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Protein

NADP nitrous oxide-forming nitric oxide reductase

Gene

CYP55A1

Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed-Annotation score: -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

Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi352Iron (heme axial ligand)1

GO - Molecular functioni

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
LigandHeme, Iron, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16203
BRENDAi1.7.1.14 2351
1.7.2.5 2351
SABIO-RKiP23295

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)DescriptionActionsGraphical viewLength
Mutagenesisi64R → E: Impairs interaction with NADH. 1 Publication1
Mutagenesisi73S → A: Decreases the NADPH-dependent activity. 1 Publication1
Mutagenesisi75S → A: Decreases the NADPH-dependent activity. 1 Publication1
Mutagenesisi75S → G: Improves the NADPH-dependent activity. 1 Publication1
Mutagenesisi76G → A: Decreases the NADPH-dependent activity. 1 Publication1
Mutagenesisi77K → A: Decreases the NADPH-dependent activity. 1 Publication1
Mutagenesisi78Q → A: Decreases the NADPH-dependent activity. 1 Publication1
Mutagenesisi174R → E: Impairs interaction with NADH. 1 Publication1
Mutagenesisi286S → V or T: Impairs catalytic activity. 2 Publications1
Mutagenesisi393D → V or L: Impairs catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000520392 – 403NADP nitrous oxide-forming nitric oxide reductaseAdd BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

PTM databases

iPTMnetiP23295

Expressioni

Inductioni

By nitrate/nitrite.1 Publication

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP23295
SMRiP23295
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23295

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

KOiK15877

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR002397 Cyt_P450_B
IPR017972 Cyt_P450_CS
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 2 hits
PRINTSiPR00359 BP450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit

Sequencei

Sequence statusi: Complete.

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

P23295-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGAPSFPF SRASGPEPPA EFAKLRATNP VSQVKLFDGS LAWLVTKHKD
60 70 80 90 100
VCFVATSEKL SKVRTRQGFP ELSASGKQAA KAKPTFVDMD PPEHMHQRSM
110 120 130 140 150
VEPTFTPEAV KNLQPYIQRT VDDLLEQMKQ KGCANGPVDL VKEFALPVPS
160 170 180 190 200
YIIYTLLGVP FNDLEYLTQQ NAIRTNGSST AREASAANQE LLDYLAILVE
210 220 230 240 250
QRLVEPKDDI ISKLCTEQVK PGNIDKSDAV QIAFLLLVAG NATMVNMIAL
260 270 280 290 300
GVATLAQHPD QLAQLKANPS LAPQFVEELC RYHTASALAI KRTAKEDVMI
310 320 330 340 350
GDKLVRANEG IIASNQSANR DEEVFENPDE FNMNRKWPPQ DPLGFGFGDH
360 370 380 390 400
RCIAEHLAKA ELTTVFSTLY QKFPDLKVAV PLGKINYTPL NRDVGIVDLP

VIF
Length:403
Mass (Da):44,372
Last modified:January 23, 2007 - v2
Checksum:i7FDD97D8E0FB9215
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63340 mRNA Translation: AAA33337.1
D14517 Genomic DNA Translation: BAA03390.1
PIRiJC5150
JC5151

Genome annotation databases

KEGGiag:AAA33337

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63340 mRNA Translation: AAA33337.1
D14517 Genomic DNA Translation: BAA03390.1
PIRiJC5150
JC5151

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5Y5FX-ray1.50A1-403[»]
5Y5GX-ray1.36A1-403[»]
5Y5HX-ray1.50A1-403[»]
5Y5IX-ray2.10A/B1-403[»]
5Y5JX-ray2.00A/B1-403[»]
5Y5KX-ray2.10A/B1-403[»]
5Y5LX-ray2.10A/B1-403[»]
5Y5MX-ray2.10A/B1-403[»]
ProteinModelPortaliP23295
SMRiP23295
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP23295

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA33337

Phylogenomic databases

KOiK15877

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16203
BRENDAi1.7.1.14 2351
1.7.2.5 2351
SABIO-RKiP23295

Miscellaneous databases

EvolutionaryTraceiP23295

Family and domain databases

Gene3Di1.10.630.10, 1 hit
InterProiView protein in InterPro
IPR001128 Cyt_P450
IPR002397 Cyt_P450_B
IPR017972 Cyt_P450_CS
IPR036396 Cyt_P450_sf
PfamiView protein in Pfam
PF00067 p450, 2 hits
PRINTSiPR00359 BP450
SUPFAMiSSF48264 SSF48264, 1 hit
PROSITEiView protein in PROSITE
PS00086 CYTOCHROME_P450, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiNOR_FUSOX
AccessioniPrimary (citable) accession number: P23295
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 115 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health

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