ID Q9RTM9_DEIRA Unreviewed; 478 AA.
AC Q9RTM9;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:AAF11289.1};
GN OrderedLocusNames=DR_1731 {ECO:0000313|EMBL:AAF11289.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11289.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF11289.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AE000513; AAF11289.1; -; Genomic_DNA.
DR PIR; E75359; E75359.
DR RefSeq; NP_295454.1; NC_001263.1.
DR RefSeq; WP_010888366.1; NZ_JMLF01000023.1.
DR AlphaFoldDB; Q9RTM9; -.
DR STRING; 243230.DR_1731; -.
DR PaxDb; 243230-DR_1731; -.
DR EnsemblBacteria; AAF11289; AAF11289; DR_1731.
DR GeneID; 69517969; -.
DR KEGG; dra:DR_1731; -.
DR PATRIC; fig|243230.17.peg.1940; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_0; -.
DR InParanoid; Q9RTM9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000002524; Chromosome I.
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:UP000002524}.
FT DOMAIN 57..229
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 50963 MW; 99191D7C8F769C33 CRC64;
MTPEKLALTT NSRARKPRSD GTPDNPLAAE LTRTLGHKKV LHHLSERLNY RYDAIQFGVT
PLAVVLPEST ADVVAAVKAA KAAGVPIVGR GAASGLSGGV TPLQESLVIS FTRMTGLHIF
PERREAVAQP GVVTLKVTEA AKPHGLMYPP DPASFRTSTI GGNLGENAGG PMCFKYGVTG
DYVRALEFVD VDGDVHRLTR DCYDLAGLLI GSEGTLGLIT EATLRLIPPP KFTRTLMSHF
AEVGQAAEAV SSAIAAGAVP SKLEFMDRAC VGAVEDYLHL GLPRDADAVL LVDTDGDDAE
IVAAELELVA QACAAAGGTV RRAANDAEAD ALWRARRSIS PSLGRIRPQR MNEDIVVPRS
ALPDVVREIR ALGDASPFHL VQFGHIGDGN LHPNIMFDPR TEDTHAVHDL AHKIALVAIR
HGGVLSGEHG IGTMKRDFMR DAVDPVTLNV LRDVKRALDP ANGLNPGKIL PDLLMDER
//
