ID A0A438ANC6_9RHOB Unreviewed; 534 AA.
AC A0A438ANC6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=EKE94_03960 {ECO:0000313|EMBL:RVW00027.1};
OS Mesobaculum littorinae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Mesobaculum.
OX NCBI_TaxID=2486419 {ECO:0000313|EMBL:RVW00027.1, ECO:0000313|Proteomes:UP000285908};
RN [1] {ECO:0000313|EMBL:RVW00027.1, ECO:0000313|Proteomes:UP000285908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M0103 {ECO:0000313|EMBL:RVW00027.1,
RC ECO:0000313|Proteomes:UP000285908};
RA Li F.;
RT "Mesobaculum littorinae gen. nov., sp. nov., isolated from Littorina scabra
RT that represents a novel genus of the order Rhodobacteraceae.";
RL Submitted (NOV-2018) 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:RVW00027.1}.
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DR EMBL; RQXX01000001; RVW00027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A438ANC6; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000285908; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000285908}.
FT DOMAIN 9..390
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 412..518
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 534 AA; 59555 MW; 0BBD2E2DEDE5DFB5 CRC64;
MSADSADFDM FVIGGGINGV GIARDAVGRG LTVGLAEMND LASATSSSST KLFHGGLRYL
EYFEFGLVRK ALIERETLLE AMPHISWPMR FVLPWHASMR FESDTPTSKL LSTVMPWMKG
RRPSWLIRLG LFMYDHLGGR KFLPGTSTVD LRTDPAGAPL QDRFEKAYEY SDCWVEDSRL
VVLNARDAAQ RGARVLTRCR VTSAERGRGR EGRLWRVHLA HEDGREETIT ARALVNAGGP
WVANIIHGAL RINSSEGIRL VRGSHIVTKK LFDHDKAYFF QGEDGRIIFA IPYETDFTLI
GTTDREQQGE DPGKPKITDA ERDYLLDFAS NYFKRPVTAE DIVWTYSGVR PLYDDGAKSA
TAATRDYVLS LDENGAPLLN VFGGKITTYR RLAESAVEKL GHYFPGTGKN WTSGVALPGG
DFPVDGVPNL IAKLQEQHPF LDDYRAGRLV RAYGTEAEKV MAGAKTEEDL GRSFGAYLSE
REVRWLMERE FAMTAEDIVW RRTKLGLRMS ADEIAALEAF MTEERARSIG AAAE
//
