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Database: UniProt
Entry: A0A0D0QEU3_9GAMM
LinkDB: A0A0D0QEU3_9GAMM
Original site: A0A0D0QEU3_9GAMM 
ID   A0A0D0QEU3_9GAMM        Unreviewed;       519 AA.
AC   A0A0D0QEU3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Glycolate dehydrogenase, subunit GlcD {ECO:0000313|EMBL:KIQ96693.1};
DE            EC=1.1.99.14 {ECO:0000313|EMBL:KIQ96693.1};
GN   ORFNames=TI01_1760 {ECO:0000313|EMBL:KIQ96693.1};
OS   Lysobacter sp. A03.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ96693.1, ECO:0000313|Proteomes:UP000032077};
RN   [1] {ECO:0000313|EMBL:KIQ96693.1, ECO:0000313|Proteomes:UP000032077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A03 {ECO:0000313|EMBL:KIQ96693.1,
RC   ECO:0000313|Proteomes:UP000032077};
RA   Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H.,
RA   Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.;
RT   "Genome sequence of Lysobacter sp. A03.";
RL   Submitted (JAN-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:KIQ96693.1}.
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DR   EMBL; JXSS01000082; KIQ96693.1; -; Genomic_DNA.
DR   RefSeq; WP_043958889.1; NZ_JXSS01000082.1.
DR   AlphaFoldDB; A0A0D0QEU3; -.
DR   STRING; 1199154.TI01_1760; -.
DR   PATRIC; fig|1199154.3.peg.1846; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000032077; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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   Oxidoreductase {ECO:0000313|EMBL:KIQ96693.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032077}.
FT   DOMAIN          38..226
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   519 AA;  55160 MW;  79131D8E3FF43295 CRC64;
     MSTTLSPDHV IAELKTRWGD GVITDPTELE YFGTDVYSQG KPLLAVLRPT SAEQIAAAVA
     ELTAAGVTLI ARGGGMSYTG GYLATRQPTV LIDTGGLDKV VEINVQDAYV VVEAGVTWEA
     LQKALQAKGV RTPYFGPMSG SHATVGGALS QGSVFHGSAR YGSSADSVLG LEVVTANGEI
     LRTGSAASGN ATPFFRWHGP DLTGVFLGDC GLLGIKVRAS LRLLPRHSHI DYLSWQFERA
     DQLMDAMGAL ARAGLASEIA AFDPSLSQIR MRRASLSSDV KSLGNVIKKG GLMQGLKLVT
     KGRDFLDPDL FTLHITLEGD SEGEISARVA AARKAVAAFG KEVENSVPKV MAANPFAAKN
     AMLGSAGERW APIHGIVPHS RSTDLFNALQ ELFAAEKAVM DEHGLFIGTL MTTVGAQATL
     IEPCIYWPDS HNAFHVRTVD PEHRAKIGCP GENLPARAAT DALKRKIADT MRAHGAASFQ
     IGKFYTYREG RDPAALAMLD AIKQQLDPKG LMNPGVLGR
//
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