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Database: UniProt
Entry: Q123I9_POLSJ
LinkDB: Q123I9_POLSJ
Original site: Q123I9_POLSJ 
ID   Q123I9_POLSJ            Unreviewed;       378 AA.
AC   Q123I9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ABE46303.1};
GN   OrderedLocusNames=Bpro_4416 {ECO:0000313|EMBL:ABE46303.1};
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46303.1, ECO:0000313|Proteomes:UP000001983};
RN   [1] {ECO:0000313|Proteomes:UP000001983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX   PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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DR   EMBL; CP000316; ABE46303.1; -; Genomic_DNA.
DR   RefSeq; WP_011485292.1; NC_007948.1.
DR   AlphaFoldDB; Q123I9; -.
DR   STRING; 296591.Bpro_4416; -.
DR   KEGG; pol:Bpro_4416; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_4_3_4; -.
DR   OrthoDB; 9805337at2; -.
DR   Proteomes; UP000001983; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT   DOMAIN          6..345
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   378 AA;  40078 MW;  01B191BFF23FE74E CRC64;
     MQTQELVVIG GGLVGAAIAY GAARAGAPVT LLDQGDIAHR ASRGNFGLVW VQSKGDKVPR
     YARWSRDALT FWPALAKELL ELTGVDVALH QPGGFWIGFS EAEMQAREAM LERINSSVGG
     IPYEMLDHAA LKARLPAIGP TVAGGSYCPL DGHANPLMLL HALHAGLKAR GARVVSSVDV
     AQITYQEKGT GFEIKSKDGK SWHAPRVVLA AGLGNNELAP QVGLHAPVLP NRGQVLITER
     LKPFLPYPTN KARQTNEGSV QLGYSVEDVG LDDSTTVSAV EWIAKRAVTT FPILSSVRLV
     RAWGALRVLT PDGLPIYQES VSCPGAFVAT SHSGVSLAAA HAHVIGPWVA GLGAAPDAFE
     VFAGERFLDP NRSFSNAH
//
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