GenomeNet

Database: UniProt
Entry: A2I9X5_CHICK
LinkDB: A2I9X5_CHICK
Original site: A2I9X5_CHICK 
ID   A2I9X5_CHICK            Unreviewed;       123 AA.
AC   A2I9X5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE            EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
DE   Flags: Fragment;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:ABM65097.1};
RN   [1] {ECO:0000313|EMBL:ABM65097.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bera A.K., Pan D., Bhattacharya D., Das S.K.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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=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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF178279; ABM65097.1; -; mRNA.
DR   AlphaFoldDB; A2I9X5; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-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   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022643};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..72
FT                   /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT                   component-like FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00667"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABM65097.1"
FT   NON_TER         123
FT                   /evidence="ECO:0000313|EMBL:ABM65097.1"
SQ   SEQUENCE   123 AA;  13828 MW;  D11E002F8DA5545E CRC64;
     RPNILEVLEE FPSAEVSTAF LLTQLPLLKP RYYSVSSSCD MTPREIHLTV AVVNYRTRDG
     QGPLHHGVCS TWLNKIALNE TVPCFVRSAD GFRLPKEPAK PCILIGPGTG IAPFRSFWQQ
     RLY
//
DBGET integrated database retrieval system