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Database: UniProt
Entry: A2S5F7_BURM9
LinkDB: A2S5F7_BURM9
Original site: A2S5F7_BURM9 
ID   A2S5F7_BURM9            Unreviewed;       362 AA.
AC   A2S5F7;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Glycolate oxidase, GlcE subunit {ECO:0000313|EMBL:ABN01251.1};
GN   Name=glcE {ECO:0000313|EMBL:ABN01251.1};
GN   OrderedLocusNames=BMA10229_A1191 {ECO:0000313|EMBL:ABN01251.1};
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022 {ECO:0000313|EMBL:ABN01251.1, ECO:0000313|Proteomes:UP000002283};
RN   [1] {ECO:0000313|EMBL:ABN01251.1, ECO:0000313|Proteomes:UP000002283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABN01251.1,
RC   ECO:0000313|Proteomes:UP000002283};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (JAN-2007) 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; CP000546; ABN01251.1; -; Genomic_DNA.
DR   RefSeq; WP_004194396.1; NC_008836.1.
DR   AlphaFoldDB; A2S5F7; -.
DR   GeneID; 56593741; -.
DR   KEGG; bml:BMA10229_A1191; -.
DR   HOGENOM; CLU_017779_0_0_4; -.
DR   Proteomes; UP000002283; Chromosome I.
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   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   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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;
FT   DOMAIN          1..172
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   362 AA;  38825 MW;  B86254EE78A082B4 CRC64;
     MEEDDIVAGW AARIRDAAAS GRALRIRGGG TKDWYGQALD GEILDTRAHH GIVSYDPAEL
     VVTARAGTSL AELEATLAER GQMLPFEPPH FGRGATLGGA VAAGLAGPRR ATTGAPRDFV
     LGVAILNGRG DRLRFGGQVV KNVAGYDVSR LMAGSLGTLG LMLELSVKVL PVPAAELTLK
     FDMSATDAVR KLNEWAGRPF PLSASAWRYG TLVLRLSGAE AAVKSAKTVL GGEAVDAVEA
     ERFWEGVREQ NDPFFSSLAP GHALWRLSLP SITEPMHLPG TQMMEWGGAQ RWWITDADAQ
     TVRMSAKQAG GHATLFRASE SYDRSAGVFT PLPAPLMKIH RGLKTAFDPA RIFNRGRLYP
     DL
//
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