ID A0A1H8PDH6_9BACL Unreviewed; 634 AA.
AC A0A1H8PDH6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN05518847_107300 {ECO:0000313|EMBL:SEO40000.1};
OS Paenibacillus sp. OV219.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1884377 {ECO:0000313|EMBL:SEO40000.1, ECO:0000313|Proteomes:UP000199330};
RN [1] {ECO:0000313|EMBL:SEO40000.1, ECO:0000313|Proteomes:UP000199330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV219 {ECO:0000313|EMBL:SEO40000.1,
RC ECO:0000313|Proteomes:UP000199330};
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|ARBA:ARBA00000153,
CC 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 -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
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; FOCJ01000007; SEO40000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PDH6; -.
DR STRING; 1884377.SAMN05518847_107300; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000199330; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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: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; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..351
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 555..613
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 634 AA; 68180 MW; DEA295FB237C8F3E CRC64;
MNEPFSASAR TMYLERMASE LLDVLIIGGG ITGAGIAWDA SRRGLRAGLV EMGDYAQGTS
SRSTKLVHGG LRYLKQGEVR LVAEVGRERA LLHRHAPHVV MPAPMLMPVY KGGTFGYYAS
SIGLYIYDRL ARVKHAERRR MYRREQTEAL EPLLKREGLR GSGRYYEYRT DDARLTLEVM
KTAHRHGASI VNYAKAEEML YRDGVICGAR VKDIRSGKSY DIYARKIVNA AGPWADHVRS
MDGKIEGKRL MLTKGVHLVV DYAKLPVKQA IYIDVSDGRM IFIIPRDGKT YFGTTDTFYN
DDPGDVITTR ADRDYLLTAV NAAFPTAALT SADIESSWAG VRPLVHEDGK SPSEISRKDE
IFISDKGLVT IAGGKLTGFR KMAEKVVDLV AADVKEGTGR KFKGCTTHKE VLSGGDYSGY
PTFEAMCEAL LLDGERQGVP KESLSGWVAR YGSNAPKLLA RYAAYERAEA NEQRAAASAG
AGLPVAAASE DVRAGVGGAG GASGVSGAGS AGGAGGAGGA GGASGAGEAG SAAAGRRITV
AVGRAEALHN ARLEWALRAE LDFAVEEEMT CSAVDFLMRR TGMILFDRGR AEKLTGAVVR
LLGQRFGWNE EKRGTELASV QAELHAAAAF PDMT
//
