ID A0A292YJA4_9BACL Unreviewed; 555 AA.
AC A0A292YJA4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=EFBL_0073 {ECO:0000313|EMBL:GAX88464.1};
OS Effusibacillus lacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Effusibacillus.
OX NCBI_TaxID=1348429 {ECO:0000313|EMBL:GAX88464.1, ECO:0000313|Proteomes:UP000217785};
RN [1] {ECO:0000313|Proteomes:UP000217785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skLN1 {ECO:0000313|Proteomes:UP000217785};
RA Watanabe M., Kojima H., Fukui M.;
RT "Draft genome sequence of Effusibacillus lacus strain skLN1.";
RL Submitted (JUL-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX88464.1}.
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DR EMBL; BDUF01000003; GAX88464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292YJA4; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000217785; Unassembled WGS sequence.
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; 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:UP000217785}.
FT DOMAIN 25..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 407..536
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 555 AA; 62464 MW; 8469ED762CE93741 CRC64;
MNTIKEFSFK GRTTRLEEMS CAPLDLLVVG GGITGAGIAL DAASRGLKVG LVEKQDFGAG
TSSRSTKLIH GGLRYLKQGE IRLVQEVGRE RDILYRNAPH LVIPEKMLLP LVEGGTFGKW
ATSFGLWVYD RLAGVKKEER RVMLSKEETE RLEPLLRKDI LKGSGLYIEY RTDDARLTIE
VMKTANSHGA LCVNYAEAAE FIYEDGKIVG ARVKDLIHGT TYDIYAKNIV NAAGPWVDKL
RDKDKSLYGK RLHLTKGVHL VVPHRRLPLR QSVYFDVPDG RMIFAIPRDE STYIGTTDTT
YSGNLEKPRV SATDVEYLLE AVNNMFPSVH ITKDDITSSW AGLRPLIHED GKSPSELSRK
DEIFHSPTGL ITIAGGKLTG FRKMAERVVD YVANVLAQEE GRIFKPCFTD RITLSGGDFS
SPDQIPDFVA KLTEVGQRFG LEENHIRSLV GKYGSNTVRI LQIAEEQYDE GNSQPPQMLM
TLAELTYGIE HEMVAHLTDF LIRRTGNLFF ERDALADRYV AVLEEMARNF QWDDGEKNVR
LREFMEEYEA AIEFV
//
