ID A0A3D8YY00_9BACL Unreviewed; 546 AA.
AC A0A3D8YY00;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=DVB69_05865 {ECO:0000313|EMBL:REB08656.1};
OS Sporosarcina sp. BI001-red.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=2282866 {ECO:0000313|EMBL:REB08656.1, ECO:0000313|Proteomes:UP000256461};
RN [1] {ECO:0000313|EMBL:REB08656.1, ECO:0000313|Proteomes:UP000256461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI001-red {ECO:0000313|EMBL:REB08656.1,
RC ECO:0000313|Proteomes:UP000256461};
RA Rajandas H., Sivachandran P., Mai C.W., Cheong K.W., Teh C.S.J.,
RA Lim E.S.H., Yap I.K.S., Convey P., Chong C.W.;
RT "Draft Genome of Sporosarcina subantarcticus.";
RL Submitted (JUL-2018) 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:REB08656.1}.
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DR EMBL; QQAK01000010; REB08656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8YY00; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000256461; 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.
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 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:UP000256461}.
FT DOMAIN 22..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 546 AA; 60968 MW; C68BE18C909B24B7 CRC64;
MKPFSHTNRT HILQQLSNSH YDVIVVGGGI TGTGIALDAT TRGLKVLLIE MQDFAAGTSS
RSTKLVHGGL RYLKQLEVKL VADVGKERAI VYENAPHVTH PEWMLLPFYK SGTFGKFSTS
FGLQVYDFLA GVKKSERRKM LSKEEVLEHE PLLNKEGLIG GGEYVEYRTD DARLTMEVAK
KAHEQGADLI NYTKVTKFLY DEQGQVNGVQ MEDQLTGEPY ATLGAIVVNA GGPWVEQVMD
LDEKVEGKKL LLTKGVHLVF DRSVLPLHQP IYFDTPDGRM IFAIPRNGKT YVGTTDTVYE
TDLKNPKMTD EDKEYLLRAI TKIFPNAFIG MSDIESTWVG VRPLIQQEGK GPSEISRKDE
VWTSSTGLLT IAGGKLTGYR KMAQSITDTI SEKLEAQGVK AGPCVTKTLP LSGGDFNKSS
DYSHYVEDRA HELTKLGLSF QDGLNIASMY GTNTNQVAEL VSRVNPSSEL PRAIQLTLLY
AIEYEMAMTP VDYFMRRTGA IFFDINWVEK WKAHVISYMK EVLNWSSEQT NQYSEELEAR
LADAKG
//
