoprotein
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular functionnitronate monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1515 Potential
PRO_0000020575
Chain16 – 378363Nitronate monooxygenase
PRO_0000020576

Regions

Nucleotide binding37 – 393FMN By similarity
Nucleotide binding229 – 2313FMN By similarity
Nucleotide binding252 – 2532FMN By similarity

Sites

Active site1961Proton acceptor Potential
Binding site1961Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01284 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E453EB43FD23E441

FASTA37839,916
        10         20         30         40         50         60 
MHFPGHSSKK EESAQAALTK LNSWFPTTKN PVIISAPMYL IANGTLAAEV SKAGGIGFVA 

        70         80         90        100        110        120 
GGSDFRPGSS HLTALSTELA SARSRLGLTD RPLTPLPGIG VGLILTHTIS VPYVTDTVLP 

       130        140        150        160        170        180 
ILIEHSPQAV WLFANDPDFE ASSEPGAKGT AKQIIEALHA SGFVVFFQVG TVKDARKAAA 

       190        200        210        220        230        240 
DGADVIVAQG IDAGGHQLAT GSGIVSLVPE VRDMLDREFK EREVVVVAAG GVADGRGVVG 

       250        260        270        280        290        300 
ALGLGAEGVV LGTRFTVAVE ASTPEFRRKV ILETNDGGLN TVKSHFHDQI NCNTIWHNVY 

       310        320        330        340        350        360 
DGRAVRNASY DDHAAGVPFE ENHKKFKEAA SSGDNSRAVT WSGTAVGLIK DQRPAGDIVR 

       370 
ELREEAKERI KKIQAFAA

« Hide

References

« Hide 'large scale' references
[1]"Purification, characterization, and mechanism of a flavin mononucleotide-dependent 2-nitropropane dioxygenase from Neurospora crassa."
Gorlatova N., Tchorzewski M., Kurihara T., Soda K., Esaki N.
Appl. Environ. Microbiol. 64:1029-1033(1998) [PubMed: 9501443] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.
Strain: ATCC 10337 / FGSC 1758 / NBRC 6067 / IMI 53239.
[2]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]"Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis."
Gadda G., Francis K.
Arch. Biochem. Biophys. 493:53-61(2010) [PubMed: 19577534] [Abstract]
Cited for: COFACTOR, SUBSTRATE SPECIFICITY, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U22530 mRNA. Translation: AAA64218.1.
BX908812 Genomic DNA. Translation: CAF06155.1.
AABX02000012 Genomic DNA. Translation: EAA28352.1.
PIRT46693.
RefSeqXP_957588.1. XM_952495.2.

3D structure databases

ProteinModelPortalQ01284.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ01284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000003619; EFNCRP00000003619; EFNCRG00000003615.
GeneID3873678.
KEGGncr:NCU03949.
NMPDRfig|5141.1.peg.1201.

Phylogenomic databases

eggNOGfuNOG14510.
GeneTreeEFGT00050000002105.
OMAVIISAPM.
OrthoDBEOG4350G8.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-302.
NCRA-XX3-01:NCRA-XX3-01-007697-MONOMER.
BRENDA1.13.11.32. 3627.

Family and domain databases

InterProIPR004136. 2Npropane_dOase.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00459.
PfamPF03060. NMO. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name2NPD_NEUCR
AccessionPrimary (citable) accession number: Q01284
Secondary accession number(s): Q7RV78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents