ID B3MLA0_DROAN Unreviewed; 1521 AA.
AC B3MLA0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN Name=Dana\GF14917 {ECO:0000313|EMBL:EDV30689.2};
GN Synonyms=dana_GLEANR_15683 {ECO:0000313|EMBL:EDV30689.2};
GN ORFNames=GF14917 {ECO:0000313|EMBL:EDV30689.2};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV30689.2, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV30689.2, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH902620; EDV30689.2; -; Genomic_DNA.
DR RefSeq; XP_001961468.2; XM_001961432.2.
DR STRING; 7217.B3MLA0; -.
DR EnsemblMetazoa; FBtr0119617; FBpp0118109; FBgn0091942.
DR GeneID; 6497732; -.
DR KEGG; dan:6497732; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_004482_1_0_1; -.
DR InParanoid; B3MLA0; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000007801; 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:0106293; F:NADH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0106292; F:superoxide-generating NADPH oxidase activity; IEA:EnsemblMetazoa.
DR GO; GO:0008365; P:adult chitin-based cuticle development; IEA:EnsemblMetazoa.
DR GO; GO:0048085; P:adult chitin-containing cuticle pigmentation; IEA:EnsemblMetazoa.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0002385; P:mucosal immune response; IEA:EnsemblMetazoa.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; IEA:EnsemblMetazoa.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 2.
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; 3.
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 ECO:0000313|EMBL:EDV30689.2}; Peroxidase {ECO:0000313|EMBL:EDV30689.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007801};
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 624..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1151..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 851..886
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 887..922
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1237..1342
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 367
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 1521 AA; 175280 MW; 6BE133A5067ED9F7 CRC64;
MSVPSAPRQG AASKNRDPCS NKKCTPRLHL LGDAASWALL LLLISLSLDL GFVHCYEKMY
SQTEKQRYDG WYNNLAHPDW GSVDSHLVRK APPSYSDGVY AMAGANRPST RRLSRLFMRG
RDGLGSKFNR TALLAFFGQV VANEIVMASE SGCPIEMHRI EIEKCDEMYD RECRGDKYIP
FHRAAYDRST GQSPNAPREQ INQMTAWIDG SFIYSTSEAW LNAMRSFHNG TLLTQKDGKL
PVRNTMRVPL FNNPVPNVMK MLSPERLFLL GDPRTNQNPA VLSFAILFLR WHNTLAQRIK
RLHPDWSDED IYQRARHTVI ASLQNVIVYE YLPAFLGSAL PPYEGYKQDV HPGIGHIFQA
AAFRFGHTMI PPGIYRRDGK CNFKETPMGY PAIRLCSTWW DSSGFFTDTS VEEVLMGLAS
QISEREDPVL CSDVRDKLFG PMEFTRRDLG ALNIMRGRDN GLPDYNTARE SYGLKRHKTW
TDINPPLFET QPELLDMLKE AYKNKLDDVD VYVGGMLESY GQPGEFFTAV IKEQFQRLRD
ADRFWFENER NGIFTPEEIA ELRKITLWDI IVNSTDVAVD EIQKDVFMWH TGDPCPQPMQ
LNATELEPCT YLEGYDYFSG SELMFIYVCV FLGFVPILCA GAGYCVVKLQ NSKRRRLKIR
QEALRAPQHK GSVDKMLARE WLHANHKRLV TVKFGPEAAI YTVDRKGEKL RTFNLQHVDV
VGVEESATNH IKKKPYILLR VPSDHDLVLE LESYGARRKF VKKLEDFLLL HKKELTVMEV
NRDIMLARAE TRERRQKRLE YFFREAYALT FGLRPGERRR RSDASSDGEV MTVMRTSLSK
AEFAAALGMK PNDMFVRKMF NIVDKDQDGR ISFQEFLETV VLFSRGKTDD KLRIIFDMCD
NDRNGVIDKG ELSEMMRSLV EIARTTSLSD DQVTELIDGM FQDVGLEHKN HLTYQDFKLM
MKEYKGDFVA IGLDCKGAKQ NFLDTSTNVA RMTSFNIEPM QDKPRHWLLG KWDAYITFLE
ENRQNIFYLS ASSTIRLWAE HTDLRHIMGV GIAITRGSAA SLSFCYSLLL LTMSRNLITK
LKEFPIQQYI PLDSHIQFHK IAACTALFFS VLHTVGHIVN FYHVSTQSHE NLRCLTREVH
FASDYKPDIT FWLFQTVTGT TGVLLFIIMC IIFVFAHPTI RKKAYNFFWN MHTLYIGLYL
LSLIHGLARL TGPPRFWMFF LGPGIVYTLD KIVSLRTKYM ALDVIETDLL PSDVIKIKFY
RPPNLKYLSG QWVRLSCTAF RPHEMHSFTL TSAPHENFLS CHIKAQGPWT WKLRNYFDPC
NYNPEDQPKI RIEGPFGGGN QDWYKFEVAV MVGGGIGVTP YASILNDLVF GTSTNRYSGV
ACKKVYFLWI CPSHKHFEWF IDVLRDVEKK DVTNVLEIHI FITQFFHKFD LRTTMLYICE
NHFQRLSKTS IFTGLKAVNH FGRPDMSSFL KFVQKKHSYV SKIGVFSCGP RPLTKSVMSA
CDEVNKTRKL PYFIHHFENF G
//
