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Database: UniProt
Entry: R4Z2T8_9ACTN
LinkDB: R4Z2T8_9ACTN
Original site: R4Z2T8_9ACTN 
ID   R4Z2T8_9ACTN            Unreviewed;       516 AA.
AC   R4Z2T8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Amine oxidase {ECO:0000313|EMBL:CCM64970.1};
GN   ORFNames=BN381_50112 {ECO:0000313|EMBL:CCM64970.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM64970.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM64970.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM64970.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCM64970.1}.
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DR   EMBL; CANL01000045; CCM64970.1; -; Genomic_DNA.
DR   RefSeq; WP_012229346.1; NZ_HG422565.1.
DR   AlphaFoldDB; R4Z2T8; -.
DR   STRING; 1229780.BN381_50112; -.
DR   GeneID; 78311986; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_026719_1_0_11; -.
DR   OrthoDB; 337830at2; -.
DR   Proteomes; UP000018291; Unassembled WGS sequence.
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   PANTHER; PTHR21197; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   PANTHER; PTHR21197:SF0; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018291}.
FT   DOMAIN          242..397
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   REGION          485..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  57621 MW;  1A7839631832DDE9 CRC64;
     MDDSRPTLAP HEADLIGTDP GEVVVIGAGP AGLTAAYQLH KYGIASTILE GSDTVGGISR
     TEVRDGWRFD IGGHRFFTKV PEVEALWHEI LPDEDFMMRP RKSRIFYNGK FYDYPLRATN
     ALRNLGIIEA IRCVLSYVWV RIRPPKDQSN FEGWVAARFG WRLYRTFFKA YTEKVWGVPA
     DQIEADWAAQ RIKNLSLFSA VVNALLPNRN QKDIASLIEE FQYPKYGPGM MWEVCRDKVV
     AEGSTMTYGA EVTGVRHVDG RATHVIATHA DGTTEEHEAD HVVSSMPISA LLAGMDPPVP
     DHVMAAATGL SYRDFITVAL VVPESKVDWN DNWIYIHDPA VKTMRIQNFG SWSPHLVKDG
     RNVLGLEYTV FETDAAWTAP DEELIEQGRR ELVHLGLIEP GDVEGGYVVR QKKAYPTYDE
     TYKANVDVLR GWLAEHTSNV HPIGRNGMFR YNNQDHSMYT AMLTAENIAT GSTHDVWTVN
     VEEEYHEEGP ADGNGSSGNT GRDAPIIPSS APRLDA
//
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