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Database: UniProt/TrEMBL
Entry: G8RZP5_ACTS5
LinkDB: G8RZP5_ACTS5
Original site: G8RZP5_ACTS5 
ID   G8RZP5_ACTS5            Unreviewed;       515 AA.
AC   G8RZP5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AEV84658.1};
DE            EC=1.1.5.3 {ECO:0000313|EMBL:AEV84658.1};
GN   Name=glpD {ECO:0000313|EMBL:AEV84658.1};
GN   OrderedLocusNames=ACPL_3763 {ECO:0000313|EMBL:AEV84658.1};
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:AEV84658.1, 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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; CP003170; AEV84658.1; -; Genomic_DNA.
DR   RefSeq; WP_014690730.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8RZP5; -.
DR   STRING; 134676.ACPL_3763; -.
DR   KEGG; ase:ACPL_3763; -.
DR   PATRIC; fig|134676.3.peg.3678; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   OMA; GVMTIMN; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000005440; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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:InterPro.
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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEV84658.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440}.
FT   DOMAIN          26..384
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          405..499
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   515 AA;  52751 MW;  A8CA3E4F1F782A0B CRC64;
     MTAGTALNAG RRARELDELA GGATVDLLVV GLGVTGAGVA LDAASRGLSV AAVDAHDLAF
     GTSRWSSKLV HGGLRYLAGG HLGLAYESAV ERDILLRRVA PHLITPLPSV IPLTPLLSAG
     QAGLARVGLA AGDLLRAGAG TPAGRLPRSR RITPVEVHRL VPAVRRSGLR GGLLGWDGQL
     VDDARLVVAL ARTAAGFGAR VITRCRVEEL TGGGASVRDT LTGERHRLRA RAVVNATGVW
     ADRLDPTISL RPSRGTHLVL RPGVLGRLGA GLTVPVPGTT SRFVFVLPQA DGHAYLGLTD
     EPVEGPVPDV PEPTPAERGF LLDVVSTVLD VPLTEADVVG AFAGLRPLLA GGAGSTADLS
     RRHAVVTSPA GVTTIVGGKL TTYRRMARDA VDAALRSAGL PAGRCRTAGL PLVGAASPER
     LAGSGAPRRL VARYGAEATA VAALAIEDPG LAEPVAEGIA VTGAELLWGV RAEGALDAAD
     LLDRRTRIGL VPADRTRAAG VAETILRRGL AMQGS
//
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