ID B7HH52_BACC4 Unreviewed; 470 AA.
AC B7HH52;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:ACK62983.1};
GN Name=glcD {ECO:0000313|EMBL:ACK62983.1};
GN OrderedLocusNames=BCB4264_A1348 {ECO:0000313|EMBL:ACK62983.1};
OS Bacillus cereus (strain B4264).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK62983.1, ECO:0000313|Proteomes:UP000007096};
RN [1] {ECO:0000313|EMBL:ACK62983.1, ECO:0000313|Proteomes:UP000007096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4264 {ECO:0000313|EMBL:ACK62983.1,
RC ECO:0000313|Proteomes:UP000007096};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus B4264.";
RL Submitted (OCT-2008) 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; CP001176; ACK62983.1; -; Genomic_DNA.
DR RefSeq; WP_000890752.1; NC_011725.1.
DR AlphaFoldDB; B7HH52; -.
DR KEGG; bcb:BCB4264_A1348; -.
DR HOGENOM; CLU_017779_9_2_9; -.
DR Proteomes; UP000007096; Chromosome.
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}.
FT DOMAIN 37..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 470 AA; 50825 MW; 41F797BA6DA0C82D CRC64;
MLEKQIIHSF VSIVGEDNVD TSNMGRLTYS YDATPNFQAM PDAVIAPRNT NEVAEVLKVC
NTHKIPVYVR GSGTNLCAGT CPLEGGIVLI FRHMNNILEI DEENLTITVQ AGVITLDIIK
AVEEKGLFYP PDPSSMKIST IGGNINENSG GLRGLKYGVT RDYVMGLELV LPNGDIIRTG
GKLAKDVAGY DLTRLFIGSE GTLGVVTEAI LKLVPMPETK KTMLALYEDI NEAARAVSSI
IANKIIPATL EFLDQPTIEV VEAFAQIGLP TDVKAILLIE QDGPPEVVNR DIEKMANVCH
SMNAVDVRVA KGETEADALR TARRSALSAL ARLKPTTILE DATVPRSQIA PMVEAINAIA
KKYNIPICTF GHAGDGNLHP TCMTDARNAE EMHRAEQAFA EIFAKAIELG GTITGEHGVG
AMKAPYLEMK LGKEGIAAMQ GIKQAFDPNN IMNPGKMFAK DTRKRVVVER
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