ID A0A0L7R8G7_9HYME Unreviewed; 1406 AA.
AC A0A0L7R8G7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=WH47_11834 {ECO:0000313|EMBL:KOC67177.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67177.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC67177.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC67177.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) 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; KQ414632; KOC67177.1; -; Genomic_DNA.
DR STRING; 597456.A0A0L7R8G7; -.
DR Proteomes; UP000053825; 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; 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; 2.
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; PTHR11972:SF175; NAD(P)H OXIDASE (H(2)O(2)-FORMING); 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
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; PR00450; RECOVERIN.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 493..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1036..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 722..757
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 758..793
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1121..1227
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1406 AA; 162489 MW; A4BB94AFEAA3EC80 CRC64;
MPAAYSDGVY MLAGQDRPSP RKLSQLFMQG DDGLPSVKNR TALFAFFGQL VTSEIIMASE
SGCPIEYHRI DVDKCDPVFD KECQGNKYIP FRRADYDRRT GRSPNSPREQ INKVTSWIDG
SFIYSSSEAW ANTMRSFKNG SLLMEPTRKF PVRNTMRAPL FNHAVPHVMR MLSPERLYLL
GDPRTNQHPP LLALGILFYR WHNVVAARIQ QDNPSMSDED IFQKARRTVI GTLQVKRKFQ
FFCELLFLQV SIKYRYLVIV YNIKNKMIKN ILEILTNSTI EELLMGMTSQ IAEKEDNLLG
TDIRNNLFGP MEFSRRDLGA LNIMRGRDNG LPDYNTARAH LKLPRRKTWN EINPESFNKN
PSLLRTLVEI HSNNLNNVDV YVGGMLESSA GPGELFSAVI KEQFLRLRDS DRFWFENEEN
GIFTKSEIEE IRRVTLWDVI VNATGIPSDS IQKKVFTWVE GDPCPQPYQL NSTMLEPCVP
LQRYDYFEGS ELVYIYACVF LGFVPILCAG AGYGLVKLQN RRRRRLKILQ EAIQKKNDGK
ICVDKMIVRE WLHANHRRLV KVKFGPEAAL HIVDRKGEKL RTFDFNDVNT VTMEESQENE
NGHRKALVLL RIPRDYDLVL ELDSLASRRK FIAKLEAFLA AHKKHFTLSQ VSRDIMLAKA
ETKERRQKKL EQFFREAYAL TFGLRPGERR RRSEDSDSGE VVTVMRTSLS KSEFASALGM
RADAVFVKKM FNIVDKDRDG RISFQEFLDT VLLFSRGKTE DKLRIIFDMC DKDSNGVIDK
EELSEMLRSL VEIARTTSLS DDHVTELIDG MFQDAGLERK DYLTYNDFKL MMKEYKGDFV
AIGLDCKGAK QNFLDTSTNV ARMTSFHIDQ LPPEDSKSWV RKQWDAVSTF LEENRQNIFY
LFVFYVTTIA LFVERFIYYS FMAEHTDLRH IMGVGIAITR GSAAALSFCY SLLLLTMSRN
LLTKLKEFSI QQYIPLDSHI QFHKIAACTA LFFSVLHTVG HMVNFYHVST QPLAHLRCLT
SELSFPSDAR LTISFWLFRT VTGLTGILLF IVMTIIFVFA HPTIRQKAYK FFWSTHSLYV
VLYALCLIHG LARLTGSPRF WIFFVGPAII YSLDKVVSLR TKYMALDIIE TELLPSDVIK
IKFYRPPNLK YLSGQWVRLS CTAFRSNEFH SFTLTSAPHE NFLSCHIKAQ GPWTWKLRNY
FDPCNYNPED EHPKIRIEGP FGGGNQDWYK FEVAVMVGGG IGVTPYASML NDLVFGTSTN
RYSGVACKKV YFLWICPSHK HFEWFIDVLR DVERKDVTDV LEIHIFITQF FHKFDLRTTM
LYICENHFQR LSKKSIFTGL KAINHFGRPD MTSFLKFVQK KHSYVSKIGV FSCGPRPLTK
SVMSSCDEVN KGRRLPYFIH HFENFG
//
