ID A0A1G8KJI9_9BURK Unreviewed; 557 AA.
AC A0A1G8KJI9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN05444748_105126 {ECO:0000313|EMBL:SDI43623.1};
OS Variovorax sp. OV700.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDI43623.1, ECO:0000313|Proteomes:UP000199505};
RN [1] {ECO:0000313|Proteomes:UP000199505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNDR01000005; SDI43623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8KJI9; -.
DR STRING; 1882826.SAMN05444748_105126; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000199505; 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}.
FT DOMAIN 39..397
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 448..535
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 61695 MW; 8831611B87607347 CRC64;
MKRRENTMAP FCDQSHESTG PFPVSDFSSN SPLPATDCDV LIVGGGINGC GIARDLAGRG
WRVVLCEKDD LASHTSSSST KLIHGGLRYL EYYEFSLVRK ALQEREVLLK SAPHIMWPLR
FVMPHDPSMR PAWMIRIGLF MYDHLAKREV LPGSRSIDLR SHAAGAPLKP QFKRGFVYSD
GWVDDARLVV LNAIDARARG AEVLTRTRCV HAQRDADGWT ATLEGADGGI RVVRARAVVN
AAGPWAESFL RGVAQSAKGE TLATRHLRLV KGSHIVVPRL FEHDHAYIFQ NPDKRIIFAI
PYQDEFTLIG TTDIELNGDD PGAARIAEEE IAYLCMQASR YFDKPIKPAD VVWTYSGVRP
LLDDASGDPS AVTRDYMLES NTAAAPLLSV WGGKITTFRK LAEDAADEVG KMLGQSSAQR
PPWTDGAFLA GGDLSAWIGA ATRPDDDFER FVAAVQARYP WLDAKLARRL ARAYGARVAE
LLGDAEAMAD MGDAVAPGLH ERELRFLQEQ EWAMSADDVL WRRSKLGLRY TAEERQQVAD
WLQAGAKNNL YMINGKR
//
