ID A0A370U9T2_9GAMM Unreviewed; 510 AA.
AC A0A370U9T2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=DN730_09055 {ECO:0000313|EMBL:RDL44531.1};
OS Marinomonas piezotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=2213058 {ECO:0000313|EMBL:RDL44531.1, ECO:0000313|Proteomes:UP000254326};
RN [1] {ECO:0000313|EMBL:RDL44531.1, ECO:0000313|Proteomes:UP000254326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-05 {ECO:0000313|EMBL:RDL44531.1,
RC ECO:0000313|Proteomes:UP000254326};
RA Yu L., Tang X.;
RT "Marinomonas sp. YLB-05 draft genome sequence.";
RL Submitted (JUN-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|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:RDL44531.1}.
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DR EMBL; QKRA01000003; RDL44531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370U9T2; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000254326; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000254326}.
FT DOMAIN 8..333
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 387..482
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 510 AA; 57574 MW; 47CA98BA359F8074 CRC64;
MSNEQMLDLF VIGGGINGAG IARDAAGRGL SVALCEKDDL AQGTSSRSGK LVHGGLRYLE
YYEFRLVREA LIEREVLLNS ASHIIWPMRF VLPHSKTDRP AWLVRLGLFL YDHLGGRKRL
PGTRALDLHR DPEGAPIKDQ YTKGFEYSDC WVDDSRLVVL NAVAASQKGA EVLTRTRCVA
AKRNPEGYWD VTTENELTKE VRTFKVKLLV NAAGPWVRKI VDDVASSKSS RNIQLVKGSH
IIVPKFWQGQ QAYLVQNYDK RVIFINPYED DKALIGTTDI PYEGKVEDVK ADESEIEYLL
AAVNRYFKET LRRQDVITTF SGVRPLFDDG QGNPSAVTRD YVFDLDETQG APLLNVFGGK
LTTFRKLSEH AIQKIEKYFP DMGGNWTSGA VLPGGDIPNA DFQSYMQACK ECYPWMPRDL
LVHYGRHYGS IIKQIVSDAS SIEGLGQHFG GNLYEAEVRY LVAHEWAMTP EDVLERRTKE
GLHLSTEQRA AFALWFESEF IKHNTDRKIS
//