ID A0A1H3CE08_9BURK Unreviewed; 554 AA.
AC A0A1H3CE08;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN04515617_104229 {ECO:0000313|EMBL:SDX52432.1};
OS Collimonas sp. OK242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDX52432.1, ECO:0000313|Proteomes:UP000198586};
RN [1] {ECO:0000313|EMBL:SDX52432.1, ECO:0000313|Proteomes:UP000198586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK242 {ECO:0000313|EMBL:SDX52432.1,
RC ECO:0000313|Proteomes:UP000198586};
RA de Groot N.N.;
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; FNOR01000004; SDX52432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3CE08; -.
DR STRING; 1798195.SAMN04515617_104229; -.
DR Proteomes; UP000198586; 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}.
FT DOMAIN 53..374
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 432..528
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 554 AA; 61985 MW; 8C70784EE76BA625 CRC64;
MFEFEQYTFE YKYSMMCGDI AGIPFCQLAI IDFVRLARYR HKEIAVASSE IVDLLVVGGG
VNGAGIARDA AGRGLSVLLC EQDDLASHTS SASTKLIHGG LRYLEHYEFS LVRKALQERE
RLLRLAPHII APLRFVMPHV SSLRPAWMIR AGMFLYDNLA KRELLAGSRA IDFRKHVAGA
PLKKTLTKGF VYSDAAVQDA RLVVLNAMDA KERGATILTK TRLIEAKRGK QYWDTTLQSS
LTGETTEIKA RCIVNAAGPW VASLLSGALH TSAQHQIRLV KGSHIVTKRL FDHDHAYIFQ
NPDKRIVFAI PYETDFTLIG TTDVEYSGDP SKVEISAEET AYLCESVSRY FEAAVTPSQV
VWSYAGVRPL LEEEIANPSA VTRDYRLELK AEEGQAPVLS VFGGKITTYR RLAEEAMEHL
QPLFGYMKAH WTADEALPGG DIANADFAEF RRIFQQRHAW LPTVLGARYA RAYGTRAARL
LAGIHDMAGL GELFGADLYE AEVRYLMRNE WALTADDILW RRSKLGLRFD AVAVDRLNRW
LERQQAPAPA VMPA
//
