ID A0A498S208_ACAVI Unreviewed; 1501 AA.
AC A0A498S208;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=NAV_LOCUS319 {ECO:0000313|EMBL:VBB25489.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB25489.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB25489.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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; UPTC01000019; VBB25489.1; -; Genomic_DNA.
DR STRING; 6277.A0A498S208; -.
DR Proteomes; UP000276991; 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; 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; 1.
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:UP000276991};
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 599..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1047..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1145..1169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1181..1198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1210..1227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 873..908
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1231..1338
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 338
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 1501 AA; 171902 MW; 452928F5D7E02C2C CRC64;
MYVGEISGCA CHAMACTPTY EKVYAYMRVW VCMGLERISE YQRYDGWFNN LANPHWGTVG
SHLHRDAPSQ YQDGVYMLNT NLPSARAISE LVFKGPSGIA NKRNVTTMLA FFSQVIAYEI
MQSSLISCPL EMHKIPVPRC DPVFDAQCVG KTEIPFVRAK YDKNTGHGFN VPREQVNERT
SWIDASFLYS TQEPWIAALR AWHNGSLLEG PMKGYPPLNG PRIPLINPAP PQIHRLMNPE
LLGDPRINEN PGLLSLGLML YRWHNIQAKR IQEEHPEWTD EEGARRWVIA TLQKITLYDF
LPLMLADEEA VPPYERYKPL VPPGISHAFA TAAFRFPHTI VPPALLFRKR ANGKCEFRDE
VGGYPALRLC QNWWNAQDIV QEYSVDEIVL GMASQIAEGE DTIVVEDLRD FVFGPMHFTR
LDVVSSSIMR GRDNGLPSYN ELRQNYNLPM RNWTTINPVM YEERPKLFRE LEKLYEGDIS
KLDAYVGGML ETNGEGPGEL FRAIILDQFL RLRDGDRFWF ENIWNGMFTE EEIKQIHLTT
LRDIIHQTTS INEDELQENV FIWHAGDPCG QPFQVNASSL EPCIPFMRFD HFTGNEVTFI
FSCIALGVIP LICIGIGYML IQKRKKMGGD MEPCFKKVFL ESTNSDNTKI EFVKKSSEKE
KLHLSAIEWI SKNYCRSVIV IVDVTPLIRL EKPRGGLLRC LRFSDVNFVN VAVSDLNSCN
YPFVMISIPK HYDLVICLSS ECQCAQFLYV LSNVLNRTNK QLIIRRCPIN YIIEMAETSE
RRQEKLDHFF REAYAKSFNI AELSGDVSSV MYGSISEEVL STTVTKAEMA DALGMRENDL
FVERIFACMT KEDPNCVTFL KFLNVIVRFA TGSVRDKLEV LFNMCDREGQ GRVRKKEFCD
FVKSLNVAVG VKIEEALQDG IIDRVLQRSG ISADSKFLSH KDFEAIFNNV DDIRHPIGVH
MRGAKLKINL DETESMNSFA IQNEEIGWVH INWYFSIISY LETYRQHIVI IFLFTAINLL
LFFERFWHYR YETEHRDLRR VMGMGIAITR GAAASLSFCM GLILITVCQN IITLLRETLI
REYVPLDSAI AFHKIVAVVA GFWATVHIVG HCVNFYHVAT QSQDGLQCLF QEAVFGSNFL
PSISYWFYGT ITGITGILLV ALMSITYVFS TPAVMKEAYH AFKITHLLNI LIYALTVLHG
LPKLLDSPKF LYYVGGPIIL FVIDRIIGMR QQYKRLQILN GAILPSDIIY IQFKRPNSFR
FRSGQWVRVS CPAFSCTFNE LHAFSLASAP QASTLELYIK AIGPWTWNLR NQIACAHSNG
TPYPVLHLHG PYGDGNQDWR NFEIAVLIGG GIGVTPYASI LTDLVYFIWV CSTHKNYEWF
IEVLRSVEES DKEDLLEIHI FVTQFFHKFD LRTTMLYICE KHFRSDSNGR SMFTGLNAVN
HFGRPNFEAL FKFIQNKHRN IQEVGVFSCG PNSINKEIGK ACRETNRIRS GALFCHRFET
F
//
