ID E2ZBW9_9FIRM Unreviewed; 464 AA.
AC E2ZBW9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Putative glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EFQ04347.1};
GN ORFNames=HMPREF9429_00951 {ECO:0000313|EMBL:EFQ04347.1};
OS Megasphaera micronuciformis F0359.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ04347.1, ECO:0000313|Proteomes:UP000003195};
RN [1] {ECO:0000313|EMBL:EFQ04347.1, ECO:0000313|Proteomes:UP000003195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0359 {ECO:0000313|EMBL:EFQ04347.1,
RC ECO:0000313|Proteomes:UP000003195};
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-2010) 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:EFQ04347.1}.
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DR EMBL; AECS01000036; EFQ04347.1; -; Genomic_DNA.
DR RefSeq; WP_006941994.1; NZ_GL538208.1.
DR AlphaFoldDB; E2ZBW9; -.
DR STRING; 706434.HMPREF9429_00951; -.
DR GeneID; 78568847; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000003195; 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; 3.30.70.2740; -; 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:UP000003195}.
FT DOMAIN 43..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 51242 MW; D5F18E63F528FB39 CRC64;
MKYNAVTEEL LQELRQVVGE KYVKTDPSVL DIYKADESLA PSYWVMPEVV VLPADARETA
EIVKLANRYK VPLTPRGAGT SVSCGAVPAQ GGIVVLTERM NRILECSEEG MYMVVEAGVR
TADIQALAKS KGLMYAGDPC SADSCLIGGN LATNAGGNKA VRYGTTRNQV YSVEVVLPNG
KIATFGSTLK KCSTGFCLDQ LIIGSEGTLG IITKATLKLV PLSPFHVDVL AVFTKLSDAA
EAVPKIVKAG INPTSVEFMD VSFVRSACEY CKLDLPHKED GYYDIITIEA FNEAELDEKT
EKLMKICEEC HATDVVEADD RVWSVRRNCL ESTRTYSKVG TSEDLVVPVT KIADCIKTLM
EESRKYDFRP FCLAHAGDGN IHFQILKCDM SDEDWEKQLE QFRAVAYPYV YSLGGRLSGE
HGIGLKRLKY MEKYTDPVEL EFMKTIKQAV DPNWIMNPGK VIEP
//
