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Database: UniProt
Entry: A0A091D5Q4_FUKDA
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ID   A0A091D5Q4_FUKDA        Unreviewed;      1155 AA.
AC   A0A091D5Q4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333};
DE            EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333};
GN   ORFNames=H920_13098 {ECO:0000313|EMBL:KFO25590.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25590.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO25590.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO25590.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC       diverse functions. {ECO:0000256|PIRNR:PIRNR000333}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC         + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC         Evidence={ECO:0000256|ARBA:ARBA00035595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC         Evidence={ECO:0000256|ARBA:ARBA00035595};
CC   -!- COFACTOR:
CC       Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC         Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000333};
CC       Note=Binds 1 FAD. {ECO:0000256|PIRNR:PIRNR000333};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000333};
CC       Note=Binds 1 FMN. {ECO:0000256|PIRNR:PIRNR000333};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000333};
CC   -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267,
CC       ECO:0000256|PIRNR:PIRNR000333}.
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DR   EMBL; KN123351; KFO25590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091D5Q4; -.
DR   STRING; 885580.ENSFDAP00000018188; -.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
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   CDD; cd00795; NOS_oxygenase_euk; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 6.10.250.410; -; 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; 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; 2.
DR   PIRSF; PIRSF000333; NOS; 3.
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; 2.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS60001; NOS; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|PIRNR:PIRNR000333};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000333};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000333};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000333};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000333};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000333};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000333};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000333};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          748..988
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          42..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         199
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   1155 AA;  131099 MW;  E76F8C7F512AFFBE CRC64;
     MREGLSAACE AARPRLYRFL RRILPPKPTR CLGRASPEIQ NDPKCCSPGK HQNGSSQPLL
     GTAEKSPESQ TKPHEPLPTC PQHMTIKNWG SGMILQDTLH NKAETNFTCK SKSCLGSVMN
     PRSLTRGPRD KSTPPDELLP QAIEFVNQYY DSFKEAKIEE HLARVEAVTK EIETTGTYQL
     TGDELIFATK LAWRNAPRCI GRIQWSNLQV FDARSCITAQ EMFEHICRHL RYATNNGNIR
     SAITVFPQRT DGKHDFRVWN AQLIRYAGYQ MPDGTIRGDP ANLEFTQLCI DLGWEPRYGR
     FDVLPLVLQA DGRDPELFEI PPDLVLEVPV EHPKYEWFQE LGLKWYALPA VANMMLEVGG
     LEFPGCPFNG WYMGTEIGAR DFCDAQRYNI LEEVGRRMGL ETHTLASLWK DRAVTEVNAA
     VLHSFQGGRL RMCEDITLGD QTISTKLTSA LEIRALGRES FIQSAKIIWT FAMCQDGAKN
     KQNVTIMDHH SAAESFMKHM QNEYRTRGGC PADWVWLVPP ISGSITPVFH QEMLNYILSP
     FYYYQVDAWK THVWQDEKRR PRRREIPFRV LGRAVLFASV LMRKMMASRV RVTILFATET
     GKSEALAQDL GALFSRAFNP KTLKKSLFML KKLTNTFRYA VFGLGSSMYP RFCAFAHDVD
     LKLSQLGASQ LTPVGEGDEL GGQEGAFRTW AVQTFKAACV AFDVRGKHHI QIPKLYTSTV
     TWEPHHYRLV QDLQPLDLNK ALSRMHAKDV FTLRLKSQQN LQSPKSSRTT LLVELSCEDS
     RGLAYLPGDH LGVFPCNQPA LVRGILERVV DSLGPHHTVR LEALDDSGSY WVKDKRLPPC
     SLSQALTYFL DITTPPTQLQ LQKLARLATK QAERQRLETL SQPSEYNKWK FTGSPTFLEV
     LEEFPSLRVP AAFLLSQLPI LKPRYYSISS CLDHTPAEVH LTVAVVAYRT QDGRGPLHHG
     VCSTWLSSLK PQDPVPCFMR RVSSFQLPKD PSHPCILIGP GTGIAPFRRV QGGRMTLVFG
     CRHPEEDHIY KEEMLEMAQK RVLHEVHTAY SRLPGKPKVY VQDVLRQQLA GEVLRVLHEE
     PGHLYVCGSV LVARDVADVL KQLLAAKLNL NEEQVEDYFF QLKSQKRYHE DIFGAVFPYE
     VKKDRAERPP GDIKL
//
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