ID H3AIH3_LATCH Unreviewed; 418 AA.
AC H3AIH3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN Name=LOC102349352 {ECO:0000313|Ensembl:ENSLACP00000009444.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000009444.1, 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:ENSLACP00000009444.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; AFYH01037299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01037300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01037301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01037302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01037303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01037304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AIH3; -.
DR STRING; 7897.ENSLACP00000009444; -.
DR Ensembl; ENSLACT00000009516.1; ENSLACP00000009444.1; ENSLACG00000008328.1.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000166107; -.
DR HOGENOM; CLU_004498_0_4_1; -.
DR InParanoid; H3AIH3; -.
DR OMA; KQYSITC; -.
DR TreeFam; TF313314; -.
DR Proteomes; UP000008672; 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:SF11; AMINE OXIDASE [FLAVIN-CONTAINING] A; 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|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 15..406
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 418 AA; 47292 MW; FD6E0E31E18F6136 CRC64;
MSVEKRDVII VGGGLSGLSA AKLLAEAGLN VLVLEARNRV GGRTYTVQGP EFQYVDLGGA
YVGPTQNRIL RVAKEFGVKT YLVNEKEQLI HYVKGKSYPF QGPFPPAWNP IVYLDYNNLW
RTLDEMGREI PAEAPWKAPC AEAWDNMTMK QLIDKLCWTR VAKDFATLFV NVNVTSEPHE
VSALWFLWYV KQCGGTKRIF STTNGGQERK FVGGSGQISE RMADRLKGHV KLNKPVVRIL
QNDKSVCVET LDGEKYESAY VISAVPPALI LNMHFSPPLP PVRNQLIQRV PMGSIIKCMV
YYKRAFWREN GYCGTMMIED EASPISLTLD DTKPDGSYPA IMGFILARKA RQLINLTKEE
RRKEKICQIY AKVLGTDEAL QAVHYEEKDW CEEQYSGGCY TAYYSPGTFY QFSRSVLR
//