ID A0A2R2MLV0_LINUN Unreviewed; 1030 AA.
AC A0A2R2MLV0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
GN Name=LOC106176019 {ECO:0000313|RefSeq:XP_023931191.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_023931191.1};
RN [1] {ECO:0000313|RefSeq:XP_023931191.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_023931191.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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DR RefSeq; XP_023931191.1; XM_024075423.1.
DR AlphaFoldDB; A0A2R2MLV0; -.
DR EnsemblMetazoa; XM_024075423.1; XP_023931191.1; LOC106176019.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.90.440.10; Nitric Oxide Synthase;Heme Domain;Chain A domain 2; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR012144; NOS_euk.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR PIRSF; PIRSF000333; NOS; 2.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56512; Nitric oxide (NO) synthase oxygenase domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000333-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000333-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000333-1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 427..565
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 615..858
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 90
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000333-1"
SQ SEQUENCE 1030 AA; 117084 MW; 2E5D8252D01EEE72 CRC64;
MASICTGAFV IKPSTVPPQE ATDRNNDQIQ VEALDFIDQY YCHLNRKDSE EHLQRKVVVA
QAIQDTGTYH IEYDELVFGA KTAWRNASRC SGRIQWKNLQ VFDAREIQTA EEMFRAICHH
LTWATNGGNI RSAMTVFPAR TNKKKDFRIW NSQFIRYAGY RMPGGHIIGD PSNLSFTQIC
ERLGWKGKGG HFDVLPLVLS ANGEPPELFE IPKEIILEVE LTHPRFDWFK ELGLKWYAVP
VVSNMLFDCG GLEFPAAPFN GWYMGTEIGA RNLCDVQRYN ILEIVGQRMG LDCRSSVNLW
KDLALVEVNI AVLHSYQKAG VSIVDHHTVA DSFVQFMLQE AKTRGGCPAD WVWIVPPISG
SITPVFHQEM VNYTIKPSFD YQEDPPLLLL NQLDKEKNMK NLVFGIFRAV LLASKLKMKI
RKCRPKCLIL FASETGKSEQ FARRLEATMG RAFNARTVCM EDYPVNSFLQ EQLVLVVTST
FGLGSPPLNG ETFFRALESF EKNLSNIRFA VFGLGSKAYP RFCAFAVHID NLLRNLGGQR
MTSLVKADSL SGQEKPFVKW SRQVYNEACA LYGLLTFKHA DDIEVTTEWH EERFRYTVVG
KEEDIIKGLS EIHGYQMQSF NIISSTNLQA KSSGLRSLSV KLQSTTNKDK LVYQHGDHML
IFPTNNIAMV TAIIQRIKDL PLCGAAVQLE TFSVKHNAWG SHPRLPPCTI QMALLHYLDI
TKPPTQDMLK GLAQLATNNK EHNRLITLAK NEEAYLQWRD YKMPTIVDVL SEFQSIQLPV
AFLLSQLPIL EPRCFSVSSS PDVHPNEIHL TVGVLQYRTN DGRLHDGLCT TWLENLGQNN
NTTTIPCAIK LHKTFQLPHD AGVPVLMLGI GTGIAPFRGF WQHRYYQMIH PMPGIKFGPM
TLFHGCRQKG VDDLYSQEIS LMQESKVLTS VHYAYSRMPG QPRIYIQHLL CEQAQTTYEQ
LVVQEGHIYI CGSITMAMDV RKTLLNILCE EGNMTTDKAQ NYMELLRKSG RYHEELFGLG
YPHHRLNHIK
//
