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Database: UniProt
Entry: A0A0N0T996_9ACTN
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Original site: A0A0N0T996_9ACTN 
ID   A0A0N0T996_9ACTN        Unreviewed;       568 AA.
AC   A0A0N0T996;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KOV85975.1};
GN   ORFNames=ADL01_07440 {ECO:0000313|EMBL:KOV85975.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV85975.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV85975.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV85975.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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}.
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:KOV85975.1}.
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DR   EMBL; LGDW01000051; KOV85975.1; -; Genomic_DNA.
DR   RefSeq; WP_053741098.1; NZ_LGDW01000051.1.
DR   AlphaFoldDB; A0A0N0T996; -.
DR   PATRIC; fig|1519490.3.peg.1624; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000037738; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
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; 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:UP000037738}.
FT   DOMAIN          24..377
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          404..528
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          539..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  61952 MW;  7EE98D3EA8BA0E6B CRC64;
     MRTAALGPAQ RAESLAAMAE RELDVLVVGA GVVGAGTALD SVTRGLSTGL VEARDWASGT
     SSRSSKLIHG GLRYLEMLDF ALVREALKER GLLLERLAPH LVKPVAFLYP LQHQGWERLY
     AGAGVALYDA MSMARGHGRG LPAHRHLSRR HALRVAPALK KDALVGALQY YDAQMDDARY
     VATLVRTAAA YGAKVANRAR VTSFLREGER VVGARVQDVE GGGEYEIRAR QIVNATGVWT
     DDTQAMVGQR GQFHVRASKG IHLVVPKDRI HSTTGLILRT EKSVLFVIPW GRHWIVGTTD
     TDWDLDKAHP AASSADIDYL LEHVNSVLAV PLTRDDVQGV YAGLRPLLAG ESDATSKLSR
     EHTVAHPVPG LVVVAGGKYT TYRVMAKDAV DAAVHGLDQR VAECVTEDVP LLGAEGYRAL
     WNARARTAAR TGLHVVRVEH LLNRYGSLAQ EVLDLIAADS SLGEPLQAAD DYLRAEIVYA
     ASHEGARHLD DVLTRRTRIS IETFDRGTRS SREAAELMAP VLGWDKDQIE REVEHYDKRV
     EAERESQRQP DDLTADAARL GAPDIAPL
//
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