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Protein

NADP nitrous oxide-forming nitric oxide reductase

Gene

CYP55A1

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

Enzyme 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

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16203.
BRENDAi1.7.1.14. 2351.
1.7.2.5. 2351.
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)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

Expressioni

Inductioni

By nitrate/nitrite.1 Publication

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Beta strandi13 – 17Combined sources5
Helixi21 – 28Combined sources8
Beta strandi30 – 35Combined sources6
Beta strandi41 – 45Combined sources5
Helixi48 – 56Combined sources9
Beta strandi64 – 66Combined sources3
Helixi74 – 79Combined sources6
Helixi86 – 88Combined sources3
Helixi93 – 98Combined sources6
Turni99 – 101Combined sources3
Helixi102 – 105Combined sources4
Helixi107 – 131Combined sources25
Beta strandi134 – 136Combined sources3
Helixi140 – 143Combined sources4
Turni144 – 146Combined sources3
Helixi147 – 157Combined sources11
Helixi161 – 163Combined sources3
Helixi164 – 175Combined sources12
Beta strandi177 – 179Combined sources3
Helixi181 – 204Combined sources24
Helixi210 – 217Combined sources8
Turni218 – 222Combined sources5
Helixi226 – 257Combined sources32
Helixi259 – 267Combined sources9
Helixi269 – 271Combined sources3
Helixi272 – 282Combined sources11
Beta strandi291 – 296Combined sources6
Beta strandi298 – 300Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi310 – 313Combined sources4
Helixi315 – 318Combined sources4
Turni322 – 324Combined sources3
Beta strandi325 – 327Combined sources3
Helixi348 – 350Combined sources3
Helixi355 – 372Combined sources18
Beta strandi377 – 380Combined sources4
Helixi382 – 384Combined sources3
Beta strandi396 – 398Combined sources3
Beta strandi400 – 402Combined sources3

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[»]
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.
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

        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.

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[»]
ProteinModelPortaliP23295.
SMRiP23295.
ModBaseiSearch...
MobiDBiSearch...

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-RKP23295.

Miscellaneous databases

EvolutionaryTraceiP23295.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 107 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.