NOR_FUSOX
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 03-AUG-2022, entry version 126.
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=H2O + NADP(+) + nitrous oxide = H(+) + NADPH + 2 nitric oxide;
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=H2O + NAD(+) + nitrous oxide = H(+) + NADH + 2 nitric oxide;
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 PDBsum; 1CL6; -.
DR PDBsum; 1CMJ; -.
DR PDBsum; 1CMN; -.
DR PDBsum; 1EHE; -.
DR PDBsum; 1EHF; -.
DR PDBsum; 1EHG; -.
DR PDBsum; 1F24; -.
DR PDBsum; 1F25; -.
DR PDBsum; 1F26; -.
DR PDBsum; 1GED; -.
DR PDBsum; 1GEI; -.
DR PDBsum; 1GEJ; -.
DR PDBsum; 1JFB; -.
DR PDBsum; 1JFC; -.
DR PDBsum; 1ROM; -.
DR PDBsum; 1ULW; -.
DR PDBsum; 1XQD; -.
DR PDBsum; 2ROM; -.
DR PDBsum; 5Y5F; -.
DR PDBsum; 5Y5G; -.
DR PDBsum; 5Y5H; -.
DR PDBsum; 5Y5I; -.
DR PDBsum; 5Y5J; -.
DR PDBsum; 5Y5K; -.
DR PDBsum; 5Y5L; -.
DR PDBsum; 5Y5M; -.
DR PDBsum; 7DVO; -.
DR AlphaFoldDB; P23295; -.
DR SMR; P23295; -.
DR iPTMnet; P23295; -.
DR PRIDE; 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:MON-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:UniProtKB-KW.
DR GO; GO:0102199; F:nitric oxide reductase activity (NAD(P)H-dependent) 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 Gene3D; 1.10.630.10; -; 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 Pfam; PF00067; p450; 2.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 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 STRAND 13..17
FT /evidence="ECO:0007829|PDB:1GED"
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 140..143
FT /evidence="ECO:0007829|PDB:1JFB"
FT TURN 144..146
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..217
FT /evidence="ECO:0007829|PDB:1JFB"
FT TURN 218..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 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
