ID A0A1W7M793_9SPHN Unreviewed; 519 AA.
AC A0A1W7M793;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=NMD1_00463 {ECO:0000313|EMBL:GAO53457.1};
OS Novosphingobium sp. MD-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1630648 {ECO:0000313|EMBL:GAO53457.1, ECO:0000313|Proteomes:UP000266860};
RN [1] {ECO:0000313|EMBL:GAO53457.1, ECO:0000313|Proteomes:UP000266860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-1 {ECO:0000313|EMBL:GAO53457.1,
RC ECO:0000313|Proteomes:UP000266860};
RA Okano K.;
RT "Draft Genome Sequence of the microcystin-degrading bacterium
RT Novosphingobium sp. MD-1.";
RL Submitted (APR-2015) 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 -!- 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:GAO53457.1}.
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DR EMBL; BBXA01000013; GAO53457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7M793; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000266860; 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:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.1890; -; 1.
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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000266860}.
FT DOMAIN 11..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 394..496
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 519 AA; 56217 MW; 83E092F9DDC9E267 CRC64;
MTKTSASPVY DIVVVGGGIN GAGIARDAAG RGLNVLLVER EDLASHTSSA STKLIHGGLR
YLEYYEFRLV REALQERERL LRIAPHIIWP LRFVLPRPKG GRPGWMIRIG LWLYDHIGGK
QSLPKSEGVS LRDPRWSDGL KPGLTSGFAY SDAWVDDARM VVLNAMDAAA RGATIRTGVA
MTGARVENGL WQVDLREEAG GVVSTVQARA LVNAAGPWAG SLLHGIGGVA HEGGIRLVKG
SHIIVPPLYK GDHAFILQNP DGRIVFTIPY QKRFTLVGTT DVLVDEAERA RPRISAEETE
YLCRTVSEYF ERQVAPADVV STYSGVRPLY DDGGDDAKAI TRDYVLKLGR EEGPQLLSVF
GGKLTTYRRL AEHALEKLAP FLPAMGPAWT GAGPLPGGDL PGGNFDAFLQ TVHARWPFLP
ADTAERVAHA YGTRVEEWLG GAEGWNALGE DFGAGLTAAE VDYLCAHEWA RTAEDILWRR
TKLGLVCPSD TAERLARYLA RRAGHETAAA PMAASGGEG
//