ID   Q2LR85_SYNAS            Unreviewed;       510 AA.
AC   Q2LR85;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ABC76597.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:ABC76597.1};
GN   ORFNames=SYN_02446 {ECO:0000313|EMBL:ABC76597.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC76597.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC76597.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC76597.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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DR   EMBL; CP000252; ABC76597.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LR85; -.
DR   STRING; 56780.SYN_02446; -.
DR   KEGG; sat:SYN_02446; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_024775_3_1_7; -.
DR   InParanoid; Q2LR85; -.
DR   Proteomes; UP000001933; Chromosome.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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; 1.
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   PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1.
DR   PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABC76597.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT   DOMAIN          30..386
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          432..485
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   510 AA;  55597 MW;  96A2A2FF78425D69 CRC64;
     MCPTGNRMNE IVKERTSKGI FRIDMTNFYD VIIIGAGVVG NAIARELSRF DIKAAVIERE
     LDVGGGTSSR NSGVVHSGIH YKPGTLRAKL NVQGNAMMGN LCKELKVKIE YLGKLTVAQD
     ETDVETLHSL KAQGDANGVP GLAILNKQQM EKLQPGIGGI MALHSPSTGI ICPYGLTIAL
     AENACANGVH FYLGQEVTAI SRTEKGFEVK TTSGERFESR VLINSAGLYS DAICRMLGID
     EYRIYPCRGE YLILDKRLAG TLSLLVYPAP HKGGAGLGIH LTNTVDGNIL IGPSNEYVDE
     ADDYACTAEI LSLLKKEGHD LLPGISAADF IRNFSGLRAK QAPPSEGGFR DFVIESRKDI
     PGFINLVGIE SPGLTSAPAI GLMVRDMVEE LLPLPFKASF IAEREGRAGF FYELSPEERA
     DLVAENPDYG EVVCRCEQIT RKEVLDAIQN PLGVKTINGI KYRSRAMMGR CQGGFCLPRI
     VQILEKEFGY KPEDYLLQHA HSPLFAGRVR
//