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Database: UniProt
Entry: K0I549_9BURK
LinkDB: K0I549_9BURK
Original site: K0I549_9BURK 
ID   K0I549_9BURK            Unreviewed;       415 AA.
AC   K0I549;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=FAD linked oxidase domain-containing protein {ECO:0000313|EMBL:AFU44001.1};
GN   ORFNames=C380_01375 {ECO:0000313|EMBL:AFU44001.1};
OS   Acidovorax sp. KKS102.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU44001.1, ECO:0000313|Proteomes:UP000006306};
RN   [1] {ECO:0000313|EMBL:AFU44001.1, ECO:0000313|Proteomes:UP000006306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KKS102 {ECO:0000313|EMBL:AFU44001.1,
RC   ECO:0000313|Proteomes:UP000006306};
RX   PubMed=23209225; DOI=10.1128/JB.01848-12;
RA   Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT   Polychlorinated-Biphenyl Degrader.";
RL   J. Bacteriol. 194:6970-6971(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003872; AFU44001.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0I549; -.
DR   STRING; 358220.C380_01375; -.
DR   KEGG; ack:C380_01375; -.
DR   PATRIC; fig|358220.3.peg.283; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_0_0_4; -.
DR   Proteomes; UP000006306; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          30..214
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   415 AA;  43890 MW;  5F3138B99F3E4A56 CRC64;
     MGLAGTNAPH GIRQSFAHPL FKKFTLLPCR VADRCRYDAR MDFSLAPITE RVRAAAAYQT
     PLRIRGGGTK DFHGLALHGE VLDTRVLRGI VSYEPSELVV TVRAGTPLAE LEAVLTEQGQ
     CLPFEPPHFA KTPADAATVG GMVAAGLSGP ARASVGAVRD YLLGVTLLNG KAELLTFGGQ
     VMKNVAGYDV ARLMAGAWGT LGLLTEVSLK VLPVAPGEAT LLFEGINQAD ALRKLHAWGG
     QPLPLNASCW VQDGGVGTLY VRLRGAVAAV EAACKTMGGT RMDNATVAAD WTACREQTLP
     WFTDRATRPD HALWRLSVPA TAPVLALPAG AQPLVEWHGA LRWVQAPESA GDALREAARA
     VGGSASVFIA AEANKTGASG AFDLQSKALE QIHSRLKHSF DPAGIFNPGR MARAW
//
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