ID   A0A0Q5HQ86_9BURK        Unreviewed;       347 AA.
AC   A0A0Q5HQ86;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glycolate oxidase {ECO:0000313|EMBL:KQQ91879.1};
GN   Name=glcE {ECO:0000313|EMBL:KQQ91879.1};
GN   ORFNames=ASF77_08080 {ECO:0000313|EMBL:KQQ91879.1};
OS   Massilia sp. Leaf139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ91879.1, ECO:0000313|Proteomes:UP000051760};
RN   [1] {ECO:0000313|EMBL:KQQ91879.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ91879.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ91879.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ91879.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQQ91879.1}.
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DR   EMBL; LMOJ01000012; KQQ91879.1; -; Genomic_DNA.
DR   RefSeq; WP_056338648.1; NZ_LMOJ01000012.1.
DR   AlphaFoldDB; A0A0Q5HQ86; -.
DR   STRING; 1736272.ASF77_08080; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000051760; Unassembled WGS sequence.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051760}.
FT   DOMAIN          1..167
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   347 AA;  36863 MW;  9CEF2CC11B9E6C2B CRC64;
     MIEHFREQIR AAAARQQPLR IRGGGSKDWY GGALLGDILD TRGHSGVVDY EPTELVITAR
     CGTPLAEIEA VLAAQNQMLA FEPPHFGEGA TFGGAVASGL SGPRRANSGA VRDFVLGAQL
     MDGKGDVLNF GGQVMKNVAG YDVSRLLAGS MGTLGLMLQL SVKVLPRTVA ETTLVFETGE
     IEAIRMLNVW GGQPLPVSGS CWHAGRLALR LSGARAAVDA AVRTLGGQEL PDASSFWTEL
     REQRHAFFAG DMPLWRLSVP PTTGAIVLHG EQLIEWGGAQ RWLRAAASDA ATIRSAVRAV
     GGHATLFRGG DKGVGVFQPL APGVARIHER LKSAFDPAQI FNPGRLF
//