ID A0A318HCB0_9BURK Unreviewed; 540 AA.
AC A0A318HCB0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=C7444_10518 {ECO:0000313|EMBL:PXW96921.1};
OS Sphaerotilus hippei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=744406 {ECO:0000313|EMBL:PXW96921.1, ECO:0000313|Proteomes:UP000247811};
RN [1] {ECO:0000313|EMBL:PXW96921.1, ECO:0000313|Proteomes:UP000247811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 566 {ECO:0000313|EMBL:PXW96921.1,
RC ECO:0000313|Proteomes:UP000247811};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-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:PXW96921.1}.
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DR EMBL; QJJS01000005; PXW96921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318HCB0; -.
DR Proteomes; UP000247811; 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:UP000247811}.
FT DOMAIN 25..382
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 434..525
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 540 AA; 59483 MW; 6E3A78385101D613 CRC64;
MATQSPLDTA SATRAEMSAA PIACDVLVVG GGINGVGIAR DLAGRGWSVV LAEQDDLAAH
TSSSSTKLIH GGLRYLEYYE FGLVRKALQE REVLLRSAPH IMWPLRFVMP HDPSMRPAWL
VRLGLFLYDH LARREVLPGS RGVDLRRHPV GAPLQPRFER GFIYSDGWVD DARLVVLNAI
EARERGAQLF TRTRCTAAQR HASGWTATLQ PADGPARTVT ARALVNAAGP WAESFLRGTA
SPATGEALAT KSLRLVKGSH IVVPRCFEHD HAYIFQNPDK RIIFAIPYEQ EFTLIGTTDQ
ELQGDPRGAR IGDDEVAYLC EQASRYFTRA VTPADVVWSY AGVRPLLDDA SGDPSAVTRD
YLLESNTAAA PLLSVWGGKI TTFRKLAEDA ATDVGRMLGE VRSPWTEPAA LPGGDLSAWI
GRPQRPDTDF ERFVTTVRQR HRWLPAALAR RLARAYGSRI DRVLGDAAAL ADLGAEVAPG
LHEAELRYLQ REEWAVSGDD VLWRRSKLGL HYTEAERARV AQWMETPVSK QRESRAAACS
//
