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Database: UniProt
Entry: Q6FBI8_ACIAD
LinkDB: Q6FBI8_ACIAD
Original site: Q6FBI8_ACIAD 
ID   Q6FBI8_ACIAD            Unreviewed;       509 AA.
AC   Q6FBI8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   SubName: Full=Putative flavin-binding monooxygenase {ECO:0000313|EMBL:CAG68574.1};
DE            EC=1.14.13.- {ECO:0000313|EMBL:CAG68574.1};
GN   OrderedLocusNames=ACIAD1733 {ECO:0000313|EMBL:CAG68574.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68574.1, ECO:0000313|Proteomes:UP000000430};
RN   [1] {ECO:0000313|EMBL:CAG68574.1, ECO:0000313|Proteomes:UP000000430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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DR   EMBL; CR543861; CAG68574.1; -; Genomic_DNA.
DR   RefSeq; WP_004926715.1; NC_005966.1.
DR   AlphaFoldDB; Q6FBI8; -.
DR   STRING; 202950.GCA_001485005_03110; -.
DR   GeneID; 45234119; -.
DR   KEGG; aci:ACIAD1733; -.
DR   eggNOG; COG2072; Bacteria.
DR   HOGENOM; CLU_006937_7_1_6; -.
DR   OrthoDB; 312624at2; -.
DR   BioCyc; ASP62977:ACIAD_RS07990-MONOMER; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR42877; -; 1.
DR   PANTHER; PTHR42877:SF4; FAD_NAD(P)-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000313|EMBL:CAG68574.1};
KW   Oxidoreductase {ECO:0000313|EMBL:CAG68574.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000430}.
SQ   SEQUENCE   509 AA;  56914 MW;  98678510B5E5AB7B CRC64;
     MTAQAKKLDS ADRKALPSHI YDSFIVGAGI SGIAAAIRLD QVGYANYKII EKASRVGGTW
     RENTYPGCGC DVPSALYSYS FAPSAQWSHL FARQPEILNY LEDVSHKFNI NEKIEFETEL
     NKAAWDNERN LWVLDTNKGQ FLSRTVVFAT GPITEAQIPK LDGLDSFKGE MFHSARWNHD
     YDLSGKRIAV IGTGASAIQF VPQIQPLAKE LFVFQRTAPW VVPKPDMELG DFSKSVIAKL
     PIIQSTWRKA VAQSLNAINF GLRNPAVLKP VGELFKQVLK SQVKDPELLK AVIPDFTIGC
     KRLLFANNYY PALQASNTKL IPHGLVKVEG NTVIAANGER HEVDVIIWGT GFEVSHPPIG
     RRVYNDKGEC LNDLWKQSSP EAYLGTNIEN VPNAFLVLGP NVLVYDSFIG LAEAQLDYIV
     DGLQKIKKHN ISKLTIKPQV IHAHNERVQK HLKTTVFNAG GCKSYYLDAN GRNFAAWPWS
     LKKLRQRLKS LNIRDYDVTY QTTTNKIDA
//
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