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Database: UniProt
Entry: D3LWV2_9FIRM
LinkDB: D3LWV2_9FIRM
Original site: D3LWV2_9FIRM 
ID   D3LWV2_9FIRM            Unreviewed;       467 AA.
AC   D3LWV2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Putative glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EFD93339.1};
GN   ORFNames=HMPREF0889_0762 {ECO:0000313|EMBL:EFD93339.1};
OS   Megasphaera genomosp. type_1 str. 28L.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=699218 {ECO:0000313|EMBL:EFD93339.1, ECO:0000313|Proteomes:UP000003242};
RN   [1] {ECO:0000313|Proteomes:UP000003242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28L {ECO:0000313|Proteomes:UP000003242};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RT   "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL   Submitted (DEC-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:EFD93339.1}.
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DR   EMBL; ADGP01000033; EFD93339.1; -; Genomic_DNA.
DR   RefSeq; WP_009381468.1; NZ_ADGP01000033.1.
DR   AlphaFoldDB; D3LWV2; -.
DR   STRING; 699218.HMPREF0889_0762; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000003242; 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   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: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}.
FT   DOMAIN          43..222
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   467 AA;  50950 MW;  E195A8DBA432E6EF CRC64;
     MSYEKVTASV QTRLRQIVGA AYVLTERETM LPYSHDEVTD PSYHHLPEAV VLPASAEETA
     AVVKLANTCH IPVVPRGGGT GLACGAVPIY GGIVLSTERL NHICEIRPDG LYAVVEAGVR
     TADLQAAAEA RGLFYAGDPC SGDSCCIGGN IATNAGGNRA VKYGTTRHQI YALQIVNPTG
     HILSVGAPLR KQSTGYCLEQ LLAGSEGTLG IITQATLKLF PKPPYCSDIL AVFPTAEAAV
     TLASTLLQKG ILPTCVEFLD QTTLHAIADF LQEPLPGQAD GHYVIIEMES ADEDERDRHL
     LQLDEYCRAG GASQVLLAEY KKIWHLRKSF AEAVRAESLC VSKEDVVVPI EREAELLQKI
     AVTTARYRLT VRLAAHAGDG NLHLNILKPP AEDYDAWQRR VQAHQQELYT YIYQLGGRLS
     GEHGIGYKRK QLMKKFTNPE ELAMMKAIKQ AWDPNNILNP GKIFDLP
//
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