ID   NOR_FUSOX               Reviewed;         403 AA.
AC   P23295;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=NADP nitrous oxide-forming nitric oxide reductase;
DE            Short=NOR;
DE            EC=1.7.1.14;
DE   AltName: Full=CYPLVA1;
DE   AltName: Full=Cytochrome P450 55A1;
DE   AltName: Full=Cytochrome P450 DNIR;
DE   AltName: Full=Cytochrome P450nor;
DE   AltName: Full=Fungal nitric oxide reductase;
GN   Name=CYP55A1; Synonyms=CYP55;
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=MT-811;
RX   PubMed=2037602; DOI=10.1016/s0021-9258(18)99270-7;
RA   Kizawa H., Tomura D., Oda M., Fukamizu A., Hoshino T., Gotoh O., Yasui T.,
RA   Shoun H.;
RT   "Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-
RT   450 cDNA from Fusarium oxysporum.";
RL   J. Biol. Chem. 266:10632-10637(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT-811;
RX   PubMed=7798191; DOI=10.1093/oxfordjournals.jbchem.a124508;
RA   Tomura D., Obika K., Fukamizu A., Shoun H.;
RT   "Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the fungus
RT   Fusarium oxysporum containing a potential binding-site for FNR, the
RT   transcription factor involved in the regulation of anaerobic growth of
RT   Escherichia coli.";
RL   J. Biochem. 116:88-94(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT ALA-2.
RX   PubMed=9010754; DOI=10.1093/oxfordjournals.jbchem.a021525;
RA   Nakahara K., Shoun H.;
RT   "N-terminal processing and amino acid sequence of two isoforms of nitric
RT   oxide reductase cytochrome P450nor from Fusarium oxysporum.";
RL   J. Biochem. 120:1082-1087(1996).
RN   [4]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=2040619; DOI=10.1016/s0021-9258(18)99130-1;
RA   Shoun H., Tanimoto T.;
RT   "Denitrification by the fungus Fusarium oxysporum and involvement of
RT   cytochrome P-450 in the respiratory nitrite reduction.";
RL   J. Biol. Chem. 266:11078-11082(1991).
RN   [5]
RP   CATALYTIC ACTIVITY.
RX   PubMed=7829493; DOI=10.1074/jbc.270.4.1617;
RA   Shiro Y., Fujii M., Iizuka T., Adachi S., Tsukamoto K., Nakahara K.,
RA   Shoun H.;
RT   "Spectroscopic and kinetic studies on reaction of cytochrome P450nor with
RT   nitric oxide. Implication for its nitric oxide reduction mechanism.";
RL   J. Biol. Chem. 270:1617-1623(1995).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF ARG-64; SER-73; SER-75; GLY-76; LYS-77; GLN-78
RP   AND ARG-174.
RX   PubMed=12105197; DOI=10.1074/jbc.m203923200;
RA   Zhang L., Kudo T., Takaya N., Shoun H.;
RT   "The B' helix determines cytochrome P450nor specificity for the electron
RT   donors NADH and NADPH.";
RL   J. Biol. Chem. 277:33842-33847(2002).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=9334748; DOI=10.1038/nsb1097-827;
RA   Park S.-Y., Shimizu H., Adachi S., Nakagawa A., Tanaka I., Nakahara K.,
RA   Shoun H., Obayashi E., Nakamura H., Iizuka T., Shiro Y.;
RT   "Crystal structure of nitric oxide reductase from denitrifying fungus
RT   Fusarium oxysporum.";
RL   Nat. Struct. Biol. 4:827-832(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-403 IN COMPLEX WITH HEME,
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-286 AND ASP-393.
RX   PubMed=10671516; DOI=10.1074/jbc.275.7.4816;
RA   Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.-Y., Nakamura H.,
RA   Adachi S., Shoun H., Shiro Y.;
RT   "Proton delivery in NO reduction by fungal nitric-oxide reductase.
RT   Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO
RT   complexes of wild-type and mutant enzymes.";
RL   J. Biol. Chem. 275:4816-4826(2000).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-402 IN COMPLEX WITH HEME OF WILD
RP   TYPE; MUTANT VAL-286 AND MUTANT THR-286, AND MUTAGENESIS OF SER-286.
RX   PubMed=11051564; DOI=10.1016/s0162-0134(00)00103-3;
RA   Shimizu H., Park S., Lee D., Shoun H., Shiro Y.;
RT   "Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val,
RT   Thr) in the ferric resting state at cryogenic temperature: a comparative
RT   analysis with monooxygenase cytochrome P450s.";
RL   J. Inorg. Biochem. 81:191-205(2000).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-402 IN COMPLEX WITH HEME.
RX   PubMed=11132616; DOI=10.1016/s0162-0134(00)00161-6;
RA   Obayashi E., Shimizu H., Park S.Y., Shoun H., Shiro Y.;
RT   "Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor
RT   on its structure and function.";
RL   J. Inorg. Biochem. 82:103-111(2000).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=11076941; DOI=10.1074/jbc.m007244200;
RA   Kudo T., Takaya N., Park S.Y., Shiro Y., Shoun H.;
RT   "A positively charged cluster formed in the heme-distal pocket of
RT   cytochrome P450nor is essential for interaction with NADH.";
RL   J. Biol. Chem. 276:5020-5026(2001).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=11258878; DOI=10.1021/bi002225s;
RA   Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.;
RT   "Structural characterization of n-butyl-isocyanide complexes of cytochromes
RT   P450nor and P450cam.";
RL   Biochemistry 40:2669-2677(2001).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=11752781; DOI=10.1107/s0907444901017383;
RA   Shimizu H., Park S.-Y., Shiro Y., Adachi S.;
RT   "X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic
RT   resolution.";
RL   Acta Crystallogr. D 58:81-89(2002).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH HEME, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=15313618; DOI=10.1016/j.jmb.2004.07.009;
RA   Oshima R., Fushinobu S., Su F., Zhang L., Takaya N., Shoun H.;
RT   "Structural evidence for direct hydride transfer from NADH to cytochrome
RT   P450nor.";
RL   J. Mol. Biol. 342:207-217(2004).
CC   -!- FUNCTION: Nitric oxide reductase which is involved in a dissimilatory
CC       reduction of nitrite. Acts as a nitric oxide reductase. Is able to
CC       reduce nitrate and nitrite to a gaseous form of N(2)O when oxygen
CC       supply is limited or discontinued. May function as a detoxification
CC       mechanism. {ECO:0000269|PubMed:12105197, ECO:0000269|PubMed:2040619}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=nitrous oxide + NADP(+) + H2O = 2 nitric oxide + NADPH + H(+);
CC         Xref=Rhea:RHEA:29611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17045, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.7.1.14;
CC         Evidence={ECO:0000269|PubMed:10671516, ECO:0000269|PubMed:15313618,
CC         ECO:0000269|PubMed:2040619, ECO:0000269|PubMed:7829493};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=nitrous oxide + NAD(+) + H2O = 2 nitric oxide + NADH + H(+);
CC         Xref=Rhea:RHEA:29607, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:17045, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.7.1.14;
CC         Evidence={ECO:0000269|PubMed:10671516, ECO:0000269|PubMed:15313618,
CC         ECO:0000269|PubMed:2040619, ECO:0000269|PubMed:7829493};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- ACTIVITY REGULATION: Cyanide, CO, and oxygen strongly inhibit catalytic
CC       activity. {ECO:0000269|PubMed:2040619}.
CC   -!- INDUCTION: By nitrate/nitrite. {ECO:0000269|PubMed:2037602}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M63340; AAA33337.1; -; mRNA.
DR   EMBL; D14517; BAA03390.1; -; Genomic_DNA.
DR   PIR; JC5150; JC5150.
DR   PIR; JC5151; JC5151.
DR   PDB; 1CL6; X-ray; 1.70 A; A=2-403.
DR   PDB; 1CMJ; X-ray; 1.70 A; A=2-403.
DR   PDB; 1CMN; X-ray; 1.70 A; A=2-403.
DR   PDB; 1EHE; X-ray; 1.70 A; A=2-403.
DR   PDB; 1EHF; X-ray; 1.70 A; A=2-403.
DR   PDB; 1EHG; X-ray; 1.70 A; A=2-403.
DR   PDB; 1F24; X-ray; 1.40 A; A=2-403.
DR   PDB; 1F25; X-ray; 1.40 A; A=2-403.
DR   PDB; 1F26; X-ray; 1.40 A; A=2-403.
DR   PDB; 1GED; X-ray; 2.00 A; A=1-403.
DR   PDB; 1GEI; X-ray; 1.60 A; A=1-403.
DR   PDB; 1GEJ; X-ray; 1.50 A; A=1-403.
DR   PDB; 1JFB; X-ray; 1.00 A; A=1-403.
DR   PDB; 1JFC; X-ray; 1.05 A; A=1-403.
DR   PDB; 1ROM; X-ray; 2.00 A; A=1-403.
DR   PDB; 1ULW; X-ray; 2.00 A; A=2-403.
DR   PDB; 1XQD; X-ray; 1.80 A; A=1-403.
DR   PDB; 2ROM; X-ray; 2.00 A; A=1-403.
DR   PDB; 5Y5F; X-ray; 1.50 A; A=1-403.
DR   PDB; 5Y5G; X-ray; 1.36 A; A=1-403.
DR   PDB; 5Y5H; X-ray; 1.50 A; A=1-403.
DR   PDB; 5Y5I; X-ray; 2.10 A; A/B=1-403.
DR   PDB; 5Y5J; X-ray; 2.00 A; A/B=1-403.
DR   PDB; 5Y5K; X-ray; 2.10 A; A/B=1-403.
DR   PDB; 5Y5L; X-ray; 2.10 A; A/B=1-403.
DR   PDB; 5Y5M; X-ray; 2.10 A; A/B=1-403.
DR   PDB; 7DVO; X-ray; 1.80 A; A/B=1-403.
DR   AlphaFoldDB; P23295; -.
DR   MDposit; P23295; -.
DR   SMR; P23295; -.
DR   iPTMnet; P23295; -.
DR   KEGG; ag:AAA33337; -.
DR   VEuPathDB; FungiDB:FOC1_g10003638; -.
DR   VEuPathDB; FungiDB:FOC4_g10005240; -.
DR   VEuPathDB; FungiDB:FOIG_14362; -.
DR   VEuPathDB; FungiDB:FOMG_14889; -.
DR   VEuPathDB; FungiDB:FOXG_12350; -.
DR   VEuPathDB; FungiDB:FOZG_13098; -.
DR   VEuPathDB; FungiDB:HZS61_006914; -.
DR   BioCyc; MetaCyc:MONOMER-16203; -.
DR   BRENDA; 1.7.1.14; 2351.
DR   BRENDA; 1.7.2.5; 2351.
DR   SABIO-RK; P23295; -.
DR   EvolutionaryTrace; P23295; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0102199; F:nitric oxide reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11030; CYP105-like; 1.
DR   FunFam; 1.10.630.10:FF:000018; Cytochrome P450 monooxygenase; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR46696:SF6; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Monooxygenase; NAD; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9010754"
FT   CHAIN           2..403
FT                   /note="NADP nitrous oxide-forming nitric oxide reductase"
FT                   /id="PRO_0000052039"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         352
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:9010754"
FT   MUTAGEN         64
FT                   /note="R->E: Impairs interaction with NADH."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         73
FT                   /note="S->A: Decreases the NADPH-dependent activity."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         75
FT                   /note="S->A: Decreases the NADPH-dependent activity."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         75
FT                   /note="S->G: Improves the NADPH-dependent activity."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         76
FT                   /note="G->A: Decreases the NADPH-dependent activity."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         77
FT                   /note="K->A: Decreases the NADPH-dependent activity."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         78
FT                   /note="Q->A: Decreases the NADPH-dependent activity."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         174
FT                   /note="R->E: Impairs interaction with NADH."
FT                   /evidence="ECO:0000269|PubMed:12105197"
FT   MUTAGEN         286
FT                   /note="S->V,T: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:10671516,
FT                   ECO:0000269|PubMed:11051564"
FT   MUTAGEN         393
FT                   /note="D->V,L: Impairs catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:10671516"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:1GEJ"
FT   HELIX           21..28
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:2ROM"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           93..98
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           102..105
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           107..131
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:1ULW"
FT   HELIX           141..145
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           147..157
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           164..175
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:1CL6"
FT   HELIX           181..204
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           210..214
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           215..219
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           226..257
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           259..267
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           272..282
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          291..296
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          298..300
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          303..305
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          310..313
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           315..318
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           335..337
FT                   /evidence="ECO:0007829|PDB:5Y5G"
FT   HELIX           348..350
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           355..372
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          377..380
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   HELIX           382..384
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          396..398
FT                   /evidence="ECO:0007829|PDB:1JFB"
FT   STRAND          400..402
FT                   /evidence="ECO:0007829|PDB:1JFB"
SQ   SEQUENCE   403 AA;  44372 MW;  7FDD97D8E0FB9215 CRC64;
     MASGAPSFPF SRASGPEPPA EFAKLRATNP VSQVKLFDGS LAWLVTKHKD VCFVATSEKL
     SKVRTRQGFP ELSASGKQAA KAKPTFVDMD PPEHMHQRSM VEPTFTPEAV KNLQPYIQRT
     VDDLLEQMKQ KGCANGPVDL VKEFALPVPS YIIYTLLGVP FNDLEYLTQQ NAIRTNGSST
     AREASAANQE LLDYLAILVE QRLVEPKDDI ISKLCTEQVK PGNIDKSDAV QIAFLLLVAG
     NATMVNMIAL GVATLAQHPD QLAQLKANPS LAPQFVEELC RYHTASALAI KRTAKEDVMI
     GDKLVRANEG IIASNQSANR DEEVFENPDE FNMNRKWPPQ DPLGFGFGDH RCIAEHLAKA
     ELTTVFSTLY QKFPDLKVAV PLGKINYTPL NRDVGIVDLP VIF
//