ID A0A0P0DIX7_SPHMC Unreviewed; 505 AA.
AC A0A0P0DIX7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=LH19_02525 {ECO:0000313|EMBL:ALJ11732.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALJ11732.1, ECO:0000313|Proteomes:UP000062472};
RN [1] {ECO:0000313|EMBL:ALJ11732.1, ECO:0000313|Proteomes:UP000062472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=203 {ECO:0000313|EMBL:ALJ11732.1,
RC ECO:0000313|Proteomes:UP000062472};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a mutant derivative (NBRC15033) of
RT polyethylene glycol-degrading strain Sphingopyxis macrogoltabidus strain
RT 203.";
RL Submitted (OCT-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}.
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DR EMBL; CP009429; ALJ11732.1; -; Genomic_DNA.
DR RefSeq; WP_054724621.1; NZ_CP013344.1.
DR AlphaFoldDB; A0A0P0DIX7; -.
DR STRING; 33050.AN936_15765; -.
DR KEGG; smaz:LH19_02525; -.
DR PATRIC; fig|33050.6.peg.510; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000062472; 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: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}.
FT DOMAIN 9..329
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 386..482
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 505 AA; 55836 MW; D2C57C2A3B4EC5BE CRC64;
MPDSAQPYDV IVVGGGVNGA GVARDAAGRG ARVLLLEAGD LAQGTSSKST KLIHGGLRYL
EHYEFGLVRE ALKEREILWS IAPHIIWPLR FVLPYRTGLR PRWLLRLGLF LYDHIGGRKK
LPATRSIDLA QHEAGTPLQS QYVRAFEYSD GWVDDARLVL LNARDAAERG ARIRTRTRAE
TMRVEGGLWV VEGSDDRGHR YRFTGKSLVN AAGPAVLDLL ARASAPPDYR MRLVRGSHIV
VRRKFAHDYA YFFQLPDGRI FFAIPYERDF TLIGTTDRDH DGPLAEVHAS ADEIAYLCEG
ASEYFREPVT PADVVWTYSG VRPLIEDGSG RPEAATRGYR IDIDVDEGAP LLTIYGGKIT
SYRHVAEHAV DELAGHLDAV STRRWTAKTP LPGGDFGIDG AAALKAEYKL AHPFLPAATV
DRVVKAYGTD ARAWLGKAED WDALGGEIAH GLSAAEAQWM IEREWARDVE DILWRRSKLG
LLFGADDVAK LAAWLQARRP AGQPA
//
