ID A0A437J8L8_9SPHN Unreviewed; 499 AA.
AC A0A437J8L8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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=ENE74_06145 {ECO:0000313|EMBL:RVT41846.1};
OS Sphingobium algorifonticola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=2008318 {ECO:0000313|EMBL:RVT41846.1, ECO:0000313|Proteomes:UP000282977};
RN [1] {ECO:0000313|EMBL:RVT41846.1, ECO:0000313|Proteomes:UP000282977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLA-22 {ECO:0000313|EMBL:RVT41846.1,
RC ECO:0000313|Proteomes:UP000282977};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVT41846.1}.
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DR EMBL; RZUL01000002; RVT41846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437J8L8; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000282977; 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.
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:UP000282977}.
FT DOMAIN 4..358
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..484
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 499 AA; 54880 MW; 3F8537FBB4CF6ACA CRC64;
MIYDICVIGG GINGTGIARD AAGRGASVLL LEKDDLASGT SSASTKLIHG GLRYLEHYEF
RLVRESLMER ERLLGIAPHI AWPMRFVLPH HPGLRPRWLL RLGLFLYDHI GGRKLLPPTR
SIDLRSDPAG TPLKPGFAHA FEYSDCWVDD ARLVVLNARD AAARGAEIRT RCAVTGATRE
GDLWRIDSRA ADGTEQTFQA RTIVNAGGPW VVRMIDASHT PRSANIRLVR GSHIVTRRLF
DHDRSYIFQN ADGRIIFAIP YERDLTLIGT TDREHESPDV PAKATDEEIA YLCAAASEYF
AKPITRDDVI WTYSGVRPLV DDGASAAQEA TRDYVLKLDK DGGAPLLSIF GGKITTYRRL
AEEAVEMLAP SLPVLKGASW TAGAALPGGD FALSERGALA DRIAREHPFL SMDDIARIVA
TYGTCAFDWL GDARDRAALG EDFGGGLTEA EVRYLVRAEW ARTADDVLWR RTKLGLRVDA
HGVARLEGLM GRLVNEVMV
//
