NOXA_DICDI
ID NOXA_DICDI Reviewed; 517 AA.
AC Q9XYS3; Q54H54;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Superoxide-generating NADPH oxidase heavy chain subunit A;
DE EC=1.-.-.-;
DE AltName: Full=NADPH oxidase A;
DE AltName: Full=Superoxide-generating NADPH oxidase flavocytochrome A;
GN Name=noxA; ORFNames=DDB_G0289653;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=AX2;
RX PubMed=15950752; DOI=10.1016/j.bbamcr.2005.02.004;
RA Lardy B., Bof M., Aubry L., Paclet M.H., Morel F., Satre M., Klein G.;
RT "NADPH oxidase homologs are required for normal cell differentiation and
RT morphogenesis in Dictyostelium discoideum.";
RL Biochim. Biophys. Acta 1744:199-212(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Critical component of the membrane-bound oxidase that
CC generates superoxide. It is the terminal component of a respiratory
CC chain that transfers single electrons from cytoplasmic NADPH across the
CC plasma membrane to molecular oxygen on the exterior (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBUNIT: Composed of a heavy chain and a light chain. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during vegetative stage.
CC Expression decreases during development and is very low in fruiting
CC bodies. {ECO:0000269|PubMed:15950752}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype on vegetative growth, but
CC prevents formation of fruiting bodies. {ECO:0000269|PubMed:15950752}.
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DR EMBL; AF123275; AAD22057.1; -; Genomic_DNA.
DR EMBL; AAFI02000148; EAL62538.1; -; Genomic_DNA.
DR RefSeq; XP_636064.1; XM_630972.1.
DR AlphaFoldDB; Q9XYS3; -.
DR SMR; Q9XYS3; -.
DR STRING; 44689.DDB0191274; -.
DR PeroxiBase; 6101; DdNOx01.
DR PaxDb; Q9XYS3; -.
DR ABCD; Q9XYS3; 1 sequenced antibody.
DR EnsemblProtists; EAL62538; EAL62538; DDB_G0289653.
DR GeneID; 8627274; -.
DR KEGG; ddi:DDB_G0289653; -.
DR dictyBase; DDB_G0289653; noxA.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_3_0_1; -.
DR InParanoid; Q9XYS3; -.
DR OMA; KPSMKYK; -.
DR PhylomeDB; Q9XYS3; -.
DR Reactome; R-DDI-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-DDI-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q9XYS3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
DR GO; GO:0043020; C:NADPH oxidase complex; ISS:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:dictyBase.
DR GO; GO:0020037; F:heme binding; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IGI:dictyBase.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IGI:dictyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR GO; GO:0042554; P:superoxide anion generation; ISS:dictyBase.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Electron transport; FAD; Flavoprotein; Heme; Iron; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..517
FT /note="Superoxide-generating NADPH oxidase heavy chain
FT subunit A"
FT /id="PRO_0000361527"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..201
FT /note="Ferric oxidoreductase"
FT DOMAIN 229..349
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 101
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:0000250"
FT BINDING 115
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:0000250"
FT BINDING 190
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:0000250"
FT BINDING 203
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:0000250"
FT BINDING 283..289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 517 AA; 59752 MW; 36A2CD07408F1E46 CRC64;
MRLPTKEEIQ RYWVNEGNKL ILVILYTLGN IAAFVYTFVH YYNSPAFEVV GYGVCFARGC
AQLLKLNCAL ILVPVLRNLL SFLRGTFLNN YVPFDKNIVF HKLIAWVICF ATFGHVMAHF
NNFRLYQDIT PQEYKRILGI DYPNLTPIKY AFATLAGWTG HVVCIVMVLM YTSAVESIRR
PMFEGFWYTH HLFVVFFGLL VVHGLHSILE PTSFWKWVIG PCALYIVERL IRLLRSKKTT
MLIQARIHPS RVIEVRMKTE RFKYKPGQYL FLNCPTIAQN EWHPFTITSA PEEDFVSCHI
NVVGNWTGKL STLLNPDKKM GIVQENVLKS PDGKPILRID GPFGAASEEV FKYKQVILVG
AGIGVTPFAS ILKHIKYQMA RTYNTTPLID KVHFYWICRD RNSFEWFSGL IGELEMENHN
NFLEIHPYLT GALSAQEIRD VMYGDEEKDL ITGFTTPTQF GRPKWDEIFA DHALRYAEKD
VGVFFCGPKL LSKSLYKAST HYTKTTTCRF HYNKENF
