NOSO_BACSU
ID NOSO_BACSU Reviewed; 363 AA.
AC O34453;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Nitric oxide synthase oxygenase;
DE EC=1.14.14.47 {ECO:0000269|PubMed:11856757};
DE AltName: Full=NOSoxy-like protein;
GN Name=nos; Synonyms=yflM; OrderedLocusNames=BSU07630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT the Bacillus subtilis genome reveal genes for a new two-component system,
RT three spore germination proteins, an iron uptake system and a general
RT stress response protein.";
RL Gene 194:191-199(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=11856757; DOI=10.1074/jbc.m201136200;
RA Adak S., Aulak K.S., Stuehr D.J.;
RT "Direct evidence for nitric oxide production by a nitric-oxide synthase-
RT like protein from Bacillus subtilis.";
RL J. Biol. Chem. 277:16167-16171(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=12220171; DOI=10.1021/bi0263715;
RA Pant K., Bilwes A.M., Adak S., Stuehr D.J., Crane B.R.;
RT "Structure of a nitric oxide synthase heme protein from Bacillus
RT subtilis.";
RL Biochemistry 41:11071-11079(2002).
CC -!- FUNCTION: Catalyzes the production of nitric oxide.
CC {ECO:0000269|PubMed:11856757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-arginine + 4 O2 + 3 reduced [flavodoxin] = 5 H(+) + 4 H2O
CC + 2 L-citrulline + 2 nitric oxide + 3 oxidized [flavodoxin];
CC Xref=Rhea:RHEA:52324, Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57743, ChEBI:CHEBI:58210; EC=1.14.14.47;
CC Evidence={ECO:0000269|PubMed:11856757};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:11856757};
CC -!- COFACTOR:
CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000269|PubMed:11856757};
CC Note=Tetrahydrobiopterin (H4B). Can also use tetrahydrofolate (THF) in
CC place of tetrahydrobiopterin (H4B) but binds THF with much lower
CC affinity than H4B. {ECO:0000269|PubMed:11856757};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11856757}.
CC -!- MISCELLANEOUS: This protein is similar to the oxygenase domain of
CC eukaryotic nitric oxide synthases but lacks the reductase domain which,
CC in eukaryotes, is responsible for transfer of electrons to the ferric
CC heme during nitric oxide synthesis.
CC -!- SIMILARITY: Belongs to the NOS family. Bacterial NOS oxygenase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22306.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D86417; BAA22306.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12592.2; -; Genomic_DNA.
DR PIR; C69811; C69811.
DR RefSeq; NP_388644.2; NC_000964.3.
DR RefSeq; WP_003243309.1; NZ_JNCM01000032.1.
DR PDB; 1M7V; X-ray; 1.95 A; A=5-363.
DR PDB; 1M7Z; X-ray; 2.14 A; A=5-363.
DR PDB; 2AMO; X-ray; 2.60 A; A/B=30-363.
DR PDB; 2AN0; X-ray; 2.60 A; A=6-363.
DR PDB; 2AN2; X-ray; 2.60 A; A=6-363.
DR PDB; 2FBZ; X-ray; 2.10 A; X=5-363.
DR PDB; 2FC1; X-ray; 2.00 A; A=5-363.
DR PDB; 2FC2; X-ray; 2.20 A; A/B=5-363.
DR PDB; 4D3I; X-ray; 2.09 A; A=1-363.
DR PDB; 4D3J; X-ray; 1.67 A; A=1-363.
DR PDB; 4D3K; X-ray; 2.02 A; A/B=1-363.
DR PDB; 4D3M; X-ray; 1.74 A; A=1-363.
DR PDB; 4D3N; X-ray; 2.13 A; A=1-363.
DR PDB; 4D3O; X-ray; 1.90 A; A=1-363.
DR PDB; 4D3T; X-ray; 1.55 A; A=1-363.
DR PDB; 4D3U; X-ray; 1.98 A; A=1-363.
DR PDB; 4D3V; X-ray; 1.88 A; A=1-363.
DR PDB; 4D7H; X-ray; 2.02 A; A=1-363.
DR PDB; 4D7I; X-ray; 1.96 A; A=1-363.
DR PDB; 4D7J; X-ray; 1.55 A; A=1-363.
DR PDB; 4LWA; X-ray; 2.06 A; A=1-363.
DR PDB; 4LWB; X-ray; 2.15 A; A=1-363.
DR PDB; 4UG5; X-ray; 2.35 A; A=1-363.
DR PDB; 4UG6; X-ray; 1.81 A; A=1-363.
DR PDB; 4UG7; X-ray; 1.76 A; A=1-363.
DR PDB; 4UG8; X-ray; 1.89 A; A=1-363.
DR PDB; 4UG9; X-ray; 1.84 A; A=1-363.
DR PDB; 4UGA; X-ray; 1.90 A; A=1-363.
DR PDB; 4UGB; X-ray; 1.91 A; A=1-363.
DR PDB; 4UGC; X-ray; 1.80 A; A=1-363.
DR PDB; 4UGD; X-ray; 2.03 A; A=1-363.
DR PDB; 4UGE; X-ray; 2.14 A; A=1-363.
DR PDB; 4UGF; X-ray; 1.81 A; A=1-363.
DR PDB; 4UGG; X-ray; 2.36 A; A=1-363.
DR PDB; 4UGH; X-ray; 1.99 A; A=1-363.
DR PDB; 4UGI; X-ray; 1.80 A; A=1-363.
DR PDB; 4UGJ; X-ray; 1.78 A; A=1-363.
DR PDB; 4UGK; X-ray; 1.62 A; A=1-363.
DR PDB; 4UGL; X-ray; 1.82 A; A=1-363.
DR PDB; 4UGM; X-ray; 2.09 A; A=1-363.
DR PDB; 4UGN; X-ray; 2.09 A; A=1-363.
DR PDB; 4UGO; X-ray; 2.38 A; A=1-363.
DR PDB; 4UGP; X-ray; 1.80 A; A=1-363.
DR PDB; 4UGQ; X-ray; 1.85 A; A=1-363.
DR PDB; 4UGR; X-ray; 2.09 A; A=1-363.
DR PDB; 4UGS; X-ray; 1.99 A; A=1-363.
DR PDB; 4UGT; X-ray; 2.03 A; A=1-363.
DR PDB; 4UGU; X-ray; 1.80 A; A=1-363.
DR PDB; 4UGV; X-ray; 1.99 A; A=1-363.
DR PDB; 4UGW; X-ray; 1.90 A; A=1-363.
DR PDB; 4UGX; X-ray; 1.86 A; A=1-363.
DR PDB; 4UGY; X-ray; 1.80 A; A=1-363.
DR PDB; 4UQR; X-ray; 1.72 A; A=1-363.
DR PDB; 4UQS; X-ray; 2.15 A; A=1-363.
DR PDB; 5G65; X-ray; 2.03 A; A=1-363.
DR PDB; 5G66; X-ray; 1.76 A; A=1-363.
DR PDB; 5G67; X-ray; 1.97 A; A=1-363.
DR PDB; 5G68; X-ray; 1.63 A; A=1-363.
DR PDB; 5G69; X-ray; 2.02 A; A=1-363.
DR PDB; 5G6A; X-ray; 1.92 A; A=1-363.
DR PDB; 5G6B; X-ray; 1.80 A; A=1-363.
DR PDB; 5G6C; X-ray; 2.13 A; A=1-363.
DR PDB; 5G6D; X-ray; 1.82 A; A=1-363.
DR PDB; 5G6E; X-ray; 2.11 A; A=1-363.
DR PDB; 5G6F; X-ray; 2.26 A; A=1-363.
DR PDB; 5G6G; X-ray; 1.98 A; A=1-363.
DR PDB; 5G6H; X-ray; 1.91 A; A=1-363.
DR PDB; 5G6I; X-ray; 1.98 A; A=1-363.
DR PDB; 5G6J; X-ray; 1.88 A; A=1-363.
DR PDB; 5G6K; X-ray; 1.95 A; A=1-363.
DR PDB; 5G6L; X-ray; 2.03 A; A=1-363.
DR PDB; 5G6M; X-ray; 1.77 A; A=1-363.
DR PDB; 5G6N; X-ray; 1.91 A; A=1-363.
DR PDB; 5G6O; X-ray; 1.72 A; A=1-363.
DR PDB; 5G6P; X-ray; 2.18 A; A=1-363.
DR PDB; 5G6Q; X-ray; 2.03 A; A=1-363.
DR PDB; 6XCX; X-ray; 2.25 A; A=1-363.
DR PDB; 6XK3; X-ray; 1.95 A; A=1-363.
DR PDB; 6XK4; X-ray; 2.13 A; A=1-363.
DR PDB; 6XK5; X-ray; 1.87 A; A=1-363.
DR PDB; 6XK6; X-ray; 1.84 A; A=1-363.
DR PDB; 6XK7; X-ray; 1.85 A; A=1-363.
DR PDB; 6XK8; X-ray; 2.25 A; A=1-363.
DR PDB; 6XMC; X-ray; 1.85 A; A=1-363.
DR PDBsum; 1M7V; -.
DR PDBsum; 1M7Z; -.
DR PDBsum; 2AMO; -.
DR PDBsum; 2AN0; -.
DR PDBsum; 2AN2; -.
DR PDBsum; 2FBZ; -.
DR PDBsum; 2FC1; -.
DR PDBsum; 2FC2; -.
DR PDBsum; 4D3I; -.
DR PDBsum; 4D3J; -.
DR PDBsum; 4D3K; -.
DR PDBsum; 4D3M; -.
DR PDBsum; 4D3N; -.
DR PDBsum; 4D3O; -.
DR PDBsum; 4D3T; -.
DR PDBsum; 4D3U; -.
DR PDBsum; 4D3V; -.
DR PDBsum; 4D7H; -.
DR PDBsum; 4D7I; -.
DR PDBsum; 4D7J; -.
DR PDBsum; 4LWA; -.
DR PDBsum; 4LWB; -.
DR PDBsum; 4UG5; -.
DR PDBsum; 4UG6; -.
DR PDBsum; 4UG7; -.
DR PDBsum; 4UG8; -.
DR PDBsum; 4UG9; -.
DR PDBsum; 4UGA; -.
DR PDBsum; 4UGB; -.
DR PDBsum; 4UGC; -.
DR PDBsum; 4UGD; -.
DR PDBsum; 4UGE; -.
DR PDBsum; 4UGF; -.
DR PDBsum; 4UGG; -.
DR PDBsum; 4UGH; -.
DR PDBsum; 4UGI; -.
DR PDBsum; 4UGJ; -.
DR PDBsum; 4UGK; -.
DR PDBsum; 4UGL; -.
DR PDBsum; 4UGM; -.
DR PDBsum; 4UGN; -.
DR PDBsum; 4UGO; -.
DR PDBsum; 4UGP; -.
DR PDBsum; 4UGQ; -.
DR PDBsum; 4UGR; -.
DR PDBsum; 4UGS; -.
DR PDBsum; 4UGT; -.
DR PDBsum; 4UGU; -.
DR PDBsum; 4UGV; -.
DR PDBsum; 4UGW; -.
DR PDBsum; 4UGX; -.
DR PDBsum; 4UGY; -.
DR PDBsum; 4UQR; -.
DR PDBsum; 4UQS; -.
DR PDBsum; 5G65; -.
DR PDBsum; 5G66; -.
DR PDBsum; 5G67; -.
DR PDBsum; 5G68; -.
DR PDBsum; 5G69; -.
DR PDBsum; 5G6A; -.
DR PDBsum; 5G6B; -.
DR PDBsum; 5G6C; -.
DR PDBsum; 5G6D; -.
DR PDBsum; 5G6E; -.
DR PDBsum; 5G6F; -.
DR PDBsum; 5G6G; -.
DR PDBsum; 5G6H; -.
DR PDBsum; 5G6I; -.
DR PDBsum; 5G6J; -.
DR PDBsum; 5G6K; -.
DR PDBsum; 5G6L; -.
DR PDBsum; 5G6M; -.
DR PDBsum; 5G6N; -.
DR PDBsum; 5G6O; -.
DR PDBsum; 5G6P; -.
DR PDBsum; 5G6Q; -.
DR PDBsum; 6XCX; -.
DR PDBsum; 6XK3; -.
DR PDBsum; 6XK4; -.
DR PDBsum; 6XK5; -.
DR PDBsum; 6XK6; -.
DR PDBsum; 6XK7; -.
DR PDBsum; 6XK8; -.
DR PDBsum; 6XMC; -.
DR AlphaFoldDB; O34453; -.
DR SMR; O34453; -.
DR STRING; 224308.BSU07630; -.
DR BindingDB; O34453; -.
DR DrugBank; DB02031; (6S)-5,6,7,8-tetrahydrofolic acid.
DR DrugBank; DB03144; N(5)-[(hydroxyamino)(imino)methyl]-L-ornithine.
DR PaxDb; O34453; -.
DR EnsemblBacteria; CAB12592; CAB12592; BSU_07630.
DR GeneID; 938802; -.
DR KEGG; bsu:BSU07630; -.
DR PATRIC; fig|224308.179.peg.829; -.
DR eggNOG; COG4362; Bacteria.
DR InParanoid; O34453; -.
DR OMA; IWNHQLI; -.
DR PhylomeDB; O34453; -.
DR BioCyc; BSUB:BSU07630-MON; -.
DR BioCyc; MetaCyc:BSU07630-MON; -.
DR BRENDA; 1.14.13.39; 658.
DR BRENDA; 1.14.14.47; 658.
DR BRENDA; 1.18.1.2; 9933.
DR SABIO-RK; O34453; -.
DR EvolutionaryTrace; O34453; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.90.1230.10; -; 1.
DR Gene3D; 3.90.340.10; -; 1.
DR Gene3D; 3.90.440.10; -; 1.
DR InterPro; IPR017142; Nitric_oxide_synthase_Oase-su.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR Pfam; PF02898; NO_synthase; 1.
DR PIRSF; PIRSF037219; NOS_oxygenase; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
DR PROSITE; PS60001; NOS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..363
FT /note="Nitric oxide synthase oxygenase"
FT /id="PRO_0000170953"
FT BINDING 66
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 HELIX 3..21
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 86..101
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:4D3T"
FT TURN 246..250
FT /evidence="ECO:0007829|PDB:4D3T"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 276..295
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 302..319
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4D3T"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4D3T"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:4D3T"
SQ SEQUENCE 363 AA; 41903 MW; 4F889E68B4BDE5C6 CRC64;
MEEKEILWNE AKAFIAACYQ ELGKEEEVKD RLADIKSEID LTGSYVHTKE ELEHGAKMAW
RNSNRCIGRL FWNSLNVIDR RDVRTKEEVR DALFHHIETA TNNGKIRPTI TIFPPEEKGE
KQVEIWNHQL IRYAGYESDG ERIGDPASCS LTAACEELGW RGERTDFDLL PLIFRMKGDE
QPVWYELPRS LVIEVPITHP DIEAFSDLEL KWYGVPIISD MKLEVGGIHY NAAPFNGWYM
GTEIGARNLA DEKRYDKLKK VASVIGIAAD YNTDLWKDQA LVELNKAVLH SYKKQGVSIV
DHHTAASQFK RFEEQEEEAG RKLTGDWTWL IPPISPAATH IFHRSYDNSI VKPNYFYQDK
PYE
