ID   G8LQP9_9FLAO            Unreviewed;       532 AA.
AC   G8LQP9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AEU09467.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:AEU09467.1};
GN   Name=glpD {ECO:0000313|EMBL:AEU09467.1};
GN   ORFNames=BLBCPU_426 {ECO:0000313|EMBL:AEU09467.1};
OS   Blattabacterium sp. (Cryptocercus punctulatus) str. Cpu.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1075399 {ECO:0000313|EMBL:AEU09467.1, ECO:0000313|Proteomes:UP000007112};
RN   [1] {ECO:0000313|EMBL:AEU09467.1, ECO:0000313|Proteomes:UP000007112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cpu {ECO:0000313|EMBL:AEU09467.1,
RC   ECO:0000313|Proteomes:UP000007112};
RX   PubMed=22094859;
RA   Neef A., Latorre A., Pereto J., Silva F.J., Pignatelli M., Moya A.;
RT   "Genome economization in the endosymbiont of the wood roach Cryptocercus
RT   punctulatus due to drastic loss of amino acid synthesis capabilities.";
RL   Genome Biol. Evol. 3:1437-1448(2011).
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; CP003015; AEU09467.1; -; Genomic_DNA.
DR   RefSeq; WP_014246355.1; NC_016621.1.
DR   AlphaFoldDB; G8LQP9; -.
DR   STRING; 1075399.BLBCPU_426; -.
DR   KEGG; bcp:BLBCPU_426; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_4_1_10; -.
DR   Proteomes; UP000007112; 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:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:AEU09467.1}.
FT   DOMAIN          21..379
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          390..512
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   532 AA;  61092 MW;  37A740FF42852B2D CRC64;
     MKGFLNRDRF LRILENINIW DIIIVGGGAT GLGIALDSAS RGFKTLLLEQ NDFSKGTSSR
     STKLIHGGIR YLAQGNIKLV YEALQERGYL LKNAPHLVKK KRFIIPIFNW KMGILYWTGL
     KIYEWLSGSL SFGNSQFLSK NEILKMFPEI RSNNLKGGIL YYDGQFDDAR LAIDLAQTCV
     QQGGVLLNYF KVKNLIKKIE NKIIGVIAYD LETKKKYSIY SKIVINATGV FSDTILKMDD
     STSTILIKPS QGTHIVLKKS FFSSSDAIVI PKTSDGRILF SIPWYDHVLV GTTDTFLEKS
     VLEPKPLEKE IDFILQTFNQ YFLYNPNKKD ILSAFSGLRP LFVPPNLSYS STKDISRSHK
     LMMSPSGLIT IIGGKWTTYR KMAEETVNKA IEIGKLKKVS SITKNLKIFG YRTDFYSCKN
     YNNWGDKYGE EEIHIQKLIE ENPLWGDPLI YQYPYHCTKA EVIWMVRYEM ARTIEDVLAR
     RFRLLFLNAK IAIDIAPIIA SLMAKELYRD KEWEESQIAS FKELAMQYYY PF
//