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Database: UniProt
Entry: G9YGW4_9FIRM
LinkDB: G9YGW4_9FIRM
Original site: G9YGW4_9FIRM 
ID   G9YGW4_9FIRM            Unreviewed;       351 AA.
AC   G9YGW4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Glycolate oxidase subunit GlcD family protein {ECO:0000313|EMBL:EHM41662.1};
GN   ORFNames=HMPREF0080_00884 {ECO:0000313|EMBL:EHM41662.1};
OS   Anaeroglobus geminatus F0357.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Anaeroglobus.
OX   NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM41662.1, ECO:0000313|Proteomes:UP000005481};
RN   [1] {ECO:0000313|EMBL:EHM41662.1, ECO:0000313|Proteomes:UP000005481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0357 {ECO:0000313|EMBL:EHM41662.1,
RC   ECO:0000313|Proteomes:UP000005481};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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:EHM41662.1}.
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DR   EMBL; AGCJ01000030; EHM41662.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9YGW4; -.
DR   STRING; 861450.HMPREF0080_00884; -.
DR   PATRIC; fig|861450.3.peg.838; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_9; -.
DR   Proteomes; UP000005481; 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   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; 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;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005481}.
FT   DOMAIN          1..105
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   351 AA;  38781 MW;  6F85475B2498C04D CRC64;
     MYGHPIYSGQ AEAKGLFYAG DPCSGDSCQI GGNIATNAGG NRAVKYGTTR HQIYAVTVVN
     PLGEIVQLGS RLKKQSTGYC LDQLIIGSEG TLGIITKATI KLLPKLPCKI DILAVFQSAD
     AAIDTVKEIL KKHITPTCVE FMDNITLHSV ERFLQTTLPG SDVGNHLIIE LEGETEDDLD
     DKIMRLDEIC TKRGAAEVLV ADSERIWKAR KSFAEAVRAE SLIVCKEDLV VPVDKEPELL
     HFILAQAQKY NLITRIAAHA GDGNIHLNIL KNEDIPYEEW EKRIANNQAE LYTYVYSLGG
     RLSGEHGIGY KRRGLMERFT DPVELSMMKA IKKALDPNNI LNPGKIFKLD D
//
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