ID J0IW00_HELPX Unreviewed; 459 AA.
AC J0IW00;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EJB29437.1};
GN Name=glcD {ECO:0000313|EMBL:EJB29437.1};
GN ORFNames=HPNQ4200_0573 {ECO:0000313|EMBL:EJB29437.1};
OS Helicobacter pylori NQ4200.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992024 {ECO:0000313|EMBL:EJB29437.1, ECO:0000313|Proteomes:UP000003358};
RN [1] {ECO:0000313|EMBL:EJB29437.1, ECO:0000313|Proteomes:UP000003358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NQ4200 {ECO:0000313|EMBL:EJB29437.1,
RC ECO:0000313|Proteomes:UP000003358};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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:EJB29437.1}.
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DR EMBL; AKNS01000005; EJB29437.1; -; Genomic_DNA.
DR RefSeq; WP_000890686.1; NZ_AKNS01000005.1.
DR AlphaFoldDB; J0IW00; -.
DR PATRIC; fig|992024.3.peg.547; -.
DR Proteomes; UP000003358; 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; 50580 MW; 21489824E7C1F03F CRC64;
MLEKQHIQYF KNLVGGEDFF TDLAHLNAYC YDATKERHLP SGVIFPKNER EISQILKYCN
EHRLIVVPRG AGSGFTGGAL SVSGGLVLSV EKHLDKILEI DTKNLIARVE PGVINKHFQN
EVEKLDLFYP PDPASENQST LGGNVAENAG GMRAAKYGIT KDYVMALRVV LANGEIIRAG
KKTIKDVAGF NIAGLMIASE GCLGVISEIT LKLLAKPPLK QSAMGVFNHI EDAMNAVYKT
MSSGVTPVAM EFLDNLSIKA VEERFSKGLP KDAGAILITQ VDGVVKEQIA WQLNEIEKHF
KANGCVDFKI AQNEQEEQDL WFSRRNASQS ISVYGKKKLN EDVTVPRASL PSLLQEVAKI
SQKYGFKIPC FGHTGDGNVH VNIMLEDPKR DLEKGHKAME EIFQAAISLE GTLSGEHGIG
LSKAKFMPLA FNHSEMELFR NIKKALDPNN ILNPFKMGL
//
