ID F3NI23_9ACTN Unreviewed; 516 AA.
AC F3NI23;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:EGG47063.1};
GN ORFNames=SGM_2787 {ECO:0000313|EMBL:EGG47063.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG47063.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG47063.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG47063.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(2011).
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:EGG47063.1}.
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DR EMBL; AEYX01000034; EGG47063.1; -; Genomic_DNA.
DR RefSeq; WP_006140489.1; NZ_AEYX01000034.1.
DR AlphaFoldDB; F3NI23; -.
DR STRING; 996637.SGM_2787; -.
DR eggNOG; COG0578; Bacteria.
DR Proteomes; UP000003022; 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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 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:UP000003022}.
FT DOMAIN 32..394
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 427..502
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 516 AA; 52903 MW; D2715D46FF2C3459 CRC64;
MTATPSPTAA TSLSAARRIR ELTATVGGGA VDVLVVGLGA TGAGVALDAA SRGLSVAAID
AHDLAFGTSR WSSKLIHGGL RYLAAGQFDV AHESAVERGV LMERTAPHLV RAQPFVLPLT
PLVSRGGAAL AWAGFRAGDA LRIAARTARA TLPAPRRLTP VETRRLAPAL RAAGLRGGLL
SWDGRLVDDA RLVTALARTA AGRGARILTR VRALELDGSG ARVRDELTGE EGVIRARAVV
NAAGVWAGGL VEGVRIRPSR GTHLVLRGDL LGPLPAGLHI PVPGEGNRFV LVLPQEDGRV
YVGLTDEPLE GTVVPDVPEV PETDIGFLLD VVGTALGVPV RRADVAGAFA GLRPLLDGGA
GPGAGTADLS RRHAVLISSE GVVTVVGGKL TTYRRMAQDA VDAAVAGGRV TAGPSRTTAL
PLVGAGPAPA GVPRRLIRRY GTEAAAVHAL GAADPGLREP VVAGYPVTRA ELWWGVRHEG
ALDEADLLDR RCRLGLVAGE REAAVGAARE ALGGVG
//
