ID A0A1A9HV94_9BURK Unreviewed; 518 AA.
AC A0A1A9HV94;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=ABE85_21550 {ECO:0000313|EMBL:ANH70802.1};
OS Mitsuaria sp. 7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1658665 {ECO:0000313|EMBL:ANH70802.1, ECO:0000313|Proteomes:UP000078154};
RN [1] {ECO:0000313|EMBL:ANH70802.1, ECO:0000313|Proteomes:UP000078154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7 {ECO:0000313|EMBL:ANH70802.1,
RC ECO:0000313|Proteomes:UP000078154};
RA Bao W., Leung F.C.C., Jiang J.;
RT "Complete Genome Sequence of Mitsuaria sp. Strain 7, a Lignin-degrading
RT Bacterium Isolated from Forest Soil.";
RL Submitted (JUL-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; CP011514; ANH70802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9HV94; -.
DR STRING; 1658665.ABE85_21550; -.
DR KEGG; miu:ABE85_21550; -.
DR PATRIC; fig|1658665.3.peg.4406; -.
DR Proteomes; UP000078154; 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.
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:UP000078154}.
FT DOMAIN 2..361
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 385..498
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 518 AA; 57658 MW; 73B3B23083998AC0 CRC64;
MLVVGGGING AGIARDLAGR GWKVVLAEAS DFAAHTSSSS TKLIHGGLRY LEYYEFSLVR
KALQEREVLL RSAPHIMWPL RFVMPHDAAM RPAWMIRIGL FLYDHLARRE VLPASEGVDL
RRSPYGEPLK AEYTKGFVYS DGWVDDARLV LLNALDAREH GAALHTRTTV TAAKRHADHW
TATLRCADGD RTLKARALVN AAGPWAEGFL REVAAPARGE ALATKSLRLV KGSHIIVHKR
FQHDHAYIFQ NPDKRIIFAI PYEDDFTLIG TTDVELAPDA LAGFGKARID EREIAYLCEQ
ASRYFREPVV ASDVVWTYAG VRPLLDDASG DPSAVTRDYL LETHADGGAP LLSVWGGKIT
TFRKLAEDAA DLLGDLLGDR RRAWTEHAHL PGGDLREWIG APQRPDTDFQ RLLSAVGQRH
PWLPPSLARR LARAYGARLG RVLGGAERLD DLGPEIAPGL HQAELEYLVR EEWARAADDV
LWRRSKLGLH YTEAQRMAVV QWFAEREHLW AKPSAAAA
//
