ID D9VNM3_9ACTN Unreviewed; 535 AA.
AC D9VNM3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:EFL14251.1};
GN ORFNames=SSNG_01503 {ECO:0000313|EMBL:EFL14251.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL14251.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL14251.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL14251.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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; GG657750; EFL14251.1; -; Genomic_DNA.
DR RefSeq; WP_007263198.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VNM3; -.
DR STRING; 253839.SSNG_01503; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_1_11; -.
DR Proteomes; UP000005763; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 35..390
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 420..516
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57454 MW; 40B2C87B2350E3BD CRC64;
MSTLQSVPAL GTHPTSGANA SRAETREQLS KATYDLLVIG GGILGTSVAW HAAQSGLRVA
MVDAGDFAGA TSSASSKLVH GGLRYLQTGA VKLVAENHHE RRVLAKDVAP HLVNPLTFYL
PVYKGGPVGA AKLGAGVFAY SALSAFGDGM GKVISPARAV ADNPGLKTDN LKAVAVYYDH
QMNDSRVAVM TVRAAVESGA VVLNHAEVTG LRMTRGRVSG AELKDRLDGT EFGVDARVVL
NATGPWVDHL RRMEDKHAMP SIRLSKGAHI VMKRKSPWKA AMATPIDKYR ITFALPWEDQ
LLLGTTDEVY EGDPADVRAT ESDIQQILDE AAFSIKDADL DRSLMTYAFA GLRVLPGGPG
GVEKAKRETV VSEGAGGMLS VAGGKWTTYR HIGRVVMDKL AKLPGSPLTE DMEPVKSLVR
RVPLPGVANP NAVAHRLLVD REPGARMDPL TARHLASHYG SLAFDIARLA NEDPALAERI
HPDGPEIWAQ VAYARDNEWA ETVDDVLRRR TTVTVRGLDD EAVRARVEEM LGRKA
//
