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Database: UniProt
Entry: Q9L0I3_STRCO
LinkDB: Q9L0I3_STRCO
Original site: Q9L0I3_STRCO 
ID   Q9L0I3_STRCO            Unreviewed;       568 AA.
AC   Q9L0I3;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Glycerol phosphate dehydrogenase {ECO:0000313|EMBL:CAB82013.1};
GN   OrderedLocusNames=SCO4774 {ECO:0000313|EMBL:CAB82013.1};
GN   ORFNames=SCD63.06 {ECO:0000313|EMBL:CAB82013.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB82013.1, ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAB82013.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA   Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939121; CAB82013.1; -; Genomic_DNA.
DR   RefSeq; NP_628932.1; NC_003888.3.
DR   RefSeq; WP_003974200.1; NZ_VNID01000016.1.
DR   AlphaFoldDB; Q9L0I3; -.
DR   STRING; 100226.gene:17762423; -.
DR   PaxDb; 100226-SCO4774; -.
DR   PATRIC; fig|100226.15.peg.4847; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   InParanoid; Q9L0I3; -.
DR   OrthoDB; 9766796at2; -.
DR   PhylomeDB; Q9L0I3; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT   DOMAIN          24..377
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          404..527
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          538..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  62062 MW;  448EFE3C08517B6E CRC64;
     MRTATLGPAQ RAESLAAMAE RELDVLVVGA GVVGAGTALD AVTRGLSVGL VEARDWASGT
     SSRSSKLIHG GLRYLEMLDF VLVREALKER GLLLERLAPH LVKPVPFLYP LQHKGWERLY
     AGSGVALYDA MSMARGHGRG LPLHRHLSRR HALRVAPALK KDALVGALQY YDAQMDDARF
     VATLVRTAAA YGAKVANRAR VTSFLREGER VVGARVQDVE AGGEYEVRAK QVVNATGVWT
     DDTQAMVGER GQFHVRASKG IHLVVPKDRI HSSTGLILRT EKSVLFVIPW GRHWIIGTTD
     TDWDLDKAHP AASSADIDYL LEHVNSVLSV PLTRDDVEGV YAGLRPLLAG ESDATSKLSR
     EHTVAHPVPG LVVVAGGKYT TYRVMAKDAV DEAVHGLDLR VADCVTEETP LLGAEGYHAQ
     WNARARIAAR TGLHVVRVEH LLNRYGSLTE ELLELVAADP SLGEPLTGAD DYLRAEVVYA
     ASHEGARHLD DVLTRRTRIS IETFDRGTRC AREAAELMAP VLGWDKGQVE REIEHYEKRV
     EAERESQRQP DDLTADAARL GAPDIAAR
//
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