ID   Q67MX2_SYMTH            Unreviewed;       545 AA.
AC   Q67MX2;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029};
DE            EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029};
GN   OrderedLocusNames=STH1986 {ECO:0000313|EMBL:BAD40971.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD40971.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD40971.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000153};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005157}.
CC   -!- SUBUNIT: Composed of a catalytic GlpA/B dimer and of membrane bound
CC       GlpC. {ECO:0000256|ARBA:ARBA00011331}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; AP006840; BAD40971.1; -; Genomic_DNA.
DR   RefSeq; WP_011196113.1; NC_006177.1.
DR   AlphaFoldDB; Q67MX2; -.
DR   STRING; 292459.STH1986; -.
DR   KEGG; sth:STH1986; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_0_1_9; -.
DR   OrthoDB; 9801699at2; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000417; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding 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; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   InterPro; IPR017752; G3P_DH_GlpA_su.
DR   NCBIfam; TIGR03377; glycerol3P_GlpA; 1.
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   Pfam; PF04324; Fer2_BFD; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000417}.
FT   DOMAIN          4..350
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          424..476
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   545 AA;  57551 MW;  090D4B0D8729D666 CRC64;
     MLQAIVIGGG ATGAGILRDL ALRSVRAALV EQGDLVHGTS SRYHGLLHSG GRYAVKDPES
     ARECAVENQI VRRIAPFAVE PCGGLFVRLE QDDPAYARRW VAACREAGIP VEEVDPDRLR
     REEPLLAGSV CEAWAVPDAA VDGWRLVRGN VAAAEARGAR VFTYRRVVGL LMDGRRVAGV
     RLLNLATGEE ERLEAELVIN AAGAWAGQIA AMAGAPLDVV ADRGVLLVYH GRLTSRVVNR
     LRKPGNGDIF VPAGSVTLLG TTATPVPDPD DISVPPEEVE ELKRLGAEML PMAATARILR
     AFAGVRPLFG SGPGGNTREI SRGFAVIDHE VEHGVPGLLS VVGGKLTTYR MMAEKAVDVA
     AARLGVTVPC RTAEEPILPP PDPDAVRRLV HLVGRDLAQA VADRHPATLP QIAEAIARPG
     GRQVVCECEQ VTAGELVGTA RELGAPSLGD LRRRTRLGMG TCQGGFCGYR AALLLAREGI
     VAPEQVPALL ARFQAERWRG VRGGLGGLEL RAAELNYALA RAQLAMEPAA GTADAVAQMG
     GAGHD
//