NOSO_STAAU
ID NOSO_STAAU Reviewed; 358 AA.
AC P0A004; Q99SX3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Nitric oxide synthase oxygenase;
DE EC=1.14.14.47 {ECO:0000250|UniProtKB:O34453};
DE AltName: Full=NOSoxy-like protein;
DE AltName: Full=SANOS;
GN Name=nos;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-346.
RX PubMed=12467576; DOI=10.1016/s0969-2126(02)00911-5;
RA Bird L.E., Ren J., Zhang J., Foxwell N., Hawkins A.R., Charles I.G.,
RA Stammers D.K.;
RT "Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase
RT protein from Staphylococcus aureus.";
RL Structure 10:1687-1696(2002).
CC -!- FUNCTION: Catalyzes the production of nitric oxide.
CC {ECO:0000250|UniProtKB:O34453}.
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:0000250|UniProtKB:O34453};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- COFACTOR:
CC Name=(6S)-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:57453;
CC Evidence={ECO:0000250|UniProtKB:O34453};
CC -!- SUBUNIT: Homodimer.
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}.
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DR RefSeq; WP_000897635.1; NZ_WTUM01000046.1.
DR PDB; 1MJT; X-ray; 2.40 A; A/B=2-346.
DR PDBsum; 1MJT; -.
DR AlphaFoldDB; P0A004; -.
DR SMR; P0A004; -.
DR OMA; IWNHQLI; -.
DR BRENDA; 1.14.14.47; 3352.
DR EvolutionaryTrace; P0A004; -.
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; IEA:InterPro.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
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.
FT CHAIN 1..358
FT /note="Nitric oxide synthase oxygenase"
FT /id="PRO_0000170960"
FT BINDING 62
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 2..16
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:1MJT"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 263..281
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 289..304
FT /evidence="ECO:0007829|PDB:1MJT"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:1MJT"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1MJT"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:1MJT"
SQ SEQUENCE 358 AA; 41710 MW; 349A3A83E8D643A1 CRC64;
MLFKEAQAFI ENMYKECHYE TQIINKRLHD IELEIKETGT YTHTEEELIY GAKMAWRNSN
RCIGRLFWDS LNVIDARDVT DEASFLSSIT YHITQATNEG KLKPYITIYA PKDGPKIFNN
QLIRYAGYDN CGDPAEKEVT RLANHLGWKG KGTNFDVLPL IYQLPNESVK FYEYPTSLIK
EVPIEHNHYP KLRKLNLKWY AVPIISNMDL KIGGIVYPTA PFNGWYMVTE IGVRNFIDDY
RYNLLEKVAD AFEFDTLKNN SFNKDRALVE LNYAVYHSFK KEGVSIVDHL TAAKQFELFE
RNEAQQGRQV TGKWSWLAPP LSPTLTSNYH HGYDNTVKDP NFFYKKKESN ANQCPFHH
