ID A0A1Y0MB31_9FLAO Unreviewed; 548 AA.
AC A0A1Y0MB31;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=BTO04_10055 {ECO:0000313|EMBL:ARV07010.1};
OS Polaribacter sp. SA4-10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=754397 {ECO:0000313|EMBL:ARV07010.1, ECO:0000313|Proteomes:UP000195822};
RN [1] {ECO:0000313|EMBL:ARV07010.1, ECO:0000313|Proteomes:UP000195822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-10 {ECO:0000313|EMBL:ARV07010.1,
RC ECO:0000313|Proteomes:UP000195822};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) 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|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019331; ARV07010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0MB31; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000195822; 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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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.
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:UP000195822}.
FT DOMAIN 22..345
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..529
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 548 AA; 62307 MW; B4211DCC11670694 CRC64;
MKKFSYLERE NSTKELQATE FDLLIIGGGI TGAGIALDAA SRGMKVALIE KNDFASGTSS
KSTKLIHGGL RYLKQFDFWL VKEVGTERAI VHKLAPHLVI PEKMILPLID GGTYGSWLTS
IGLKVYDILA SVEGEDKRVM LDKEEALEKE PLLPESILNG AGYYAEYRTD DARLTIEVLK
TALDYDAKLL NYAEATEFIY KDERVVGAKV KDTFTDASFE IKAKYVVNAC GPWVDELRQM
NHSKTGKRLH LTKGVHLVVP HEKLPVKQSV YFDVPDGRMM FAIPRGKVTY FGTTDTNYQL
DKNNVETNLV DATYLISAVN NMFPEISLTL EDVQSSWAGL RPLIHEEGKS ASELSRKDEI
FVSDTELISI AGGKLTGYRK MAERIVDLVS KKYNRRYDKE FSAIKTEEIN LSGGTFKNSS
EVKSYIDAIH NRIAEVDFDE KDAEYLVHNY GKQTDTILQK FDDLYHDDMQ EKMIMAEVWF
AVNYEMACTP TDFFMRRTGR LFFDKPSVDL FKNLTLKEFT NHFKWDEKTA KMHLNELDEK
INLASSFN
//
