ID F7L0P8_9FUSO Unreviewed; 475 AA.
AC F7L0P8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EGN66740.1};
GN ORFNames=HMPREF0401_01419 {ECO:0000313|EMBL:EGN66740.1};
OS Fusobacterium animalis 11_3_2.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=457403 {ECO:0000313|EMBL:EGN66740.1, ECO:0000313|Proteomes:UP000004160};
RN [1] {ECO:0000313|EMBL:EGN66740.1, ECO:0000313|Proteomes:UP000004160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11_3_2 {ECO:0000313|EMBL:EGN66740.1,
RC ECO:0000313|Proteomes:UP000004160};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., White A.P.,
RA Crowley S., Surette M., Strauss J.C., Ambrose C.E., Allen-Vercoe E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 11_3_2.";
RL Submitted (MAY-2011) 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:EGN66740.1}.
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DR EMBL; ACUO01000020; EGN66740.1; -; Genomic_DNA.
DR RefSeq; WP_005910602.1; NZ_GL945392.1.
DR AlphaFoldDB; F7L0P8; -.
DR GeneID; 79809062; -.
DR PATRIC; fig|457403.8.peg.1432; -.
DR HOGENOM; CLU_017779_9_2_0; -.
DR Proteomes; UP000004160; Unassembled WGS sequence.
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;
FT DOMAIN 43..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 475 AA; 52257 MW; 45C41B2EB2CB4596 CRC64;
MGNHIYNKVS EDLVEKFKKI VPGKVYTKDE INKDFFHDEM PIYGEGEPEV VIDVTTTEAI
SEIMKLCYEN NIPVTPRGAG TGLTGAAVAV TGGVMLNMTK MNKILGYDYE NFVVKVEPGV
LLNDLAEDAL KQGLLYPPDP GEKFATLGGN VSTNAGGMRA VKYGTTRDYV RAMTVVLPTG
EIIKLGATVS KTSTGYSLLN LMIGSEGTLG VITELTLKLI PAPKETISLI IPYENLDECI
ATVPKFFMNH LQPQALEFME REIVLASERY IGKSVFPQKL EGVDIGAYLL VTFDGNNMEE
LEEITERASE VVLEAGALDV LVADTPAKKK DAWAARSSFL EAIEAETKLL DECDVVVPVN
QIAPYLHYVN ETGKKYDFAV KSFGHAGDGN LHIYACSNDM EMGEFKRQVE EFLMDIYKKA
SELGGLISGE HGIGYGKMQF LADFSGEVNM RLMRGIKEVF DPKMILNPNK VCYKA
//
