ID A0A226EPH4_FOLCA Unreviewed; 1497 AA.
AC A0A226EPH4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=Fcan01_07917 {ECO:0000313|EMBL:OXA58721.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA58721.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA58721.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA58721.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA58721.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA58721.1}.
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DR EMBL; LNIX01000003; OXA58721.1; -; Genomic_DNA.
DR STRING; 158441.A0A226EPH4; -.
DR OMA; VTSEIIM; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000198287; 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; cd00051; EFh; 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; IPR018247; EF_Hand_1_Ca_BS.
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; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 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; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SMART; SM00054; EFh; 2.
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; PS00018; EF_HAND_1; 2.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000198287};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1497
FT /note="NAD(P)H oxidase (H2O2-forming)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013211699"
FT TRANSMEM 594..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1162..1183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 814..849
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 850..885
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1212..1318
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 337
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 1497 AA; 172640 MW; 7F1138AC8858661F CRC64;
MSSGNWIYPC VLFFVIINGR TAWTSSERAQ SFTEKQRYDG WYNNLAHPEW GSVDSQLTRR
TPPAYADGVY MLAGQNRPSP RKLSQVFLKG IDGLPSAKNR TAMLAFFGQV VSSEILMASE
SGCPIEMHRI DIDQCDEMYD SDCRGNRYMP FHRAGYDRKT GQSPNRPREQ INKATSWIDG
SFVYSTSEAW VAALRSFVNG SLRTDSTGKL PPRNAERVPL NSAPSPHVLR MLDPEKMFLV
GDPRSNQNPA LLAFGILFFK WHNVVASRIQ EKHPTWTDEE IFQRTRRFVI ATMQNVIMYE
YLPAFLNTNL PPYEGYKPDM HPGITHVFQS AAFRFGHTLI PPGIYMRDAS CKFRKTEEGG
SAIRLCASWW DSDDVFHSGI FEEIIRGLSS QIAEREDVIL CSDVRDRLFG PMDFSRRDLG
ALNIMRGRDN GLPDYNTVRK YFGLARVSNW SEINPILFKE EPHVFAKLSE LYKGDLNNID
VYLGGMLESH DGPGPLFTAI IKEQFTRIRD ADRLWFENED NGMFTKQEIE DLRKIKLHDI
IVNSTSMAND EIQENVFFWH NGDPCPQPMQ LNASVLEPCS YLRGFDYFAG SEVVYIYACV
FLCFVPIICA GAGYGVVKLQ NSRRRRLKMK QEENNNGKSV DKMIVKEWLH QNHKRLVKVK
FGPEEALYTM NRKGEKIRCV NLRGCDTLVI EVTQDARKKP MMLVRVPRDH DLVLEFDSTH
SRAKFLAKLD AFLKSLKKSL ETIATYREPM LANAETKERR QKRLEHFFRE AYALTFGLKP
GEKRKLEDVS SDVIMVMRTS LSQAEFAGAL GMKGDAVFVK KMFNIVDKDG DGRISFQEFL
DTVVLFSKGK TEDKLRIIFD MCDNDRNGVI DKSEFSDMLR SLVDIAKTNS LSKEEVTELI
DGMFTNSGIE TKDYLTYEDF KLMMKEYKGD FVAIGLDCKG AKQNFLDTST NVARMTSFHI
ETVHDKYRSK IRKQWDCITT FLEENRQHIF YLFVFYVVTI ALFVERFIHY SFMTEHTDLR
HIMGVGIAIT RGSAASLSFC YSLLLLTMSR NLLTKLKDFP IQQYIPLDSH IQFHKIVACT
ALFFSLLHTA GHIVNFYHVS TQPVEHLRCL TKEMLFPSDF RPTIFYWLFE TVTGITGVIL
FVTMVIIFVF AHPTIRKNAY GFFFSAHKLY IVLYILCLIH GLARLTGAPR FWMFFVGPGI
IYTLDKVVSL RTKYMELDII ETELLPSDVI KIRYYRPPNF KYLSGQWVRL ACTAFRPHEF
HSFTLTSAPH ENFLSCHIKA QGPWTWKLRN YFDPCNYNPE EDSPKIRLEG PFGGGNQDWY
KFEVAVMVGG GIGVTPYASI LNDLVFGTST NRYSGVACKK VYFLWICPSH RHFEWFIDVL
RDVEKKDVTN VLEIHIFITQ FFHKFDLRTT MLYICENHFQ RLSKRSMFTG LKAINHFGRP
DMTAFLKFVQ KKHSYVSKIG VFSCGPRPLT KSIMSSCEEV NKGRKLPYFI HHFENFG
//
