NADP nitrous oxide-forming nitric oxide reductase - Fusarium oxysporum (Panama disease fungus)

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P23295 (NOR_FUSOX) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Fusarium oxysporum (Panama disease fungus)

Taxonomic identifier

5507 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › mitosporic Nectriaceae › Fusarium › Fusarium oxysporum species complex

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding NAD NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 403

402

NADP nitrous oxide-forming nitric oxide reductase

PRO_0000052039

Sites

Metal binding

352

Iron (heme axial ligand)

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Experimental info

Mutagenesis

R → E: Impairs interaction with NADH. Ref.6

Mutagenesis

S → A: Decreases the NADPH-dependent activity. Ref.6

Mutagenesis

S → A: Decreases the NADPH-dependent activity. Ref.6

Mutagenesis

S → G: Improves the NADPH-dependent activity. Ref.6

Mutagenesis

G → A: Decreases the NADPH-dependent activity. Ref.6

Mutagenesis

K → A: Decreases the NADPH-dependent activity. Ref.6

Mutagenesis

Q → A: Decreases the NADPH-dependent activity. Ref.6

Mutagenesis

174

R → E: Impairs interaction with NADH. Ref.6

Mutagenesis

286

S → V or T: Impairs catalytic activity. Ref.8 Ref.9

Mutagenesis

393

D → V or L: Impairs catalytic activity. Ref.8

Secondary structure

403

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23295 [UniParc].

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

403

44,372

        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.

PIR

JC5150.
JC5151.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CL6	X-ray	1.70	A	2-403	[»]
1CMJ	X-ray	1.70	A	2-403	[»]
1CMN	X-ray	1.70	A	2-403	[»]
1EHE	X-ray	1.70	A	2-402	[»]
1EHF	X-ray	1.70	A	2-402	[»]
1EHG	X-ray	1.70	A	2-402	[»]
1F24	X-ray	1.40	A	2-402	[»]
1F25	X-ray	1.40	A	2-402	[»]
1F26	X-ray	1.40	A	2-402	[»]
1GED	X-ray	2.00	A	1-403	[»]
1GEI	X-ray	1.60	A	1-403	[»]
1GEJ	X-ray	1.50	A	1-403	[»]
1JFB	X-ray	1.00	A	1-403	[»]
1JFC	X-ray	1.05	A	1-403	[»]
1ROM	X-ray	2.00	A	1-403	[»]
1ULW	X-ray	2.00	A	2-402	[»]
1XQD	X-ray	1.80	A	1-403	[»]
2ROM	X-ray	2.00	A	1-403	[»]

ProteinModelPortal

P23295.

SMR

P23295. Positions 5-403.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16203.

SABIO-RK

P23295.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]

Pfam

PF00067. p450. 2 hits.
[Graphical view]

PRINTS

PR00359. BP450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23295.

Entry information

Entry name

NOR_FUSOX

Accession

Primary (citable) accession number: P23295

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents