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P23295

- NOR_FUSOX

UniProt

P23295 - NOR_FUSOX

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Protein

NADP nitrous oxide-forming nitric oxide reductase

Gene
CYP55A1, CYP55
Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Nitrous oxide + NAD(P)+ + H2O = 2 nitric oxide + NAD(P)H.4 Publications

Cofactori

Heme group.

Enzyme regulationi

Cyanide, CO, and oxygen strongly inhibit catalytic activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi352 – 3521Iron (heme axial ligand)

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. monooxygenase activity Source: UniProtKB-KW
  4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16203.
SABIO-RKP23295.

Names & Taxonomyi

Protein namesi
Recommended name:
NADP nitrous oxide-forming nitric oxide reductase (EC:1.7.1.14)
Short name:
NOR
Alternative name(s):
CYPLVA1
Cytochrome P450 55A1
Cytochrome P450 DNIR
Cytochrome P450nor
Fungal nitric oxide reductase
Gene namesi
Name:CYP55A1
Synonyms:CYP55
OrganismiFusarium oxysporum (Fusarium vascular wilt)
Taxonomic identifieri5507 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium oxysporum species complex

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641R → E: Impairs interaction with NADH. 1 Publication
Mutagenesisi73 – 731S → A: Decreases the NADPH-dependent activity. 1 Publication
Mutagenesisi75 – 751S → A: Decreases the NADPH-dependent activity. 1 Publication
Mutagenesisi75 – 751S → G: Improves the NADPH-dependent activity. 1 Publication
Mutagenesisi76 – 761G → A: Decreases the NADPH-dependent activity. 1 Publication
Mutagenesisi77 – 771K → A: Decreases the NADPH-dependent activity. 1 Publication
Mutagenesisi78 – 781Q → A: Decreases the NADPH-dependent activity. 1 Publication
Mutagenesisi174 – 1741R → E: Impairs interaction with NADH. 1 Publication
Mutagenesisi286 – 2861S → V or T: Impairs catalytic activity. 2 Publications
Mutagenesisi393 – 3931D → V or L: Impairs catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 403402NADP nitrous oxide-forming nitric oxide reductasePRO_0000052039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Expressioni

Inductioni

By nitrate/nitrite.2 Publications

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93
Beta strandi13 – 175
Helixi21 – 288
Beta strandi30 – 356
Beta strandi41 – 455
Helixi48 – 569
Beta strandi64 – 663
Helixi74 – 796
Helixi86 – 883
Helixi93 – 986
Turni99 – 1013
Helixi102 – 1054
Helixi107 – 13125
Beta strandi134 – 1363
Helixi140 – 1434
Turni144 – 1463
Helixi147 – 15711
Helixi161 – 1633
Helixi164 – 17512
Beta strandi177 – 1793
Helixi181 – 20424
Helixi210 – 2178
Turni218 – 2225
Helixi226 – 25732
Helixi259 – 2679
Helixi269 – 2713
Helixi272 – 28211
Beta strandi291 – 2966
Beta strandi298 – 3003
Beta strandi303 – 3053
Beta strandi310 – 3134
Helixi315 – 3184
Turni322 – 3243
Beta strandi325 – 3273
Helixi348 – 3503
Helixi355 – 37218
Beta strandi377 – 3804
Helixi382 – 3843
Beta strandi396 – 3983
Beta strandi400 – 4023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP23295.
SMRiP23295. Positions 5-403.

Miscellaneous databases

EvolutionaryTraceiP23295.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
PfamiPF00067. p450. 2 hits.
[Graphical view]
PRINTSiPR00359. BP450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23295-1 [UniParc]FASTAAdd to Basket

« Hide

MASGAPSFPF SRASGPEPPA EFAKLRATNP VSQVKLFDGS LAWLVTKHKD    50
VCFVATSEKL SKVRTRQGFP ELSASGKQAA KAKPTFVDMD PPEHMHQRSM 100
VEPTFTPEAV KNLQPYIQRT VDDLLEQMKQ KGCANGPVDL VKEFALPVPS 150
YIIYTLLGVP FNDLEYLTQQ NAIRTNGSST AREASAANQE LLDYLAILVE 200
QRLVEPKDDI ISKLCTEQVK PGNIDKSDAV QIAFLLLVAG NATMVNMIAL 250
GVATLAQHPD QLAQLKANPS LAPQFVEELC RYHTASALAI KRTAKEDVMI 300
GDKLVRANEG IIASNQSANR DEEVFENPDE FNMNRKWPPQ DPLGFGFGDH 350
RCIAEHLAKA ELTTVFSTLY QKFPDLKVAV PLGKINYTPL NRDVGIVDLP 400
VIF 403
Length:403
Mass (Da):44,372
Last modified:January 23, 2007 - v2
Checksum:i7FDD97D8E0FB9215
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63340 mRNA. Translation: AAA33337.1.
D14517 Genomic DNA. Translation: BAA03390.1.
PIRiJC5150.
JC5151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63340 mRNA. Translation: AAA33337.1 .
D14517 Genomic DNA. Translation: BAA03390.1 .
PIRi JC5150.
JC5151.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-403 [» ]
1EHF X-ray 1.70 A 2-403 [» ]
1EHG X-ray 1.70 A 2-403 [» ]
1F24 X-ray 1.40 A 2-403 [» ]
1F25 X-ray 1.40 A 2-403 [» ]
1F26 X-ray 1.40 A 2-403 [» ]
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 2-403 [» ]
1XQD X-ray 1.80 A 1-403 [» ]
2ROM X-ray 2.00 A 1-403 [» ]
ProteinModelPortali P23295.
SMRi P23295. Positions 5-403.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16203.
SABIO-RK P23295.

Miscellaneous databases

EvolutionaryTracei P23295.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view ]
Pfami PF00067. p450. 2 hits.
[Graphical view ]
PRINTSi PR00359. BP450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNOR_FUSOX
AccessioniPrimary (citable) accession number: P23295
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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