ID A7I3P7_CAMHC Unreviewed; 460 AA.
AC A7I3P7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:ABS51565.1};
GN Name=glcD {ECO:0000313|EMBL:ABS51565.1};
GN OrderedLocusNames=CHAB381_1615 {ECO:0000313|EMBL:ABS51565.1};
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107 {ECO:0000313|EMBL:ABS51565.1, ECO:0000313|Proteomes:UP000002407};
RN [1] {ECO:0000313|Proteomes:UP000002407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A
RC {ECO:0000313|Proteomes:UP000002407};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-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; CP000776; ABS51565.1; -; Genomic_DNA.
DR RefSeq; WP_012109443.1; NC_009714.1.
DR AlphaFoldDB; A7I3P7; -.
DR STRING; 360107.CHAB381_1615; -.
DR KEGG; cha:CHAB381_1615; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_7; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000002407; Chromosome.
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 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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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 Reference proteome {ECO:0000313|Proteomes:UP000002407}.
FT DOMAIN 35..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 460 AA; 49865 MW; 0A1D2A001D628FB0 CRC64;
MNAKHINFLK NSVGADNVYD DDAHLTAYCY DATKNRFKPD AVIFPRNEED VSKILKYCNE
NKIAVVPRGA GSGFTGGSLP ANGGIILAFE KHMNKILEID MQNLVAVVQP GVINKDLQKA
AEAKGLFYPP DPASQDYCTI GGNVSENAGG MRAAKYGITK DYVMALRAVL PNGEIIRAGK
RTIKDVAGYN TAGILIASEG TLAVITEITL KLIAKPKMSE TAMGIFDSVD EAMNAVYKTM
AGGVVPVAME FLDNLSIRAV EEKFHKGLSV DAGAILITEV DGNSKDDLSR QLDLIEAAFK
ENGCTNFKRA KDKQESDDIW FARRNVSQAI TIYGNKKLNE DITVPRSKLP ELLKKIGEVA
QEHALKVPCF GHTGDGNVHT NVMVEDGNDK AQLENGQKAI EKIFKIAVDL GGTLSGEHGI
GLSKAPFMHL AFSEAEMNLF RTVKKAFDPN NILNPGKMGL
//
