ID   A7ZRK7_ECO24            Unreviewed;       496 AA.
AC   A7ZRK7;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:ABV20944.1};
GN   Name=glcD {ECO:0000313|EMBL:ABV20944.1};
GN   OrderedLocusNames=EcE24377A_3439 {ECO:0000313|EMBL:ABV20944.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV20944.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000800; ABV20944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7ZRK7; -.
DR   KEGG; ecw:EcE24377A_3439; -.
DR   HOGENOM; CLU_017779_9_2_6; -.
DR   Proteomes; UP000001122; 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; 3.30.70.2190; -; 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; 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:SF1; 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:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122}.
FT   DOMAIN          49..227
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   496 AA;  53498 MW;  50335F9AE4F5281C CRC64;
     MYEERLDGAL PDVDRTSVLM ALREHVPGLE ILHTDEEIIP YECDGLSAYR TRPLLVVLPK
     QMEQVTAILA VCHRLRVPVV TRGAGTGLSG GALPLEKGVL LVMARFKEIL DINPVGRRAR
     VQPGVRNLAI SQAVAPHNLY YAPDPSSQIA CSIGGNVAEN AGGVHCLKYG LTVHNLLKIE
     VQTLDGEALT LGSDALDSPG FDLLALFTGS EGMLGVTTEV TVKLLPKPPV ARVLLASFDS
     VEKAGLAVGD IIANGIIPGG LEMMDNLSIR AAEDFIHAGY PVDAEAILLC ELDGVESDVQ
     EDCERVNDIL LKAGATDVRL AQDEAERVRF WAGRKNAFPA VGRISPDYYC MDGTIPRRAL
     PGVLEGIARL SQQYDLRVAN VFHAGDGNMH PLILFDANEP GEFARAEELG GKILELCVEV
     GGSISGEHGI GREKINQMCA QFNSDEITTF HAVKAAFDPD GLLNPGKNIP TLHRCAEFGA
     MHVHHGHLPF PELERF
//