ID A0A1E7K3Y0_9ACTN Unreviewed; 538 AA.
AC A0A1E7K3Y0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:OEU98595.1};
GN ORFNames=AN217_13100 {ECO:0000313|EMBL:OEU98595.1};
OS Streptomyces qinglanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943816 {ECO:0000313|EMBL:OEU98595.1, ECO:0000313|Proteomes:UP000175829};
RN [1] {ECO:0000313|EMBL:OEU98595.1, ECO:0000313|Proteomes:UP000175829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEU98595.1,
RC ECO:0000313|Proteomes:UP000175829};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEU98595.1}.
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DR EMBL; LJGV01000022; OEU98595.1; -; Genomic_DNA.
DR RefSeq; WP_027760515.1; NZ_LJGV01000022.1.
DR AlphaFoldDB; A0A1E7K3Y0; -.
DR PATRIC; fig|943816.4.peg.2060; -.
DR Proteomes; UP000175829; 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:UP000175829}.
FT DOMAIN 35..390
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 425..519
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"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 57490 MW; E54B944E9CE10BAB CRC64;
MNTSQSVPTL GTHPTAGSNP GRAETRGLLA NATYDLLVIG GGILGTSVAW HAAQSGLRVA
MVDAGDFAGA TSSASSKLVH GGLRYLQTGA VKLVAENHHE RRVLAKDVAP HLVNPLTFYL
PVYKGGPHGA TKLGAGVFAY SALSAFGDGV GRVISPAKAA ADNPALRTDN LKAVAVYGDH
QMNDSRMAVM TVRAAVESGA VVLNHAEVTG LRFTRGRVTG AELRDRTDGA EFGVDARLVL
NATGPWVDHL RTMEDSGAAP SIRLSKGAHL VLKQKSPWGA AMATPIDKYR ITFALPWEDQ
LLLGTTDEEY TGDPADVRAT EADIQQILDE AAFSVRDADL DRDLMTYAFA GLRVLPGGPG
GVESAKRETV VTEGRGGMLS VAGGKWTTYR HIGRTVMDKL EKLPGGALAA SMESAVPVKD
LVRRTPLPGI ANPNAVAHRL LVDREPGVRM DPLTARQLAT HYGSLSFDIA RLVNEDPSLG
ERIHPDGPEI WAQVVYARDH EWAETVDDVA RRRTTLTIRG LDDEKVRGRI EELLGQRD
//
