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Database: UniProt
Entry: G3I526_CRIGR
LinkDB: G3I526_CRIGR
Original site: G3I526_CRIGR 
ID   G3I526_CRIGR            Unreviewed;       480 AA.
AC   G3I526;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   ORFNames=I79_018567 {ECO:0000313|EMBL:EGV97092.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV97092.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-adrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde +
CC         H2O2 + methylamine; Xref=Rhea:RHEA:51168, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC         ChEBI:CHEBI:71406, ChEBI:CHEBI:180943;
CC         Evidence={ECO:0000256|ARBA:ARBA00033614};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-noradrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde
CC         + H2O2 + NH4(+); Xref=Rhea:RHEA:69076, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:72587, ChEBI:CHEBI:180943;
CC         Evidence={ECO:0000256|ARBA:ARBA00033618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:225237; Evidence={ECO:0000256|ARBA:ARBA00033669};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetylputrescine + O2 = 4-acetamidobutanal + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:70283, ChEBI:CHEBI:7386, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58263; Evidence={ECO:0000256|ARBA:ARBA00035873};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70284;
CC         Evidence={ECO:0000256|ARBA:ARBA00035873};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:327995; Evidence={ECO:0000256|ARBA:ARBA00033622};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzylamine + H2O + O2 = benzaldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:225238; Evidence={ECO:0000256|ARBA:ARBA00036746};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC         Evidence={ECO:0000256|ARBA:ARBA00036746};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dopamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:27946, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:59905; Evidence={ECO:0000256|ARBA:ARBA00033704};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362067};
CC   -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
CC       similar size). Each subunit contains a covalently bound flavin.
CC       Enzymatically active as monomer. {ECO:0000256|ARBA:ARBA00025863}.
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; JH001278; EGV97092.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3I526; -.
DR   STRING; 10029.G3I526; -.
DR   PaxDb; 10029-XP_007626886-1; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; G3I526; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF1; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW   Transmembrane {ECO:0000256|RuleBase:RU362067};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362067"
FT   DOMAIN          1..430
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   480 AA;  54297 MW;  C5060CEC14BC7F7A CRC64;
     MAAAKLLHDS GLSVVVLEAR DRVGGRTYTV RKCFDSHLYS FLMEKQNENV KYVDLGGSYV
     GPTQNRILRL AKELGLETYK VNEVERLIHY VKGKPYAFRG PFPPVWNPIT YLDHNNLWRT
     MDEMGEEIPS DAPWKAPLAE EWDYMTMKEL LDKICWTKSA KQLATLFVNL CVTAETHEVS
     ALWFLWYVKQ CGGTTRIIST TNGGQERKFI GGSGQVSERI MGLLGDRVKL ERPVIHIDQN
     GENVVVETLN HEIYEAKYVI SAIPPVLGMK IHYSPPLPML RNQLITRVPL GSVIKCIVYY
     KEPFWRKKDF CGTMIIEGEE APIGYTLDDT KPDGTYAAII GLKKLCELYA KVLNSQEALQ
     PVHYEEKNWC EEQYSGGCYT TYFPPGIMTQ YGRVLRQPVG RIFFAGTETA SHWSGYMEGA
     VQAGERAARE DVPARPITST FLERYLPSVP GLLKLLGLTT IFSATALGFL AHKRGLLVRF
//
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