ID A0A1J5LFR3_9PROT Unreviewed; 534 AA.
AC A0A1J5LFR3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=BM562_10355 {ECO:0000313|EMBL:OIQ29795.1};
OS Alphaproteobacteria bacterium MedPE-SWcel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ29795.1, ECO:0000313|Proteomes:UP000183546};
RN [1] {ECO:0000313|EMBL:OIQ29795.1, ECO:0000313|Proteomes:UP000183546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ29795.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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:OIQ29795.1}.
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DR EMBL; MPDC01000014; OIQ29795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5LFR3; -.
DR STRING; 1860092.BM562_10355; -.
DR Proteomes; UP000183546; 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 20..397
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 419..520
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 534 AA; 60052 MW; 8D7A3980BB68EC7E CRC64;
MTDSSDIPPH TSADTAPIVD LFVIGGGING CGIARDAAGR GLSVTLAEMK DLASATSSAS
TKLFHGGLRY LEYFEFRLVQ EALIEREVLL RAMPHISWPM RFVLPFHKDM RFDNTTPTSK
LLTTIMPWMK GRRPAWLIRL GLFMYDTLGK RGILPGTRSL DLTKDEAGKP LKDKFQTAFE
YSDCWVEDAR LVVLNARDAE ARGAEILTRT EVTRADRHAD HWEVHIKDLH SGAETVRRAR
MLVNAGGPWV ADVLRQKLGQ NSRENVRLVR GSHIVVPKLY DHGRCYFFQG QDGRIIFAIP
YEEDFTLIGT TDADHPDPQT RPECTPEEQD YLVDFASTYF HRPVAREQIV WTYSGVRPLY
DDGASSATAA TREYVLTLDT SRAPLLNVFG GKITTYRKLA EAALAKVAEV FPDLPADWTA
GVALPGGDFP VNDVVHLQDK LAADYPFLSA YATRRLIRAY GTEAWTVLGD AREESDLGQR
FGATITAREL NWAIDREWVR TGEDYLWRRT KLGLRLNEAE RAEVDTYIRA RATV
//
