ID F5L4S5_CALTT Unreviewed; 362 AA.
AC F5L4S5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Nitric oxide synthase oxygenase {ECO:0000256|ARBA:ARBA00018859, ECO:0000256|PIRNR:PIRNR037219};
DE EC=1.14.14.47 {ECO:0000256|ARBA:ARBA00012735, ECO:0000256|PIRNR:PIRNR037219};
GN ORFNames=CathTA2_0788 {ECO:0000313|EMBL:EGL83674.1}, HUR95_05300
GN {ECO:0000313|EMBL:QZT34722.1};
OS Caldalkalibacillus thermarum (strain TA2.A1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL83674.1, ECO:0000313|Proteomes:UP000010716};
RN [1] {ECO:0000313|EMBL:EGL83674.1, ECO:0000313|Proteomes:UP000010716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL83674.1,
RC ECO:0000313|Proteomes:UP000010716};
RX PubMed=21685297; DOI=10.1128/JB.05035-11;
RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA Cook G.M.;
RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT thermarum strain TA2.A1.";
RL J. Bacteriol. 193:4290-4291(2011).
RN [2] {ECO:0000313|EMBL:QZT34722.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT34722.1};
RX PubMed=33030592;
RA de Jong S.I., van den Broek M.A., Merkel A.Y., de la Torre Cortes P.,
RA Kalamorz F., Cook G.M., van Loosdrecht M.C.M., McMillan D.G.G.;
RT "Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic
RT alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic
RT bacteria and plant life.";
RL Extremophiles 24:923-935(2020).
RN [3] {ECO:0000313|EMBL:QZT34722.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT34722.1};
RA de Jong S., van den Broek M., Merkel A., de la Torre Cortes P.,
RA Kalamorz F., Cook G., van Loosdrecht M., McMillan D.;
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the production of nitric oxide.
CC {ECO:0000256|ARBA:ARBA00002642, ECO:0000256|PIRNR:PIRNR037219}.
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:0000256|ARBA:ARBA00000737};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR037219, ECO:0000256|PIRSR:PIRSR037219-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR037219}.
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. {ECO:0000256|PIRNR:PIRNR037219}.
CC -!- SIMILARITY: Belongs to the NOS family. Bacterial NOS oxygenase
CC subfamily. {ECO:0000256|ARBA:ARBA00005411,
CC ECO:0000256|PIRNR:PIRNR037219}.
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DR EMBL; AFCE01000091; EGL83674.1; -; Genomic_DNA.
DR EMBL; CP082237; QZT34722.1; -; Genomic_DNA.
DR RefSeq; WP_007503311.1; NZ_CP082237.1.
DR AlphaFoldDB; F5L4S5; -.
DR KEGG; cthu:HUR95_05300; -.
DR eggNOG; COG4362; Bacteria.
DR OrthoDB; 3398374at2; -.
DR Proteomes; UP000010716; Unassembled WGS sequence.
DR Proteomes; UP000825179; 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; IEA:InterPro.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR CDD; cd00575; NOS_oxygenase; 1.
DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 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 PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR PIRSF; PIRSF037219; NOS_oxygenase; 1.
DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR PROSITE; PS60001; NOS; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR037219};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR037219};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037219};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR037219};
KW Reference proteome {ECO:0000313|Proteomes:UP000010716}.
FT DOMAIN 65..72
FT /note="Nitric oxide synthase (NOS)"
FT /evidence="ECO:0000259|PROSITE:PS60001"
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 /evidence="ECO:0000256|PIRSR:PIRSR037219-1"
SQ SEQUENCE 362 AA; 42552 MW; 1F04A03F988EF218 CRC64;
MTEKETLFHE AKQFITACYH ELNKPDIIEE RLKEIKSEIN RYGYYEHTYE ELAYGARVAW
RNSNRCIGRL FWRSLHVFDA RHLATEQGIY EALLNHITYA TNEGKIRPAI TIFKPQIKQE
PQVRIWNHQL IRYAGYETEN GVTGDPASLS LTRACQEMGW KGKGSRFDVL PLVIQVQQRP
PKWFEIPEEL VLEVPIRHPE YDWFEDLNIK WYAVPIISDM CLEIGGIHYT ASPFNGWYME
TEIGARNLAD TFRYNLLPEV AKRMGLEISR NASLWKDKAL VELNVAVLHS YKQDGVSIVD
HHTAAEQFKQ FEQQERDSGR KVTGDWTWLI PPLSPATTHI FHQTYENRIL KPNYFYQDRP
YE
//
