ID C6BNM5_RALP1 Unreviewed; 498 AA.
AC C6BNM5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Amine oxidase (Flavin-containing) {ECO:0000313|EMBL:ACS65683.1};
DE EC=1.4.3.4 {ECO:0000313|EMBL:ACS65683.1};
GN OrderedLocusNames=Rpic12D_4441 {ECO:0000313|EMBL:ACS65683.1};
OS Ralstonia pickettii (strain 12D).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=428406 {ECO:0000313|EMBL:ACS65683.1};
RN [1] {ECO:0000313|EMBL:ACS65683.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12D {ECO:0000313|EMBL:ACS65683.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Marsh T., Richardson P.;
RT "Complete sequence chromosome 2 of Ralstonia pickettii 12D.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; CP001645; ACS65683.1; -; Genomic_DNA.
DR AlphaFoldDB; C6BNM5; -.
DR STRING; 428406.Rpic12D_4441; -.
DR KEGG; rpf:Rpic12D_4441; -.
DR HOGENOM; CLU_004498_0_4_4; -.
DR OMA; EWTRGAY; -.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:UniProtKB-EC.
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; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACS65683.1}.
FT DOMAIN 64..486
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 498 AA; 53361 MW; BF360E0A3B67C104 CRC64;
MDDIAKKHDE APEAAALTRR GFLGMAASVT AAATAAVLPN VASAVTAASD SRDVLEVAII
GAGLAGLTAA RDLKRAGCES FVVLEARDRV GGRTLNHDLG NGYFSEAGGQ WIGPGQTAIA
NLARELGVGT FLTHWEGDLV MLAGNARTTL ANDGGFDTDP KLRRELEEMA RSVPTAAPWT
SPRAAEFDAM SLADWLATKH LTPEDQIGWA LAAQLTTGTA PEKLSMLHYL SLINSADCNY
RQLEAIKGGA QESRISGGSQ ILSIKMAEAL GDKVRLSTPV LRIENWQNGP VTIHTAKGVV
RARSLIVALS PSLCNQIAFD PPLPEKRREM QRRWPAYAPM RKTAHVYKKA FWRDKGLDGM
LVQLKGPVQF AYDNSPEDVS FGVISAFVNN GVLPSDPKAA ETELSRIYAQ AFGDEALHPV
AYHEHDWGKA DNWSLSCTSP IPPGFLTKYG DVLHPPIGRL IWAGTETAEI WITTMDGAIR
SGHKAALQAL QAAAGGKA
//