NOXB_DICDI
ID NOXB_DICDI Reviewed; 698 AA.
AC Q86GL4; Q54KY4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Superoxide-generating NADPH oxidase heavy chain subunit B;
DE EC=1.-.-.-;
DE AltName: Full=NADPH oxidase B;
DE AltName: Full=Superoxide-generating NADPH oxidase flavocytochrome B;
GN Name=noxB; ORFNames=DDB_G0287101;
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.
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: Expressed during development. Expressed during
CC aggregation and shows a marked decrease in fruiting bodies.
CC {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; AY221173; AAO62421.1; -; Genomic_DNA.
DR EMBL; AAFI02000096; EAL63915.1; -; Genomic_DNA.
DR RefSeq; XP_637386.1; XM_632294.1.
DR AlphaFoldDB; Q86GL4; -.
DR SMR; Q86GL4; -.
DR STRING; 44689.DDB0191445; -.
DR PeroxiBase; 5485; DdNOx02.
DR PaxDb; Q86GL4; -.
DR ABCD; Q86GL4; 4 sequenced antibodies.
DR EnsemblProtists; EAL63915; EAL63915; DDB_G0287101.
DR GeneID; 8625916; -.
DR KEGG; ddi:DDB_G0287101; -.
DR dictyBase; DDB_G0287101; noxB.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_3_1_1; -.
DR InParanoid; Q86GL4; -.
DR OMA; HRTYISK; -.
DR PhylomeDB; Q86GL4; -.
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:Q86GL4; -.
DR Proteomes; UP000002195; Chromosome 4.
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; IMP: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: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; IMP: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..698
FT /note="Superoxide-generating NADPH oxidase heavy chain
FT subunit B"
FT /id="PRO_0000361528"
FT TOPO_DOM 1..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 225..375
FT /note="Ferric oxidoreductase"
FT DOMAIN 404..528
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
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 282
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 364
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 377
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 460..466
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 698 AA; 81239 MW; 47DFFD42D2D9BE1B CRC64;
MNEKKELQQE LELQEFQTPK NQQLEKLQEP NGEISSTGNE TSESGISSPP ISQNDNSNNE
NESLNITPNK PFVSMQEELQ NLDIENIPIP PTIQTPKIYK NTNNLIHSKN NLSLPISLSQ
ENIVKLDKVD IESNDQVNSN TDNNNNTNNN NNTNNNKNEK IGLRSKIFKS KIFIKIRGWW
WHRGISTYIM LFYIALNIGV GVHMFYNMYH SDIFKFLGLS FCFSRTAARL INLNSAVILL
PVLRNFLSWL RGTIVNNYIP IDKHLNFHKL CAFMLFCCTI IHCVGHYISF KKINDDVLKI
DDGKSVAGDY LNININNFPD EKYLFFKSVP GITGHIMLLI LILIVSSSMW RIRRPMFEIF
WYVHHLFIPF YILLCFHGYS KILKKDPQSW MWIIAPFILY SIERLIRIAR SKKRVILEKA
IMHPSKVLEL RMKRDNDNFN FKPGQYLYLN CPSIAYHEWH PFTITSAPDD PFISVHINIV
GNWTRKLFKL LNPDNKLGLI QEDLKSTQNR GKRRILKIDG PFGAPAENFF KYRNLVLIGA
GIGVTPFSSI LRHLKNQNDK QTNADENHLK INKIYFIWIS RQKNSFQWFT DILAELENDE
RIDSILEIHI FLTGALELDD YAKIKNAQKC HITNLHSKTL FGRPNFRSIF NQLTQLHQRE
KIGVFYCGNK ALGKNIIKNC NKFNGKNNCH LIFHKENF
