ID W5KX81_ASTMX Unreviewed; 1075 AA.
AC W5KX81;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Nitric oxide synthase {ECO:0000256|PIRNR:PIRNR000333};
DE EC=1.14.13.39 {ECO:0000256|PIRNR:PIRNR000333};
GN Name=NOS2 {ECO:0000313|Ensembl:ENSAMXP00000012193.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000012193.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000012193.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00001970,
CC 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 AlphaFoldDB; W5KX81; -.
DR STRING; 7994.ENSAMXP00000012193; -.
DR Ensembl; ENSAMXT00000012193.2; ENSAMXP00000012193.2; ENSAMXG00000011861.2.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000159752; -.
DR HOGENOM; CLU_001570_17_7_1; -.
DR InParanoid; W5KX81; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000011861; Expressed in mesonephros and 5 other cell types or tissues.
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; -; 2.
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; 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.
DR PROSITE; PS60001; NOS; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW 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:UP000018467}.
FT DOMAIN 486..624
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 673..916
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 146
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 1075 AA; 121136 MW; 7A75F245C5B3D16C CRC64;
MGKTIVENEL PQAKANTKVS EKKVSRCPMA MQMKNFQNGS SHQDTLYHRA IKNQLCKPKV
CEGSVMNPKT LIRSPANTPP GPNELLIQAI DFINQYYKSF KTSKIEEHLA RVDEVAQEID
ATGTYQLTTE ELAFGAKQAW RNAPRCIGRI QWANLQLFDA RHCKTAKEMF QFMCSHLKFA
TNGGNLRSAI TVFPQRTDGE HDFRVWNGQL IKYAGYQMED GSVVGDPASV EFTELCIQLG
WTPKYGLFDV LPLVLQANGE DPELFEIPPE LILEVEMEHP HYEWFKDLNL RWYALPAVAN
MLMEIGGLEF TACPFNGWYM GTEIGVRDFC DPQRYNILEK VGCYMGLETQ KLSSLWKDEA
LVAINVAVIH SFQKNKVTIT DHHSAAESFM KHMETEVRLR GGCPADWIWL VPPMSGSLTP
VFHQEMISYI LSPFFYYQTD PWLTHVWKDE EKGLKKRKRI SFGALTKAVV FSQILMQKAL
ENRVPCTILY ATETGKSQTF AKKLKSMLSC AFNPRLLCME DYRFGDLEKE RLLIVVTSTF
GNGESPGNGE TFQKKLMGKK QLKNNLRYCV FGLGSRMYPQ FCAFAHAVDD KLAELGAKCV
TPIGEGDELN GQDEAFSAWA CTAFKAVCKE FGIEGQLSGA ERLTDSWDPQ KIRVQPDSST
LDCISALSAL HSKTVFPMKL KRRKNLQSSQ SRRSTILVEL EVHGAKDVLN YAPGDHVGVF
PENSPELVTG ILKHIPSVPP TNQSLHLEYQ ANSGGVGWQK DERLPACSLT QALTYLLDIT
TPPSQGLLRK LSQVSKKEDD RQRLLALASD FKSYSEWKEF RKPNFLEVLE EFPSLEVSAA
FVLSQLPLMK PRLYSLSSSP DLHPNELHLT VSVVNYRTQD GKGPLHHGVC STWLNTLKDG
HTVPCFIHGS SGFHLPPDPT TPTILIGAGS GIAPFRSFWQ QRYHDKEKKG LKESPMMLVF
GCRDSDTDHL YKEETYEMRE NGTLKSITPA YSRQPGHPKV YVQDVLKKQL SEEVWQALQK
AGHVYVCGGM NMAREVAHTI QDIVAGQLGV PFSEAGGYLE RLKAEKRYHE DIFGA
//
