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
//