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Database: UniProt
Entry: A0A1W7M793_9SPHN
LinkDB: A0A1W7M793_9SPHN
Original site: A0A1W7M793_9SPHN 
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
//
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