ID A0A1H8KC80_9BURK Unreviewed; 511 AA.
AC A0A1H8KC80;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN05428959_103702 {ECO:0000313|EMBL:SEN90583.1};
OS Duganella sp. CF517.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEN90583.1, ECO:0000313|Proteomes:UP000198691};
RN [1] {ECO:0000313|Proteomes:UP000198691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA Varghese N., Submissions S.;
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; FODC01000003; SEN90583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8KC80; -.
DR STRING; 1881038.SAMN05428959_103702; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000198691; 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:UP000198691}.
FT DOMAIN 11..332
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 386..500
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 511 AA; 56549 MW; 07F58D3E00689CE2 CRC64;
MAEPQHTLDC DVLIVGGGIN GAGIARDAAG RGLSVVLCEK DDLASHTSSA STKLIHGGLR
YLEYYEFNLV RKALIERETL LRAAPHIMWP MRFVMPHAKG QRPALLIRAG LVLYDLLAKR
ELLPASSGVN LRCHAAGKPL KPEFQRGFIY SDGWVDDARL VVLNAIDACE KGATILTQAV
CNALVRKAAG WEATLYKPSC GNIRVNARYV VNAAGPWTAD LLHAALPKEG GGTLRLIKGS
HIVVKRIFEH DNAYIFQHPD GRIVFAIPYE RDFTLIGTTD LDYHGDANQV AIGEDEIAYL
CELASQYFVE PIVPADVVWT YSGVRPLVED GADAKAVTRD YRLEVDSDGP PMLSVFGGKI
TTFRKLAEEA VDLIAKSLDN HHGGWTHNAC LPGGDVYGAE PQNKSVLQFD AWVRTMQARY
AWLPPLLVLR YARAYGTRIH TLLCDRSEVA DMGEQIAPGL YATEVEYLRR YEWARTAQDI
LWRRSKLGLH LPADTADALQ AWLNANPMRR T
//
