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Database: UniProt
Entry: T1IN90_STRMM
LinkDB: T1IN90_STRMM
Original site: T1IN90_STRMM 
ID   T1IN90_STRMM            Unreviewed;      1047 AA.
AC   T1IN90;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR002467-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR002467-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
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:0000256|ARBA:ARBA00036170};
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:0000256|ARBA:ARBA00036674};
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:0000256|ARBA:ARBA00036934};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC         Evidence={ECO:0000256|ARBA:ARBA00036934};
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=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:0000256|ARBA:ARBA00001138};
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; JH431152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1IN90; -.
DR   STRING; 126957.T1IN90; -.
DR   EnsemblMetazoa; SMAR002467-RA; SMAR002467-PA; SMAR002467.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_291573_0_0_1; -.
DR   OrthoDB; 5471885at2759; -.
DR   PhylomeDB; T1IN90; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
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; -; 2.
DR   Gene3D; 6.10.250.130; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 2.
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; 2.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Catecholamine metabolism {ECO:0000256|ARBA:ARBA00022939};
KW   FAD {ECO:0000256|RuleBase:RU362067};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362067};
KW   Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW   Transmembrane {ECO:0000256|RuleBase:RU362067};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT   TRANSMEM        1010..1031
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362067"
FT   DOMAIN          16..455
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          534..970
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   1047 AA;  118152 MW;  222AAE01490334D2 CRC64;
     MTTERTAQVV VIGGGISGLT AAKLLHEEKI NVIVLEAQDR VGGRTFTKRD PPRVKYVDIG
     GAYVGPTQNH ILRLAKELNV ETYKINEDKP IVHMKNGARR LFENSYYPTS WNPLIILDMN
     NLFRTIDQMG LEIPPEAPWK APHAEEWDHM TVRQFAKEVT WSKSVRDFLE TFININITTE
     AYEASLLWFL WYVKQCGGTR RIFSVTNGGQ ERKFVGGSQQ ISERIAAKLE GRVFLKKPVV
     GIKQSGGGVE ITTLDGQKFK ADFVISAIPP ILLLKIHFDP PFSALKNQLI QRVPMGSVIK
     CIIYYRRNFW REKGICGESM CEGDEFPLSI TLDDTKPDGS EPAIMGFILA NKARRMTQLT
     EDERKDAIAK SLVKVLGSEE ALHPVHYEEK NWMEMPYAGG CYTAMYPPGC MTKYAKVMRE
     PHDRVFFAGT ETAIKWSGYM DGAASSGERA ARQILHAMGK ISTDQIWIEA PESKEVPGLP
     FKNSMCERYL PSATGFVHFL GISTVGLAIV IYLCDTFSSC INCLWITYSI LRSLSAAKYL
     HEAGISVIVL EARDRVGGRT LTKKDPTIKY VDLGASYVGP TQNYLLRMAK ELGVETYKVN
     EEESVVHYNG TRRFFGRNGI PKFWNPIVNL DMNNLFRTLD KYGAEIPSDA PWDALHAEEW
     DRMTVQQLTD QIICTGAVRD SFRTYITASV TSEAYEASAL WFLWYIRQCG GVKRIFSTTN
     GGQERKFVGG SQQISERIAS RLRDRVQLQK PVVGIDQTSQ QTIVLTTLDG HKYRADYVIT
     AIPPPLLLKI HFNPALPTLK NQLIQRVPMG SVFKCIVYYE KYFWRAKGMC GSALIDGDDE
     HPFSFTFDDT KPDGTSPAIV GFITADKIRR LSGLNKDERK KIICQSLAKV FDTEDALNPI
     HYEEKNWMEE QYSGGCYTIM YPPGCMTMYG KVLRTPFSRV YFAGTETATQ WSGYMDGAIS
     AGERAAREIL HAMGKITKDK IIREEPENKE VPAIPFNNSL SEKILPSAPV FIRIISMTTF
     LGVSVALCFI LHQKKLFKFP ENLFNQT
//
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