ID H3AY73_LATCH Unreviewed; 518 AA.
AC H3AY73;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN Name=LOC102352327 {ECO:0000313|Ensembl:ENSLACP00000014594.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000014594.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000014594.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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; AFYH01119883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01119892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AY73; -.
DR Ensembl; ENSLACT00000014695.1; ENSLACP00000014594.1; ENSLACG00000012844.2.
DR GeneTree; ENSGT00940000166107; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000012844; Expressed in pectoral fin and 6 other cell types or tissues.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
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 InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF21; AMINE OXIDASE [FLAVIN-CONTAINING] B; 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|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362067}; Membrane {ECO:0000256|RuleBase:RU362067};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362067};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362067}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..518
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003580721"
FT TRANSMEM 489..510
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362067"
FT DOMAIN 12..445
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 444..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 58377 MW; 73358ED364437CC9 CRC64;
NFLLLQRNFL LGLSAAKLLT ESGLNVVVLE ARDRVGGRTF TTRNKHVKYV DLGGAYVGPT
QNRILRLSKE LGIETYKVNE VERFIHHIKG KSYPFQGPFP PMWNPLAFLD YNNLWRTLDE
MGKEIPREAP WKAPHAEEWD KMTMKDLIDK ICWTEAAKQF ATLFVNVNVT SEPCEVSALW
FLWYVKQCGG TTRIFSIGNG GQERKFVGGS GQISEKMMEI LGDRVKLQGP VISIDQSGDG
VVVETLNHEK YEAKYVISAI PPSLSMKIHY KPPLPPIRNQ FIYRVPIGSV IKCMVYYKEA
FWKKKDFCGC MMIEDEEAPI GVTLDDTKPD GTVPAIMGFI LARKARRLAH ITKEERKTKI
CELYARVLGS EEALHPVHYE EKNWCEEEYS GGCYAAYFPP GIMTQFGKVI RQPVGRIFFA
GTETATEWSG YMEGAVQAGE RAARESRRHA ASSKTREKPG GTKPDKHDVP ASPITTAFWE
RNLPSVPGFL RLLGFSAFLT STAAVGLFAY KRGLLIKN
//
