ID A0A1V9XLI6_9ACAR Unreviewed; 490 AA.
AC A0A1V9XLI6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=monoamine oxidase {ECO:0000256|ARBA:ARBA00012804};
DE EC=1.4.3.4 {ECO:0000256|ARBA:ARBA00012804};
GN ORFNames=BIW11_09157 {ECO:0000313|EMBL:OQR74326.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR74326.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR74326.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR74326.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000205};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004362}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004362}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004362}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR74326.1}.
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DR EMBL; MNPL01008220; OQR74326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XLI6; -.
DR STRING; 418985.A0A1V9XLI6; -.
DR InParanoid; A0A1V9XLI6; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 6.10.250.130; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF21; AMINE OXIDASE [FLAVIN-CONTAINING] B; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000192247}.
FT DOMAIN 12..416
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 490 AA; 55907 MW; 77F41013ABEA9EA6 CRC64;
MFTVFEQGDK FGYVDIGGAY VGATQNYLLR TLQELNLQDK LYHINVQDKF MFMINGRRYT
HPAEDFPHFW NPLAEMDVNN FFRTLDDMGK EIPVQAPWDA PHAGEWDKMT YKEFIQKTCW
TKAGREFAEF FIQINVTSEP YEASLLWFLW YIKQCGGVKR IVSIKGGGQE MKMKGGMQQL
SEKMAESLGD RVKLSHAVVS VKHSNHGVLV RCINGIEFEG SHIILATAPP MQMKIHFSPN
LGPLRTQLMQ RVPMGSVWKL QVYYKTAWWH ELGFNGAVGS TPSETYAPVI YTIDDTKPDG
SFPSLIGFMP ADRARKLLHL TPQQRCDMLK KMYNHAFQTD KANDVVHYLE HNWMGEEYTG
GCYSCMFPPG VLTTFRGTLR DPIGRVHFAG TETAWEWSGY INGGIMSGER AAKEVLYELG
RIDQATRDAK EPVNYFIPIE DFTNTFYETY LPSVPGFLRL LGIASACFAI YNAHKKGVGI
ELLQRLCQHN
//
