ID Q47NJ0_THEFY Unreviewed; 433 AA.
AC Q47NJ0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=FAD-linked oxidoreductase {ECO:0000313|EMBL:AAZ55979.1};
GN OrderedLocusNames=Tfu_1946 {ECO:0000313|EMBL:AAZ55979.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55979.1};
RN [1] {ECO:0000313|EMBL:AAZ55979.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ55979.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005147}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000088; AAZ55979.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47NJ0; -.
DR STRING; 269800.Tfu_1946; -.
DR KEGG; tfu:Tfu_1946; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_003896_4_3_11; -.
DR OrthoDB; 9800184at2; -.
DR UniPathway; UPA00132; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_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; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR01679; bact_FAD_ox; 1.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 4: Predicted;
KW Ascorbate biosynthesis {ECO:0000256|ARBA:ARBA00022644};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 13..183
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 433 AA; 47970 MW; FBB66EC275B8030B CRC64;
MTRTLWHNWA DTCRITPTRI ATPTSTAEVV AEVRAAAAAG SRIRMVGSGH SFTDIAATDG
TLLSPAALAS VRSVDLAAGR ATVEAGMRLC DLNETLAAHG AALTNMGDIA VQTLAGATQT
GTHGTGRASA SLAAQIQQLE LVLADGSVVT CSRDEDPDLF DAARAGLGAF GVVTAITMAV
EPAFLLHARE TPMPLGEVLE RLEELRTTND HFEFFWFPHT ERTITKRNNR VPGPARPLSA
FRAWLDDEFL SNSVFEVVNR MARRLPRLIP AINQISARAL TAREYVDVSY RVFTSPRRVK
FVEMEYAIPV EHLPDVLHDM RAVFASSRHR ISFPVEVRFA PADDVWLSPG YGRESAYVAV
HVYQGCPWQE YFADLEAIFT AAAGRPHWGK MHTRTLSYLD KVYPRLRDAL EVRERVDPHR
RFTNAYLDRV WGE
//
