ID A0A0K0F7T2_STRVS Unreviewed; 1559 AA.
AC A0A0K0F7T2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-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 Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0487900.1};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_0487900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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; 75913.A0A0K0F7T2; -.
DR WBParaSite; SVE_0487900.1; SVE_0487900.1; SVE_0487900.
DR Proteomes; UP000035680; 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; 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; 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 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:UP000035680};
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 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1050..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1137..1158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1223..1240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1252..1269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 914..949
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1273..1380
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 361
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 1559 AA; 178969 MW; 047F02D52D2C4D5A CRC64;
MNWKVGYSPE LQNQKANIRL IKDIRQKVNY NFTFIYIILL TIIQFVSVTC LQKTHEFQRY
DGWFNNLANP EWGSVGSRLH RDSPANYEDG VYKINSSLPS ARKVSDIVFK GPSGIKNKRN
ITTMLAFFSQ VVAYEIMQSS QTGCPLENIP IPVEECDSVF DPSCEGKTNI PFMRTKYDTE
TGHGLNSPRE QINERTSWID ASFLYSTNEP WVAALRSWHE GTLTEGEVEG YPPLNKKIIP
LINPAPPQIH RLMDPERLFT LGDPRINENP GLLTFGLILF RWHNFQALKI AQKNPDWTDE
EIFQGARRMV IASLQNIILY EYLPEVLGVD KSEIPKYDKY NAHIPPGISH SFATAAFRFH
HTIVPPGMLF RKKRTSKNEC IFREDIGGFP ALRLCQNWWN AQDIVQEYTV DEIILGMASQ
ISEAEDTIIV EDLRDFIFGP MYFTRLDVVS SSIMRGRDNG IPFYNDLRRN FALDTKTWET
INPQLYKTNK ELFDKLKDLY KDISYLDAYV GGMLETTENG IGELFKHIIR DQFLRLRDGD
RFWFENRQNG IFTEEEIEEI KTITLSKILR STTNIEPNEI QDNVFIFNET SPCPQPFQVN
TTGMEQCIPM MRYDHFNGNE VTYIFTLIAI ACVPLICIGV ARYLIIRRRK LGVTLIDMPK
IISKDSYNNS VIDSQSELDS TSDSSSTKYY QIPHTVEDKF KMPAIEWLSD SFCRSVNFEL
DTTTGEICIK RPRSKGILRK LNMGKADKVF FTLTDPTTKS TYGPFIIITI PKNYDMVIRL
HNDTHCAQFM KVAGDCLKKL NIPLTIKHLD NDVLLQTAET KEKRQKKLDL FFREAYAKSF
QTPQLSDDNI EYNEDLSRDI LGISISKSEL ADALGMREDN HFVDRLFACM VKNGEDSVSF
ESFLELLKKF SNGSIRDKMN LLFNMCDYNG DGQVERSEFI QFFKSLSDTA GVKLDKHVQE
DMLDGVLLVH GVDTTSKYLT EEDLEKIFTE VDGVNRPVGV HLRGAKLKVN LDDSSSLSSF
ALPADEEKSK IIRSKLSILL SFLETYRQHI AWTFIFFSIN ALLFLERFWH YRFEVEHRDL
RRVLGTGIAI TRGAAAAISF SMSLILLTVC RNLITVIRVT PVGEYIPLDS AISFHKIVGY
TIAFFSAVHT IGHLVNFYNI ATQSQEGLQC LFQEAVFGSN FAPTVKYWFF GTMTGLTGIL
IVIVMCIVYI FSIPSFMHQN YNAFIFTHWL NIAFYGLTLL HGLPKLLDSP KFWYQMLGPL
ILFIIDKIIG MRQQYKQLRI IEASILPSDI IYIQFKRPHS FNFYSGQWVR ISCPDISCTF
NEDHAFSMAA APQSPSLELY IKAVGPWTRQ LRSILQDCQA NGLPYPTINL SGPFGDGNQE
WTGYDIAVMV GGGIGITPYA SILMDLVLNK SSGRHTNIKC KKVYFLWICP SHKNYEWFVD
VLKDVETLDT HGILENHIFI TQFFHKFDLR TTMLYICEKH FRTDNNGRSM FTGLRAVNHF
GRPDFDSFFK FLQSKHNNVE QIGVFSCGPA TVNKKIRQSC TEANRARNAP SFVHRFETF
//
