ID A0A0N5A5D1_PARTI Unreviewed; 1530 AA.
AC A0A0N5A5D1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001691400.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001691400.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 STRING; 131310.A0A0N5A5D1; -.
DR WBParaSite; PTRK_0001691400.1; PTRK_0001691400.1; PTRK_0001691400.
DR Proteomes; UP000038045; Unplaced.
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; 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; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
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 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 15..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1158..1182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1194..1211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1223..1240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 885..920
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1244..1351
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 344
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 1530 AA; 175711 MW; C74B96C78DA781AF CRC64;
MNWRFGFSPT VNDNYLYVYL LLLTFIQLKY VISLEKTHEF QRYDGWFNNL ANPEWGSVGS
RLHRDSPANY EDGVYKINSS LPSARHISDI VFKGPSGMQN KRNITTMFVF FSQVVAYEIM
QSSQTGCPLE NVPIPVADCD PIFDPSCEGK TNIPFMRTKY DTETGHGLNS PREQINERTS
WIDASFLYST NEPWVAALRS WHEGTLTEGE IEGYPPLNKK IIPFINPAPP QIHRLMDPER
LFTLGDPRIN ENPGLLTFGL ILFRWHNFQA LKIAQKNPDW TDEEIFQGAR RMVIASLQNI
VLYEFLPEVL GVTKADIPKY DKYNAHIPPG ISHSFATAAF RFHHTIVPPE CVFRDDIGGF
PALRLCQNWW NAQDIVQEYT VDEIILGMAS QISEAEDTII VEDLRDFIFG PMYFTRLDVV
SSSIMRGRDN GIPFYNDLRK NFALETKTWE TINPQLYKTN KKLFDQLKKL YKNISYLDAY
VGGMLETNEN GAGELFKHII RDQFLRLRDG DRFWFENKQN GIFSDEEIDE IKNITLSHIL
RSTTNIDPDE IQDNVFIFDE KSPCPQPFQV NTTKMEQCIP MMRYDHFNGN EVTYIFTLIA
LACVPLICIG IARYLIIRRR KLGVTLIDMP KIIPKDNFDS SVIDSQSELD SSSDSASTKY
YQIPHTVEDK FKMPAIEWLS DSFCRSVNFE LDTTTGGICI KRPRSKGILR KLNMGKADKV
TFTLTDPTTK STYGPFIIIT IPKNYDMVIR LHNDTHCAQF MKVVGDCLKK LDIPLTIKHL
DNDVLLHTAE TKEKRQKKLD LFFREAYAKS FQTPQLSDDN VEYNEDLSRD ILGISISKSE
LADALGMREE NHFVDRLFAC MVKNGEDSVS FESFLELLKK FTNGTTKDKM NLLFNMCDYN
GDGQVERSEF IQFFKSLSDT AGVRLDKHVQ EDMLDGVLLI HGVDTSSKYL TEEDLEKMFT
EVDGINRPVG VHLRGAKLKV NLDDSSSLSS FAVPADVEKS KISRSKLSIL LSFLETYRQH
IAWTFVFFSV NALLFLERFW HYRFEVEHRD LRRVLGTGIA ITRGAAAAIS FSMSLILLTV
CRNVITVIRE TPIGEYIPFD SAIAFHKIVG YTIAFFAAVH TIGHLVNFYN IATQSQEGLQ
CLFQEAVFGS NFAPTVKYWF FATMTGLTGI LIVVVMCIVY IFSIPSFMRQ NYNAFRFTHW
FNIAFYGLTL LHGLPKLLDS PKFWYQMLGP LILFIIDKII GMRQQYKQLR IIEAAILPSD
IIYIQFKRPY SFIFRSGQWV RISCPDISCT FNEDHAFSMA AAPQSPSLEL YIKVVGPWTR
QLRSILQDCQ ANGLSYPTIN LSGPFGDGNQ EWTSYDVTVM VGGGIGITPY ASILMDLVLD
KSSGRHTNIK CKKVYFLWIC PTHKNYEWFV DVLKDVETLD THGILENHIF ITQFFHKFDL
RTTMLYICEK HFRTDNNGRS MFTGLRAVNH FGRPDFDSFF KYLQNKHNNV EQIGVFSCGP
ATVNKKIRQS CTEANRVRNA PSFVHRFEIF
//
