ID D1C9L6_SPHTD Unreviewed; 550 AA.
AC D1C9L6;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ACZ40509.1};
GN OrderedLocusNames=Sthe_3109 {ECO:0000313|EMBL:ACZ40509.1};
OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ40509.1, 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 2 of Sphaerobacter thermophilus DSM 20745.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ40509.1, 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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; CP001824; ACZ40509.1; -; Genomic_DNA.
DR RefSeq; WP_012873544.1; NC_013524.1.
DR AlphaFoldDB; D1C9L6; -.
DR STRING; 479434.Sthe_3109; -.
DR KEGG; sti:Sthe_3109; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_0; -.
DR InParanoid; D1C9L6; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000002027; Chromosome 2.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
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; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002027}.
FT DOMAIN 20..349
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..526
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 550 AA; 60926 MW; CBD8F0B2DC04C877 CRC64;
MAGAETPRRI PDEIGRRTFD LIVVGAGVNG AGIARDAAMR GLSVLLIEKE DIGSGTTDSS
TRLIHGGLRY LEYYEFGLVR ESLREREILL HIAPHLVRPL GFLIPIYGDM KRGPGMIRLG
MIAYDVLSYD KSLPRHQMLD REATLRREPG LDPDGLVGAA FYYDAQVPYP ERLTVENALS
ARDHGAVVLT YAKVDRLLIE NDQVVGVHFT DMLNGGEHEA RGRLVVNAAG PWVDEVLRGI
GAPRMIGGTK GTHIVVDPFP GAPTEALYVE ARADGRPYFI VPWNGRYLIG TTDTRYNDDL
DRVFPTEDEI DYLISETNRV LPSAGLTRDD VLYAYAGVRP LPYKEEGSPG SITRSHIIYD
HARHEPQLGG LISIIGGKIT TYRSLAEETV DLVFEKLNRP APPCRTGRIP LPGGNTRDWE
AFAANFVATS GLDEPVAKRL LRIYGTFAPT VRRLAGDDAR LLAPLGPNSL AIGAEIPYAV
RWELAQTLID VFMRRAMVGW DPDVGRDEIE TAGEIARDYL GWDDARVQRE VADYRAYTER
FRPREPAVAS
//