ID A0A098EXH2_9BACI Unreviewed; 478 AA.
AC A0A098EXH2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:CEG26593.1};
GN Name=ysfC {ECO:0000313|EMBL:CEG26593.1};
GN ORFNames=BN1002_01442 {ECO:0000313|EMBL:CEG26593.1};
OS Bacillus sp. B-jedd.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26593.1, ECO:0000313|Proteomes:UP000042335};
RN [1] {ECO:0000313|EMBL:CEG26593.1, ECO:0000313|Proteomes:UP000042335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-jedd {ECO:0000313|EMBL:CEG26593.1,
RC ECO:0000313|Proteomes:UP000042335};
RA Urmite Genomes Urmite Genomes;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CCXR01000001; CEG26593.1; -; Genomic_DNA.
DR RefSeq; WP_048824274.1; NZ_CCXR01000001.1.
DR AlphaFoldDB; A0A098EXH2; -.
DR STRING; 1476857.BN1002_01442; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000042335; Unassembled WGS sequence.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase 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; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00387; glcD; 1.
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:UP000042335}.
FT DOMAIN 45..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 478 AA; 52112 MW; D67A9BE988163AEF CRC64;
MLVQSSKTKI GEDIKKKFIA VVSPVNYEDS QTSRLVYSYD STPNFQAMPD AVISPRNTQE
VSEVIKICDE HKIPIVPRGS GTNLCGGTCP VEGGIVLLFK HMNKILELDE SNLTITVQPG
VITSEIIAAV EPKGLFYPPD PGSMKISTIG GNINENAGGL RGLKYGVTRD YVIGLEAVLP
NGDIIRTGGK LAKDVAGYDF TRLFVGSEGT LCIITEAILK LLPLPETKKT ALALYEDLES
AARSVSKIIA NKIIPTTLEF LDQETVRVVE DYVKIGLPTD AKAVLLIEQD GPPEVVERDM
QKISEICIQE HAFSVQVAKT EQEAEALRTA RRTALSALAR LAPTTILEDA TVPRSEIARM
VKSINEIAEK YKVKICTFGH AGDGNLHPTC PTDIRNKEEM ERVEKAFEEI FERAIELGGT
ITGEHGVGIM KAPYLELKLG KEGVAAMRAV KASLDPNNIM NPGKIFAKDN RKRVVVSK
//