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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//