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AOFA_HORSE
ID   AOFA_HORSE              Reviewed;         527 AA.
AC   Q5NU32;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000250|UniProtKB:P21397};
DE            EC=1.4.3.21 {ECO:0000250|UniProtKB:P21396};
DE            EC=1.4.3.4 {ECO:0000250|UniProtKB:P21396};
DE   AltName: Full=Monoamine oxidase type A;
DE            Short=MAO-A;
GN   Name=MAOA {ECO:0000250|UniProtKB:P21397};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Momozawa Y., Mori Y.;
RT   "Equus caballus monoamine oxidase A (MAOA), mRNA.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC       secondary amine such as neurotransmitters, with concomitant reduction
CC       of oxygen to hydrogen peroxide and has important functions in the
CC       metabolism of neuroactive and vasoactive amines in the central nervous
CC       system and peripheral tissues. Preferentially oxidizes serotonin. Also
CC       catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-
CC       3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline.
CC       {ECO:0000250|UniProtKB:P21396}.
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:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58001; EC=1.4.3.21;
CC         Evidence={ECO:0000250|UniProtKB:P21396};
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:0000250|UniProtKB:P21396};
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:0000250|UniProtKB:P21396};
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:0000250|UniProtKB:P21396};
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:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + serotonin = (5-hydroxyindol-3-yl)acetaldehyde +
CC         H2O2 + NH4(+); Xref=Rhea:RHEA:69072, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:50157, ChEBI:CHEBI:350546;
CC         Evidence={ECO:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + kynuramine + O2 = 3-(2-aminophenyl)-3-oxopropanal + H2O2
CC         + NH4(+); Xref=Rhea:RHEA:59596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:180898,
CC         ChEBI:CHEBI:180899; Evidence={ECO:0000250|UniProtKB:P21396};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC         Evidence={ECO:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4(+);
CC         Xref=Rhea:RHEA:59416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57887; Evidence={ECO:0000250|UniProtKB:P21396};
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:0000250|UniProtKB:P21396};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P21397};
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P21397}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P21396}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:P21396}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P21396}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB178282; BAD80721.1; -; mRNA.
DR   RefSeq; NP_001075301.1; NM_001081832.1.
DR   AlphaFoldDB; Q5NU32; -.
DR   SMR; Q5NU32; -.
DR   STRING; 9796.ENSECAP00000043359; -.
DR   PaxDb; Q5NU32; -.
DR   PeptideAtlas; Q5NU32; -.
DR   GeneID; 100033867; -.
DR   KEGG; ecb:100033867; -.
DR   CTD; 4128; -.
DR   HOGENOM; CLU_004498_0_1_1; -.
DR   InParanoid; Q5NU32; -.
DR   OMA; EWTRGAY; -.
DR   OrthoDB; 1034142at2759; -.
DR   TreeFam; TF313314; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0097621; F:monoamine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:RHEA.
DR   GO; GO:0008131; F:primary amine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Catecholamine metabolism; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..527
FT                   /note="Amine oxidase [flavin-containing] A"
FT                   /id="PRO_0000099849"
FT   TOPO_DOM        1..497
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        498..518
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        519..527
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   REGION          520..522
FT                   /note="Interaction with membrane phospholipid headgroups"
FT                   /evidence="ECO:0000250"
FT   SITE            335
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000250"
FT   SITE            374
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P21397"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21396"
FT   MOD_RES         406
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P21397"
SQ   SEQUENCE   527 AA;  59580 MW;  177988F29564E35B CRC64;
     MASQEKASMA GHMFDVVVIG GGISGLSAAK LLAEHETNVL VLEARDRVGG RTYTVRNKHV
     NYVDVGGAYV GPTQNRILRL SKELGLETYK VNVNERLVQY VKGKSYPFRG AFPPVWNPIA
     YLDYNNLWRT MDNMGKEIPA DAPWEAPHAE EWDKMTMKDL IDKICWTKTA RQFASLFVNI
     NVTSEPHQVS ALWFLWYVKQ CGGTTRIFSI TNGGQERKFV GGSGQVSERI MELLGDRVKL
     EHPVTYVDQS GDNIIVETLN HEHFECKYVI SAIPPALTAK IHFKPELPSE RNQLIQRLPM
     GAIIKCMMYY KEAFWKKKDY CGSMIIEDEE APISITLDDS KPDGSLPAIM GFILARKADR
     LAKLHKEMRK KKICELYAKV LGSQEALQPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG
     RVIRQPVGRI YFAGTETATR WSGYMEGAVE AGERAAREIL NALGKVAEKD IWLQEPESKD
     VPAVEITHSF WERNLPSVGG LLKIIGFSTS ITALWIVVYK FKLLTRS
 
 
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