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Database: UniProt
Entry: E8PMZ4_THESS
LinkDB: E8PMZ4_THESS
Original site: E8PMZ4_THESS 
ID   E8PMZ4_THESS            Unreviewed;       455 AA.
AC   E8PMZ4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Oxidase, FAD-binding protein {ECO:0000313|EMBL:ADW21345.1};
GN   OrderedLocusNames=TSC_c07180 {ECO:0000313|EMBL:ADW21345.1};
OS   Thermus scotoductus (strain ATCC 700910 / SA-01).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21345.1, ECO:0000313|Proteomes:UP000008087};
RN   [1] {ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA   Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA   Gottschalk G., van Heerden E., Litthauer D.;
RT   "The genome sequence of Thermus scotoductus SA-01.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADW21345.1, ECO:0000313|Proteomes:UP000008087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX   PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA   Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA   Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA   Berenguer J., van Heerden E., Litthauer D.;
RT   "Sequence of the hyperplastic genome of the naturally competent Thermus
RT   scotoductus SA-01.";
RL   BMC Genomics 12:577-577(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001962; ADW21345.1; -; Genomic_DNA.
DR   RefSeq; WP_015716626.1; NC_014974.1.
DR   AlphaFoldDB; E8PMZ4; -.
DR   STRING; 743525.TSC_c07180; -.
DR   KEGG; tsc:TSC_c07180; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_0; -.
DR   Proteomes; UP000008087; 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; 3.30.70.2740; -; 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; 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          42..214
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   455 AA;  49392 MW;  639AC7552D206107 CRC64;
     MGVRKLPSLA EAVRSELRIL FGPRVLLSRS EKGVYRYDAI LVGPEPLAVV LPESREEVQA
     LVRLARKHGL SLVARGAGSG LSGGAVPEEG ALVVAFTRMT RLELDPRGRT AWAEPGVTTA
     RISEEARLYG LFYPPDPASW RTSTLGGNLG ENAGGPLCFK YGVTGDYVLE LEFVDAWGEV
     HRLGRQAYDL PGLLIGSEGT LGLITGVRVR LLPLPRYRAT LMAAFPEVGA LAQAVSQAIA
     RGAVPARLEF LDPICVNAVE DYLGMGLPRG HALLLAETDG DDLEVVQEEL SLVEETAASL
     GARVQRARDE REAEALWRAR RSVSPALGRI RPKRVNEDIA VPRSHLPQVV QEISALGEAY
     GLVVAQFGHI GDGNLHPNIL FDPRRESEER VWELAHEIAR VALRHGGVLS GEHGIGLMKR
     EFMREAVDEA TLEAFRTIKA TLDPEGILNP GKLLP
//
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