ID   E1R9C9_SEDSS            Unreviewed;       402 AA.
AC   E1R9C9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ADK83098.1};
GN   OrderedLocusNames=Spirs_4014 {ECO:0000313|EMBL:ADK83098.1};
OS   Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS   (Spirochaeta smaragdinae).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Sediminispirochaeta.
OX   NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK83098.1, ECO:0000313|Proteomes:UP000002318};
RN   [1] {ECO:0000313|EMBL:ADK83098.1, ECO:0000313|Proteomes:UP000002318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC   {ECO:0000313|Proteomes:UP000002318};
RX   PubMed=21304743; DOI=10.4056/sigs.1143106;
RA   Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA   Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA   Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA   Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT   4228).";
RL   Stand. Genomic Sci. 3:136-144(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; CP002116; ADK83098.1; -; Genomic_DNA.
DR   RefSeq; WP_013256555.1; NC_014364.1.
DR   AlphaFoldDB; E1R9C9; -.
DR   STRING; 573413.Spirs_4014; -.
DR   KEGG; ssm:Spirs_4014; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_0_1_12; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000002318; Chromosome.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985:SF36; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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:UP000002318}.
FT   DOMAIN          5..360
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   402 AA;  43904 MW;  AC994F61372630D8 CRC64;
     MDQKRIVIIG GGGTGAAVAR DLGLRGYSVL LLERDEFTGG TTGRHHGQLH SGARYAMGDR
     EIARECLRET EILRRIAPDL IEDNGGLFVA VTDEEADYAS QFRGACAEAD IRTELISGKQ
     AREIEPALSQ AVRCAVTVPA DGSFDAWRLP AAFFASAMEH GAKLFRYANV IGIETSGGSV
     SAVRVLDRMT NKEHKIEADV VINAGGPWVG KIAALAGIDM EVTPSPGTMV AVQGRFADKV
     ISRLRPPNDG DIIVPQRSFS IIGTTQWITD DPDRIETPPE EIPRMLHLAD EMIPAFSSAP
     FRAAWSAARP LAKRAHEVKA ARALSRDFDC VHHENEGAAG LFSLVGGKAT VLRAMGEIVA
     DQVCSYIGEE RQGSSDQEKL PPYRRFYRFL KEQESERKFS WI
//