ID   G8SBX1_ACTS5            Unreviewed;       563 AA.
AC   G8SBX1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=glpD {ECO:0000313|EMBL:AEV86512.1};
GN   OrderedLocusNames=ACPL_5625 {ECO:0000313|EMBL:AEV86512.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV86512.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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; CP003170; AEV86512.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8SBX1; -.
DR   STRING; 134676.ACPL_5625; -.
DR   KEGG; ase:ACPL_5625; -.
DR   PATRIC; fig|134676.3.peg.5543; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000005440; Chromosome.
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:UP000005440}.
FT   DOMAIN          22..371
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          398..523
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          535..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  61379 MW;  5BB09D988ADC7177 CRC64;
     MTVLSPERRD AALAALAAAE VDVLVIGGGV VGAGCALDAV TRGLSVGLVE ARDFASGTSS
     RSSKLIHGGL RYLEMLDFGL VHEALRERGL ILSRLAPHLA RPVRFLYPLQ HRGWERLYTG
     AGVALYDTMA WSGSLPNHRH LTRRGALRAC PALRKESLVG ALQYYDAQVD DARHTMFLAR
     TAAAYGAHVA NRVEVVGFLR EGERVTGVTV RDLEYDRTFE IRAQQVINAT GVWTDETQSL
     VGERGQFHVR ASKGIHLVVP RDRIQSTTGL ILRTASSVLF VIPWGRHWIV GTTDTDWALD
     KAHPAASAKD IDYLLTEVNK VLARPLERAD VQGVYAGLRP LLSGESESTS KLSREHMVGS
     PVPGLVVVAG GKYTTYRVMA KDAVDACAFN LNRSVARCCT DRIPLLGAEG YPALWNRRGL
     IAAGSGLHIA RVEHLLGRYG SLIHDLLALI EDDPTLGRPL TGADDYLRAE VVYAAAAEGA
     RHLVDVLTRR TRISIETFDR GTSSAAEAAE LMARVLGWTP AQRDREVENY RLRVEAERAS
     QEQQTDETAD ATRLGAPDVI PLS
//