ID B8KM99_9GAMM Unreviewed; 498 AA.
AC B8KM99;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative amine oxidase [flavin-containing] B {ECO:0000313|EMBL:EED31149.1};
DE EC=1.4.3.4 {ECO:0000313|EMBL:EED31149.1};
GN ORFNames=NOR53_2729 {ECO:0000313|EMBL:EED31149.1};
OS gamma proteobacterium NOR5-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=566466 {ECO:0000313|EMBL:EED31149.1};
RN [1] {ECO:0000313|EMBL:EED31149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NOR5-3 {ECO:0000313|EMBL:EED31149.1};
RA Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (SEP-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS999407; EED31149.1; -; Genomic_DNA.
DR AlphaFoldDB; B8KM99; -.
DR STRING; 566466.NOR53_2729; -.
DR eggNOG; COG1231; Bacteria.
DR HOGENOM; CLU_004498_0_4_6; -.
DR OrthoDB; 337830at2; -.
DR Proteomes; UP000003977; Unassembled WGS sequence.
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 PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF1; FLAVIN-CONTAINING MONOAMINE OXIDASE B-RELATED; 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:EED31149.1}.
FT DOMAIN 61..486
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 498 AA; 54337 MW; 5EFC64B90D931B2E CRC64;
MQDRSNSKSP LDNGLSRRQI LVAAASTAAA TATLGAAAQT SSPRSAVDES VLDVVVIGAG
LAGLTAARDL QLAGCESFVV LEGNDRVGGR TLNHHLQNGH YSEAGGQWVG PGQTAVYDLC
RELNIGMHPT YLKGKSVYAA QDGSLYEEDS GGGFSVSPNM QRVVDKLNEL AADVPSGAAW
TAPKAKELDA LSLADFIEPY NLEAMDLLSF DVGFRLTDTI HYQEVSLLYA LSRINYAGSY
EQLEGFTGGA QEQRIENGSQ YISEVMAQQV GDRLHLSSPV RKITDWDSDT VSVHSDSGVY
RARRVILAIS PALCNKVQFQ PELPQARREL QQGWPGYSPG RKTCHVYERP FWRDMGYNGW
FFTIGGEVMW AYDNSPEDES IGVINAFIYP SMPNDPDVLA PMLANMYARA FGDEALRYTE
FHDQDWGQEP WCPACVSPLT PGFLTSGLMP ALRDPIGGLV WSGTETAEIW HTYMDGAVRS
GHRAALEALH GLSQSQRV
//