ID R9LZJ5_9FIRM Unreviewed; 468 AA.
AC R9LZJ5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EOS61102.1};
GN ORFNames=C815_00667 {ECO:0000313|EMBL:EOS61102.1};
OS Firmicutes bacterium M10-2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1235796 {ECO:0000313|EMBL:EOS61102.1, ECO:0000313|Proteomes:UP000014154};
RN [1] {ECO:0000313|EMBL:EOS61102.1, ECO:0000313|Proteomes:UP000014154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M10-2 {ECO:0000313|EMBL:EOS61102.1,
RC ECO:0000313|Proteomes:UP000014154};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Firmicutes bacterium M10-2.";
RL Submitted (APR-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:EOS61102.1}.
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DR EMBL; ASTB01000020; EOS61102.1; -; Genomic_DNA.
DR AlphaFoldDB; R9LZJ5; -.
DR STRING; 1235796.C815_00667; -.
DR PATRIC; fig|1235796.3.peg.667; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000014154; 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;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000014154}.
FT DOMAIN 43..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 51827 MW; ADB92CA440F053AC CRC64;
MTEYKRVDAN DIETIRRMIN DDTRVIYDTD ISEDYGHDEL GGIFSLPDVV VKILSAKEAS
DIMKYANENH ISVTPRGAGT GLVGSSVPLE HGIMIDTSLM NHILELDDEN LTIDVEPGVL
LMDLAAYVED NDFFYPPDPG EKSATIGGNI STNAGGMRAV KYGVTRDFVR ALEVVLPNGD
IVNFGGKVVK NSSGYDLKDL MIGSEGTLGL ITKATLKLLP KPKKVISLLI PFPSLKDAIN
TVPLIIKSKS IPTAIEFMQR EVIEDAEEYL GKPFPDKQSD AYLLLKFDGN SQEEIEKAYD
TVAKLCLEQG AVDVLISDTE EREESIWKAR GAFLEAIKGS TTYMDEVDMV VPRNRVNEMV
EYLHDLQPEV GLRIKSFGHA GDGNLHAYML KDNLSDEEWE LRVSAAMEKV YAKARDLKGQ
VSGEHGIGYA KKPYLRESLP IDSLELMNGI KSVFDPNNIL NPHKIAQR
//
