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Database: UniProt
Entry: D1C9L6_SPHTD
LinkDB: D1C9L6_SPHTD
Original site: D1C9L6_SPHTD 
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}.
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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
//
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