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P23295

- NOR_FUSOX

UniProt

P23295 - NOR_FUSOX

Protein

NADP nitrous oxide-forming nitric oxide reductase

Gene

CYP55A1

Organism
Fusarium oxysporum (Fusarium vascular wilt)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23295.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    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: October 1, 2014
    This is version 99 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