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Database: UniProt
Entry: E6VE66_RHOPX
LinkDB: E6VE66_RHOPX
Original site: E6VE66_RHOPX 
ID   E6VE66_RHOPX            Unreviewed;       485 AA.
AC   E6VE66;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Amine oxidase {ECO:0000313|EMBL:ADU41679.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rpdx1_0035 {ECO:0000313|EMBL:ADU41679.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU41679.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002418; ADU41679.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VE66; -.
DR   STRING; 652103.Rpdx1_0035; -.
DR   KEGG; rpx:Rpdx1_0035; -.
DR   eggNOG; COG1231; Bacteria.
DR   HOGENOM; CLU_004498_10_3_5; -.
DR   OMA; WDQDECL; -.
DR   OrthoDB; 9790035at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS00175-MONOMER; -.
DR   Proteomes; UP000001402; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF405; PEROXISOMAL N(1)-ACETYL-SPERMINE/SPERMIDINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
FT   DOMAIN          47..440
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          443..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  50897 MW;  91DEEAC10564B875 CRC64;
     MTISRRSLLE GLLGATAGLA LLPVLGGRAN AALPREAEVV VVGAGAAGIA AARRLVAAGR
     KVIVVEAASE IGGRCVTDTT SFAAPFDRGA RWLHNPDSNP LVWLARSSGF AVTPIAPGQK
     VRIGRRNARS RETEDFLAAF VRASRAISEA SRGKTDISCA AALPKDLGDW AATIEYVLGP
     ATTSKDLRAL SAMDTARTLD RTALLGCPQG VGSLLTQLAS SLPIALSTPV KRIVWSGRDL
     AVETAAGRIG ARAIIVTAST NVLTSGNLAF SPELPKRQLD AAARLSLGST DRIALQLKGN
     PLGLSRDETI IERADDIRTA TLVGNIGGSS LCTVDVAGSF GRQLAAQGEA AMQDFAIEWL
     GKLFGSDVAG AVERKAVTRW NEMPYVLGAM SAAEPGGQPS RKVLGEPLGN LFFAGEATHE
     TLFGTVQGAW ESGERAADAA LKKIGAVKEP APEKPARKQK PRREPQRQRE QRPPATASGT
     PSWWR
//
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