ID G0PCN8_CAEBE Unreviewed; 1500 AA.
AC G0PCN8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN ORFNames=CAEBREN_24129 {ECO:0000313|EMBL:EGT51247.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000518};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000547};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000256|ARBA:ARBA00005644}.
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DR EMBL; GL380249; EGT51247.1; -; Genomic_DNA.
DR STRING; 135651.G0PCN8; -.
DR EnsemblMetazoa; CBN24129.1; CBN24129.1; WBGene00162854.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_004482_1_0_1; -.
DR InParanoid; G0PCN8; -.
DR OMA; NINWETQ; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 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; IPR034821; DUOX_peroxidase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11475:SF144; NAD(P)H OXIDASE (H(2)O(2)-FORMING); 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 593..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1067..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1128..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1164..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1193..1213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 820..855
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 856..891
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1214..1321
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 333
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:PIRSR619791-2"
SQ SEQUENCE 1500 AA; 171203 MW; F07280546A99213E CRC64;
MRSKSILYIA ILYYCSHLIS HVIGIQQNEE FQRYDGWYNN LANSEWGSAG SRLHRDARSH
YSDGVYSVNN SLPSARELSD TMFKGESGIP NTRGCTTLLA FFSQVVAYEI MQSNGVSCPL
ETLKIQVPLC DSVFDKECQG KTEIPFTRAK YDKATGNGLN SPREQINERT SWIDGSFIYG
TTQPWVSSLR SFKQGRLAEG VPGYPPLNNP HIPLNNPAPP QVHRLMSPDR LFMLGDSRVN
ENPGLLSFGL ILFRWHNYNA NQIHRKHPEW TDEQIFQAAR RLVIASMQKI IAYDFVPALL
GEDVRLSNYT KYMPHVPPGI SHAFGAAAFR FPHSIVPPAM LLRKRGNKCE FRTEVGGYPA
LRLCQNWWNA QDIVKEYSVD EIILGMASQI AERDDNIVVE DLRDYIFGPM HFSRLDVVAS
SIMRGRDNGI PPYNELRRTF GLPPKTWETI NEDFYKKHTD KVQRLKSLYG GNILYLDAYI
GGMLEGGENG PGELFKEIIK DQFTRIRDGD RFWFENKLNG IFTDEEIQMI HGITLRDIIK
ATTDIDETML QKDVFFFKEG DPCPQPFQVN TTGLEPCVPF MQSTYWTDND TTYVFTLIGL
ACVPLICYGI GRFLVNRRIA IGHDSACDSL TTDFRAASYN PKGDIYSVNA LEWLQEEFIR
QVRIEIENTT LTVKKPSGRM LRKIRFEAEQ RIDLLHSTPN PSAMHGPFVL LSQKNNHHLV
IRLPSDRDLS NFLDQIREAA RSINAEVNVA DEENAVLLSQ ATTEKRRQDR LDQFFREAYA
KAFNDDELRD AENSVDSTND DILNETISRE ELASAMGMKS DNDFVKKMFA MTAKNDDDSL
SFNEFLKVLK EFVNASQKKK LQTIFKMCDS RGENRVLKKD LTELVKSLNQ TAGVRINERM
QSKLLDEVLH KSGANEDSKY LTYEEFNNLF SDLPDNQPVG LPFNRRSFQP SIGETSSLNS
FAVVDRSINS SAPLTLFHKI CAFLETYRQH VFIVFCFVAI NLVLFFERFW HYRYMTENRD
LRRVMGAGIA ITRGAAGALS FCMALILLTV CRNIITLLRE TVISQYIPFD SAIAFHKIVA
LFAAFWATLH TVGHCVNFYH VGTQSQEGLA CLFQEAFFGS NFLPSISYWF YGTITGLTGI
ALVAVMCIIY VFALPCFIKR AYHAFRLTHL LNIAFYALTI LHGLPKLLDS PKFGYYVVGP
IVIFVIDRII GLMQYYKKLP IKDAEILPSD IIYIEFERPR SFQYKSGQWV TISSPSISCT
FNESHAFSIA SCPQDDRVKL YIKAVGPWTW KLRSELLRAR TTGSPYPLIH LKGPYGDGNQ
EWMNYEVAIM VGGGIGVTPY ASTLNDLVQR TSGKGYHTVR CKKVYFLWVC PSHKNYEWFV
DVLKNVENQD TQGILETHIF VTQLFHKFDL RTTMLYICEK HFRATNAGMS MFTGLHAKTH
FGRPNFKAFF QFIQSEHREQ SEIGVFSCGP VNLNEKIAEG CAEANRQRDA PSFAHRFETF
//
