ID A0A026WLE4_OOCBI Unreviewed; 1511 AA.
AC A0A026WLE4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=X777_02723 {ECO:0000313|EMBL:EZA56872.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA56872.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA56872.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107154; EZA56872.1; -; Genomic_DNA.
DR STRING; 2015173.A0A026WLE4; -.
DR EnsemblMetazoa; XM_026971829.1; XP_026827630.1; LOC105277837.
DR OMA; VTSEIIM; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0005886; C: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: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; 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 Reference proteome {ECO:0000313|Proteomes:UP000053097};
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..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1141..1164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1176..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1203..1222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 827..862
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 863..898
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1226..1332
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 342
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 1511 AA; 174073 MW; ACE46CB37F7DD2CA CRC64;
MTRRRWSVRG IGSRLCAITW TFWIILPART GAGLSYADNK QRYDGFYNNL AHPDWGAIDS
RLIRKVPAAY SDGVYAMAGQ NRPSPRKLSD LFMQGDDGLP SVKNRTALFA FFGQLVTSEI
IMASESGCPI EFHRIDVDKC DPVFDKECQG NKYIPFLRAD YDRQTGRSPN SPREQINKVT
SWIDGSFVYS SSEAWANTMR SFKNGSLLME QTRQFPVRNT MRAPLFNHAV PHVMRMLSPE
RLFLLGDPRT NQHPPLLALG ILFYRYHNVI AARVQEEHPD MSDEEIFQKA RRIVIGTIQN
IIFYEYLPAF LNEDLPSYTG YKPDLHPGIS HIFQSAAFRF GHTLIPPGIY RRNENCEYRK
TNMGQPAIRL CSTWWDSNEV LANSTIEELI MGMASQLAEK EDTLLGTDIR NNLFGPMEFS
RRDLGALNIM RGRDNGLPDY NTAREYFKLA KRKTWNEINP GLFSKNSSLL RTLIEIYSNN
LNNIDVYVGG MLESKDGPGE LFTAVIKEQF LRLRDSDRFW FENEENGIFT KNEIEVIRRV
SLWDVIINAT DIPSDAIQRR VFIWQDGDPC PQPFQLNSTI LEPCVPLQRY DYFEGSELVY
IYACVFLGFV PILCAGAGYG LVKLQNRRRR RLKILQEAIQ KRSDGICVDK MIVREWLHAN
HRRLVKVKFG PEAALHIVDR KGEKLRTFDF SGVNTITMEE SQESETGHRK ALVLLRIPRD
YDLVLELDSL ASRRKFIAKL EAFLASQKKH FTLTPIARDI MLAKAETKER RQKKLEQFFR
EAYALTFGLR PGERRRRSDD SDTGEVVTVM RTSLSKSEFA SALGMRPDAV FVKKMFNIVD
KDGDGRISFQ EFLDTVLLFS RGKTEDKLRI IFDMCDKDSN GVIDKEELSE MLRSLVEIAR
TTSLSDDHVT ELIDGMFQDA GLERKEYLTY NDFKLMMKEY KGDFVAIGLD CKGAKQNFLD
TSTNVARMTS FHIDQLPSED SKSWTRKQWD AVSTFVEENR QNIFYLFVFY VVTIALFVER
FIHYSFMAEH TDLRHIMGVG IAITRGSAAA LSFCYSLLLL TMSRNLLTKL KEFSIQQYIP
LDSHIQFHKI AACTALFFSV LHTVGHIVNF YHVSTQPIAH LRCLTSEISF PSDARPTISF
WLFRTVTGLT GLLLFVVMTI IFVFAHPTVR QKAYKFFWST HSLYVVLYAL CLIHGLARLT
GAPRFWIFFV GPAIIYALDK VVSLRTKYMS LDIIETELLP SDVIKIKFYR PPNLKYLSGQ
WVRLACTAFR SNEFHSFTLT SAPHENVLSC HIKAQGPWTW KLRNYFDPCN YNPEDELPKI
RIEGPFGGGN QDWYKFEVAV MVGGGIGVTP YASMLNDLVF GTSTNRYSGV ACKKVYFLWI
CPSHKHFEWF IDVLRDVERK DVTDVLEIHI FITQFFHKFD LRTTMLYICE NHFQRLSKKS
IFTGLKAINH FGRPDMTSFL KFVQKKHSYV SKIGVFSCGP RPLTKSVMSA CDEVNKTRRL
PYFIHHFENF G
//
