ID D1C788_SPHTD Unreviewed; 377 AA.
AC D1C788;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ACZ39734.1};
GN OrderedLocusNames=Sthe_2313 {ECO:0000313|EMBL:ACZ39734.1};
OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ39734.1, ECO:0000313|Proteomes:UP000002027};
RN [1] {ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA Goeker M., Klenk H.P., Eisen J.A.;
RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ39734.1, ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP001823; ACZ39734.1; -; Genomic_DNA.
DR RefSeq; WP_012872775.1; NC_013523.1.
DR AlphaFoldDB; D1C788; -.
DR STRING; 479434.Sthe_2313; -.
DR KEGG; sti:Sthe_2313; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_0; -.
DR InParanoid; D1C788; -.
DR OrthoDB; 9794226at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002027; Chromosome 1.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012727; Gly_oxidase_ThiO.
DR NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002027}.
FT DOMAIN 11..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 377 AA; 38607 MW; AD9AF04863DEFAC1 CRC64;
MSGMGYEAVE VAIVGGGIIG CAIAYELARK GHRVAVVERG AIGGEASGAS AGIIAPPSNK
DTPAVRVELT ARSLSAYPWL VAALQDETGF DVGYRQWGAL LVASNENDHA RLRALLSWQE
DLGFDSEWVE PAELRHLEPA LPEGLLGGML ANDAGSVNVR RLTRALAAAA ARRGALVLEH
TPALGVATSG DLATGVRLAD GTLPAAQVVL AAGAWTARFG LELGQALPTV PVKGQMLALG
GLLHPPRTII GGAGGYLVPW TDGTVGVAAT EEEAGFDTRV TPAGLRALVG LIEALAPGLL
DGEVVATWAG LRPGTPDREP IVGLVPGYDN LWVASGHFRT GVQLAIGTAE VLVASLLSGA
PDPLLAPLSP ARFAQAV
//
