ID D0VWP7_STRSP Unreviewed; 607 AA.
AC D0VWP7;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Alpha-glycerophosphate oxidase {ECO:0000256|ARBA:ARBA00021658};
DE EC=1.1.3.21 {ECO:0000256|ARBA:ARBA00013104};
DE AltName: Full=Glycerol-3-phosphate oxidase {ECO:0000256|ARBA:ARBA00032349};
GN Name=glpO {ECO:0000313|PDB:2RGO};
OS Streptococcus sp.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1306 {ECO:0000313|PDB:2RGO};
RN [1] {ECO:0000313|PDB:2RGO, ECO:0007829|PDB:2RGO}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=18154320; DOI=10.1021/bi701685u;
RA Colussi T., Parsonage D., Boles W., Matsuoka T., Mallett T.C.,
RA Karplus P.A., Claiborne A.;
RT "Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a
RT template for the mitochondrial alpha-glycerophosphate dehydrogenase.";
RL Biochemistry 47:965-977(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate +
CC H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642; EC=1.1.3.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000275};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 2RGO; X-ray; 2.40 A; A/B=1-607.
DR PDBsum; 2RGO; -.
DR AlphaFoldDB; D0VWP7; -.
DR SMR; D0VWP7; -.
DR EvolutionaryTrace; D0VWP7; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0004369; F:glycerol-3-phosphate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; 2.
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 NCBIfam; NF033461; glycerol3P_ox_1; 1.
DR PANTHER; PTHR11985:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0000313|PDB:2RGO, ECO:0007829|PDB:2RGO};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0007829|PDB:2RGO};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0007829|PDB:2RGO};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0007829|PDB:2RGO};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..348
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 461..584
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 396..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
FT BINDING 197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2RGO"
SQ SEQUENCE 607 AA; 67572 MW; 863055EC7F8A503B CRC64;
MFSNKTRQDS IQKMQQEELD LLIIGGGITG AGVAVQAAAS GIKTGLIEMQ DFAEGTSSRS
TKLVHGGIRY LKTFDVEVVA DTVGERAVVQ GIAPHIPKPD PMLLPIYEDE GATTFNMFSV
KVAMDLYDKL ANVTGTKYEN YTLTPEEVLE REPFLKKEGL KGAGVYLDFR NNDARLVIDN
IKKAAEDGAY LVSKMKAVGF LYEGDQIVGV KARDLLTDEV IEIKAKLVIN TSGPWVDKVR
NLNFTRPVSP KMRPTKGIHL VVDAKKLPVP QPTYFDTGKQ DGRMVFAIPR ENKTYFGTTD
TDYQGDFTDP KVTQEDVDYL LDVINHRYPE ANITLADIEA SWAGLRPLLI GNSGSDYNGG
DNGSISDKSF NKVVDTVSEY KENKVSRAEV EDVLNHLENS RDEKAPSTIS RGSSLEREPD
GLLTLSGGKI TDYRKMAEGA LRLIRQLLKE EYGIETKEID SKKYQISGGN FDPTKLEETV
TELAKEGVAA GLEEEDATYI ADFYGTNARR IFELAKEMAP YPGLSLAESA RLRYGLEEEM
VLAPGDYLIR RTNHLLFERD QLDEIKQPVI DAIAEYFGWT EEEKAQQTKR LEALIAESDL
RELKGEK
//
