ID A0A093IYJ6_EURHL Unreviewed; 1552 AA.
AC A0A093IYJ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
DE Flags: Fragment;
GN ORFNames=N326_03642 {ECO:0000313|EMBL:KFW06738.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW06738.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFW06738.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW06738.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Generates hydrogen peroxide which is required for the
CC activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a
CC role in thyroid hormones synthesis and lactoperoxidase-mediated
CC antimicrobial defense at the surface of mucosa. May have its own
CC peroxidase activity through its N-terminal peroxidase-like domain.
CC {ECO:0000256|ARBA:ARBA00003796}.
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 -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005197}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; KK569831; KFW06738.1; -; Genomic_DNA.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000054232; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma 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:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 3.
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; PTHR11972:SF175; NAD(P)H OXIDASE (H(2)O(2)-FORMING); 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13202; EF-hand_5; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054232};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1552
FT /note="NAD(P)H oxidase (H2O2-forming)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001887706"
FT TRANSMEM 583..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1043..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1077..1100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1148..1169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1181..1207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1219..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 806..841
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 842..877
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1268..1374
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 961..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW06738.1"
FT NON_TER 1552
FT /evidence="ECO:0000313|EMBL:KFW06738.1"
SQ SEQUENCE 1552 AA; 176388 MW; B16A9799A56EF32C CRC64;
LSLTMVLVVI WTLGRAQESI SWEIQRYDGW YNNLLHHSRG SVGARLLRLL PANYADGVYE
ALQEPHVPNA RQLSNVVARG PSGLPSHRNT TVLAVFFGFH VLSDIVGTEK PGCPAEFLNI
HIPSGDFVFD PAGTGDVVLP FQRIHWAVET GQSPNSPREQ TNEVTGWLDG SSIYGPSHSW
SDALRSFSGG QLAAGPGGRL PRETDGRIPM WKALDPSTGQ GGPQGIYDLG NAWGNENRFL
QAESIAWFRY HNHLAATLAQ AHPTWSDEDL FQHARKWVIA TFQSIVMYEW LPTLLGRHVP
EYKGYQQHLD PSLSPEFVAA AGQFLATMVP PGVYKRDPKC NFQEVPGPSG SFPAVRLCNS
YWSRESTRLQ QAEDVDVDNL LLGMSSQIAE REDNIVVEDL QDYWYGPLKY SRTDYVASWL
QRGRDLGLPT YNQARERFGL DPLQNWSDLA PHLDQQVLEK VAALYANNTA GLELLPGGML
EVDSSLFSAI ILDQFVRLRD GDRFWFENTK NGLFTAEETR EIRNTTYHKV LAAVTYAEPT
DLQPHVFVWS TGDPCPQPQQ LTAQQLANCT PMMVLDYFEG SGAGFGIIIV VLCCLPLVTL
FVAWIVAVFR KRDFKKLQKT HGSSVRREVT SEAIHAMEWR GPKTDSSPVY IQLQADKVLK
VLDGRGSVLR SINLKAYQSV EVILSSNKGN KALLLKSPKE YDLVLLFSEE TERSNFIGKL
QGYLEDSNLD LHLSEMKEQN LMKRAVTQEQ RKQILETFFR HLFAQVLEID KSDAGELNFE
SSQKAKESLT CELSRAEFAE ALGLKAHSMF VDSMFSLADK DGNGYISFRE FLDILVVFMK
GSPEEKSKVM FRMYDIDENG FLSKEEFLRM LRSFIEISNN CLSRDQAEQV TESMFQASGF
QDRDELTWED FHYMLRDHDS ELRLTQLCIK GHCLFFWLPK GVPEVLKQNL HNRVSFIKKD
EPKGRSSLPN RTISDEEKDP NLDTVSHYVE REGQELRKRP GRKVNQYQLH LYTEAQRKKY
ERNKVQQKIQ EFKRFIENYR RHIVCVVLFS AITAGVFVER AYYYAFASPS TGIAQTTFVG
IIVSRGSAAC ISFMYSYILL TMCRNLITIL RETFLNHYIP FDAAVDFHRW VAMAALIFSV
LHTAGHVVNI YIFSVMPLSV LSCLFSSVFM DDGSQLPQKY YWWFFQTIPG MTGVLLLVIL
AVMYVFATHH FRRVSFQGFW ITHHLYVLLY VLVIIHGSYA LIQQPRFHIY FIIPALIYGA
DKLLSLSRKK VEISVVKAEL LPSGVTHLRF QRPQDFDYKS GQWVRIACVA LGTTEYHPFT
LTSAPHEDTL SLHIRAVGPW TTRLRELYAP ESVALIGKLP KLYLDGPFGE GHQEWNKFEV
SVLVGGGIGV TPFASILKDL VFKSSISSKL LCKKIYFIWV TRTQRQFEWL ADIIREVEEA
DRTDLVSVHI YITQLAEKFD LRTTMLYICE RHFQKVLNKS LFTGLRSQDK GGLVEGSAGA
AGFDPSGSLP PQVQKIGVFS CGPPGMTKNV EKACRQLNKK DQTYFAHHYE NF
//
