ID A0A101QW37_9ACTN Unreviewed; 538 AA.
AC A0A101QW37;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KUN37210.1};
GN ORFNames=AQJ30_18585 {ECO:0000313|EMBL:KUN37210.1};
OS Streptomyces longwoodensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN37210.1, ECO:0000313|Proteomes:UP000053271};
RN [1] {ECO:0000313|EMBL:KUN37210.1, ECO:0000313|Proteomes:UP000053271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN37210.1,
RC ECO:0000313|Proteomes:UP000053271};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT for the species Streptomyces longwoodensis.";
RL Submitted (OCT-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:KUN37210.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMWS01000020; KUN37210.1; -; Genomic_DNA.
DR RefSeq; WP_067235150.1; NZ_KQ948554.1.
DR AlphaFoldDB; A0A101QW37; -.
DR STRING; 68231.AQJ30_18585; -.
DR Proteomes; UP000053271; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053271}.
FT DOMAIN 38..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 423..535
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 57619 MW; 7B1EB26BB0FEDBD9 CRC64;
MTTQSTLQSV PALGTHPSSG SAPSRAETRE QLSKASYDLL VIGGGILGIS TAWHAAQSGL
RVALVDAGDF AGATSSASSK LLHGGLRYLQ TGAVKLVAEN HFERRAVSRQ VAPHLANPLT
FYLPVYKGGP HGAAKLGAGV FAYSALSAFG DGVGHLLSPA KAAQDVPELR TENLKAVAVY
GDDQMNDARM ALMTVRAAVE SGAVVLNHAE VTGLRFTRGR VTGADLKDRT TGDEFGVNAR
LVLNATGPWV DHLRRMEDPD AAPSIRLSKG AHLVLKRTSP WKAALATPID KYRITFALPW
EDMLLLGTTD EEFEGDPADV SVTEKDMAQI LDEAAFSVRD QQLSRDLITY SFAGLRVLPG
GPGDTAKAKR ETVVTEGRGG MLSVAGGKWT TFRHIGRTVM KKLEALPGHP LGDDFEPIAS
LPKKLPLPGV ANPRAVAHRL LVDNPAPGPR MAADTAKHLA THYGSLAFDI ARLANEDPEL
GRRVHPDAPE IWAQVVYARD HEWAETADDV LRRRTTLTIR GLATDEVRAK VQDVLDGK
//
