ID B1Y8X9_PYRNV Unreviewed; 444 AA.
AC B1Y8X9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACB40208.1};
GN OrderedLocusNames=Tneu_1281 {ECO:0000313|EMBL:ACB40208.1};
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157 {ECO:0000313|EMBL:ACB40208.1, ECO:0000313|Proteomes:UP000001694};
RN [1] {ECO:0000313|EMBL:ACB40208.1, ECO:0000313|Proteomes:UP000001694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta
RC {ECO:0000313|Proteomes:UP000001694};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001014; ACB40208.1; -; Genomic_DNA.
DR AlphaFoldDB; B1Y8X9; -.
DR STRING; 444157.Tneu_1281; -.
DR KEGG; tne:Tneu_1281; -.
DR eggNOG; arCOG00337; Archaea.
DR HOGENOM; CLU_017779_9_2_2; -.
DR OrthoDB; 26910at2157; -.
DR Proteomes; UP000001694; 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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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 33..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 444 AA; 47705 MW; 6108470A49F06CD6 CRC64;
MDLGWLRRRF GDRFVEDGAV AALYVRDASF MEFSRSAIGV VFPEEEEEVV ELVRWAVENR
TPLFPQGCAT SLSGNAAATA PGLVVSFERM AKVEVDPVDG VAVVGPGVKL EELNLALARY
GLFFPVDPGS VKSATVGGAI ANGAGGMRGA KYGTMKDWVL GLRVVTGRGD VLRLGCRTYK
CRNGYDLVRL FVGSEGTLGL ITEATLKLAP VPESAAAVLA YYRDVETLVE DVVRVRASRV
WPLFAEFLDA PTSALVGLEE KNALFIGVDV NAGAEEKVIN KLRGLLRGEV ALEAAGWEAS
MRLLEPRRRL FYGQIKAAGG GVLVIEDVAV PISKLPDAVR GLKAAAARHG VPLLLGGHVG
DGNIHPATWY RREEGPARVE NFIRDMAELV AKLGGTISAE HGIGVLKREL AKAELGEAAL
SYMRELKRLF DPYNVLNPGK VLPG
//
