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Database: UniProt
Entry: A0A2J7RFP4_9NEOP
LinkDB: A0A2J7RFP4_9NEOP
Original site: A0A2J7RFP4_9NEOP 
ID   A0A2J7RFP4_9NEOP        Unreviewed;       551 AA.
AC   A0A2J7RFP4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   Name=maoA_1 {ECO:0000313|EMBL:PNF39652.1};
GN   ORFNames=B7P43_G05635 {ECO:0000313|EMBL:PNF39652.1};
OS   Cryptotermes secundus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX   NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF39652.1, ECO:0000313|Proteomes:UP000235965};
RN   [1] {ECO:0000313|EMBL:PNF39652.1, ECO:0000313|Proteomes:UP000235965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole body {ECO:0000313|EMBL:PNF39652.1};
RA   Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA   Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA   Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA   Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA   Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA   Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA   Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA   Bornberg-Bauer E.;
RT   "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362067};
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   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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:PNF39652.1}.
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DR   EMBL; NEVH01004410; PNF39652.1; -; Genomic_DNA.
DR   EMBL; NEVH01004410; PNF39653.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J7RFP4; -.
DR   STRING; 105785.A0A2J7RFP4; -.
DR   InParanoid; A0A2J7RFP4; -.
DR   OrthoDB; 5471885at2759; -.
DR   Proteomes; UP000235965; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU362067};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235965}.
FT   DOMAIN          32..483
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   551 AA;  60888 MW;  099B6B64A66B68C4 CRC64;
     MTHYAISASN CVERGEKGMM TETDVIIVGA GISGLTAAYR LLRRDSSLRI LVLEAKDRVG
     GRTLTVPLKT SNLLTEQFDL GGQWVSSSQP HILRLLQELN LHTYPQYSAG CKVVLAGATV
     FEKYSSSFPY FGSFYSCYEL RQFVLKIEQM LSKVTIVDPL KCIFAEELDS ITMETLLLRH
     LSTKAAQDIV RAAIRSTFGT EASQLSALYV IALSNGTHGL LNQFSASATG ARELRIKGGA
     QQIALKLSAQ IGNKLIILNT PVTEIEQSES GVQVTTQSGQ VHRSKYIVVA LPPSEVLRIL
     FSPPLPLKHR QLLQRYPVGH LTKFVITYPK AFWREKGFSG EVFSCGGHEA EHICDGGPIS
     AAYDATTHDG QPAIAGYMAS KTGIEWSSKD PCHRKQSVLQ TLSEFWGDWV HDPIDYVEKN
     WSDETYVGGC PMHGTSPGVM GWFHHIRASF GRIYWAGTET ATQWCGYMDG AVQAGERSAL
     EVLRELRPEI VTAADLQAIN LILRSSSPVH VLPVSHVYRW TLCLPLVLIA MGWTAYALRR
     HFWVVGVGRI A
//
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