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P23295 (NOR_FUSOX) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADP nitrous oxide-forming nitric oxide reductase

Short name=NOR
EC=1.7.1.14
Alternative name(s):
CYPLVA1
Cytochrome P450 55A1
Cytochrome P450 DNIR
Cytochrome P450nor
Fungal nitric oxide reductase
Gene names
Name:CYP55A1
Synonyms:CYP55
OrganismFusarium oxysporum (Fusarium vascular wilt)
Taxonomic identifier5507 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nitric oxide reductase which is involved in a dissimilatory reduction of nitrite. Acts as a nitric oxide reductase. Is able to reduce nitrate and nitrite to a gaseous form of N2O when oxygen supply is limited or discontinued. May function as a detoxification mechanism. Ref.4 Ref.6

Catalytic activity

Nitrous oxide + NAD(P)+ + H2O = 2 nitric oxide + NAD(P)H. Ref.4 Ref.5 Ref.8 Ref.14

Cofactor

Heme group.

Enzyme regulation

Cyanide, CO, and oxygen strongly inhibit catalytic activity. Ref.4

Induction

By nitrate/nitrite. Ref.1 Ref.4

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 403402NADP nitrous oxide-forming nitric oxide reductase
PRO_0000052039

Sites

Metal binding3521Iron (heme axial ligand)

Amino acid modifications

Modified residue21N-acetylalanine Ref.3

Experimental info

Mutagenesis641R → E: Impairs interaction with NADH. Ref.6
Mutagenesis731S → A: Decreases the NADPH-dependent activity. Ref.6
Mutagenesis751S → A: Decreases the NADPH-dependent activity. Ref.6
Mutagenesis751S → G: Improves the NADPH-dependent activity. Ref.6
Mutagenesis761G → A: Decreases the NADPH-dependent activity. Ref.6
Mutagenesis771K → A: Decreases the NADPH-dependent activity. Ref.6
Mutagenesis781Q → A: Decreases the NADPH-dependent activity. Ref.6
Mutagenesis1741R → E: Impairs interaction with NADH. Ref.6
Mutagenesis2861S → V or T: Impairs catalytic activity. Ref.8 Ref.9
Mutagenesis3931D → V or L: Impairs catalytic activity. Ref.8

Secondary structure

......................................................................... 403
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23295 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7FDD97D8E0FB9215

FASTA40344,372
        10         20         30         40         50         60 
MASGAPSFPF SRASGPEPPA EFAKLRATNP VSQVKLFDGS LAWLVTKHKD VCFVATSEKL 

        70         80         90        100        110        120 
SKVRTRQGFP ELSASGKQAA KAKPTFVDMD PPEHMHQRSM VEPTFTPEAV KNLQPYIQRT 

       130        140        150        160        170        180 
VDDLLEQMKQ KGCANGPVDL VKEFALPVPS YIIYTLLGVP FNDLEYLTQQ NAIRTNGSST 

       190        200        210        220        230        240 
AREASAANQE LLDYLAILVE QRLVEPKDDI ISKLCTEQVK PGNIDKSDAV QIAFLLLVAG 

       250        260        270        280        290        300 
NATMVNMIAL GVATLAQHPD QLAQLKANPS LAPQFVEELC RYHTASALAI KRTAKEDVMI 

       310        320        330        340        350        360 
GDKLVRANEG IIASNQSANR DEEVFENPDE FNMNRKWPPQ DPLGFGFGDH RCIAEHLAKA 

       370        380        390        400 
ELTTVFSTLY QKFPDLKVAV PLGKINYTPL NRDVGIVDLP VIF 

« Hide

References

[1]"Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum."
Kizawa H., Tomura D., Oda M., Fukamizu A., Hoshino T., Gotoh O., Yasui T., Shoun H.
J. Biol. Chem. 266:10632-10637(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INDUCTION.
Strain: MT-811.
[2]"Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the fungus Fusarium oxysporum containing a potential binding-site for FNR, the transcription factor involved in the regulation of anaerobic growth of Escherichia coli."
Tomura D., Obika K., Fukamizu A., Shoun H.
J. Biochem. 116:88-94(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MT-811.
[3]"N-terminal processing and amino acid sequence of two isoforms of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum."
Nakahara K., Shoun H.
J. Biochem. 120:1082-1087(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2.
[4]"Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction."
Shoun H., Tanimoto T.
J. Biol. Chem. 266:11078-11082(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION.
[5]"Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism."
Shiro Y., Fujii M., Iizuka T., Adachi S., Tsukamoto K., Nakahara K., Shoun H.
J. Biol. Chem. 270:1617-1623(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[6]"The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH."
Zhang L., Kudo T., Takaya N., Shoun H.
J. Biol. Chem. 277:33842-33847(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-64; SER-73; SER-75; GLY-76; LYS-77; GLN-78 AND ARG-174.
[7]"Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum."
Park S.-Y., Shimizu H., Adachi S., Nakagawa A., Tanaka I., Nakahara K., Shoun H., Obayashi E., Nakamura H., Iizuka T., Shiro Y.
Nat. Struct. Biol. 4:827-832(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes."
Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.-Y., Nakamura H., Adachi S., Shoun H., Shiro Y.
J. Biol. Chem. 275:4816-4826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-403 IN COMPLEX WITH HEME, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-286 AND ASP-393.
[9]"Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s."
Shimizu H., Park S., Lee D., Shoun H., Shiro Y.
J. Inorg. Biochem. 81:191-205(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-402 IN COMPLEX WITH HEME OF WILD TYPE; MUTANT VAL-286 AND MUTANT THR-286, MUTAGENESIS OF SER-286.
[10]"Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function."
Obayashi E., Shimizu H., Park S.Y., Shoun H., Shiro Y.
J. Inorg. Biochem. 82:103-111(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-402 IN COMPLEX WITH HEME.
[11]"A positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH."
Kudo T., Takaya N., Park S.Y., Shiro Y., Shoun H.
J. Biol. Chem. 276:5020-5026(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH HEME.
[12]"Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam."
Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.
Biochemistry 40:2669-2677(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME.
[13]"X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution."
Shimizu H., Park S.-Y., Shiro Y., Adachi S.
Acta Crystallogr. D 58:81-89(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH HEME.
[14]"Structural evidence for direct hydride transfer from NADH to cytochrome P450nor."
Oshima R., Fushinobu S., Su F., Zhang L., Takaya N., Shoun H.
J. Mol. Biol. 342:207-217(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH HEME, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63340 mRNA. Translation: AAA33337.1.
D14517 Genomic DNA. Translation: BAA03390.1.
PIRJC5150.
JC5151.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CL6X-ray1.70A2-403[»]
1CMJX-ray1.70A2-403[»]
1CMNX-ray1.70A2-403[»]
1EHEX-ray1.70A2-403[»]
1EHFX-ray1.70A2-403[»]
1EHGX-ray1.70A2-403[»]
1F24X-ray1.40A2-403[»]
1F25X-ray1.40A2-403[»]
1F26X-ray1.40A2-403[»]
1GEDX-ray2.00A1-403[»]
1GEIX-ray1.60A1-403[»]
1GEJX-ray1.50A1-403[»]
1JFBX-ray1.00A1-403[»]
1JFCX-ray1.05A1-403[»]
1ROMX-ray2.00A1-403[»]
1ULWX-ray2.00A2-403[»]
1XQDX-ray1.80A1-403[»]
2ROMX-ray2.00A1-403[»]
ProteinModelPortalP23295.
SMRP23295. Positions 5-403.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16203.
SABIO-RKP23295.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
PfamPF00067. p450. 2 hits.
[Graphical view]
PRINTSPR00359. BP450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23295.

Entry information

Entry nameNOR_FUSOX
AccessionPrimary (citable) accession number: P23295
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 98 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references