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Database: UniProt
Entry: M7T0R9_HELPX
LinkDB: M7T0R9_HELPX
Original site: M7T0R9_HELPX 
ID   M7T0R9_HELPX            Unreviewed;       459 AA.
AC   M7T0R9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EMR60315.1};
GN   Name=glcD {ECO:0000313|EMBL:EMR60315.1};
GN   ORFNames=HPCPY1662_0855 {ECO:0000313|EMBL:EMR60315.1};
OS   Helicobacter pylori CPY1662.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992015 {ECO:0000313|EMBL:EMR60315.1, ECO:0000313|Proteomes:UP000012020};
RN   [1] {ECO:0000313|EMBL:EMR60315.1, ECO:0000313|Proteomes:UP000012020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPY1662 {ECO:0000313|EMBL:EMR60315.1,
RC   ECO:0000313|Proteomes:UP000012020};
RA   Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA   Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT   "Comparitive Sequence Analysis of H. pylori Isolates.";
RL   Submitted (FEB-2013) 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:EMR60315.1}.
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DR   EMBL; AOTT01000005; EMR60315.1; -; Genomic_DNA.
DR   RefSeq; WP_001919700.1; NZ_AOTT01000005.1.
DR   AlphaFoldDB; M7T0R9; -.
DR   PATRIC; fig|992015.3.peg.847; -.
DR   Proteomes; UP000012020; 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;
FT   DOMAIN          36..216
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   459 AA;  50497 MW;  0A3F2A43AB74020D CRC64;
     MLEKQHIQYF KNLIGGEDFF TDLAHLNAYC YDATKERHLP SGVIFPKNEQ EISQILKYCN
     EHRIIVVPRG AGSGFTGGAL SVSGGLVLSV EKHLDKILEI DTKNLIARVE PGVINKHFQN
     EVEKLNLFYP PDPASENQST LGGNVAENAG GMRAAKYGIT KDYVMAMRVV LANGEIIRAG
     KKTIKDVAGF NVAGLMIASE GCLGVISEIT LKLLAKPPLK QSAMGVFNHI EDAMNAVYKT
     MSSGVTPVAM EFLDNLSIKA VEERFSKGLP KDAGAILITQ VDGVVKEQIA WQLNEIEKHF
     KANGCVGFKI AQNEQEEQDL WFSRRNASQS ISVYGKKKLN EDVTVPRASL PSLLQEVAKI
     SQKYGFKIPC FGHTGDGNVH VNIMLEDPNR DLEKGHQAME EIFQAAISLE GTLSGEHGIG
     LSKAKFMPLA FNHSEMELFR NIKKALDPNN ILNPFKMGL
//
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