ID G8S986_ACTS5 Unreviewed; 686 AA.
AC G8S986;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=gpd2 {ECO:0000313|EMBL:AEV88862.1};
GN OrderedLocusNames=ACPL_7984 {ECO:0000313|EMBL:AEV88862.1};
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:AEV88862.1, 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; AEV88862.1; -; Genomic_DNA.
DR AlphaFoldDB; G8S986; -.
DR STRING; 134676.ACPL_7984; -.
DR KEGG; ase:ACPL_7984; -.
DR PATRIC; fig|134676.3.peg.7912; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_11; -.
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 42..408
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 432..555
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 594..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 73192 MW; 8C7EE523CB232B85 CRC64;
MTPGRANLGR VRDPSVSRYT AGRLSPIRRT ADLRRLRDEQ FDVLVIGGGV TGAGAAVDAA
SRGLKVALVE ARDFAAGTSS RSSKLIHGGL RYLEQLELHL VHEALTERGL LATRLAPHLV
RPVPILVPLP AANPVKRVWQ RGYYGLGVAA YDVFAGVLGG GRGMPLHRHL SRDGARHLFP
SLRADKITGA IRYYDGQMDD ARLVVNLART AAAQGAAVVT SARVTGFVRE AREVVGVRVK
DLESPGSPEF EVRAKTVVAA TGVWSDDMAE MLRDVGVRPG LRVRASKGVH LVVPRSAITG
EAGLILRTAT SVLFVLPWGG HWIIGTTDTD WELDRSHPAA SARDISYLLD QVNTILDRPL
TTDDIEGVYA GLRPLLSGEA DSTSKLSREH AVVEPMLGLL LVAGGKYTTY RVMAADVIDQ
AVRRLGGAFR PSRTDQLPLL GADGYAAAWR DRQDTARRHG VTTGVIEHLL ERYGTLTVHL
LAMMAADPAL AVPLEGAPEY LAVEVAYAAL AEGALHLDDV LTRRTRISFE TAHRGVESAA
HTARIMGAVL GWNETVRDRE VEHYLARVTA ERQSQTMPDD LTADAARVGA PDVRGLAGDR
AHPPAAASHL EAAASPHPET AASHPETAAS HPETAASHPE TAASHPETAA SHPETAASQL
EAGGSPRPEA GGSAHPDRTG LLEAER
//
