ID A0A0D0WUW5_9ACTN Unreviewed; 610 AA.
AC A0A0D0WUW5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=TK50_17810 {ECO:0000313|EMBL:KIR62806.1};
OS Micromonospora haikouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR62806.1, ECO:0000313|Proteomes:UP000032254};
RN [1] {ECO:0000313|EMBL:KIR62806.1, ECO:0000313|Proteomes:UP000032254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR62806.1,
RC ECO:0000313|Proteomes:UP000032254};
RA Long Z., Huang Y., Jiang Y.;
RT "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT genome.";
RL Submitted (JAN-2015) 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:KIR62806.1}.
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DR EMBL; JXSX01000002; KIR62806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0WUW5; -.
DR PATRIC; fig|47853.6.peg.3725; -.
DR Proteomes; UP000032254; 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; 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.
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:UP000032254}.
FT DOMAIN 32..405
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 428..552
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 566..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 65455 MW; C824B906B56EAE19 CRC64;
MRDPNVSRSV AGQLSPARRA ADLRRLRAER FDVLVIGGGV TGAGAALDAA SRGLKVALVE
ARDFAAGTSS RSSKLIHGGL RYLEQLEFHL VHEALTERGL LATRLAPHLV RPVPILVPLP
AGKGVRDLPG RTFRRSYYGL GVAAYDAFAG LFGGGRGMPL HRHLTREGAR RVFPSLRADG
LAGAIRYYDG QVDDARLVVT LARTAASLGA TVVSSTRAVG LVRQAREVTG VRVRDLEAPT
GSPDAEFEVR ARTVVAATGV WTDDMSRMLN DVGLRRGVRV RASKGVHLVV PRSAITGETG
LILRTATSVL FVIPWGGHWI IGTTDTDWRL DRSHPAASAR DIAYLLEQVN TVLDRPLTTD
DIEGVYAGLR PLLAGEADST SKLSREHAVV EPMLGLLLVA GGKYTTYRVM ASDVVDRAAR
RLGGVRPSRT ADLPLLGADG YAAMWRDRAD LARRHGVPVG VVEHLLERYG TLTLDLLALV
DADPLLASPL AGAPEYLAAE VTYAARAEGA LHLEDVLTRR TRISFETAHR GLESAEHTAE
LMGAVLGWDA ATRAREVAHY RARVEAERES QLMPDDATAD AARLGAPDVR GFAADRGADG
DPVELPSSPR
//
