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Database: UniProt
Entry: K0DKY7_9BURK
LinkDB: K0DKY7_9BURK
Original site: K0DKY7_9BURK 
ID   K0DKY7_9BURK            Unreviewed;       525 AA.
AC   K0DKY7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Glycolate oxidase {ECO:0000313|EMBL:AFT85505.1};
GN   ORFNames=BUPH_01934 {ECO:0000313|EMBL:AFT85505.1};
OS   Paraburkholderia phenoliruptrix BR3459a.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT85505.1, ECO:0000313|Proteomes:UP000010105};
RN   [1] {ECO:0000313|EMBL:AFT85505.1, ECO:0000313|Proteomes:UP000010105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR3459a {ECO:0000313|EMBL:AFT85505.1,
RC   ECO:0000313|Proteomes:UP000010105};
RX   PubMed=23144415; DOI=10.1128/JB.01821-12;
RA   de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA   Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA   Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA   Ribeiro de Vasconcelos A.T.;
RT   "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT   Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL   J. Bacteriol. 194:6675-6676(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003863; AFT85505.1; -; Genomic_DNA.
DR   RefSeq; WP_015002402.1; NC_018695.1.
DR   AlphaFoldDB; K0DKY7; -.
DR   STRING; 1229205.BUPH_01934; -.
DR   GeneID; 27796663; -.
DR   KEGG; bpx:BUPH_01934; -.
DR   PATRIC; fig|1229205.11.peg.1561; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_024402_0_1_4; -.
DR   Proteomes; UP000010105; Chromosome 1.
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   Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016170; Cytok_DH_C_sf.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 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;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT   DOMAIN          49..236
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   525 AA;  57302 MW;  C8CC777187E3D997 CRC64;
     MSRQLPPKLS AAQFDAALAA WRAIVGEQHV VDSAAGRSAY LDPFAPGERA AFAASAALLP
     ASVEEIRAIL RVANHYRIPL WTVSTGRNFA YGGAAPRLTG SVVLDLQRMN RILEVNETLA
     YALVEPGVSY FDLHAHLRER GYRLWVDPPA AGWGSVVGNT LERGFGYTPY GDHAATQCGM
     EVVLANGDVL RTGMGAIDTS TAWQLYQPGY GPSFDAMFMQ SNYGVVTQLG VWLMPAPPAY
     LLGEIQFRHE TDLEAIVEIL RPLRLDETIR NQAVIEGGLR RAAGLSARRE WYDGPGAMPE
     NAVAAMLDKL NVGRWNLHFA LYGTPELIDA RYAIVQRAFA RVKDARLSAR RYSGDAEPVA
     GGDRNLAGIP AMSAFRMLDW RGGAGAHVDF APVCPATGRD ALRQYFMVKA RAAEYGFDYY
     GGFTAGVRHL HHIFAAIFDR DDAGQVEQAG ALLRSLMSDA RAAGYGEYRA HLAYMDSAAA
     QYSFNDGALL RLSETIKDAL DPNGILAPGK QGIWPAAWRD RRGYT
//
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