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Database: UniProt
Entry: T1FMW5_HELRO
LinkDB: T1FMW5_HELRO
Original site: T1FMW5_HELRO 
ID   T1FMW5_HELRO            Unreviewed;       518 AA.
AC   T1FMW5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   Name=20210164 {ECO:0000313|EnsemblMetazoa:HelroP185502};
GN   ORFNames=HELRODRAFT_185502 {ECO:0000313|EMBL:ESO05715.1};
OS   Helobdella robusta (Californian leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX   NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP185502, ECO:0000313|Proteomes:UP000015101};
RN   [1] {ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ESO05715.1, ECO:0000313|Proteomes:UP000015101}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:HelroP185502}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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}.
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DR   EMBL; AMQM01003859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB096325; ESO05715.1; -; Genomic_DNA.
DR   RefSeq; XP_009016348.1; XM_009018100.1.
DR   AlphaFoldDB; T1FMW5; -.
DR   STRING; 6412.T1FMW5; -.
DR   EnsemblMetazoa; HelroT185502; HelroP185502; HelroG185502.
DR   GeneID; 20210164; -.
DR   KEGG; hro:HELRODRAFT_185502; -.
DR   CTD; 20210164; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_004498_0_3_1; -.
DR   InParanoid; T1FMW5; -.
DR   OMA; GPTWFWP; -.
DR   OrthoDB; 5471885at2759; -.
DR   Proteomes; UP000015101; Unassembled WGS sequence.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 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   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:UP000015101}.
FT   DOMAIN          15..462
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   518 AA;  57252 MW;  D1702D7ED39EE184 CRC64;
     MSSEVLDVVV IGAGLSGVAA AHELFHKNAK LRFVILEAKE RIGGRTLGTK LRTSSGEDFW
     DLGGQWIGRC QPHIYSLVEK LQLKMYEQSC SGKKLVQLDS AGSIMQYTSD IPPISLLALL
     ELHCFIWKVS YFIKKMDSKV FMSSGLVAKL DGMTVEQFKR SYFWTQGAKN ALDSCCRCIF
     GSDPVHMSML YFLMYAHRSN NFEALLSCKK NFGAQELKIN GGAWQICHEL MKQIPGDTLN
     TSSPVVSIDQ KQDKHVHVRV LNGTVFVCQY VILAIPPNEI CKISFNPCLP LQKFNVLQRM
     PVGCLTKIIV TYAEAFWQKN GFSGEVLTSG ANGAHPLCVV FDATSANKNP ALVAFVGGTQ
     QIKFSSVQES SRKSLVLETL ASFFGAEALH PLDYMEKNWN EEAYNGGCPV NVATPGVCTT
     LHTALSRPFY RVFFAGTESA SRWCGFLNGA VQAGHRAAHE VLYNVSPECV TDKDLVDTCY
     ANEEAQPTNE LPNATPFCKL AIITFIAASL LAYKRFFT
//
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