ID   E6Q1I0_9ZZZZ            Unreviewed;       460 AA.
AC   E6Q1I0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Glycolate oxidase subunit, FAD-linked {ECO:0000313|EMBL:CBI01040.1};
GN   Name=glcD {ECO:0000313|EMBL:CBI01040.1};
GN   ORFNames=CARN4_0393 {ECO:0000313|EMBL:CBI01040.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI01040.1};
RN   [1] {ECO:0000313|EMBL:CBI01040.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) 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:CBI01040.1}.
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DR   EMBL; CABO01000013; CBI01040.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6Q1I0; -.
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; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 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;
FT   DOMAIN          32..207
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   460 AA;  48418 MW;  F2F676C1F49BC26C CRC64;
     MLIERLTEAL GADAVKTSPE DLACYSFDAY SQGVLPSAVV LPTSAAQVSA VVKIARELEE
     PLIARGSGTG LCGGATPVRA GIVLSFARMN QLLELDIENR RVRVAPGLVN LQLSERIAPT
     GYFYAPDPAS QRASTIGGNI GTNAGGPHCL AYGTTVNHVL ALEIVDDRGE CFTTGVEDLG
     YDLTALLVGS EGTLGIVTSA WVRLLRIPPA TGVWLAAFPS IESASEAVSA IVGAGIVPTA
     LEMMDATIVR AVESAYAAGY PEDAAAVLLV ESSGEPEEVA SADAAIARIA RAHGATKWQA
     AKNAEQRDAL WRGRKGAAGA VGRIAPNYYT QDVCVPRTRL PEMLAAVDEA ARKHEIVVGN
     VFHAGDGNLH PLLLYDKRDT RQVAAVIEIG NIVLARAVEL GGTISGEHGV GIEKRSGMSM
     VYRTEDLAAM ACVRDVFDPH ALLNPEKIFP AGISCREMRT
//