ID   E6TQU4_EVAC2            Unreviewed;       531 AA.
AC   E6TQU4;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Bcell_3477 {ECO:0000313|EMBL:ADU31719.1};
OS   Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM
OS   9156 / N-4) (Bacillus cellulosilyticus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX   NCBI_TaxID=649639 {ECO:0000313|EMBL:ADU31719.1, ECO:0000313|Proteomes:UP000001401};
RN   [1] {ECO:0000313|EMBL:ADU31719.1, ECO:0000313|Proteomes:UP000001401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4
RC   {ECO:0000313|Proteomes:UP000001401};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Brumm P., Mead D.,
RA   Woyke T.;
RT   "Complete sequence of Bacillus cellulosilyticus DSM 2522.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; CP002394; ADU31719.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6TQU4; -.
DR   STRING; 649639.Bcell_3477; -.
DR   KEGG; bco:Bcell_3477; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000001401; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001401}.
FT   DOMAIN          27..352
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          410..518
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   531 AA;  60189 MW;  23CC4C359A98A61E CRC64;
     MFVIMVRTFS QQNRQHFLNE MSSGELDLLI IGGGITGCGI ALDAANRGLK VGLLEMQDFA
     AGTSSRSTKL IHGGLRYLKQ LEIKLVKEVG RERAILHENA PHIVKPEPML LPLIKNGSFG
     KISTSFGLYV YDRLAQVKKQ ERRKMLSKEE ALKKEPLLRD EGLKGAGLYY EYQTDDARLT
     LEVVKTAFSL GANAVNYCGV EELIYNESGK VNGGVAFDSI SGKTHHIYAK KIVNATGPWV
     DSIRKQDRSL TGKHLHVTKG VHIVVDQKRF PLRQAMYFDV EDGRMIFAIP RADKTYIGTT
     DTTYRGDLAD PTVSIEDKNY LIKATNNMFP SINISVDDIE SSWAGLRPLI HEEGKSPSDL
     SRKDEIFLSN SGLITIAGGK LTGFRKMAEK TVNLVVKQLA EEYRGSYPRC ETQHITLSGG
     DVGGANRWEN FVKEKLELAS KIGFEKKKAW TLIHRYGTNV DKVFERFVEL NKYRFNTECE
     LKAELYYCVE EEMVVKAEDY LIRRTGDYYF NWRKSMNRSD LVNRLLYMIQ K
//