ID A0A1V9DPG3_9GAMM Unreviewed; 502 AA.
AC A0A1V9DPG3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=B2J69_03695 {ECO:0000313|EMBL:OQP35615.1};
OS Pantoea latae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1964541 {ECO:0000313|EMBL:OQP35615.1, ECO:0000313|Proteomes:UP000192769};
RN [1] {ECO:0000313|EMBL:OQP35615.1, ECO:0000313|Proteomes:UP000192769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS1 {ECO:0000313|EMBL:OQP35615.1,
RC ECO:0000313|Proteomes:UP000192769};
RA Lata P., Govindarajan S., Qi F., Li J.-L., Maurya S.K., Sahoo M.K.;
RT "Whole genome shotgun sequence of Pantoea agglomerans strain AS1 isolated
RT from a cycad, Zamia floridana in Central Florida, USA.";
RL Submitted (FEB-2017) 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:OQP35615.1}.
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DR EMBL; MWUE01000005; OQP35615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9DPG3; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000192769; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 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}.
FT DOMAIN 5..323
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..487
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 502 AA; 56827 MW; 248E01769371C8A5 CRC64;
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEARDLACA TSSASSKLIH GGLRYLEHYE
FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRTGLFLYDH LGKRTSLPGS
KSLRFGADSA LKPEITRGFE YSDCWVDDAR LVVLNAQEVV KRGGDVRTRT RVTRAWRENG
LWMVEAEDVD SGKTYTWRAK ALVNAAGPWV KQFFDDGLKL KSPYGIRLIK GSHIVVPRVH
NEKQSYILQN EDNRIVFVIP WMDDFSIIGT TDVEYKGDPK NVKIDESEID YLLKIYNSHF
KKPLARNDVV WTYSGVRPLC DDESDSPQAI TRDYTLDVRD DNGQAPLLSV FGGKLTTYRK
LAEHALEKLT KYFPNAGPAW TKNCVLPGGD IAGTREDYAA SLRRRYPFIT EGMARHFART
YGSSTETLLD GATRLEDLGE NFGHDFYEAE LRYLVQNEWV RELDDAIWRR TKQGMWLNEA
QQARVAEWLA THSQKPSLSL AS
//
